|
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: 513.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 1 MSAIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGEITIDTGKSISQQKGLI 80
Cdd:PRK11264 1 MSAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLSQQKGLI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 81 RRLRQHVGFVFQNFNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALA 160
Cdd:PRK11264 81 RQLRQHVGFVFQNFNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 161 MRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFANPQQPRT 240
Cdd:PRK11264 161 MRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPRT 240
|
250
....*....|
gi 495775764 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 |
1.14e-166 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 459.84 E-value: 1.14e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGeitidtGKSISQQKGLIRRL 83
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVD------GEDLTDSKKDINKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 84 RQHVGFVFQNFNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRP 163
Cdd:COG1126 76 RRKVGMVFQQFNLFPHLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 164 DVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFANPQQPRTRQF 243
Cdd:COG1126 156 KVMLFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHERTRAF 235
|
....
gi 495775764 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 |
3.78e-136 |
|
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: 381.49 E-value: 3.78e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGeitidtGKSISQQKGLIRRL 83
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIID------GLKLTDDKKNINEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 84 RQHVGFVFQNFNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRP 163
Cdd:cd03262 75 RQKVGMVFQQFNLFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNP 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 495775764 164 DVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRI 222
Cdd:cd03262 155 KVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
3-244 |
1.21e-132 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 374.52 E-value: 1.21e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 3 AIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGEITIDT-----GKSISQQK 77
Cdd:COG4598 8 ALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLkpdrdGELVPADR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 78 GLIRRLRQHVGFVFQNFNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIAR 157
Cdd:COG4598 88 RQLQRIRTRLGMVFQSFNLWSHMTVLENVIEAPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIAR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 158 ALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFANPQQ 237
Cdd:COG4598 168 ALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVFGNPKS 247
|
....*..
gi 495775764 238 PRTRQFL 244
Cdd:COG4598 248 ERLRQFL 254
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
4-245 |
3.21e-113 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 324.74 E-value: 3.21e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGEITIDTGKSIsqqkglIRRL 83
Cdd:PRK09493 2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVD------ERLI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 84 RQHVGFVFQNFNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRP 163
Cdd:PRK09493 76 RQEAGMVFQQFYLFPHLTALENVMFGPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 164 DVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFANPQQPRTRQF 243
Cdd:PRK09493 156 KLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEF 235
|
..
gi 495775764 244 LE 245
Cdd:PRK09493 236 LQ 237
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
4-244 |
1.81e-101 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 298.53 E-value: 1.81e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 4 IDVKNLVKKFHGQ----TVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGeitidtGKSISQ--QK 77
Cdd:COG1135 2 IELENLSKTFPTKggpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVD------GVDLTAlsER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 78 GLiRRLRQHVGFVFQNFNLFPHRTVLENIiEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIAR 157
Cdd:COG1135 76 EL-RAARRKIGMIFQHFNLLSSRTVAENV-ALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIAR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 158 ALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFANPQ 236
Cdd:COG1135 154 ALANNPKVLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQ 233
|
....*...
gi 495775764 237 QPRTRQFL 244
Cdd:COG1135 234 SELTRRFL 241
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1-244 |
1.05e-97 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 285.37 E-value: 1.05e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 1 MSaIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGEITIDTGKSISQQKglI 80
Cdd:COG4161 1 MS-IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDFSQKPSEKA--I 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 81 RRLRQHVGFVFQNFNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALA 160
Cdd:COG4161 78 RLLRQKVGMVFQQYNLWPHLTVMENLIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 161 MRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAkSLFANPQQPRT 240
Cdd:COG4161 158 MEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDA-SHFTQPQTEAF 236
|
....
gi 495775764 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 |
1.09e-97 |
|
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding protein of a conserved four gene ABC transporter operon found next to ectoine unilization operons and ectoine biosynthesis operons. Ectoine is a compatible solute that protects enzymes from high osmolarity. It is released by some species in response to hypoosmotic shock, and it is taken up by a number of bacteria as a compatible solute or for consumption. This family shows strong sequence similiarity to a number of amino acid ABC transporter ATP-binding proteins.
Pssm-ID: 132050 [Multi-domain] Cd Length: 252 Bit Score: 285.96 E-value: 1.09e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRV-GEITID----TGKSISQQKG 78
Cdd:TIGR03005 1 VRFSDVTKRFGILTVLDGLNFSVAAGEKVALIGPSGSGKSTILRILMTLEPIDEGQIQVeGEQLYHmpgrNGPLVPADEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 79 LIRRLRQHVGFVFQNFNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARA 158
Cdd:TIGR03005 81 HLRQMRNKIGMVFQSFNLFPHKTVLDNVTEAPVLVLGMARAEAEKRAMELLDMVGLADKADHMPAQLSGGQQQRVAIARA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 159 LAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFANPQQ 237
Cdd:TIGR03005 161 LAMRPKVMLFDEVTSALDPELVGEVLNVIRRLASEhDLTMLLVTHEMGFAREFADRVCFFDKGRIVEQGKPDEIFRQPKE 240
|
250
....*....|.
gi 495775764 238 PRTRQFLEKFL 248
Cdd:TIGR03005 241 ERTREFLSKVI 251
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
3-244 |
1.14e-95 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 280.36 E-value: 1.14e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 3 AIDVKNlVKKFHGQT-VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGEITIDTGKSISQQKglIR 81
Cdd:PRK11124 2 SIQLNG-INCFYGAHqALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSKTPSDKA--IR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 82 RLRQHVGFVFQNFNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAM 161
Cdd:PRK11124 79 ELRRNVGMVFQQYNLWPHLTVQQNLIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 162 RPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAkSLFANPQQPRTR 241
Cdd:PRK11124 159 EPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDA-SCFTQPQTEAFK 237
|
...
gi 495775764 242 QFL 244
Cdd:PRK11124 238 NYL 240
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
4-236 |
1.96e-90 |
|
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: 266.75 E-value: 1.96e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 4 IDVKNLVKKFHGQ----TVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGeitidtGKSISQQKGL 79
Cdd:cd03258 2 IELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVD------GTDLTLLSGK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 80 -IRRLRQHVGFVFQNFNLFPHRTVLENIiEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARA 158
Cdd:cd03258 76 eLRKARRRIGMIFQHFNLLSSRTVFENV-ALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495775764 159 LAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFANPQ 236
Cdd:cd03258 155 LANNPKVLLCDEATSALDPETTQSILALLRDINRELGlTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-225 |
3.29e-90 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 265.75 E-value: 3.29e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 1 MSA-IDVKNLVKKFH----GQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGEITIDTGKSisQ 75
Cdd:COG1136 1 MSPlLELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSE--R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 76 QKGLIRRlrQHVGFVFQNFNLFPHRTVLENIiEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAI 155
Cdd:COG1136 79 ELARLRR--RHIGFVFQFFNLLPELTALENV-ALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495775764 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 |
1.99e-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: 1.99e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 4 IDVKNLVKKFHGQ----TVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGeitidtGKSISQ--QK 77
Cdd:cd03255 1 IELKNLSKTYGGGgekvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVD------GTDISKlsEK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 78 GLIRRLRQHVGFVFQNFNLFPHRTVLENIiEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIAR 157
Cdd:cd03255 75 ELAAFRRRHIGFVFQSFNLLPDLTALENV-ELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495775764 158 ALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEK-RTMVIVTHEMSFARDvADRAIFMDQGRI 222
Cdd:cd03255 154 ALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAgTTIVVVTHDPELAEY-ADRIIELRDGKI 218
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
4-244 |
5.57e-88 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 261.44 E-value: 5.57e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGEITIDTGKSISQQ-----KG 78
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGQlkvadKN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 79 LIRRLRQHVGFVFQNFNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGK-ETSYPRRLSGGQQQRVAIAR 157
Cdd:PRK10619 86 QLRLLRTRLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERaQGKYPVHLSGGQQQRVSIAR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 158 ALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFANPQQ 237
Cdd:PRK10619 166 ALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQS 245
|
....*..
gi 495775764 238 PRTRQFL 244
Cdd:PRK10619 246 PRLQQFL 252
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-245 |
2.16e-87 |
|
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: 268.31 E-value: 2.16e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 4 IDVKNLVKKF-----HGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGeitidtGKSISQQKG 78
Cdd:COG1123 261 LEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFD------GKDLTKLSR 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 79 L-IRRLRQHVGFVFQNFN--LFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGL-AGKETSYPRRLSGGQQQRVA 154
Cdd:COG1123 335 RsLRELRRRVQMVFQDPYssLNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVA 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 155 IARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFA 233
Cdd:COG1123 415 IARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFA 494
|
250
....*....|..
gi 495775764 234 NPQQPRTRQFLE 245
Cdd:COG1123 495 NPQHPYTRALLA 506
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-241 |
1.22e-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: 261.19 E-value: 1.22e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 1 MSAIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGeitidtGKSISqqkGLI 80
Cdd:COG3842 3 MPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLD------GRDVT---GLP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 81 --RRlrqHVGFVFQNFNLFPHRTVLENIIEGPViVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARA 158
Cdd:COG3842 74 peKR---NVGMVFQDYALFPHLTVAENVAFGLR-MRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 159 LAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFanpQQ 237
Cdd:COG3842 150 LAPEPRVLLLDEPLSALDAKLREEMREELRRLQRElGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIY---ER 226
|
....
gi 495775764 238 PRTR 241
Cdd:COG3842 227 PATR 230
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-236 |
1.91e-84 |
|
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: 251.10 E-value: 1.91e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 4 IDVKNLVKKFHGQT-VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGeitidtGKSISQQKglIRR 82
Cdd:COG1122 1 IELENLSFSYPGGTpALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVD------GKDITKKN--LRE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 83 LRQHVGFVFQN-FN-LFpHRTVLENIIEGPVIvKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALA 160
Cdd:COG1122 73 LRRKVGLVFQNpDDqLF-APTVEEDVAFGPEN-LGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495775764 161 MRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFANPQ 236
Cdd:COG1122 151 MEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYE 226
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
3-244 |
8.53e-84 |
|
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: 249.90 E-value: 8.53e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 3 AIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGeitidtGKSISQ--QKGLi 80
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVD------GQDITGlsEKEL- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 81 RRLRQHVGFVFQNFNLFPHRTVLENI----IEGPVIvkgePKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIA 156
Cdd:COG1127 78 YELRRRIGMLFQGGALFDSLTVFENVafplREHTDL----SEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 157 RALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFANP 235
Cdd:COG1127 154 RALALDPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASD 233
|
....*....
gi 495775764 236 qQPRTRQFL 244
Cdd:COG1127 234 -DPWVRQFL 241
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
3-244 |
1.20e-82 |
|
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: 247.21 E-value: 1.20e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 3 AIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGEITIDtGKSISQQKGLIRR 82
Cdd:TIGR00972 1 AIEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMNDLVPGVRIEGKVLFD-GQDIYDKKIDVVE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 83 LRQHVGFVFQNFNLFPhRTVLENIIEGPVIVKGEPKEEATARARELLAKVGL----AGKETSYPRRLSGGQQQRVAIARA 158
Cdd:TIGR00972 80 LRRRVGMVFQKPNPFP-MSIYDNIAYGPRLHGIKDKKELDEIVEESLKKAALwdevKDRLHDSALGLSGGQQQRLCIARA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 159 LAMRPDVILFDEPTSALDPELVGEVLNTIRQLAqEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFANPQQP 238
Cdd:TIGR00972 159 LAVEPEVLLLDEPTSALDPIATGKIEELIQELK-KKYTIVIVTHNMQQAARISDRTAFFYDGELVEYGPTEQIFTNPKEK 237
|
....*.
gi 495775764 239 RTRQFL 244
Cdd:TIGR00972 238 RTEDYI 243
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
2-231 |
3.02e-81 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 243.81 E-value: 3.02e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 2 SAIDVKNLVKKFHGQT-VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGeitidtGKSISQQKG-L 79
Cdd:COG3638 1 PMLELRNLSKRYPGGTpALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVD------GQDVTALRGrA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 80 IRRLRQHVGFVFQNFNLFPHRTVLENIIEG--------PVIVKGEPKEEaTARARELLAKVGLAGKETSYPRRLSGGQQQ 151
Cdd:COG3638 75 LRRLRRRIGMIFQQFNLVPRLSVLTNVLAGrlgrtstwRSLLGLFPPED-RERALEALERVGLADKAYQRADQLSGGQQQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 152 RVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVT-HEMSFARDVADRAIFMDQGRIVEQGPAKS 230
Cdd:COG3638 154 RVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNlHQVDLARRYADRIIGLRDGRVVFDGPPAE 233
|
.
gi 495775764 231 L 231
Cdd:COG3638 234 L 234
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-224 |
4.48e-80 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 241.15 E-value: 4.48e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 1 MSAIDVKNLVKKFH----GQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGeitidtGKSIsqq 76
Cdd:COG1116 5 APALELRGVSKRFPtgggGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVD------GKPV--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 77 kgliRRLRQHVGFVFQNFNLFPHRTVLENIIEGPVIvKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIA 156
Cdd:COG1116 76 ----TGPGPDRGVVFQEPALLPWLTVLDNVALGLEL-RGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 157 RALAMRPDVILFDEPTSALDP----ELVGEVLntiRQLAQEKRTMVIVTHemsfarDV------ADRAIFMDQ--GRIVE 224
Cdd:COG1116 151 RALANDPEVLLMDEPFGALDAltreRLQDELL---RLWQETGKTVLFVTH------DVdeavflADRVVVLSArpGRIVE 221
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
4-243 |
1.04e-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: 239.33 E-value: 1.04e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGEITIDTGKSISQQkglirRL 83
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELY-----RL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 84 RQHVGFVFQNFNLFPHRTVLENIiEGPVIVKGE-PKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMR 162
Cdd:cd03261 76 RRRMGMLFQSGALFDSLTVFENV-AFPLREHTRlSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 163 PDVILFDEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFANpQQPRTR 241
Cdd:cd03261 155 PELLLYDEPTAGLDPIASGVIDDLIRSLKKELGlTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRAS-DDPLVR 233
|
..
gi 495775764 242 QF 243
Cdd:cd03261 234 QF 235
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-244 |
1.10e-79 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 243.13 E-value: 1.10e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 1 MSaIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGEITIDTGKSIsqqkgli 80
Cdd:COG1118 1 MS-IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNLPP------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 81 rRLRqHVGFVFQNFNLFPHRTVLENIIEGPViVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALA 160
Cdd:COG1118 73 -RER-RVGFVFQHYALFPHMTVAENIAFGLR-VRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 161 MRPDVILFDEPTSALD----PELVGEVLNTIRQLaqeKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFANPQ 236
Cdd:COG1118 150 VEPEVLLLDEPFGALDakvrKELRRWLRRLHDEL---GGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPA 226
|
....*...
gi 495775764 237 QPRTRQFL 244
Cdd:COG1118 227 TPFVARFL 234
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-245 |
4.39e-78 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 235.34 E-value: 4.39e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGeitidtGKSISQQKgliRRL 83
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVL------GEDVARDP---AEV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 84 RQHVGFVFQNFNLFPHRTVLENIIegpVI--VKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAM 161
Cdd:COG1131 72 RRRIGYVPQEPALYPDLTVRENLR---FFarLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLH 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 162 RPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLfanpqqprTR 241
Cdd:COG1131 149 DPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL--------KA 220
|
....
gi 495775764 242 QFLE 245
Cdd:COG1131 221 RLLE 224
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
4-228 |
4.43e-78 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 234.95 E-value: 4.43e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 4 IDVKNLVKKF-HGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGeitidtGKSISQQKGL-IR 81
Cdd:COG2884 2 IRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVN------GQDLSRLKRReIP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 82 RLRQHVGFVFQNFNLFPHRTVLENIiEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAM 161
Cdd:COG2884 76 YLRRRIGVVFQDFRLLPDRTVYENV-ALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVN 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495775764 162 RPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPA 228
Cdd:COG2884 155 RPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLVRDEAR 221
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
4-244 |
4.68e-77 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 236.24 E-value: 4.68e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 4 IDVKNLVKKFHGQ----TVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGeitidtGKSISQ--QK 77
Cdd:PRK11153 2 IELKNISKVFPQGgrtiHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVD------GQDLTAlsEK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 78 GLiRRLRQHVGFVFQNFNLFPHRTVLENIIEgPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIAR 157
Cdd:PRK11153 76 EL-RKARRQIGMIFQHFNLLSSRTVFDNVAL-PLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIAR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 158 ALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFANPQ 236
Cdd:PRK11153 154 ALASNPKVLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPK 233
|
....*...
gi 495775764 237 QPRTRQFL 244
Cdd:PRK11153 234 HPLTREFI 241
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-245 |
7.87e-75 |
|
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: 227.38 E-value: 7.87e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 3 AIDVKNLVKKF----HGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGeitidtGKSISQQKG 78
Cdd:COG1124 1 MLEVRNLSVSYgqggRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFD------GRPVTRRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 79 liRRLRQHVGFVFQN----FNlfPHRTVLENIIEgPVIVKGEPkeEATARARELLAKVGLAGKE-TSYPRRLSGGQQQRV 153
Cdd:COG1124 75 --KAFRRRVQMVFQDpyasLH--PRHTVDRILAE-PLRIHGLP--DREERIAELLEQVGLPPSFlDRYPHQLSGGQRQRV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 154 AIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQL-AQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLF 232
Cdd:COG1124 148 AIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLrEERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLL 227
|
250
....*....|...
gi 495775764 233 ANPQQPRTRQFLE 245
Cdd:COG1124 228 AGPKHPYTRELLA 240
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-244 |
1.56e-74 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 226.84 E-value: 1.56e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 2 SAIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTiRV-GEITIDtGKSISQQKGLI 80
Cdd:COG1117 10 PKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIPGA-RVeGEILLD-GEDIYDPDVDV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 81 RRLRQHVGFVFQNFNLFPHrTVLENIIEGPVIVKGEPKEEATARARELLAKVGL----AGKETSYPRRLSGGQQQRVAIA 156
Cdd:COG1117 88 VELRRRVGMVFQKPNPFPK-SIYDNVAYGLRLHGIKSKSELDEIVEESLRKAALwdevKDRLKKSALGLSGGQQQRLCIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 157 RALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAqEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFANPQ 236
Cdd:COG1117 167 RALAVEPEVLLMDEPTSALDPISTAKIEELILELK-KDYTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIFTNPK 245
|
....*...
gi 495775764 237 QPRTRQFL 244
Cdd:COG1117 246 DKRTEDYI 253
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-221 |
2.58e-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: 223.60 E-value: 2.58e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGeitidtGKSISQQKGLIRRL 83
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILID------GEDLTDLEDELPPL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 84 RQHVGFVFQNFNLFPHRTVLENIIEGpvivkgepkeeatararellakvglagketsyprrLSGGQQQRVAIARALAMRP 163
Cdd:cd03229 75 RRRIGMVFQDFALFPHLTVLENIALG-----------------------------------LSGGQQQRVALARALAMDP 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 495775764 164 DVILFDEPTSALDPELVGEVLNTIRQL-AQEKRTMVIVTHEMSFARDVADRAIFMDQGR 221
Cdd:cd03229 120 DVLLLDEPTSALDPITRREVRALLKSLqAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
4-244 |
3.21e-74 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 228.05 E-value: 3.21e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 4 IDVKNLVKKF-HGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGeitidtGKSISQQKglIRR 82
Cdd:COG1125 2 IEFENVTKRYpDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILID------GEDIRDLD--PVE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 83 LRQHVGFVFQNFNLFPHRTVLENIiegpVIV---KGEPKEEATARARELLAKVGLAGKETS--YPRRLSGGQQQRVAIAR 157
Cdd:COG1125 74 LRRRIGYVIQQIGLFPHMTVAENI----ATVprlLGWDKERIRARVDELLELVGLDPEEYRdrYPHELSGGQQQRVGVAR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 158 ALAMRPDVILFDEPTSALDP----ELVGEVLNTIRQLaqeKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFA 233
Cdd:COG1125 150 ALAADPPILLMDEPFGALDPitreQLQDELLRLQREL---GKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILA 226
|
250
....*....|.
gi 495775764 234 NPQQPRTRQFL 244
Cdd:COG1125 227 NPANDFVADFV 237
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-226 |
3.94e-74 |
|
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: 224.32 E-value: 3.94e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGeitidtGKSISqqkGLIRRL 83
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILID------GRDVT---GVPPER 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 84 RqHVGFVFQNFNLFPHRTVLENIIEGPViVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRP 163
Cdd:cd03259 72 R-NIGMVFQDYALFPHLTVAENIAFGLK-LRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495775764 164 DVILFDEPTSALDPELVGEVLNTIRQL-AQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQG 226
Cdd:cd03259 150 SLLLLDEPLSALDAKLREELREELKELqRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-231 |
5.89e-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: 225.14 E-value: 5.89e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 4 IDVKNLVKKF-HGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGEITIdtgksISQQKGLIRR 82
Cdd:cd03256 1 IEVENLSKTYpNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDI-----NKLKGKALRQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 83 LRQHVGFVFQNFNLFPHRTVLENIIEG--------PVIVKGEPKEEaTARARELLAKVGLAGKETSYPRRLSGGQQQRVA 154
Cdd:cd03256 76 LRRQIGMIFQQFNLIERLSVLENVLSGrlgrrstwRSLFGLFPKEE-KQRALAALERVGLLDKAYQRADQLSGGQQQRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495775764 155 IARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEK-RTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSL 231
Cdd:cd03256 155 IARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEgITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-225 |
2.46e-73 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 222.73 E-value: 2.46e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 4 IDVKNLVKKFHG----QTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGeitidtGKSIsqqkgl 79
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVD------GEPV------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 80 iRRLRQHVGFVFQNFNLFPHRTVLENIIEGPVIvKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARAL 159
Cdd:cd03293 69 -TGPGPDRGYVFQQDALLPWLTVLDNVALGLEL-QGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARAL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495775764 160 AMRPDVILFDEPTSALDP---ELVGEVLntIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQ--GRIVEQ 225
Cdd:cd03293 147 AVDPDVLLLDEPFSALDAltrEQLQEEL--LDIWRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRIVAE 215
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-231 |
7.37e-73 |
|
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: 221.67 E-value: 7.37e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGEITIDtGKSISQQKGLIRRL 83
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGAPDEGEVLLD-GKDIYDLDVDVLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 84 RQHVGFVFQNFNLFPhRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAG--KETSYPRRLSGGQQQRVAIARALAM 161
Cdd:cd03260 80 RRRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALWDevKDRLHALGLSGGQQQRLCLARALAN 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 162 RPDVILFDEPTSALDPELVGEVLNTIRQLAQEkRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSL 231
Cdd:cd03260 159 EPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
6-221 |
1.78e-72 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 220.03 E-value: 1.78e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 6 VKNLVKKFHGQT--VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGeitidtGKSISQQKglIRRL 83
Cdd:cd03225 2 LKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVD------GKDLTKLS--LKEL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 84 RQHVGFVFQNFNL-FPHRTVLENIIEGPVIvKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMR 162
Cdd:cd03225 74 RRKVGLVFQNPDDqFFGPTVEEEVAFGLEN-LGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 495775764 163 PDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGR 221
Cdd:cd03225 153 PDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-235 |
2.01e-72 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 224.95 E-value: 2.01e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 1 MSAIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGEITIdTGKSISQqkgli 80
Cdd:COG3839 1 MASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDV-TDLPPKD----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 81 RRlrqhVGFVFQNFNLFPHRTVLENIiEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALA 160
Cdd:COG3839 75 RN----IAMVFQSYALYPHMTVYENI-AFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 161 MRPDVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHE----MSFardvADRAIFMDQGRIVEQGPAKSLFANP 235
Cdd:COG3839 150 REPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRlGTTTIYVTHDqveaMTL----ADRIAVMNDGRIQQVGTPEELYDRP 225
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
4-226 |
2.56e-71 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 217.76 E-value: 2.56e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 4 IDVKNLVKKFHGQ----TVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGeitidtGKSISQQKGL 79
Cdd:cd03257 2 LEVKNLSVSFPTGggsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFD------GKDLLKLSRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 80 IRRLR-QHVGFVFQN--FNLFPHRTVLENIIEGPVIVKGEPKEEATARAR-ELLAKVGLAGK-ETSYPRRLSGGQQQRVA 154
Cdd:cd03257 76 LRKIRrKEIQMVFQDpmSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVlLLLVGVGLPEEvLNRYPHELSGGQRQRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495775764 155 IARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEK-RTMVIVTHEMSFARDVADRAIFMDQGRIVEQG 226
Cdd:cd03257 156 IARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELgLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-241 |
4.33e-71 |
|
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: 220.31 E-value: 4.33e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 4 IDVKNLVKKFHGQ----TVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTirVGEITIDtGKSISQQKG- 78
Cdd:COG0444 2 LEVRNLKVYFPTRrgvvKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGIT--SGEILFD-GEDLLKLSEk 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 79 LIRRLR-QHVGFVFQN----FNlfPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKET---SYPRRLSGGQQ 150
Cdd:COG0444 79 ELRKIRgREIQMIFQDpmtsLN--PVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLPDPERrldRYPHELSGGMR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 151 QRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAK 229
Cdd:COG0444 157 QRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGlAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVE 236
|
250
....*....|..
gi 495775764 230 SLFANPQQPRTR 241
Cdd:COG0444 237 ELFENPRHPYTR 248
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-237 |
2.01e-69 |
|
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: 221.70 E-value: 2.01e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 1 MS-AIDVKNLVKKFHGQT--VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLeQPEGGTIRvGEITIDtGKSISQQK 77
Cdd:COG1123 1 MTpLLEVRDLSVRYPGGDvpAVDGVSLTIAPGETVALVGESGSGKSTLALALMGL-LPHGGRIS-GEVLLD-GRDLLELS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 78 GLIRRlrQHVGFVFQNF--NLFPHrTVLENIIEGPVIvKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAI 155
Cdd:COG1123 78 EALRG--RRIGMVFQDPmtQLNPV-TVGDQIAEALEN-LGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 156 ARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEK-RTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFAN 234
Cdd:COG1123 154 AMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERgTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAA 233
|
...
gi 495775764 235 PQQ 237
Cdd:COG1123 234 PQA 236
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
4-246 |
8.60e-69 |
|
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: 211.78 E-value: 8.60e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 4 IDVKNLVKKF-HGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGeitidtGKSISQQKGLirR 82
Cdd:cd03295 1 IEFENVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFID------GEDIREQDPV--E 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 83 LRQHVGFVFQNFNLFPHRTVLENIIEGPVIvKGEPKEEATARARELLAKVGLAGKE--TSYPRRLSGGQQQRVAIARALA 160
Cdd:cd03295 73 LRRKIGYVIQQIGLFPHMTVEENIALVPKL-LKWPKEKIRERADELLALVGLDPAEfaDRYPHELSGGQQQRVGVARALA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 161 MRPDVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFANPQQPR 239
Cdd:cd03295 152 ADPPLLLMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDF 231
|
....*..
gi 495775764 240 TRQFLEK 246
Cdd:cd03295 232 VAEFVGA 238
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-228 |
2.32e-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: 210.37 E-value: 2.32e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 2 SAIDVKNLVKKFHGQ----TVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGeitidtGKSISQ-- 75
Cdd:COG4181 7 PIIELRGLTKTVGTGagelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLA------GQDLFAld 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 76 QKGLIRRLRQHVGFVFQNFNLFPHRTVLENIIEgPVIVKGEPkeEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAI 155
Cdd:COG4181 81 EDARARLRARHVGFVFQSFQLLPTLTALENVML-PLELAGRR--DARARARALLERVGLGHRLDHYPAQLSGGEQQRVAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495775764 156 ARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDvADRAIFMDQGRIVEQGPA 228
Cdd:COG4181 158 ARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGtTLVLVTHDPALAAR-CDRVLRLRAGRLVEDTAA 230
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
16-247 |
6.39e-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: 6.39e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 16 QTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGEITIDTGKsisqqKGLIRRLRQHVGFVFQnfn 95
Cdd:TIGR04521 18 KKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKK-----KKKLKDLRKKVGLVFQ--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 96 lFPH-----RTVLENIIEGPVIVkGEPKEEATARARELLAKVGL--AGKETSyPRRLSGGQQQRVAIARALAMRPDVILF 168
Cdd:TIGR04521 90 -FPEhqlfeETVYKDIAFGPKNL-GLSEEEAEERVKEALELVGLdeEYLERS-PFELSGGQMRRVAIAGVLAMEPEVLIL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 169 DEPTSALDPELVGEVLNTIRQLAQEK-RTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFANPqqprtrQFLEKF 247
Cdd:TIGR04521 167 DEPTAGLDPKGRKEILDLFKRLHKEKgLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDV------DELEKI 240
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
7-245 |
9.89e-67 |
|
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: 207.50 E-value: 9.89e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 7 KNLVKKFHGQTV-LHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGeitidtGKSISQ-QKGLIRRLR 84
Cdd:cd03294 27 KEEILKKTGQTVgVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLID------GQDIAAmSRKELRELR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 85 QH-VGFVFQNFNLFPHRTVLENIIEGpVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRP 163
Cdd:cd03294 101 RKkISMVFQSFALLPHRTVLENVAFG-LEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDP 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 164 DVILFDEPTSALDPELVGEVLNTIRQL-AQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFANPQQPRTRQ 242
Cdd:cd03294 180 DILLMDEAFSALDPLIRREMQDELLRLqAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVRE 259
|
...
gi 495775764 243 FLE 245
Cdd:cd03294 260 FFR 262
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
4-231 |
1.41e-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: 206.38 E-value: 1.41e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 4 IDVKNLVKKF-HGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGtirvgEITIDtGKSISQQKGL-IR 81
Cdd:TIGR02315 2 LEVENLSKVYpNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSG-----SILLE-GTDITKLRGKkLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 82 RLRQHVGFVFQNFNLFPHRTVLENIIEGPVIVK-------GEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVA 154
Cdd:TIGR02315 76 KLRRRIGMIFQHYNLIERLTVLENVLHGRLGYKptwrsllGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495775764 155 IARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVT-HEMSFARDVADRAIFMDQGRIVEQGPAKSL 231
Cdd:TIGR02315 156 IARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINlHQVDLAKKYADRIVGLKAGEIVFDGAPSEL 233
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
1-235 |
8.05e-66 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 209.19 E-value: 8.05e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 1 MSAIDVKNLVKKF-----------------------HGQTV-LHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPE 56
Cdd:COG4175 1 MPKIEVRNLYKIFgkrperalklldqgkskdeilekTGQTVgVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 57 GGTIRVGeitidtGKSISQ--QKGLiRRLRQH-VGFVFQNFNLFPHRTVLENIiEGPVIVKGEPKEEATARARELLAKVG 133
Cdd:COG4175 81 AGEVLID------GEDITKlsKKEL-RELRRKkMSMVFQHFALLPHRTVLENV-AFGLEIQGVPKAERRERAREALELVG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 134 LAGKETSYPRRLSGGQQQRVAIARALAMRPDVILFDEPTSALDP----ELVGEVLntirQL-AQEKRTMVIVTHEMSFAR 208
Cdd:COG4175 153 LAGWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDPlirrEMQDELL----ELqAKLKKTIVFITHDLDEAL 228
|
250 260
....*....|....*....|....*..
gi 495775764 209 DVADRAIFMDQGRIVEQGPAKSLFANP 235
Cdd:COG4175 229 RLGDRIAIMKDGRIVQIGTPEEILTNP 255
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
3-244 |
1.14e-65 |
|
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: 203.72 E-value: 1.14e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 3 AIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGeitidtGKSISQQKGlirR 82
Cdd:cd03296 2 SIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFG------GEDATDVPV---Q 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 83 LRQhVGFVFQNFNLFPHRTVLENIIEGPVIVKGE---PKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARAL 159
Cdd:cd03296 73 ERN-VGFVFQHYALFRHMTVFDNVAFGLRVKPRSerpPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 160 AMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFANPQQP 238
Cdd:cd03296 152 AVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHvTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASP 231
|
....*.
gi 495775764 239 RTRQFL 244
Cdd:cd03296 232 FVYSFL 237
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-234 |
1.37e-65 |
|
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: 204.59 E-value: 1.37e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 4 IDVKNLVKKFHGQT--VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGEITIDTGKSISQqkglir 81
Cdd:TIGR04520 1 IEVENVSFSYPESEkpALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEENLWE------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 82 rLRQHVGFVFQN-FNLFPHRTV-------LENIiegpvivkGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRV 153
Cdd:TIGR04520 75 -IRKKVGMVFQNpDNQFVGATVeddvafgLENL--------GVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 154 AIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQL-AQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKSLF 232
Cdd:TIGR04520 146 AIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLnKEEGITVISITHDMEEAVL-ADRVIVMNKGKIVAEGTPREIF 224
|
..
gi 495775764 233 AN 234
Cdd:TIGR04520 225 SQ 226
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
4-244 |
4.88e-63 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 196.90 E-value: 4.88e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 4 IDVKNLVKKFHGQTvLHgIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGEITIdTGKSISQQKglirrl 83
Cdd:COG3840 2 LRLDDLTYRYGDFP-LR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDL-TALPPAERP------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 84 rqhVGFVFQNFNLFPHRTVLENIIEG--PvivKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAM 161
Cdd:COG3840 73 ---VSMLFQENNLFPHLTVAQNIGLGlrP---GLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 162 RPDVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFANPQQPRT 240
Cdd:COG3840 147 KRPILLLDEPFSALDPALRQEMLDLVDELCRErGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPAL 226
|
....
gi 495775764 241 RQFL 244
Cdd:COG3840 227 AAYL 230
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-236 |
2.46e-62 |
|
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: 195.35 E-value: 2.46e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGEITIdTGKSISQ--QKGLIR 81
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDI-TGLPPHEiaRLGIGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 82 rlrqhvgfVFQNFNLFPHRTVLENIIEGPVIVKGEP---------KEEATARARELLAKVGLAGKETSYPRRLSGGQQQR 152
Cdd:cd03219 80 --------TFQIPRLFPELTVLENVMVAAQARTGSGlllararreEREARERAEELLERVGLADLADRPAGELSYGQQRR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 153 VAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLF 232
Cdd:cd03219 152 LEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVR 231
|
....
gi 495775764 233 ANPQ 236
Cdd:cd03219 232 NNPR 235
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4-222 |
3.13e-62 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 193.88 E-value: 3.13e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGeitidtGKSISQQKglIRRL 83
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLD------GKPLSAMP--PPEW 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 84 RQHVGFVFQNFNLFPHrTVLENIIEGPVIVKGEPKEEataRARELLAKVGLA----GKETSyprRLSGGQQQRVAIARAL 159
Cdd:COG4619 73 RRQVAYVPQEPALWGG-TVRDNLPFPFQLRERKFDRE---RALELLERLGLPpdilDKPVE---RLSGGERQRLALIRAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495775764 160 AMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEK-RTMVIVTHEMSFARDVADRAIFMDQGRI 222
Cdd:COG4619 146 LLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEgRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-236 |
7.86e-62 |
|
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: 193.99 E-value: 7.86e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGeitidtGKSISQqkglIRRL 83
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLD------GKDITN----LPPH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 84 RQHVGFVFQNFNLFPHRTVLENIIEGpVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRP 163
Cdd:cd03300 71 KRPVNTVFQNYALFPHLTVFENIAFG-LRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEP 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495775764 164 DVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFANPQ 236
Cdd:cd03300 150 KVLLLDEPLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPA 223
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
1-247 |
1.27e-61 |
|
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: 197.18 E-value: 1.27e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 1 MSAIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGeitidtGKSISqqkgli 80
Cdd:TIGR03265 2 SPYLSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQG------GRDIT------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 81 rRL---RQHVGFVFQNFNLFPHRTVLENIIEGpVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIAR 157
Cdd:TIGR03265 70 -RLppqKRDYGIVFQSYALFPNLTVADNIAYG-LKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALAR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 158 ALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFanpQ 236
Cdd:TIGR03265 148 ALATSPGLLLLDEPLSALDARVREHLRTEIRQLQRRlGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIY---R 224
|
250
....*....|.
gi 495775764 237 QPRTRqFLEKF 247
Cdd:TIGR03265 225 HPATP-FVADF 234
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-232 |
3.16e-61 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 192.95 E-value: 3.16e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 3 AIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGeitidtGKSISQQKGliRR 82
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLD------GRDLASLSR--RE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 83 LRQHVGFVFQN----FNL----------FPHRTVLeniiegpvivkGEPKEEATARARELLAKVGLAGKETSYPRRLSGG 148
Cdd:COG1120 73 LARRIAYVPQEppapFGLtvrelvalgrYPHLGLF-----------GRPSAEDREAVEEALERTGLEHLADRPVDELSGG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 149 QQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEK-RTMVIVTHEMSFARDVADRAIFMDQGRIVEQGP 227
Cdd:COG1120 142 ERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERgRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGP 221
|
....*
gi 495775764 228 AKSLF 232
Cdd:COG1120 222 PEEVL 226
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
4-241 |
5.23e-61 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 194.95 E-value: 5.23e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 4 IDVKNLVKKF---------HGQTV--LHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGeitidtGKS 72
Cdd:COG4608 8 LEVRDLKKHFpvrgglfgrTVGVVkaVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFD------GQD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 73 ISQQKGL-IRRLRQHVGFVFQN----FNlfPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGL----AGKetsYPR 143
Cdd:COG4608 82 ITGLSGReLRPLRRRMQMVFQDpyasLN--PRMTVGDIIAEPLRIHGLASKAERRERVAELLELVGLrpehADR---YPH 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 144 RLSGGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLaQEKR--TMVIVTHEMSFARDVADRAIFMDQGR 221
Cdd:COG4608 157 EFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDL-QDELglTYLFISHDLSVVRHISDRVAVMYLGK 235
|
250 260
....*....|....*....|
gi 495775764 222 IVEQGPAKSLFANPQQPRTR 241
Cdd:COG4608 236 IVEIAPRDELYARPLHPYTQ 255
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-236 |
5.35e-61 |
|
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: 192.56 E-value: 5.35e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 1 MSAIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGEITIdTGKSISQ--QKG 78
Cdd:COG0411 2 DPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDI-TGLPPHRiaRLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 79 LIRrlrqhvgfVFQNFNLFPHRTVLENIIEGPVIVKGEP--------------KEEATARARELLAKVGLAGKETSYPRR 144
Cdd:COG0411 81 IAR--------TFQNPRLFPELTVLENVLVAAHARLGRGllaallrlprarreEREARERAEELLERVGLADRADEPAGN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 145 LSGGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIV 223
Cdd:COG0411 153 LSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDErGITILLIEHDMDLVMGLADRIVVLDFGRVI 232
|
250
....*....|...
gi 495775764 224 EQGPAKSLFANPQ 236
Cdd:COG0411 233 AEGTPAEVRADPR 245
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-222 |
1.83e-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: 188.38 E-value: 1.83e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGeitidtGKSISQQKGLIRRl 83
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVL------GKDIKKEPEEVKR- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 84 rqHVGFVFQNFNLFPHRTVLENIiegpvivkgepkeeatararellakvglagketsyprRLSGGQQQRVAIARALAMRP 163
Cdd:cd03230 74 --RIGYLPEEPSLYENLTVRENL-------------------------------------KLSGGMKQRLALAQALLHDP 114
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 495775764 164 DVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRI 222
Cdd:cd03230 115 ELLILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
4-248 |
1.19e-59 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 192.24 E-value: 1.19e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRV-GEitiDTGKSISQQKGLIrr 82
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIdGE---DVTHRSIQQRDIC-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 83 lrqhvgFVFQNFNLFPHRTVLENIIEGpVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMR 162
Cdd:PRK11432 82 ------MVFQSYALFPHMSLGENVGYG-LKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 163 PDVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFanpQQPRTR 241
Cdd:PRK11432 155 PKVLLFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELY---RQPASR 231
|
....*..
gi 495775764 242 qFLEKFL 248
Cdd:PRK11432 232 -FMASFM 237
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
4-250 |
3.37e-59 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 187.37 E-value: 3.37e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGEITIDTGKsisqqkgliRRL 83
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEP---------REA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 84 RQHVGFVFQNFNLFPHRTVLENI-IEGPVivKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMR 162
Cdd:COG4555 73 RRQIGVLPDERGLYDRLTVRENIrYFAEL--YGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 163 PDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFANPQQPRtrq 242
Cdd:COG4555 151 PKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGEEN--- 227
|
....*...
gi 495775764 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 |
6.41e-59 |
|
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: 185.51 E-value: 6.41e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 6 VKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGEITIDTGKSIsqQKGLIRRlrQ 85
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSK--KASKFRR--E 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 86 HVGFVFQNFNLFPHRTVLENIIEGPVIVKGePKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPDV 165
Cdd:TIGR03608 77 KLGYLFQNFALIENETVEENLDLGLKYKKL-SKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 495775764 166 ILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFArDVADRAIFM 217
Cdd:TIGR03608 156 ILADEPTGSLDPKNRDEVLDLLLELNDEGKTIIIVTHDPEVA-KQADRVIEL 206
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-232 |
5.74e-58 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 184.52 E-value: 5.74e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 1 MSAIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGeitidtGKSIsqqkgli 80
Cdd:COG1121 4 MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLF------GKPP------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 81 RRLRQHVGFVFQNFNL---FPhRTVLEniiegpvIVK----------GEPKEEATARARELLAKVGLAGKETSYPRRLSG 147
Cdd:COG1121 71 RRARRRIGYVPQRAEVdwdFP-ITVRD-------VVLmgrygrrglfRRPSRADREAVDEALERVGLEDLADRPIGELSG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 148 GQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEqGP 227
Cdd:COG1121 143 GQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLVAH-GP 221
|
....*
gi 495775764 228 AKSLF 232
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 |
1.07e-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: 183.02 E-value: 1.07e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 4 IDVKNLVKkFHGQT-VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGeitidtGKSISQQKgLIRR 82
Cdd:cd03224 1 LEVENLNA-GYGKSqILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFD------GRDITGLP-PHER 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 83 LRQHVGFVFQNFNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKvgLAGKETSYPRRLSGGQQQRVAIARALAMR 162
Cdd:cd03224 73 ARAGIGYVPEGRRIFPELTVEENLLLGAYARRRAKRKARLERVYELFPR--LKERRKQLAGTLSGGEQQMLAIARALMSR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495775764 163 PDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFAN 234
Cdd:cd03224 151 PKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-245 |
4.80e-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: 189.90 E-value: 4.80e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 1 MSAIDVKNLVKKFHG----QTVLHGIDLEVEQGEVVAIIGPSGSGKT-TLLRSINLLeqPEGGTIRVGEITIDtGKSISQ 75
Cdd:COG4172 4 MPLLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILRLL--PDPAAHPSGSILFD-GQDLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 76 --QKGLiRRLR-QHVGFVFQ------NfnlfPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKET---SYPR 143
Cdd:COG4172 81 lsEREL-RRIRgNRIAMIFQepmtslN----PLHTIGKQIAEVLRLHRGLSGAAARARALELLERVGIPDPERrldAYPH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 144 RLSGGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRT-MVIVTHEMSFARDVADRAIFMDQGRI 222
Cdd:COG4172 156 QLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMaLLLITHDLGVVRRFADRVAVMRQGEI 235
|
250 260
....*....|....*....|...
gi 495775764 223 VEQGPAKSLFANPQQPRTRQFLE 245
Cdd:COG4172 236 VEQGPTAELFAAPQHPYTRKLLA 258
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
3-233 |
1.06e-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: 191.97 E-value: 1.06e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 3 AIDVKNLVKKFHGQT--VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGEITIdtgKSISqqkglI 80
Cdd:COG2274 473 DIELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDL---RQID-----P 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 81 RRLRQHVGFVFQNFNLFpHRTVLENIIEGpvivkgepKEEAT-ARARELLAKVGLAGKETSYP-----------RRLSGG 148
Cdd:COG2274 545 ASLRRQIGVVLQDVFLF-SGTIRENITLG--------DPDATdEEIIEAARLAGLHDFIEALPmgydtvvgeggSNLSGG 615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 149 QQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQeKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPA 228
Cdd:COG2274 616 QRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK-GRTVIIIAHRLSTIRL-ADRIIVLDKGRIVEDGTH 693
|
....*
gi 495775764 229 KSLFA 233
Cdd:COG2274 694 EELLA 698
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-248 |
1.31e-56 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 184.13 E-value: 1.31e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 1 MSaIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGeitidtGKSISQqkgLI 80
Cdd:PRK10851 1 MS-IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFH------GTDVSR---LH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 81 RRLRQhVGFVFQNFNLFPHRTVLENIIEGPVIVKGEPKEEATA---RARELLAKVGLAGKETSYPRRLSGGQQQRVAIAR 157
Cdd:PRK10851 71 ARDRK-VGFVFQHYALFRHMTVFDNIAFGLTVLPRRERPNAAAikaKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALAR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 158 ALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGpakslfaNPQ 236
Cdd:PRK10851 150 ALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAG-------TPD 222
|
250
....*....|....*.
gi 495775764 237 Q----PRTRQFLEkFL 248
Cdd:PRK10851 223 QvwrePATRFVLE-FM 237
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
11-246 |
1.43e-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: 181.97 E-value: 1.43e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 11 KKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGtirvgEITIDtGKSISQQKG--LIRRLRQHVG 88
Cdd:TIGR01186 1 KKTGGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAG-----QIFID-GENIMKQSPveLREVRRKKIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 89 FVFQNFNLFPHRTVLENIIEGPVIVkGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPDVILF 168
Cdd:TIGR01186 75 MVFQQFALFPHMTILQNTSLGPELL-GWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLM 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495775764 169 DEPTSALDPELVGEVLNTIRQL-AQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFANPQQPRTRQFLEK 246
Cdd:TIGR01186 154 DEAFSALDPLIRDSMQDELKKLqATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIGK 232
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-236 |
1.77e-55 |
|
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: 177.48 E-value: 1.77e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 1 MSAIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGeitidtGKSISQQKGLi 80
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFD------GEDITGLPPH- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 81 RRLRQHVGFVFQNFNLFPHRTVLENIIEGPVIVKGEPKEEATA--------RARELLAKvgLAGketsyprRLSGGQQQR 152
Cdd:COG0410 74 RIARLGIGYVPEGRRIFPSLTVEENLLLGAYARRDRAEVRADLervyelfpRLKERRRQ--RAG-------TLSGGEQQM 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 153 VAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLF 232
Cdd:COG0410 145 LAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELL 224
|
....
gi 495775764 233 ANPQ 236
Cdd:COG0410 225 ADPE 228
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
4-226 |
2.19e-55 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 179.90 E-value: 2.19e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 4 IDVKNLVKKFHGQT-----VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTI----------------RV 62
Cdd:PRK13651 3 IKVKNIVKIFNKKLptelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkekEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 63 GEITIDTGKSISQQKGLIRRLRQHVGFVFQ--NFNLFpHRTVLENIIEGPVIVkGEPKEEATARARELLAKVGLagkETS 140
Cdd:PRK13651 83 VLEKLVIQKTRFKKIKKIKEIRRRVGVVFQfaEYQLF-EQTIEKDIIFGPVSM-GVSKEEAKKRAAKYIELVGL---DES 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 141 Y----PRRLSGGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIF 216
Cdd:PRK13651 158 YlqrsPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIF 237
|
250
....*....|
gi 495775764 217 MDQGRIVEQG 226
Cdd:PRK13651 238 FKDGKIIKDG 247
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
19-236 |
2.74e-55 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 179.06 E-value: 2.74e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 19 LHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGEITIDTGKSisqQKGLiRRLRQHVGFVFQnfnlFP 98
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKK---NKKL-KPLRKKVGIVFQ----FP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 99 H-----RTVLENIIEGPvIVKGEPKEEATARARELLAKVGLAGK-ETSYPRRLSGGQQQRVAIARALAMRPDVILFDEPT 172
Cdd:PRK13634 95 EhqlfeETVEKDICFGP-MNFGVSEEDAKQKAREMIELVGLPEElLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPT 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495775764 173 SALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFANPQ 236
Cdd:PRK13634 174 AGLDPKGRKEMMEMFYKLHKEKGlTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-226 |
9.26e-55 |
|
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: 175.14 E-value: 9.26e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGEITI-DTGKSisqqkglirr 82
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVtDLPPK---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 83 lRQHVGFVFQNFNLFPHRTVLENIiEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMR 162
Cdd:cd03301 71 -DRDIAMVFQNYALYPHMTVYDNI-AFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVRE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495775764 163 PDVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQG 226
Cdd:cd03301 149 PKVFLMDEPLSNLDAKLRVQMRAELKRLQQRlGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
4-222 |
1.43e-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: 1.43e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 4 IDVKNLVKKF-HGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVgeitidTGKSISQQKG-LIR 81
Cdd:cd03292 1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRV------NGQDVSDLRGrAIP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 82 RLRQHVGFVFQNFNLFPHRTVLENIIEgPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAM 161
Cdd:cd03292 75 YLRRKIGVVFQDFRLLPDRNVYENVAF-ALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVN 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495775764 162 RPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRI 222
Cdd:cd03292 154 SPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
3-245 |
2.36e-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: 183.43 E-value: 2.36e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 3 AIDVKNLVKKFHGQT--VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGeitidtGKSISQQKGli 80
Cdd:COG4987 333 SLELEDVSFRYPGAGrpVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLG------GVDLRDLDE-- 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 81 RRLRQHVGFVFQNFNLFpHRTVLENIIEGpvivkgepKEEAT-ARARELLAKVGLAGKETSYP-----------RRLSGG 148
Cdd:COG4987 405 DDLRRRIAVVPQRPHLF-DTTLRENLRLA--------RPDATdEELWAALERVGLGDWLAALPdgldtwlgeggRRLSGG 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 149 QQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEkRTMVIVTHEMSfARDVADRAIFMDQGRIVEQGPA 228
Cdd:COG4987 476 ERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAG-RTVLLITHRLA-GLERMDRILVLEDGRIVEQGTH 553
|
250
....*....|....*..
gi 495775764 229 KSLFAnpQQPRTRQFLE 245
Cdd:COG4987 554 EELLA--QNGRYRQLYQ 568
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
4-245 |
3.73e-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: 182.19 E-value: 3.73e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 4 IDVKNLVKKFHGQ-----------TVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSI-NLLEQpeGGTIRVGeitidtGK 71
Cdd:COG4172 276 LEARDLKVWFPIKrglfrrtvghvKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALlRLIPS--EGEIRFD------GQ 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 72 SISQQKG-LIRRLRQHVGFVFQN-FN-LFPHRTVLENIIEGPVIVK-GEPKEEATARARELLAKVGL-AGKETSYPRRLS 146
Cdd:COG4172 348 DLDGLSRrALRPLRRRMQVVFQDpFGsLSPRMTVGQIIAEGLRVHGpGLSAAERRARVAEALEEVGLdPAARHRYPHEFS 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 147 GGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLaQEKR--TMVIVTHEMSFARDVADRAIFMDQGRIVE 224
Cdd:COG4172 428 GGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDL-QREHglAYLFISHDLAVVRALAHRVMVMKDGKVVE 506
|
250 260
....*....|....*....|.
gi 495775764 225 QGPAKSLFANPQQPRTRQFLE 245
Cdd:COG4172 507 QGPTEQVFDAPQHPYTRALLA 527
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-221 |
6.24e-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: 6.24e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 4 IDVKNLVKKFHG--QTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGEITIdtgKSISQqkgliR 81
Cdd:cd03228 1 IEFKNVSFSYPGrpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDL---RDLDL-----E 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 82 RLRQHVGFVFQNFNLFpHRTVLENIiegpvivkgepkeeatararellakvglagketsyprrLSGGQQQRVAIARALAM 161
Cdd:cd03228 73 SLRKNIAYVPQDPFLF-SGTIRENI--------------------------------------LSGGQRQRIAIARALLR 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 162 RPDVILFDEPTSALDPELVGEVLNTIRQLAQEkRTMVIVTHEMSFARDvADRAIFMDQGR 221
Cdd:cd03228 114 DPPILILDEATSALDPETEALILEALRALAKG-KTVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
6-221 |
8.43e-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: 170.89 E-value: 8.43e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 6 VKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGEITIdtgksisqQKGLIRRLRQ 85
Cdd:cd00267 2 IENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDI--------AKLPLEELRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 86 HVGFVFQnfnlfphrtvleniiegpvivkgepkeeatararellakvglagketsyprrLSGGQQQRVAIARALAMRPDV 165
Cdd:cd00267 74 RIGYVPQ----------------------------------------------------LSGGQRQRVALARALLLNPDL 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 495775764 166 ILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGR 221
Cdd:cd00267 102 LLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-226 |
1.37e-53 |
|
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: 171.08 E-value: 1.37e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 5 DVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGeitidtGKSISQQKglIRRLR 84
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLD------GKDLASLS--PKELA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 85 QHVGFVFQnfnlfphrtvleniiegpvivkgepkeeatarareLLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPD 164
Cdd:cd03214 73 RKIAYVPQ-----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPP 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495775764 165 VILFDEPTSALDPELVGEVLNTIRQLAQEK-RTMVIVTHEMSFARDVADRAIFMDQGRIVEQG 226
Cdd:cd03214 118 ILLLDEPTSHLDIAHQIELLELLRRLARERgKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
15-227 |
2.35e-53 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 181.13 E-value: 2.35e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 15 GQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLlrsINLLE---QPEGGTIRVGEITIdtgKSISQQkglirRLRQHVGFVF 91
Cdd:COG1132 352 DRPVLKDISLTIPPGETVALVGPSGSGKSTL---VNLLLrfyDPTSGRILIDGVDI---RDLTLE-----SLRRQIGVVP 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 92 QNFNLFpHRTVLENIIEGpvivkgepKEEAT----------ARARELLAK--------VGLAGketsypRRLSGGQQQRV 153
Cdd:COG1132 421 QDTFLF-SGTIRENIRYG--------RPDATdeeveeaakaAQAHEFIEAlpdgydtvVGERG------VNLSGGQRQRI 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495775764 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 |
2.41e-53 |
|
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: 176.06 E-value: 2.41e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 22 IDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRV-GEITIDTGKSISqqkglIRRLRQHVGFVFQNFNLFPHR 100
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLgGEVLQDSARGIF-----LPPHRRRIGYVFQEARLFPHL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 101 TVLENIIEGpviVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPDVILFDEPTSALDPELV 180
Cdd:COG4148 93 SVRGNLLYG---RKRAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARK 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 495775764 181 GEVLNTIRQLAQEKRT-MVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFANP 235
Cdd:COG4148 170 AEILPYLERLRDELDIpILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP 225
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
4-244 |
4.28e-53 |
|
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: 171.75 E-value: 4.28e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 4 IDVKNLVKKFhGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVgeitidTGKSISQQKGLIRRl 83
Cdd:cd03299 1 LKVENLSKDW-KEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILL------NGKDITNLPPEKRD- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 84 rqhVGFVFQNFNLFPHRTVLENIIEGpVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRP 163
Cdd:cd03299 73 ---ISYVPQNYALFPHMTVYKNIAYG-LKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 164 DVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVI-VTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFANPQQPRTRQ 242
Cdd:cd03299 149 KILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLhVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAE 228
|
..
gi 495775764 243 FL 244
Cdd:cd03299 229 FL 230
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
4-221 |
5.47e-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: 5.47e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 4 IDVKNLVKKFHGQT-VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGeitidtGKSISQQKG-LIR 81
Cdd:TIGR02673 2 IEFHNVSKAYPGGVaALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIA------GEDVNRLRGrQLP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 82 RLRQHVGFVFQNFNLFPHRTVLENIIEgPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAM 161
Cdd:TIGR02673 76 LLRRRIGVVFQDFRLLPDRTVYENVAL-PLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVN 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 162 RPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGR 221
Cdd:TIGR02673 155 SPPLLLADEPTGNLDPDLSERILDLLKRLNKRGTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
4-235 |
6.94e-53 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 175.14 E-value: 6.94e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGtirvgEITIDtGKSISQQKGLIRrl 83
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSG-----RIMLD-GQDITHVPAENR-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 84 rqHVGFVFQNFNLFPHRTVLENIIEGpVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRP 163
Cdd:PRK09452 87 --HVNTVFQSYALFPHMTVFENVAFG-LRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495775764 164 DVILFDEPTSALDPELVGEVLNTIRQLaQEKR--TMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFANP 235
Cdd:PRK09452 164 KVLLLDESLSALDYKLRKQMQNELKAL-QRKLgiTFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEP 236
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
4-233 |
2.58e-52 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 170.97 E-value: 2.58e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 4 IDVKNLVKKFHGQT--VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGEITIDTgKSISQqkglir 81
Cdd:PRK13635 6 IRVEHISFRYPDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSE-ETVWD------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 82 rLRQHVGFVFQN-FNLFPHRTV-------LENIiegpvivkGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRV 153
Cdd:PRK13635 79 -VRRQVGMVFQNpDNQFVGATVqddvafgLENI--------GVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 154 AIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVI-VTHEMSFARDvADRAIFMDQGRIVEQGPAKSLF 232
Cdd:PRK13635 150 AIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLsITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIF 228
|
.
gi 495775764 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 |
2.81e-51 |
|
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: 163.97 E-value: 2.81e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 19 LHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGeitidtGKSISQQKglIRRLRQHVGFVFQNFNLFP 98
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLD------GQDLTDDE--RKSLRKEIGYVFQDPQLFP 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495775764 99 HRTVLENIIEGpVIVKGEPKEEATARARELLAKVGLAGKE----TSYPRRLSGGQQQRVAIARALAMRPDVILFDEPTS 173
Cdd:pfam00005 73 RLTVRENLRLG-LLLKGLSKREKDARAEEALEKLGLGDLAdrpvGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-234 |
4.59e-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: 174.56 E-value: 4.59e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 2 SAIDVKNLVKKFH-GQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGEITIDtgkSISQQkgli 80
Cdd:COG4988 335 PSIELEDVSFSYPgGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLS---DLDPA---- 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 81 rRLRQHVGFVFQNFNLFpHRTVLENIIEGpvivkgepKEEAT-ARARELLAKVGLAGKETSYP-----------RRLSGG 148
Cdd:COG4988 408 -SWRRQIAWVPQNPYLF-AGTIRENLRLG--------RPDASdEELEAALEAAGLDEFVAALPdgldtplgeggRGLSGG 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 149 QQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEkRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPA 228
Cdd:COG4988 478 QAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKG-RTVILITHRLALLAQ-ADRILVLDDGRIVEQGTH 555
|
....*.
gi 495775764 229 KSLFAN 234
Cdd:COG4988 556 EELLAK 561
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1-244 |
6.72e-51 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 168.60 E-value: 6.72e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 1 MSAIDVKNL--VKK--FHGQ-TV--LHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGtirvgEITIDTGKSI 73
Cdd:PRK11308 6 LQAIDLKKHypVKRglFKPErLVkaLDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGG-----ELYYQGQDLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 74 SQQKGLIRRLRQHVGFVFQN--FNLFPHRTVlENIIEGPVIVKGE-PKEEATARARELLAKVGLAGKETS-YPRRLSGGQ 149
Cdd:PRK11308 81 KADPEAQKLLRQKIQIVFQNpyGSLNPRKKV-GQILEEPLLINTSlSAAERREKALAMMAKVGLRPEHYDrYPHMFSGGQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 150 QQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRT-MVIVTHEMSFARDVADRAIFMDQGRIVEQGPA 228
Cdd:PRK11308 160 RQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLsYVFISHDLSVVEHIADEVMVMYLGRCVEKGTK 239
|
250
....*....|....*.
gi 495775764 229 KSLFANPQQPRTRQFL 244
Cdd:PRK11308 240 EQIFNNPRHPYTQALL 255
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
4-239 |
8.74e-51 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 166.79 E-value: 8.74e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 4 IDVKNLVKKF-HGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGtirvgEITIDtGKSISQQKGLIRR 82
Cdd:PRK13639 2 LETRDLKYSYpDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSG-----EVLIK-GEPIKYDKKSLLE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 83 LRQHVGFVFQNFN--LFPhRTVLENIIEGPVIVkGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALA 160
Cdd:PRK13639 76 VRKTVGIVFQNPDdqLFA-PTVEEDVAFGPLNL-GLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495775764 161 MRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFANPQQPR 239
Cdd:PRK13639 154 MKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIETIR 232
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
22-226 |
1.19e-50 |
|
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: 164.78 E-value: 1.19e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 22 IDLEVEqGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGEITIDTgksiSQQKGLIRRLRQHVGFVFQNFNLFPHRT 101
Cdd:cd03297 17 IDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFD----SRKKINLPPQQRKIGLVFQQYALFPHLN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 102 VLENIIEGpviVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPDVILFDEPTSALDPELVG 181
Cdd:cd03297 92 VRENLAFG---LKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 495775764 182 EVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQG 226
Cdd:cd03297 169 QLLPELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
18-247 |
1.28e-50 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 174.91 E-value: 1.28e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 18 VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGeitidtGKSISQQKG--LIRRLRQHVGFVFQNFN 95
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVA------GQDVATLDAdaLAQLRREHFGFIFQRYH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 96 LFPHRTVLENIiEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPDVILFDEPTSAL 175
Cdd:PRK10535 97 LLSHLTAAQNV-EVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGAL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 176 DPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAK--------SLFANPQQPRTRQFLEKF 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 |
1.23e-49 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 161.93 E-value: 1.23e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 6 VKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGeitidtGKSISQQkglirrlRQ 85
Cdd:cd03235 2 VEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVF------GKPLEKE-------RK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 86 HVGFVFQNFNL---FPhRTVLENIIEGPVIVKG---EPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARAL 159
Cdd:cd03235 69 RIGYVPQRRSIdrdFP-ISVRDVVLMGLYGHKGlfrRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARAL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495775764 160 AMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDqGRIVEQG 226
Cdd:cd03235 148 VQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLN-RTVVASG 213
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
18-222 |
2.56e-49 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 161.42 E-value: 2.56e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 18 VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGEITIdTGKSISQQKGLIRRLrqhVGFVFQNFNLF 97
Cdd:NF038007 20 VLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEV-TNLSYSQKIILRREL---IGYIFQSFNLI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 98 PHRTVLENIiEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPDVILFDEPTSALDP 177
Cdd:NF038007 96 PHLSIFDNV-ALPLKYRGVAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSNPALLLADEPTGNLDS 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 495775764 178 ELVGEVLNTIRQLAQEKRTMVIVTHEMSfARDVADRAIFMDQGRI 222
Cdd:NF038007 175 KNARAVLQQLKYINQKGTTIIMVTHSDE-ASTYGNRIINMKDGKL 218
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
5-223 |
9.10e-49 |
|
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: 159.34 E-value: 9.10e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 5 DVKNLVKKFHGQT-VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGeitidtGKSISQqkgliRRL 83
Cdd:cd03226 1 RIENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLN------GKPIKA-----KER 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 84 RQHVGFVFQN--FNLFpHRTVLENIIEGpvivkGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAM 161
Cdd:cd03226 70 RKSIGYVMQDvdYQLF-TDSVREELLLG-----LKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLS 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495775764 162 RPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIV 223
Cdd:cd03226 144 GKDLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-244 |
1.66e-48 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 160.39 E-value: 1.66e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 1 MSAIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSIN-LLEQPEGGTIRvGEITIdTGKSISQQKGL 79
Cdd:PRK14267 2 KFAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNrLLELNEEARVE-GEVRL-FGRNIYSPDVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 80 IRRLRQHVGFVFQNFNLFPHRTVLENIIEGPVIVK-GEPKEEATARARELLAKVGL----AGKETSYPRRLSGGQQQRVA 154
Cdd:PRK14267 80 PIEVRREVGMVFQYPNPFPHLTIYDNVAIGVKLNGlVKSKKELDERVEWALKKAALwdevKDRLNDYPSNLSGGQRQRLV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 155 IARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEkRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFAN 234
Cdd:PRK14267 160 IARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFEN 238
|
250
....*....|
gi 495775764 235 PQQPRTRQFL 244
Cdd:PRK14267 239 PEHELTEKYV 248
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-231 |
3.30e-48 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 165.96 E-value: 3.30e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 3 AIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVG--EITIDTGKSiSQQKGli 80
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDgePVRFRSPRD-AQAAG-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 81 rrlrqhVGFVFQNFNLFPHRTVLENI-----IEGPVIVKgepKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAI 155
Cdd:COG1129 81 ------IAIIHQELNLVPNLSVAENIflgrePRRGGLID---WRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495775764 156 ARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSL 231
Cdd:COG1129 152 ARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
15-207 |
3.67e-48 |
|
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: 157.58 E-value: 3.67e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 15 GQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGEITIDTGKsisqqKGLIRRlRQHVGFVFQNF 94
Cdd:TIGR01166 4 GPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDYSR-----KGLLER-RQRVGLVFQDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 95 N--LFpHRTVLENIIEGPVIVkGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPDVILFDEPT 172
Cdd:TIGR01166 78 DdqLF-AADVDQDVAFGPLNL-GLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPT 155
|
170 180 190
....*....|....*....|....*....|....*
gi 495775764 173 SALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFA 207
Cdd:TIGR01166 156 AGLDPAGREQMLAILRRLRAEGMTVVISTHDVDLA 190
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-244 |
7.58e-48 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 159.49 E-value: 7.58e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 3 AIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGEITIDtGKSISQQKGLIRr 82
Cdd:PRK14271 21 AMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLG-GRSIFNYRDVLE- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 83 LRQHVGFVFQNFNLFPhRTVLENIIEGPVIVKGEPKEEATARARELLAKVGL----AGKETSYPRRLSGGQQQRVAIARA 158
Cdd:PRK14271 99 FRRRVGMLFQRPNPFP-MSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLwdavKDRLSDSPFRLSGGQQQLLCLART 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 159 LAMRPDVILFDEPTSALDPELVGEVLNTIRQLAqEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFANPQQP 238
Cdd:PRK14271 178 LAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLA-DRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHA 256
|
....*.
gi 495775764 239 RTRQFL 244
Cdd:PRK14271 257 ETARYV 262
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
4-235 |
1.14e-47 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 160.40 E-value: 1.14e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 4 IDVKNLVKKFHGQT-----VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGEITIDTGKSISQQKG 78
Cdd:PRK13631 22 LRVKNLYCVFDEKQenelvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNHELIT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 79 L--------IRRLRQHVGFVFQ--NFNLFpHRTVLENIIEGPVIVkGEPKEEATARARELLAKVGLagkETSY----PRR 144
Cdd:PRK13631 102 NpyskkiknFKELRRRVSMVFQfpEYQLF-KDTIEKDIMFGPVAL-GVKKSEAKKLAKFYLNKMGL---DDSYlersPFG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 145 LSGGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVE 224
Cdd:PRK13631 177 LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILK 256
|
250
....*....|.
gi 495775764 225 QGPAKSLFANP 235
Cdd:PRK13631 257 TGTPYEIFTDQ 267
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
34-235 |
1.67e-47 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 159.97 E-value: 1.67e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 34 IIGPSGSGKTTLLRSINLLEQPEGGTIRVGeitidtGKSISQQKGLIRrlrqHVGFVFQNFNLFPHRTVLENIIEgPVIV 113
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLD------GEDVTNVPPHLR----HINMVFQSYALFPHMTVEENVAF-GLKM 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 114 KGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLaQE 193
Cdd:TIGR01187 70 RKVPRAEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTI-QE 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 495775764 194 KR--TMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFANP 235
Cdd:TIGR01187 149 QLgiTFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEP 192
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
6-244 |
2.57e-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: 2.57e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 6 VKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGeitidtGKSISQQKGLiRRLRQ 85
Cdd:TIGR03410 3 VSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLD------GEDITKLPPH-ERARA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 86 HVGFVFQNFNLFPHRTVLENIIEGPVIVKGEPK---EEATAR---ARELLAkvglagketsypRR---LSGGQQQRVAIA 156
Cdd:TIGR03410 76 GIAYVPQGREIFPRLTVEENLLTGLAALPRRSRkipDEIYELfpvLKEMLG------------RRggdLSGGQQQQLAIA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 157 RALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLfanp 235
Cdd:TIGR03410 144 RALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGmAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL---- 219
|
....*....
gi 495775764 236 QQPRTRQFL 244
Cdd:TIGR03410 220 DEDKVRRYL 228
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4-203 |
2.81e-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: 155.71 E-value: 2.81e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGeitidtGKSISQQKgliRRL 83
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWN------GEPIRDAR---EDY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 84 RQHVGFVFQNFNLFPHRTVLENIIegpVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRP 163
Cdd:COG4133 74 RRRLAYLGHADGLKPELTVRENLR---FWAALYGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 495775764 164 DVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHE 203
Cdd:COG4133 151 PLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQ 190
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
4-244 |
7.58e-47 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 156.09 E-value: 7.58e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGEITIDtGKSISQQKGLIRRL 83
Cdd:PRK14239 6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNPEVTITGSIVYN-GHNIYSPRTDTVDL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 84 RQHVGFVFQNFNLFPHrTVLENIIEGpVIVKGEPKEEATARARELLAKVGLAGKET-----SYPRRLSGGQQQRVAIARA 158
Cdd:PRK14239 85 RKEIGMVFQQPNPFPM-SIYENVVYG-LRLKGIKDKQVLDEAVEKSLKGASIWDEVkdrlhDSALGLSGGQQQRVCIARV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 159 LAMRPDVILFDEPTSALDPELVGEVLNTIRQLaQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFANPQQP 238
Cdd:PRK14239 163 LATSPKIILLDEPTSALDPISAGKIEETLLGL-KDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPKHK 241
|
....*.
gi 495775764 239 RTRQFL 244
Cdd:PRK14239 242 ETEDYI 247
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-244 |
8.09e-47 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 156.35 E-value: 8.09e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 1 MSAIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGEITIdTGKSISQQKGLI 80
Cdd:PRK14258 5 IPAIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRVEGRVEF-FNQNIYERRVNL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 81 RRLRQHVGFVFQNFNLFPhRTVLENIIEGPVIVKGEPK------EEATARARELLAKVglAGKETSYPRRLSGGQQQRVA 154
Cdd:PRK14258 84 NRLRRQVSMVHPKPNLFP-MSVYDNVAYGVKIVGWRPKleiddiVESALKDADLWDEI--KHKIHKSALDLSGGQQQRLC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 155 IARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLA-QEKRTMVIVTHEMSFARDVADRAIFMDQ-----GRIVEQGPA 228
Cdd:PRK14258 161 IARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLT 240
|
250
....*....|....*.
gi 495775764 229 KSLFANPQQPRTRQFL 244
Cdd:PRK14258 241 KKIFNSPHDSRTREYV 256
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-225 |
1.95e-46 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 155.41 E-value: 1.95e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 1 MSAIDVKNLVKKFHG----QTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGEITIdTGKSISQq 76
Cdd:COG4525 1 MSMLTVRHVSVRYPGggqpQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPV-TGPGADR- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 77 kglirrlrqhvGFVFQNFNLFPHRTVLENIIEGPVIvKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIA 156
Cdd:COG4525 79 -----------GVVFQKDALLPWLNVLDNVAFGLRL-RGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495775764 157 RALAMRPDVILFDEPTSALDP---ELVGEVLNTIRQLAQekRTMVIVTHEMSFARDVADRAIFMD--QGRIVEQ 225
Cdd:COG4525 147 RALAADPRFLLMDEPFGALDAltrEQMQELLLDVWQRTG--KGVFLITHSVEEALFLATRLVVMSpgPGRIVER 218
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-231 |
5.37e-46 |
|
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: 153.04 E-value: 5.37e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 4 IDVKNLVKKFHG--QTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGeitidtGKSISQQkglIR 81
Cdd:cd03263 1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYIN------GYSIRTD---RK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 82 RLRQHVGFVFQNFNLFPHRTVLENI-IEGpvIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALA 160
Cdd:cd03263 72 AARQSLGYCPQFDALFDELTVREHLrFYA--RLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495775764 161 MRPDVILFDEPTSALDPELVGEVLNTIRQLaQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSL 231
Cdd:cd03263 150 GGPSVLLLDEPTSGLDPASRRAIWDLILEV-RKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-221 |
8.95e-46 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 152.59 E-value: 8.95e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 1 MSA-IDVKNLVKKF--HGQ-----TVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRV--GEITIDTG 70
Cdd:COG4778 1 MTTlLEVENLSKTFtlHLQggkrlPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWVDLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 71 KSISQQkglIRRLRQH-VGFVFQNFNLFPHRTVLENIIEgPVIVKGEPKEEATARARELLAKVGLagketsyPRRL---- 145
Cdd:COG4778 81 QASPRE---ILALRRRtIGYVSQFLRVIPRVSALDVVAE-PLLERGVDREEARARARELLARLNL-------PERLwdlp 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 146 ----SGGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGR 221
Cdd:COG4778 150 patfSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
4-234 |
1.29e-45 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 153.70 E-value: 1.29e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 4 IDVKNLVKKFHG------QTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGEItiDTGKsisqqK 77
Cdd:PRK13633 5 IKCKNVSYKYESneesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGL--DTSD-----E 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 78 GLIRRLRQHVGFVFQNfnlfPHRTVLENIIEGPVIVKGE----PKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRV 153
Cdd:PRK13633 78 ENLWDIRNKAGMVFQN----PDNQIVATIVEEDVAFGPEnlgiPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 154 AIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKSLF 232
Cdd:PRK13633 154 AIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGiTIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIF 232
|
..
gi 495775764 233 AN 234
Cdd:PRK13633 233 KE 234
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
8-226 |
1.45e-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: 151.49 E-value: 1.45e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 8 NLVKKFHGQTVLHgIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGEITIDTGKSIsqqkglirrlRQHV 87
Cdd:cd03298 4 DKIRFSYGEQPMH-FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA----------DRPV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 88 GFVFQNFNLFPHRTVLENIIEG--PVIVKGEPKEEATARArelLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPDV 165
Cdd:cd03298 73 SMLFQENNLFAHLTVEQNVGLGlsPGLKLTAEDRQAIEVA---LARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495775764 166 ILFDEPTSALDPELVGEVLNTIRQL-AQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQG 226
Cdd:cd03298 150 LLLDEPFAALDPALRAEMLDLVLDLhAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1-234 |
1.48e-45 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 153.66 E-value: 1.48e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 1 MSaIDVKNLVKKFHGQT-----VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGEITIdTGKSISq 75
Cdd:PRK13637 1 MS-IKIENLTHIYMEGTpfekkALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDI-TDKKVK- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 76 qkglIRRLRQHVGFVFQ--NFNLFpHRTVLENIIEGPVIVkGEPKEEATARARELLAKVGLAG---KETSyPRRLSGGQQ 150
Cdd:PRK13637 78 ----LSDIRKKVGLVFQypEYQLF-EETIEKDIAFGPINL-GLSEEEIENRVKRAMNIVGLDYedyKDKS-PFELSGGQK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 151 QRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAK 229
Cdd:PRK13637 151 RRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPR 230
|
....*
gi 495775764 230 SLFAN 234
Cdd:PRK13637 231 EVFKE 235
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-244 |
2.11e-45 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 152.37 E-value: 2.11e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 1 MSAIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQ--PEGgtiRV-GEITIDtGKSISQQK 77
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEA---RVsGEVYLD-GQDIFKMD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 78 glIRRLRQHVGFVFQNFNLFPHRTVLENIIEGPVIVK-GEPKEEATARARELLAKVGL----AGKETSYPRRLSGGQQQR 152
Cdd:PRK14247 77 --VIELRRRVQMVFQIPNPIPNLSIFENVALGLKLNRlVKSKKELQERVRWALEKAQLwdevKDRLDAPAGKLSGGQQQR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 153 VAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKrTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLF 232
Cdd:PRK14247 155 LCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDM-TIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVF 233
|
250
....*....|..
gi 495775764 233 ANPQQPRTRQFL 244
Cdd:PRK14247 234 TNPRHELTEKYV 245
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
3-228 |
2.68e-45 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 152.23 E-value: 2.68e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 3 AIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGeitidtGKSISQQKG--LI 80
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLN------GRPLADWSPaeLA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 81 RR---LRQH--VGFVFqnfnlfphrTVLEnIIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAI 155
Cdd:PRK13548 76 RRravLPQHssLSFPF---------TVEE-VVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 156 ARALA------MRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVI-VTHEMSFARDVADRAIFMDQGRIVEQGPA 228
Cdd:PRK13548 146 ARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIvVLHDLNLAARYADRIVLLHQGRLVADGTP 225
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-227 |
3.42e-45 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 151.81 E-value: 3.42e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGeitidtGKSISQQKG--LIR 81
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLN------GRPLAAWSPweLAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 82 R---LRQH--VGFVFqnfnlfphrTVLENIIEGpVIVKGEPKEEATARARELLAKVGLAG-KETSYPRrLSGGQQQRVAI 155
Cdd:COG4559 76 RravLPQHssLAFPF---------TVEEVVALG-RAPHGSSAAQDRQIVREALALVGLAHlAGRSYQT-LSGGEQQRVQL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495775764 156 ARALA-------MRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGP 227
Cdd:COG4559 145 ARVLAqlwepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGT 223
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-232 |
5.84e-45 |
|
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: 151.01 E-value: 5.84e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 1 MSAIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQP-EGGTIRV-GEitidtgksisqQKG 78
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPtYGNDVRLfGE-----------RRG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 79 L--IRRLRQHVGFV----FQNFNlfPHRTVLEniiegpVIVKG---------EPKEEATARARELLAKVGLAGKETSYPR 143
Cdd:COG1119 70 GedVWELRKRIGLVspalQLRFP--RDETVLD------VVLSGffdsiglyrEPTDEQRERARELLELLGLAHLADRPFG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 144 RLSGGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRI 222
Cdd:COG1119 142 TLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEgAPTLVLVTHHVEEIPPGITHVLLLKDGRV 221
|
250
....*....|
gi 495775764 223 VEQGPAKSLF 232
Cdd:COG1119 222 VAAGPKEEVL 231
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-226 |
9.01e-45 |
|
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: 149.27 E-value: 9.01e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 4 IDVKNLVKKFHGQTVLHGIDLEVEQGeVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGeitidtGKSISQQKgliRRL 83
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRID------GQDVLKQP---QKL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 84 RQHVGFVFQNFNLFPHRTVLEnIIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRP 163
Cdd:cd03264 71 RRRIGYLPQEFGVYPNFTVRE-FLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495775764 164 DVILFDEPTSALDPELVGEVLNTIRQLAQEkRTMVIVTHEMSFARDVADRAIFMDQGRIVEQG 226
Cdd:cd03264 150 SILIVDEPTAGLDPEERIRFRNLLSELGED-RIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
19-237 |
1.42e-44 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 151.47 E-value: 1.42e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 19 LHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGEITIdTGKSISQQkglIRRLRQHVGFVFQnfnlFP 98
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITI-THKTKDKY---IRPVRKRIGMVFQ----FP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 99 HRTVLENIIEGPVIVK----GEPKEEATARARELLAKVGLAGKETSY-PRRLSGGQQQRVAIARALAMRPDVILFDEPTS 173
Cdd:PRK13646 95 ESQLFEDTVEREIIFGpknfKMNLDEVKNYAHRLLMDLGFSRDVMSQsPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495775764 174 ALDPELVGEVLNTIRQLAQEK-RTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFANPQQ 237
Cdd:PRK13646 175 GLDPQSKRQVMRLLKSLQTDEnKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKDKKK 239
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-246 |
6.17e-44 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 148.99 E-value: 6.17e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 2 SAIDVKNLVKKFHGQT--VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRvgeitIDtGKSISQQKgl 79
Cdd:PRK13632 6 VMIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIK-----ID-GITISKEN-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 80 IRRLRQHVGFVFQN-FNLFPHRTV-------LENiiegpvivKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQ 151
Cdd:PRK13632 78 LKEIRKKIGIIFQNpDNQFIGATVeddiafgLEN--------KKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 152 RVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARdVADRAIFMDQGRIVEQGPAKS 230
Cdd:PRK13632 150 RVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTrKKTLISITHDMDEAI-LADKVIVFSEGKLIAQGKPKE 228
|
250
....*....|....*.
gi 495775764 231 LFANpqqprtRQFLEK 246
Cdd:PRK13632 229 ILNN------KEILEK 238
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
6-222 |
6.50e-44 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 148.67 E-value: 6.50e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 6 VKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGEITIDTgksisqqkglirrLRQ 85
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAE-------------ARE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 86 HVGFVFQNFNLFPHRTVLENIIEGpviVKGEPKEeataRARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPDV 165
Cdd:PRK11247 82 DTRLMFQDARLLPWKKVIDNVGLG---LKGQWRD----AALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 495775764 166 ILFDEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADRAIFMDQGRI 222
Cdd:PRK11247 155 LLLDEPLGALDALTRIEMQDLIESLWQQHGfTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
19-232 |
6.78e-44 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 149.51 E-value: 6.78e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 19 LHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGEITIdtgKSISQQKGlIRRLRQHVGFVFQnfnlFP 98
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLI---TSTSKNKD-IKQIRKKVGLVFQ----FP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 99 H-----RTVLENIIEGPVIVkGEPKEEATARARELLAKVGLAGK--ETSyPRRLSGGQQQRVAIARALAMRPDVILFDEP 171
Cdd:PRK13649 95 EsqlfeETVLKDVAFGPQNF-GVSQEEAEALAREKLALVGISESlfEKN-PFELSGGQMRRVAIAGILAMEPKILVLDEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495775764 172 TSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLF 232
Cdd:PRK13649 173 TAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIF 233
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-231 |
7.86e-44 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 149.49 E-value: 7.86e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 3 AIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGeitidtGKSISqqkgliRR 82
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWD------GEPLD------PE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 83 LRQHVGFVFQNFNLFPHRTVLEniiegpVIV-----KGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIAR 157
Cdd:COG4152 69 DRRRIGYLPEERGLYPKMKVGE------QLVylarlKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIA 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495775764 158 ALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSL 231
Cdd:COG4152 143 ALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI 216
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
2-229 |
1.36e-43 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 148.24 E-value: 1.36e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 2 SAIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGEITIDTGKSISQQKGLIR 81
Cdd:PRK09984 3 TIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAGSHIELLGRTVQREGRLARDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 82 RLRQHVGFVFQNFNLFPHRTVLENIIEGPVivKGEP---------KEEATARARELLAKVGLAGKETSYPRRLSGGQQQR 152
Cdd:PRK09984 83 KSRANTGYIFQQFNLVNRLSVLENVLIGAL--GSTPfwrtcfswfTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495775764 153 VAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVT-HEMSFARDVADRAIFMDQGRIVEQGPAK 229
Cdd:PRK09984 161 VAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTlHQVDYALRYCERIVALRQGHVFYDGSSQ 238
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-225 |
3.34e-43 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 149.61 E-value: 3.34e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 1 MSAIDVKNLVKKFHGQT-VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEqpeggTIRVGEITIDtGKSISQQKGL 79
Cdd:PRK11650 1 MAGLKLQAVRKSYDGKTqVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLE-----RITSGEIWIG-GRVVNELEPA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 80 IRrlrqHVGFVFQNFNLFPHRTVLENIIEGPVIvKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARAL 159
Cdd:PRK11650 75 DR----DIAMVFQNYALYPHMSVRENMAYGLKI-RGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495775764 160 AMRPDVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIvEQ 225
Cdd:PRK11650 150 VREPAVFLFDEPLSNLDAKLRVQMRLEIQRLHRRlKTTSLYVTHDQVEAMTLADRVVVMNGGVA-EQ 215
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-226 |
5.17e-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: 144.67 E-value: 5.17e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGtirvgEITIDtGKSISQQKGLIRRl 83
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSG-----EITFD-GKSYQKNIEALRR- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 84 rqhVGFVFQNFNLFPHRTVLENIIEGPVIvKGEPKEeataRARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRP 163
Cdd:cd03268 74 ---IGALIEAPGFYPNLTARENLRLLARL-LGIRKK----RIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNP 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495775764 164 DVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQG 226
Cdd:cd03268 146 DLLILDEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
22-238 |
6.26e-43 |
|
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: 148.72 E-value: 6.26e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 22 IDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRV-GEITIDTGKSIsqqkgLIRRLRQHVGFVFQNFNLFPHR 100
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLnGRTLFDSRKGI-----FLPPEKRRIGYVFQEARLFPHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 101 TVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKetsYPRRLSGGQQQRVAIARALAMRPDVILFDEPTSALDPELV 180
Cdd:TIGR02142 91 SVRGNLRYGMKRARPSERRISFERVIELLGIGHLLGR---LPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRK 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 495775764 181 GEVLNTIRQLAQEKRT-MVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFANPQQP 238
Cdd:TIGR02142 168 YEILPYLERLHAEFGIpILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLP 226
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-236 |
1.15e-42 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 144.79 E-value: 1.15e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 1 MSAIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGEITIdTGKSISqqkgli 80
Cdd:COG1137 1 MMTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDI-THLPMH------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 81 RRLRQHVGFVFQNFNLFPHRTVLENI---IEgpviVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIAR 157
Cdd:COG1137 74 KRARLGIGYLPQEASIFRKLTVEDNIlavLE----LRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIAR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 158 ALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQekRTM-VIVT-HEMSFARDVADRAIFMDQGRIVEQGPAKSLFANP 235
Cdd:COG1137 150 ALATNPKFILLDEPFAGVDPIAVADIQKIIRHLKE--RGIgVLITdHNVRETLGICDRAYIISEGKVLAEGTPEEILNNP 227
|
.
gi 495775764 236 Q 236
Cdd:COG1137 228 L 228
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-233 |
1.52e-42 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 145.64 E-value: 1.52e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 1 MSAIDVKNLVKKFHGQT---VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVG--EITIDTgksisq 75
Cdd:PRK13650 2 SNIIEVKNLTFKYKEDQekyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDgdLLTEEN------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 76 qkglIRRLRQHVGFVFQN-FNLFPHRTV-------LENiiegpvivKGEPKEEATARARELLAKVGLAGKETSYPRRLSG 147
Cdd:PRK13650 76 ----VWDIRHKIGMVFQNpDNQFVGATVeddvafgLEN--------KGIPHEEMKERVNEALELVGMQDFKEREPARLSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 148 GQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVI-VTHEMSfarDVA--DRAIFMDQGRIVE 224
Cdd:PRK13650 144 GQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVIsITHDLD---EVAlsDRVLVMKNGQVES 220
|
....*....
gi 495775764 225 QGPAKSLFA 233
Cdd:PRK13650 221 TSTPRELFS 229
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
4-231 |
2.30e-42 |
|
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: 143.66 E-value: 2.30e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVgeitidTGKSISQQKGLIRRl 83
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATV------AGHDVVREPREVRR- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 84 rqHVGFVFQNFNLFPHRTVLENI-IEGPVivKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMR 162
Cdd:cd03265 74 --RIGIVFQDLSVDDELTGWENLyIHARL--YGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 163 PDVILFDEPTSALDPELVGEVLNTIRQL-AQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSL 231
Cdd:cd03265 150 PEVLFLDEPTIGLDPQTRAHVWEYIEKLkEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
21-233 |
3.63e-42 |
|
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: 150.34 E-value: 3.63e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 21 GIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGT--IRVGEITIDTGKSISQQKGlirRLRQHVGFVFQNFNLFP 98
Cdd:TIGR03269 302 NVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEvnVRVGDEWVDMTKPGPDGRG---RAKRYIGILHQEYDLYP 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 99 HRTVLENIIEGpvIVKGEPKEEATARARELLAKVGLAGKET-----SYPRRLSGGQQQRVAIARALAMRPDVILFDEPTS 173
Cdd:TIGR03269 379 HRTVLDNLTEA--IGLELPDELARMKAVITLKMVGFDEEKAeeildKYPDELSEGERHRVALAQVLIKEPRIVILDEPTG 456
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495775764 174 ALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFA 233
Cdd:TIGR03269 457 TMDPITKVDVTHSILKAREEmEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIVE 517
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-226 |
4.56e-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: 142.42 E-value: 4.56e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVgeitidTGKSISQQKglirrl 83
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLF------DGKPLDIAA------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 84 RQHVGFVFQNFNLFPHRTVLENIIEGPVIvKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRP 163
Cdd:cd03269 69 RNRIGYLPEERGLYPKMKVIDQLVYLAQL-KGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDP 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495775764 164 DVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQG 226
Cdd:cd03269 148 ELLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
4-244 |
8.80e-42 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 146.52 E-value: 8.80e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGtirvgEITIDtGKSISQqkglIRRL 83
Cdd:PRK11607 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAG-----QIMLD-GVDLSH----VPPY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 84 RQHVGFVFQNFNLFPHRTVLENIIEGpviVKGE--PKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAM 161
Cdd:PRK11607 90 QRPINMMFQSYALFPHMTVEQNIAFG---LKQDklPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 162 RPDVILFDEPTSALDPELVGEV-LNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFANPQQPRT 240
Cdd:PRK11607 167 RPKLLLLDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYS 246
|
....
gi 495775764 241 RQFL 244
Cdd:PRK11607 247 AEFI 250
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
19-232 |
9.46e-42 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 144.11 E-value: 9.46e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 19 LHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGEITIdtgKSISQQKGlIRRLRQHVGFVFQnfnlFP 98
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVV---SSTSKQKE-IKPVRKKVGVVFQ----FP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 99 H-----RTVLENIIEGPVIVkGEPKEEATARARELLAKVGLAGK--ETSyPRRLSGGQQQRVAIARALAMRPDVILFDEP 171
Cdd:PRK13643 94 EsqlfeETVLKDVAFGPQNF-GIPKEKAEKIAAEKLEMVGLADEfwEKS-PFELSGGQMRRVAIAGILAMEPEVLVLDEP 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495775764 172 TSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLF 232
Cdd:PRK13643 172 TAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-223 |
1.41e-41 |
|
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: 139.49 E-value: 1.41e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGeitidtGKSISQqKGLIRRL 83
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVD------GKEVSF-ASPRDAR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 84 RQHVGFVFQnfnlfphrtvleniiegpvivkgepkeeatararellakvglagketsyprrLSGGQQQRVAIARALAMRP 163
Cdd:cd03216 74 RAGIAMVYQ----------------------------------------------------LSVGERQMVEIARALARNA 101
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 164 DVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIV 223
Cdd:cd03216 102 RLLILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
3-236 |
1.84e-41 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 142.95 E-value: 1.84e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 3 AIDVKNLVKKFH-GQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVgeitidTGKSISQQKglIR 81
Cdd:PRK13647 4 IIEVEDLHFRYKdGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKV------MGREVNAEN--EK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 82 RLRQHVGFVFQNFN--LFPhRTVLENIIEGPVIVkGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARAL 159
Cdd:PRK13647 76 WVRSKVGLVFQDPDdqVFS-STVWDDVAFGPVNM-GLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495775764 160 AMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGpAKSLFANPQ 236
Cdd:PRK13647 154 AMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEG-DKSLLTDED 229
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-229 |
1.96e-41 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 147.87 E-value: 1.96e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 3 AIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGeitidtGKSISqqkglIRR 82
Cdd:COG3845 5 ALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILID------GKPVR-----IRS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 83 ----LRQHVGFVFQNFNLFPHRTVLENIIEG--PVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIA 156
Cdd:COG3845 74 prdaIALGIGMVHQHFMLVPNLTVAENIVLGlePTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEIL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495775764 157 RALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAK 229
Cdd:COG3845 154 KALYRGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTA 226
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
14-233 |
3.06e-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: 140.82 E-value: 3.06e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 14 HGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGgtirvGEITIDtGKSISQQKglIRRLRQHVGFVFQN 93
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQK-----GQILID-GIDIRDIS--RKSLRSMIGVVLQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 94 FNLFPhRTVLENIIEGPVIVKGEPKEEA--TARARELLAK--------VGLAGKetsyprRLSGGQQQRVAIARALAMRP 163
Cdd:cd03254 86 TFLFS-GTIMENIRLGRPNATDEEVIEAakEAGAHDFIMKlpngydtvLGENGG------NLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 164 DVILFDEPTSALDPELVGEVLNTIRQLaQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKSLFA 233
Cdd:cd03254 159 KILILDEATSNIDTETEKLIQEALEKL-MKGRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEGTHDELLA 226
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-226 |
3.42e-41 |
|
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: 147.64 E-value: 3.42e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTL---LRSINLLEQPEGGTI----------------RVGE 64
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLmhvLRGMDQYEPTSGRIIyhvalcekcgyverpsKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 65 ITIDTGKSISQQ--------KGLIRRLRQHVGFVFQ-NFNLFPHRTVLENIIEG-PVIvkGEPKEEATARARELLAKVGL 134
Cdd:TIGR03269 81 PCPVCGGTLEPEevdfwnlsDKLRRRIRKRIAIMLQrTFALYGDDTVLDNVLEAlEEI--GYEGKEAVGRAVDLIEMVQL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 135 AGKETSYPRRLSGGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADR 213
Cdd:TIGR03269 159 SHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGiSMVLTSHWPEVIEDLSDK 238
|
250
....*....|...
gi 495775764 214 AIFMDQGRIVEQG 226
Cdd:TIGR03269 239 AIWLENGEIKEEG 251
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
1-245 |
5.18e-41 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 141.51 E-value: 5.18e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 1 MSA-IDVKNLVKKFHGQT---------VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGEITIDTG 70
Cdd:COG4167 1 MSAlLEVRNLSKTFKYRTglfrrqqfeAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 71 kSISQQKGLIRrlrqhvgFVFQNFN--LFPHRTVLEnIIEGPVIVKGE-PKEEATARARELLAKVGLAGKETS-YPRRLS 146
Cdd:COG4167 81 -DYKYRCKHIR-------MIFQDPNtsLNPRLNIGQ-ILEEPLRLNTDlTAEEREERIFATLRLVGLLPEHANfYPHMLS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 147 GGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLaQEKR--TMVIVTHEMSFARDVADRAIFMDQGRIVE 224
Cdd:COG4167 152 SGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLEL-QEKLgiSYIYVSQHLGIVKHISDKVLVMHQGEVVE 230
|
250 260
....*....|....*....|.
gi 495775764 225 QGPAKSLFANPQQPRTRQFLE 245
Cdd:COG4167 231 YGKTAEVFANPQHEVTKRLIE 251
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-235 |
1.04e-40 |
|
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: 139.60 E-value: 1.04e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGeitidtGKSISQQKgLIRRL 83
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLD------GQDITKLP-MHKRA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 84 RQHVGFVFQNFNLFPHRTVLENII---EgpviVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALA 160
Cdd:cd03218 74 RLGIGYLPQEASIFRKLTVEENILavlE----IRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495775764 161 MRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFANP 235
Cdd:cd03218 150 TNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANE 224
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
23-226 |
1.42e-40 |
|
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: 138.84 E-value: 1.42e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 23 DLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGEITIdTGKSISQQKglirrlrqhVGFVFQNFNLFPHRTV 102
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSH-TGLAPYQRP---------VSMLFQENNLFAHLTV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 103 LENI---IEGPVIVKGEPKEEATARAREllakVGLAGKETSYPRRLSGGQQQRVAIARALAMRPDVILFDEPTSALDPEL 179
Cdd:TIGR01277 88 RQNIglgLHPGLKLNAEQQEKVVDAAQQ----VGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 495775764 180 VGEVLNTIRQLAQEK-RTMVIVTHEMSFARDVADRAIFMDQGRIVEQG 226
Cdd:TIGR01277 164 REEMLALVKQLCSERqRTLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
15-233 |
3.15e-40 |
|
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: 138.52 E-value: 3.15e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 15 GQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGEITIdtgKSISQQKglirrLRQHVGFVFQNF 94
Cdd:cd03253 13 GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDI---REVTLDS-----LRRAIGVVPQDT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 95 NLFpHRTVLENIIEGPVIVKGEPKEEATARAR---ELLA-------KVGLAGketsypRRLSGGQQQRVAIARALAMRPD 164
Cdd:cd03253 85 VLF-NDTIGYNIRYGRPDATDEEVIEAAKAAQihdKIMRfpdgydtIVGERG------LKLSGGEKQRVAIARAILKNPP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495775764 165 VILFDEPTSALDPELVGEVLNTIRQLAQeKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKSLFA 233
Cdd:cd03253 158 ILLLDEATSALDTHTEREIQAALRDVSK-GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEELLA 224
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
19-247 |
4.58e-40 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 139.58 E-value: 4.58e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 19 LHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVG--EITIDTGksisqQKGLiRRLRQHVGFVFQnfnl 96
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAgyHITPETG-----NKNL-KKLRKKVSLVFQ---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 97 FPH-----RTVLENIIEGPVIVkGEPKEEATARARELLAKVGLAGKETSY-PRRLSGGQQQRVAIARALAMRPDVILFDE 170
Cdd:PRK13641 93 FPEaqlfeNTVLKDVEFGPKNF-GFSEDEAKEKALKWLKKVGLSEDLISKsPFELSGGQMRRVAIAGVMAYEPEILCLDE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 171 PTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFANPQ--------QPRTRQ 242
Cdd:PRK13641 172 PAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKEwlkkhyldEPATSR 251
|
....*
gi 495775764 243 FLEKF 247
Cdd:PRK13641 252 FASKL 256
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
3-226 |
4.80e-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: 137.72 E-value: 4.80e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 3 AIDVKNLVKKFHGQT--VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGEITIdtgKSISQQKgli 80
Cdd:cd03245 2 RIEFRNVSFSYPNQEipALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDI---RQLDPAD--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 81 rrLRQHVGFVFQNFNLFpHRTVLENIIEGPVIVKGEPKEEATARA--RELLAK--------VGLAGketsypRRLSGGQQ 150
Cdd:cd03245 76 --LRRNIGYVPQDVTLF-YGTLRDNITLGAPLADDERILRAAELAgvTDFVNKhpngldlqIGERG------RGLSGGQR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495775764 151 QRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKrTMVIVTHEMSFArDVADRAIFMDQGRIVEQG 226
Cdd:cd03245 147 QAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDK-TLIIITHRPSLL-DLVDRIIVMDSGRIVADG 220
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-227 |
4.89e-40 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 139.05 E-value: 4.89e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 1 MSAIDVKNLVKKFHG---------QTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVgeitidTGK 71
Cdd:PRK10419 1 MTLLNVSGLSHHYAHgglsgkhqhQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSW------RGE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 72 SISQQKGLIRR-LRQHVGFVFQN----FNlfPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKETS-YPRRL 145
Cdd:PRK10419 75 PLAKLNRAQRKaFRRDIQMVFQDsisaVN--PRKTVREIIREPLRHLLSLDKAERLARASEMLRAVDLDDSVLDkRPPQL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 146 SGGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRT-MVIVTHEMSFARDVADRAIFMDQGRIVE 224
Cdd:PRK10419 153 SGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTaCLFITHDLRLVERFCQRVMVMDNGQIVE 232
|
...
gi 495775764 225 QGP 227
Cdd:PRK10419 233 TQP 235
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
23-231 |
7.21e-40 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 137.41 E-value: 7.21e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 23 DLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRV-GEITIDTGKSisqqkglirrlRQHVGFVFQNFNLFPHRT 101
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLnGQDHTTTPPS-----------RRPVSMLFQENNLFSHLT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 102 VLENIIEGPvivkgEPKEEATARARELLA----KVGLAGKETSYPRRLSGGQQQRVAIARALAMRPDVILFDEPTSALDP 177
Cdd:PRK10771 88 VAQNIGLGL-----NPGLKLNAAQREKLHaiarQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDP 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 495775764 178 ELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSL 231
Cdd:PRK10771 163 ALRQEMLTLVSQVCQERQlTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDEL 217
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
6-227 |
8.48e-40 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 136.46 E-value: 8.48e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 6 VKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSInlleqpeGGT----IRV-GEITIDtGKSISQQKGLI 80
Cdd:COG4136 4 LENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAI-------AGTlspaFSAsGEVLLN-GRRLTALPAEQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 81 RrlrqHVGFVFQNFNLFPHRTVLENIIEGpvIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALA 160
Cdd:COG4136 76 R----RIGILFQDDLLFPHLSVGENLAFA--LPPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495775764 161 MRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRT-MVIVTHemsfarDVADRAifmDQGRIVEQGP 227
Cdd:COG4136 150 AEPRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIpALLVTH------DEEDAP---AAGRVLDLGN 208
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
11-231 |
9.16e-40 |
|
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: 139.06 E-value: 9.16e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 11 KKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVgeitidTGKSISQQKgliRRLRQHVGFV 90
Cdd:TIGR01188 1 KVYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARV------AGYDVVREP---RKVRRSIGIV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 91 FQNFNLFPHRTVLENIiEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPDVILFDE 170
Cdd:TIGR01188 72 PQYASVDEDLTGRENL-EMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDE 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495775764 171 PTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSL 231
Cdd:TIGR01188 151 PTTGLDPRTRRAIWDYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEEL 211
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
19-245 |
2.04e-39 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 137.22 E-value: 2.04e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 19 LHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGEITIDtGKSISQQKGLIRRLRQHVGFVFQNFNLFP 98
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPGFRVEGKVTFH-GKNLYAPDVDPVEVRRRIGMVFQKPNPFP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 99 hRTVLENIIEGPVI--VKGEPKE--EATARARELLAKVGLAGKETSYPrrLSGGQQQRVAIARALAMRPDVILFDEPTSA 174
Cdd:PRK14243 105 -KSIYDNIAYGARIngYKGDMDElvERSLRQAALWDEVKDKLKQSGLS--LSGGQQQRLCIARAIAVQPEVILMDEPCSA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 175 LDPELVGEVLNTIRQLaQEKRTMVIVTHEMSFARDVADRAIFMD---------QGRIVEQGPAKSLFANPQQPRTRQFLE 245
Cdd:PRK14243 182 LDPISTLRIEELMHEL-KEQYTIIIVTHNMQQAARVSDMTAFFNveltegggrYGYLVEFDRTEKIFNSPQQQATRDYVS 260
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
19-220 |
2.10e-39 |
|
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: 136.44 E-value: 2.10e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 19 LHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVgeitidTGKSIsQQKGLIRRLrqhvgfVFQNFNLFP 98
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVIL------EGKQI-TEPGPDRMV------VFQNYSLLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 99 HRTVLENI-IEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPDVILFDEPTSALDP 177
Cdd:TIGR01184 68 WLTVRENIaLAVDRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 495775764 178 ELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADRAIFMDQG 220
Cdd:TIGR01184 148 LTRGNLQEELMQIWEEHRvTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
4-227 |
2.95e-39 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 136.37 E-value: 2.95e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGeitidtGKSISQQKG--LIR 81
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVD------GLDVATTPSreLAK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 82 R---LRQHVGFVFQ-------NFNLFPHRtvleniiegpvivKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQ 151
Cdd:COG4604 76 RlaiLRQENHINSRltvrelvAFGRFPYS-------------KGRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQ 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495775764 152 RVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEK-RTMVIVTHEMSFARDVADRAIFMDQGRIVEQGP 227
Cdd:COG4604 143 RAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELgKTVVIVLHDINFASCYADHIVAMKDGRVVAQGT 219
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
15-235 |
3.15e-39 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 137.04 E-value: 3.15e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 15 GQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGeiTIDTGkSISQQKGlIRRLrqhVGFVFQNF 94
Cdd:PRK13644 14 GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVS--GIDTG-DFSKLQG-IRKL---VGIVFQNP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 95 NL-FPHRTVLENIIEGPVIVkGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPDVILFDEPTS 173
Cdd:PRK13644 87 ETqFVGRTVEEDLAFGPENL-CLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTS 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495775764 174 ALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKSLFANP 235
Cdd:PRK13644 166 MLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGEPENVLSDV 226
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
8-225 |
4.44e-39 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 135.71 E-value: 4.44e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 8 NLVKKFH-GQT---VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIrvgeitIDTGKSISQQKGLIR-R 82
Cdd:PRK11629 10 NLCKRYQeGSVqtdVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDV------IFNGQPMSKLSSAAKaE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 83 LRQH-VGFVFQNFNLFPHRTVLENIIEgPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAM 161
Cdd:PRK11629 84 LRNQkLGFIYQFHHLLPDFTALENVAM-PLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVN 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495775764 162 RPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRT-MVIVTHEMSFARDVaDRAIFMDQGRIVEQ 225
Cdd:PRK11629 163 NPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTaFLVVTHDLQLAKRM-SRQLEMRDGRLTAE 226
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
4-233 |
4.65e-39 |
|
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: 135.44 E-value: 4.65e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 4 IDVKNLVKKF--HGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLlrsINLLeqPEGGTIRVGEITIDtGKSISQQKglIR 81
Cdd:cd03251 1 VEFKNVTFRYpgDGPPVLRDISLDIPAGETVALVGPSGSGKSTL---VNLI--PRFYDVDSGRILID-GHDVRDYT--LA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 82 RLRQHVGFVFQNFNLFpHRTVLENIIEGpvivkgepKEEATARARELLAKVGLA---------GKETSYPRR---LSGGQ 149
Cdd:cd03251 73 SLRRQIGLVSQDVFLF-NDTVAENIAYG--------RPGATREEVEEAARAANAhefimelpeGYDTVIGERgvkLSGGQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 150 QQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLaQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAK 229
Cdd:cd03251 144 RQRIAIARALLKDPPILILDEATSALDTESERLVQAALERL-MKNRTTFVIAHRLSTIEN-ADRIVVLEDGKIVERGTHE 221
|
....
gi 495775764 230 SLFA 233
Cdd:cd03251 222 ELLA 225
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
3-233 |
8.00e-39 |
|
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: 142.79 E-value: 8.00e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 3 AIDVKNLVKKFH--GQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIrvgeiTIDtGKSISqqkGL- 79
Cdd:TIGR03797 451 AIEVDRVTFRYRpdGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSV-----FYD-GQDLA---GLd 521
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 80 IRRLRQHVGFVFQNFNLFPHrTVLENIIEGPVIvkgePKEEATARAREllakVGLAGKETSYP-----------RRLSGG 148
Cdd:TIGR03797 522 VQAVRRQLGVVLQNGRLMSG-SIFENIAGGAPL----TLDEAWEAARM----AGLAEDIRAMPmgmhtviseggGTLSGG 592
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 149 QQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLaqeKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPA 228
Cdd:TIGR03797 593 QRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERL---KVTRIVIAHRLSTIRN-ADRIYVLDAGRVVQQGTY 668
|
....*
gi 495775764 229 KSLFA 233
Cdd:TIGR03797 669 DELMA 673
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
3-239 |
1.38e-38 |
|
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: 141.93 E-value: 1.38e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 3 AIDVKNLVKKFHGQT--VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIrvgeiTIDtGKSISQqkglI 80
Cdd:TIGR03375 463 EIEFRNVSFAYPGQEtpALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSV-----LLD-GVDIRQ----I 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 81 RR--LRQHVGFVFQNFNLFpHRTVLENIIEGpvivkgepkeEATARARELLAKVGLAGKET---SYP-----------RR 144
Cdd:TIGR03375 533 DPadLRRNIGYVPQDPRLF-YGTLRDNIALG----------APYADDEEILRAAELAGVTEfvrRHPdgldmqigergRS 601
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 145 LSGGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKrTMVIVTHEMSFArDVADRAIFMDQGRIVE 224
Cdd:TIGR03375 602 LSGGQRQAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLAGK-TLVLVTHRTSLL-DLVDRIIVMDNGRIVA 679
|
250
....*....|....*
gi 495775764 225 QGPAKSLFANPQQPR 239
Cdd:TIGR03375 680 DGPKDQVLEALRKGR 694
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
4-234 |
1.46e-38 |
|
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: 134.20 E-value: 1.46e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 4 IDVKNLvkKFH-----GQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLlrsINLLEQ---PeggtiRVGEITIDtGKSISQ 75
Cdd:cd03249 1 IEFKNV--SFRypsrpDVPILKGLSLTIPPGKTVALVGSSGCGKSTV---VSLLERfydP-----TSGEILLD-GVDIRD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 76 QKglIRRLRQHVGFVFQNFNLFPhRTVLENIIEGPVIVKGEPKEEAT--ARARELLAK--------VGLAGKEtsyprrL 145
Cdd:cd03249 70 LN--LRWLRSQIGLVSQEPVLFD-GTIAENIRYGKPDATDEEVEEAAkkANIHDFIMSlpdgydtlVGERGSQ------L 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 146 SGGQQQRVAIARALAMRPDVILFDEPTSALDPE---LVGEVLNTIRqlaqEKRTMVIVTHEMSFARDvADRAIFMDQGRI 222
Cdd:cd03249 141 SGGQKQRIAIARALLRNPKILLLDEATSALDAEsekLVQEALDRAM----KGRTTIVIAHRLSTIRN-ADLIAVLQNGQV 215
|
250
....*....|..
gi 495775764 223 VEQGPAKSLFAN 234
Cdd:cd03249 216 VEQGTHDELMAQ 227
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
3-244 |
2.18e-38 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 134.44 E-value: 2.18e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 3 AIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGEITIDtGKSISQqkglirr 82
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVE-GPGAER------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 83 lrqhvGFVFQNFNLFPHRTVLENIIEGpVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMR 162
Cdd:PRK11248 73 -----GVVFQNEGLLPWRNVQDNVAFG-LQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAAN 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 163 PDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMV-IVTHEMSFARDVADRAIFM--DQGRIVEQ------------GP 227
Cdd:PRK11248 147 PQLLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVlLITHDIEEAVFMATELVLLspGPGRVVERlplnfarrfvagES 226
|
250
....*....|....*..
gi 495775764 228 AKSLFANPQQPRTRQFL 244
Cdd:PRK11248 227 SRSIKSDPQFIAMREYV 243
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
24-244 |
4.52e-38 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 137.09 E-value: 4.52e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 24 LEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGeiTIDTGKSISQQKGLIRRlrQHVGFVFQNFNLFPHRTVL 103
Cdd:PRK10070 49 LAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLID--GVDIAKISDAELREVRR--KKIAMVFQSFALMPHMTVL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 104 ENIIEGpVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEV 183
Cdd:PRK10070 125 DNTAFG-MELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495775764 184 LNTIRQL-AQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFANPQQPRTRQFL 244
Cdd:PRK10070 204 QDELVKLqAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFF 265
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-236 |
6.41e-38 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 135.93 E-value: 6.41e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 1 MSAIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEqpeggTIRVGEITIDtgksiSQQKGLI 80
Cdd:PRK11000 1 MASVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLE-----DITSGDLFIG-----EKRMNDV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 81 RRLRQHVGFVFQNFNLFPHRTVLENIIEGpVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALA 160
Cdd:PRK11000 71 PPAERGVGMVFQSYALYPHLSVAENMSFG-LKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495775764 161 MRPDVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFANPQ 236
Cdd:PRK11000 150 AEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRlGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPA 226
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
15-241 |
7.52e-38 |
|
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: 139.11 E-value: 7.52e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 15 GQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGEITIDTGKSisqqkgliRRLRQHVGFVFQNF 94
Cdd:COG4618 344 KRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDR--------EELGRHIGYLPQDV 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 95 NLFPHrTVLENIiegpvivkGEPKEEA------TARARELLAK--------VGLAGketsypRRLSGGQQQRVAIARALA 160
Cdd:COG4618 416 ELFDG-TIAENIar-----fGDADPEKvvaaakLAGVHEMILRlpdgydtrIGEGG------ARLSGGQRQRIGLARALY 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 161 MRPDVILFDEPTSALDPElvGE--VLNTIRQLAQEKRTMVIVTHEMSFARdVADRAIFMDQGRIVEQGPAKSLFANPQQP 238
Cdd:COG4618 484 GDPRLVVLDEPNSNLDDE--GEaaLAAAIRALKARGATVVVITHRPSLLA-AVDKLLVLRDGRVQAFGPRDEVLARLARP 560
|
...
gi 495775764 239 RTR 241
Cdd:COG4618 561 AAA 563
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
4-222 |
1.60e-37 |
|
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: 129.64 E-value: 1.60e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 4 IDVKNLVKKFHG--QTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGeitidtGKSISQQKglIR 81
Cdd:cd03246 1 LEVENVSFRYPGaePPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLD------GADISQWD--PN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 82 RLRQHVGFVFQNFNLFPHrTVLENIiegpvivkgepkeeatararellakvglagketsyprrLSGGQQQRVAIARALAM 161
Cdd:cd03246 73 ELGDHVGYLPQDDELFSG-SIAENI--------------------------------------LSGGQRQRLGLARALYG 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495775764 162 RPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARdVADRAIFMDQGRI 222
Cdd:cd03246 114 NPRILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLA-SADRILVLEDGRV 173
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
15-243 |
1.70e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 132.66 E-value: 1.70e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 15 GQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGEITIDTGKsisqqKGLIRrLRQHVGFVFQ-- 92
Cdd:PRK13636 18 GTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSR-----KGLMK-LRESVGMVFQdp 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 93 NFNLFPhRTVLENIIEGPVIVkGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPDVILFDEPT 172
Cdd:PRK13636 92 DNQLFS-ASVYQDVSFGAVNL-KLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPT 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495775764 173 SALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFANPQQPRTRQF 243
Cdd:PRK13636 170 AGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAEKEMLRKVNL 241
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
14-207 |
2.24e-37 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 131.05 E-value: 2.24e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 14 HGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVgeitidTGKSISQQKGLIR-RLR-QHVGFVF 91
Cdd:PRK10584 21 HELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSL------VGQPLHQMDEEARaKLRaKHVGFVF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 92 QNFNLFPHRTVLENIiEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPDVILFDEP 171
Cdd:PRK10584 95 QSFMLIPTLNALENV-ELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEP 173
|
170 180 190
....*....|....*....|....*....|....*..
gi 495775764 172 TSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFA 207
Cdd:PRK10584 174 TGNLDRQTGDKIADLLFSLNREhGTTLILVTHDLQLA 210
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-244 |
2.78e-37 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 131.71 E-value: 2.78e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 2 SAIDVKNLVKKF---HGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGEITIDTGKSISQQKG 78
Cdd:PRK14246 6 SAEDVFNISRLYlyiNDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDIFQIDA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 79 LirRLRQHVGFVFQNFNLFPHRTVLENIIEgPVIVKG-EPKEEATARARELLAKVGL----AGKETSYPRRLSGGQQQRV 153
Cdd:PRK14246 86 I--KLRKEVGMVFQQPNPFPHLSIYDNIAY-PLKSHGiKEKREIKKIVEECLRKVGLwkevYDRLNSPASQLSGGQQQRL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 154 AIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKrTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFA 233
Cdd:PRK14246 163 TIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEI-AIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFT 241
|
250
....*....|.
gi 495775764 234 NPQQPRTRQFL 244
Cdd:PRK14246 242 SPKNELTEKYV 252
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
15-233 |
4.63e-37 |
|
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: 130.30 E-value: 4.63e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 15 GQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGEITIDTGKSISqqkglirrLRQHVGFVFQNF 94
Cdd:cd03252 14 GPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAW--------LRRQVGVVLQEN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 95 NLFpHRTVLENIIEGPVIVKGEPKEEAT--ARARELLAKVGLaGKETSYPRR---LSGGQQQRVAIARALAMRPDVILFD 169
Cdd:cd03252 86 VLF-NRSIRDNIALADPGMSMERVIEAAklAGAHDFISELPE-GYDTIVGEQgagLSGGQRQRIAIARALIHNPRILIFD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495775764 170 EPTSALDPELVGEVLNTIRQLAqEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKSLFA 233
Cdd:cd03252 164 EATSALDYESEHAIMRNMHDIC-AGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLA 225
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
21-241 |
5.08e-37 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 132.91 E-value: 5.08e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 21 GIDLEVEQGEVVAIIGPSGSGKTTLLRS-INLLEQPEGGTIRVGEITIDtgksisQQKGLIRRLRQHVGFVFQN--FNLF 97
Cdd:PRK15079 39 GVTLRLYEGETLGVVGESGCGKSTFARAiIGLVKATDGEVAWLGKDLLG------MKDDEWRAVRSDIQMIFQDplASLN 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 98 PHRTVLENIIEGPVIVKGE-PKEEATARARELLAKVGLAGKETS-YPRRLSGGQQQRVAIARALAMRPDVILFDEPTSAL 175
Cdd:PRK15079 113 PRMTIGEIIAEPLRTYHPKlSRQEVKDRVKAMMLKVGLLPNLINrYPHEFSGGQCQRIGIARALILEPKLIICDEPVSAL 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495775764 176 DPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFANPQQPRTR 241
Cdd:PRK15079 193 DVSIQAQVVNLLQQLQREMGlSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPYTK 259
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
14-226 |
1.07e-36 |
|
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: 128.05 E-value: 1.07e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 14 HGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINllEQPEGGTIRvGEITIDtGKSISQqkgliRRLRQHVGFVFQN 93
Cdd:cd03213 20 SGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALA--GRRTGLGVS-GEVLIN-GRPLDK-----RSFRKIIGYVPQD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 94 FNLFPHRTVleniiegpvivkgepkEEATARARELlakvglagketsypRRLSGGQQQRVAIARALAMRPDVILFDEPTS 173
Cdd:cd03213 91 DILHPTLTV----------------RETLMFAAKL--------------RGLSGGERKRVSIALELVSNPSLLFLDEPTS 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 495775764 174 ALDPELVGEVLNTIRQLAQEKRTMVIVTHEMS---FArdVADRAIFMDQGRIVEQG 226
Cdd:cd03213 141 GLDSSSALQVMSLLRRLADTGRTIICSIHQPSseiFE--LFDKLLLLSQGRVIYFG 194
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-217 |
2.15e-36 |
|
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: 134.72 E-value: 2.15e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 2 SAIDVKNLVKKFHGQT-VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGEITIDTGKSISqqkgli 80
Cdd:TIGR02857 320 SSLEFSGVSVAYPGRRpALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADS------ 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 81 rrLRQHVGFVFQNFNLFPhRTVLENIIEGpvivKGEPKEEATARArelLAKVGLAGKETSYP-----------RRLSGGQ 149
Cdd:TIGR02857 394 --WRDQIAWVPQHPFLFA-GTIAENIRLA----RPDASDAEIREA---LERAGLDEFVAALPqgldtpigeggAGLSGGQ 463
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495775764 150 QQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQeKRTMVIVTHEMSFARDvADRAIFM 217
Cdd:TIGR02857 464 AQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ-GRTVLLVTHRLALAAL-ADRIVVL 529
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-222 |
3.78e-36 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 133.65 E-value: 3.78e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 6 VKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINlleqpeggtirvGEITIDTGkSISQQKGLirrlrq 85
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILA------------GELEPDSG-EVSIPKGL------ 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 86 HVGFVFQNFNLFPHRTVLENIIEG--PVIVKGEPKEEAT-----------------------------ARARELLAKVGL 134
Cdd:COG0488 62 RIGYLPQEPPLDDDLTVLDTVLDGdaELRALEAELEELEaklaepdedlerlaelqeefealggweaeARAEEILSGLGF 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 135 AGKETSYP-RRLSGGQQQRVAIARALAMRPDVILFDEPTSALDpelvgevLNTIR----QLAQEKRTMVIVTHEMSFARD 209
Cdd:COG0488 142 PEEDLDRPvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLD-------LESIEwleeFLKNYPGTVLVVSHDRYFLDR 214
|
250
....*....|...
gi 495775764 210 VADRAIFMDQGRI 222
Cdd:COG0488 215 VATRILELDRGKL 227
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
15-223 |
4.25e-36 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 127.68 E-value: 4.25e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 15 GQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGeitidtGKSISQQKGL-IRRLRQHVGFVFQN 93
Cdd:PRK10908 14 GRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFS------GHDITRLKNReVPFLRRQIGMIFQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 94 FNLFPHRTVLENIiEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPDVILFDEPTS 173
Cdd:PRK10908 88 HHLLMDRTVYDNV-AIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTG 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 495775764 174 ALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIV 223
Cdd:PRK10908 167 NLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
18-226 |
6.52e-36 |
|
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: 127.00 E-value: 6.52e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 18 VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLeQPEGGTIRvGEITIDtGKSISQQKglirrLRQHVGFVFQNFNLF 97
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGR-VEGGGTTS-GQILFN-GQPRKPDQ-----FQKCVAYVRQDDILL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 98 PHRTVLENIIEGPVIVKGEPKEEATARAR---ELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPDVILFDEPTSA 174
Cdd:cd03234 94 PGLTVRETLTYTAILRLPRKSSDAIRKKRvedVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 495775764 175 LDPELVGEVLNTIRQLAQEKRTMVIVTHE-MSFARDVADRAIFMDQGRIVEQG 226
Cdd:cd03234 174 LDSFTALNLVSTLSQLARRNRIVILTIHQpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
2-244 |
8.75e-36 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 127.51 E-value: 8.75e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 2 SAIDVKNLVKKFHGQTVlHGIDLEVEQGEVVAIIGPSGSGKT-TLLRSINLLeqPEGGTIRVGEITIDtGKSISQQKgli 80
Cdd:PRK10418 3 QQIELRNIALQAAQPLV-HGVSLTLQRGRVLALVGGSGSGKSlTCAAALGIL--PAGVRQTAGRVLLD-GKPVAPCA--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 81 rrLR-QHVGFVFQN----FNlfPHRTVLENIIEgPVIVKGEPKEEATARAreLLAKVGLAGKET---SYPRRLSGGQQQR 152
Cdd:PRK10418 76 --LRgRKIATIMQNprsaFN--PLHTMHTHARE-TCLALGKPADDATLTA--ALEAVGLENAARvlkLYPFEMSGGMLQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 153 VAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRT-MVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSL 231
Cdd:PRK10418 149 MMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALgMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETL 228
|
250
....*....|...
gi 495775764 232 FANPQQPRTRQFL 244
Cdd:PRK10418 229 FNAPKHAVTRSLV 241
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
13-213 |
1.79e-35 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 125.04 E-value: 1.79e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 13 FHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGeitidTGKSIS---QQKGLIRRL----RQ 85
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRA-----GGARVAyvpQRSEVPDSLpltvRD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 86 HVGFvfqnfNLFPHRTVLeniiegpvivkGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPDV 165
Cdd:NF040873 77 LVAM-----GRWARRGLW-----------RRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADL 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 495775764 166 ILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDvADR 213
Cdd:NF040873 141 LLLDEPTTGLDAESRERIIALLAEEHARGATVVVVTHDLELVRR-ADP 187
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-223 |
2.87e-35 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 126.35 E-value: 2.87e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 4 IDVKNLVKKFHGQTV-----LHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINlleqpegGTIRV--GEITIDtGKSISQQ 76
Cdd:COG1101 2 LELKNLSKTFNPGTVnekraLDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIA-------GSLPPdsGSILID-GKDVTKL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 77 KgLIRRLRqHVGFVFQNFNL--FPHRTVLENII------EGPVIVKGEPKEEaTARARELLAKVGLaGKETsyprR---- 144
Cdd:COG1101 74 P-EYKRAK-YIGRVFQDPMMgtAPSMTIEENLAlayrrgKRRGLRRGLTKKR-RELFRELLATLGL-GLEN----Rldtk 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 145 ---LSGGQQQrvaiARALAM----RPDVILFDEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADRAIF 216
Cdd:COG1101 146 vglLSGGQRQ----ALSLLMatltKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNlTTLMVTHNMEQALDYGNRLIM 221
|
....*..
gi 495775764 217 MDQGRIV 223
Cdd:COG1101 222 MHEGRII 228
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
15-233 |
3.21e-35 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 131.76 E-value: 3.21e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 15 GQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGtirvgEITIDtgkSISQQKGLIRRLRQHVGFVFQNF 94
Cdd:TIGR02203 344 DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSG-----QILLD---GHDLADYTLASLRRQVALVSQDV 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 95 NLFpHRTVLENIIEGPVIVKGEPKEEATARARELLAKV-----GLAGKETSYPRRLSGGQQQRVAIARALAMRPDVILFD 169
Cdd:TIGR02203 416 VLF-NDTIANNIAYGRTEQADRAEIERALAAAYAQDFVdklplGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILD 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495775764 170 EPTSALDPELVGEVLNTIRQLAQEkRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKSLFA 233
Cdd:TIGR02203 495 EATSALDNESERLVQAALERLMQG-RTTLVIAHRLSTIEK-ADRIVVMDDGRIVERGTHNELLA 556
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
19-234 |
3.61e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 127.05 E-value: 3.61e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 19 LHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGEITIDTG-KSISQqkglIRRLRQHVGFVFQ--NFN 95
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANlKKIKE----VKRLRKEIGLVFQfpEYQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 96 LFpHRTVLENIIEGPVIVkGEPKEEATARARELLAKVGLAGKETS-YPRRLSGGQQQRVAIARALAMRPDVILFDEPTSA 174
Cdd:PRK13645 103 LF-QETIEKDIAFGPVNL-GENKQEAYKKVPELLKLVQLPEDYVKrSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGG 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495775764 175 LDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFAN 234
Cdd:PRK13645 181 LDPKGEEDFINLFERLNKEyKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN 241
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-235 |
4.41e-35 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 129.19 E-value: 4.41e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 1 MSAIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGEITID--TGKSISQQkg 78
Cdd:PRK09536 1 MPMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEalSARAASRR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 79 lIRRLRQHVGFVFQnfnlFPHRTVLEnIIEGPVIVKGEPKEEATARA-RELLAKVGLAGKETSYPRRLSGGQQQRVAIAR 157
Cdd:PRK09536 79 -VASVPQDTSLSFE----FDVRQVVE-MGRTPHRSRFDTWTETDRAAvERAMERTGVAQFADRPVTSLSGGERQRVLLAR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495775764 158 ALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFANP 235
Cdd:PRK09536 153 ALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTAD 230
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
4-226 |
5.31e-35 |
|
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: 124.40 E-value: 5.31e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 4 IDVKNLVKKFHGQT----VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIrvgeiTIDtGKSISQQKgl 79
Cdd:cd03266 2 ITADALTKRFRDVKktvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFA-----TVD-GFDVVKEP-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 80 iRRLRQHVGFVFQNFNLFPHRTVLENIiEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARAL 159
Cdd:cd03266 74 -AEARRRLGFVSDSTGLYDRLTARENL-EYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495775764 160 AMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQG 226
Cdd:cd03266 152 VHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-235 |
9.04e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 125.69 E-value: 9.04e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 1 MSAIDVKNLVKKFHGQT-VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVgeitidTGKSISQQKgl 79
Cdd:PRK13652 1 MHLIETRDLCYSYSGSKeALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLI------RGEPITKEN-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 80 IRRLRQHVGFVFQNFN--LFPhRTVLENIIEGPVIVkGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIAR 157
Cdd:PRK13652 73 IREVRKFVGLVFQNPDdqIFS-PTVEQDIAFGPINL-GLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495775764 158 ALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFANP 235
Cdd:PRK13652 151 VIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
4-232 |
9.32e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 125.25 E-value: 9.32e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 4 IDVKNLVKKFHGQT--VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIrvgeitIDTGKSISQQKglIR 81
Cdd:PRK13648 8 IVFKNVSFQYQSDAsfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEI------FYNNQAITDDN--FE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 82 RLRQHVGFVFQN-FNLFPHRTV-------LENiiegpvivKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRV 153
Cdd:PRK13648 80 KLRKHIGIVFQNpDNQFVGSIVkydvafgLEN--------HAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 154 AIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVI-VTHEMSFARDvADRAIFMDQGRIVEQGPAKSLF 232
Cdd:PRK13648 152 AIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIIsITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIF 230
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-229 |
1.04e-34 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 124.42 E-value: 1.04e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 1 MS-AIDVKNLVKKFHGQ----------------------TVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEG 57
Cdd:COG1134 1 MSsMIEVENVSKSYRLYhepsrslkelllrrrrtrreefWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 58 GTIRV-GEIT--IDTGksisqqkglirrlrqhVGFVfqnfnlfPHRTVLENIIEGPVIVkGEPKEEATARARELLAKVGL 134
Cdd:COG1134 81 GRVEVnGRVSalLELG----------------AGFH-------PELTGRENIYLNGRLL-GLSRKEIDEKFDEIVEFAEL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 135 aGKETSYP-RRLSGGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADR 213
Cdd:COG1134 137 -GDFIDQPvKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGAVRRLCDR 215
|
250
....*....|....*.
gi 495775764 214 AIFMDQGRIVEQGPAK 229
Cdd:COG1134 216 AIWLEKGRLVMDGDPE 231
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
29-244 |
1.12e-34 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 130.75 E-value: 1.12e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 29 GEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGEITIDTgksISQQKglIRRLRQHVGFVFQN--FNLFPHRTVLENI 106
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDT---LSPGK--LQALRRDIQFIFQDpyASLDPRQTVGDSI 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 107 IEgPVIVKG-EPKEEATARARELLAKVGLAGKET-SYPRRLSGGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVL 184
Cdd:PRK10261 425 ME-PLRVHGlLPGKAAAARVAWLLERVGLLPEHAwRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQII 503
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495775764 185 NTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFANPQQPRTRQFL 244
Cdd:PRK10261 504 NLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLM 564
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
6-244 |
1.55e-34 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 130.36 E-value: 1.55e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 6 VKNLVKKFH--GQTV--LHGIDLEVEQGEVVAIIGPSGSGKT-TLLRSINLLEQpEGGTIRVGEI--------TIDTGKS 72
Cdd:PRK10261 15 VENLNIAFMqeQQKIaaVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQ-AGGLVQCDKMllrrrsrqVIELSEQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 73 ISQQkglIRRLR-QHVGFVFQN--FNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKET---SYPRRLS 146
Cdd:PRK10261 94 SAAQ---MRHVRgADMAMIFQEpmTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTilsRYPHQLS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 147 GGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVI-VTHEMSFARDVADRAIFMDQGRIVEQ 225
Cdd:PRK10261 171 GGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIfITHDMGVVAEIADRVLVMYQGEAVET 250
|
250
....*....|....*....
gi 495775764 226 GPAKSLFANPQQPRTRQFL 244
Cdd:PRK10261 251 GSVEQIFHAPQHPYTRALL 269
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-233 |
2.33e-34 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 125.30 E-value: 2.33e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 2 SAIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVgeitidTGKSISQQKgliR 81
Cdd:PRK13537 6 APIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISL------CGEPVPSRA---R 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 82 RLRQHVGFVFQNFNLFPHRTVLENI-IEGPVIvkGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALA 160
Cdd:PRK13537 77 HARQRVGVVPQFDNLDPDFTVRENLlVFGRYF--GLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495775764 161 MRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFA 233
Cdd:PRK13537 155 NDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIE 227
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
3-247 |
2.54e-34 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 129.17 E-value: 2.54e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 3 AIDVKNLVKKFHGQT--VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGEITIdtgKSISQQkgli 80
Cdd:PRK11160 338 SLTLNNVSFTYPDQPqpVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPI---ADYSEA---- 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 81 rRLRQHVGFVFQNFNLFPHrTVLENIIEGpvivkgepKEEAT-ARARELLAKVGLAGKETSYP----------RRLSGGQ 149
Cdd:PRK11160 411 -ALRQAISVVSQRVHLFSA-TLRDNLLLA--------APNASdEALIEVLQQVGLEKLLEDDKglnawlgeggRQLSGGE 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 150 QQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKrTMVIVTHEMSfARDVADRAIFMDQGRIVEQGPAK 229
Cdd:PRK11160 481 QRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNK-TVLMITHRLT-GLEQFDRICVMDNGQIIEQGTHQ 558
|
250
....*....|....*...
gi 495775764 230 SLFAnpQQPRTRQFLEKF 247
Cdd:PRK11160 559 ELLA--QQGRYYQLKQRL 574
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
16-235 |
2.62e-34 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 130.23 E-value: 2.62e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 16 QTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGtirvgEITIDtGKSISQQKGliRRLRQHVGFVFQNFN 95
Cdd:TIGR00958 494 VPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGG-----QVLLD-GVPLVQYDH--HYLHRQVALVGQEPV 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 96 LFpHRTVLENIIEGpviVKGEPKEEATARARELLAKVGLAGKETSYPR-------RLSGGQQQRVAIARALAMRPDVILF 168
Cdd:TIGR00958 566 LF-SGSVRENIAYG---LTDTPDEEIMAAAKAANAHDFIMEFPNGYDTevgekgsQLSGGQKQRIAIARALVRKPRVLIL 641
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495775764 169 DEPTSALDPElvgevlntIRQLAQE-----KRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKSLFANP 235
Cdd:TIGR00958 642 DEATSALDAE--------CEQLLQEsrsraSRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
4-245 |
2.64e-34 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 124.11 E-value: 2.64e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSInlleqpeGGTIR--VGEITIDTGKSISQQKGLIR 81
Cdd:PRK11831 8 VDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLI-------GGQIApdHGEILFDGENIPAMSRSRLY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 82 RLRQHVGFVFQNFNLFPHRTVLENIiegpvivkGEPKEEATARAREL--------LAKVGLAGKETSYPRRLSGGQQQRV 153
Cdd:PRK11831 81 TVRKRMSMLFQSGALFTDMNVFDNV--------AYPLREHTQLPAPLlhstvmmkLEAVGLRGAAKLMPSELSGGMARRA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 154 AIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLF 232
Cdd:PRK11831 153 ALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSAlGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQ 232
|
250
....*....|...
gi 495775764 233 ANPqQPRTRQFLE 245
Cdd:PRK11831 233 ANP-DPRVRQFLD 244
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
4-244 |
2.65e-34 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 129.05 E-value: 2.65e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 4 IDVKNLVKKFHGQ----TVLHGIDLEVEQGEVVAIIGPSGSGKT-TLLRSINLLEQPE----GGTIRVgeitidTGKSI- 73
Cdd:PRK15134 6 LAIENLSVAFRQQqtvrTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRF------HGESLl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 74 --SQQKglIRRLR-QHVGFVFQN--FNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGL---AGKETSYPRRL 145
Cdd:PRK15134 80 haSEQT--LRGVRgNKIAMIFQEpmVSLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIrqaAKRLTDYPHQL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 146 SGGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVE 224
Cdd:PRK15134 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNGRCVE 237
|
250 260
....*....|....*....|
gi 495775764 225 QGPAKSLFANPQQPRTRQFL 244
Cdd:PRK15134 238 QNRAATLFSAPTHPYTQKLL 257
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
19-226 |
2.83e-34 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 129.31 E-value: 2.83e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 19 LHGIDLEVEQGEVVAIIGPSGSGKTTLlrsINLLEQ---PEGGTIRVGEITIdtgKSISqqkglIRRLRQHVGFVFQNFN 95
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTL---INLLQRvfdPQSGRILIDGTDI---RTVT-----RASLRRNIAVVFQDAG 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 96 LFpHRTVLENIIEGpvivkgepKEEAT----------ARARELLAK--------VGLAGketsypRRLSGGQQQRVAIAR 157
Cdd:PRK13657 420 LF-NRSIEDNIRVG--------RPDATdeemraaaerAQAHDFIERkpdgydtvVGERG------RQLSGGERQRLAIAR 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495775764 158 ALAMRPDVILFDEPTSALDPEL---VGEVLNTIRQlaqeKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQG 226
Cdd:PRK13657 485 ALLKDPPILILDEATSALDVETeakVKAALDELMK----GRTTFIIAHRLSTVRN-ADRILVFDNGRVVESG 551
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
17-245 |
2.87e-34 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 128.67 E-value: 2.87e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 17 TVLHGIDLEVEQGEVVAIIGPSGSGKTT----LLRSINlleqpeggtiRVGEITIDtGKSISQqkgLIRR----LRQHVG 88
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN----------SQGEIWFD-GQPLHN---LNRRqllpVRHRIQ 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 89 FVFQNFN--LFPHRTVLENIIEG-PVIVKGEPKEEATARARELLAKVGL-AGKETSYPRRLSGGQQQRVAIARALAMRPD 164
Cdd:PRK15134 366 VVFQDPNssLNPRLNVLQIIEEGlRVHQPTLSAAQREQQVIAVMEEVGLdPETRHRYPAEFSGGQRQRIAIARALILKPS 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 165 VILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVI-VTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFANPQQPRTRQF 243
Cdd:PRK15134 446 LIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLfISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEYTRQL 525
|
..
gi 495775764 244 LE 245
Cdd:PRK15134 526 LA 527
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
18-236 |
3.12e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 124.14 E-value: 3.12e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 18 VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVgeITIDtGKSISQQKglIRRLRQHVGFVFQN-FNL 96
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSK--ITVD-GITLTAKT--VWDIREKVGIVFQNpDNQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 97 FPHRTV-------LENiiegpvivKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPDVILFD 169
Cdd:PRK13640 97 FVGATVgddvafgLEN--------RAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495775764 170 EPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFArDVADRAIFMDQGRIVEQGPAKSLFANPQ 236
Cdd:PRK13640 169 ESTSMLDPAGKEQILKLIRKLKKKNNlTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKVE 235
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
17-226 |
6.89e-34 |
|
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: 128.40 E-value: 6.89e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 17 TVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRsinLLEQ---PEGGTIRVGEITIdtgKSISQQKglirrLRQHVGFVFQN 93
Cdd:COG5265 372 PILKGVSFEVPAGKTVAIVGPSGAGKSTLAR---LLFRfydVTSGRILIDGQDI---RDVTQAS-----LRAAIGIVPQD 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 94 FNLFpHRTVLENIIEGpvivkgepKEEAT-------ARARELLAKV-GL-AGKETSYPRR---LSGGQQQRVAIARALAM 161
Cdd:COG5265 441 TVLF-NDTIAYNIAYG--------RPDASeeeveaaARAAQIHDFIeSLpDGYDTRVGERglkLSGGEKQRVAIARTLLK 511
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495775764 162 RPDVILFDEPTSALDPELVGEVLNTIRQLAQEkRTMVIVTHEMSFARDvADRAIFMDQGRIVEQG 226
Cdd:COG5265 512 NPPILIFDEATSALDSRTERAIQAALREVARG-RTTLVIAHRLSTIVD-ADEILVLEAGRIVERG 574
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
6-235 |
9.38e-34 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 122.41 E-value: 9.38e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 6 VKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGEITID--TGKSISqQKGLIRrl 83
Cdd:PRK11300 8 VSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEglPGHQIA-RMGVVR-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 84 rqhvgfVFQNFNLFPHRTVLEN------------IIEG----PVIVKGEpkEEATARARELLAKVGLagkeTSYPRR--- 144
Cdd:PRK11300 85 ------TFQHVRLFREMTVIENllvaqhqqlktgLFSGllktPAFRRAE--SEALDRAATWLERVGL----LEHANRqag 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 145 -LSGGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMV-IVTHEMSFARDVADRAIFMDQGRI 222
Cdd:PRK11300 153 nLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVlLIEHDMKLVMGISDRIYVVNQGTP 232
|
250
....*....|...
gi 495775764 223 VEQGPAKSLFANP 235
Cdd:PRK11300 233 LANGTPEEIRNNP 245
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
6-244 |
1.12e-33 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 122.34 E-value: 1.12e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 6 VKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTI----RVGEITIDTGKSISQQKGLir 81
Cdd:PRK11701 9 VRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVhyrmRDGQLRDLYALSEAERRRL-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 82 rLRQHVGFVFQNF--NLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKETS-YPRRLSGGQQQRVAIARA 158
Cdd:PRK11701 87 -LRTEWGFVHQHPrdGLRMQVSAGGNIGERLMAVGARHYGDIRATAGDWLERVEIDAARIDdLPTTFSGGMQQRLQIARN 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 159 LAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFANPQQ 237
Cdd:PRK11701 166 LVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGlAVVIVTHDLAVARLLAHRLLVMKQGRVVESGLTDQVLDDPQH 245
|
....*..
gi 495775764 238 PRTrQFL 244
Cdd:PRK11701 246 PYT-QLL 251
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
4-226 |
2.84e-33 |
|
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: 118.95 E-value: 2.84e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 4 IDVKNLVKKFHGQ--TVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPeggtiRVGEITIDtGKSISQQKGLir 81
Cdd:cd03247 1 LSINNVSFSYPEQeqQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKP-----QQGEITLD-GVPVSDLEKA-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 82 rLRQHVGFVFQNFNLFpHRTVLENIiegpvivkgepkeeatararellakvglagketsyPRRLSGGQQQRVAIARALAM 161
Cdd:cd03247 73 -LSSLISVLNQRPYLF-DTTLRNNL-----------------------------------GRRFSGGERQRLALARILLQ 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495775764 162 RPDVILFDEPTSALDPELVGEVLNTIRQLAQEKrTMVIVTHEMSfARDVADRAIFMDQGRIVEQG 226
Cdd:cd03247 116 DAPIVLLDEPTVGLDPITERQLLSLIFEVLKDK-TLIWITHHLT-GIEHMDKILFLENGKIIMQG 178
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
10-242 |
4.86e-33 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 122.68 E-value: 4.86e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 10 VKKFHGQTVLHgIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGEIT-IDTGKSISqqkgLIRRLRqHVG 88
Cdd:PRK11144 6 FKQQLGDLCLT-VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVlFDAEKGIC----LPPEKR-RIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 89 FVFQNFNLFPHRTVLENIIEGpviVKGEPKEEatarareLLAKVGLAGKE---TSYPRRLSGGQQQRVAIARALAMRPDV 165
Cdd:PRK11144 80 YVFQDARLFPHYKVRGNLRYG---MAKSMVAQ-------FDKIVALLGIEpllDRYPGSLSGGEKQRVAIGRALLTAPEL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 166 ILFDEPTSALDPELVGEVLNTIRQLAQEKRT-MVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFANPQ----QPRT 240
Cdd:PRK11144 150 LLMDEPLASLDLPRKRELLPYLERLAREINIpILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSAmrpwLPKE 229
|
..
gi 495775764 241 RQ 242
Cdd:PRK11144 230 EQ 231
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
4-241 |
5.51e-33 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 120.32 E-value: 5.51e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGEITIDTGKSISQQKGLIRRL 83
Cdd:TIGR02323 4 LQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAELELYQLSEAERRRL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 84 -RQHVGFVFQNFNLFPHRTVLE--NIIEGPVIVKGEPKEEATARARELLAKVGL-AGKETSYPRRLSGGQQQRVAIARAL 159
Cdd:TIGR02323 84 mRTEWGFVHQNPRDGLRMRVSAgaNIGERLMAIGARHYGNIRATAQDWLEEVEIdPTRIDDLPRAFSGGMQQRLQIARNL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 160 AMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFANPQQP 238
Cdd:TIGR02323 164 VTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGlAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQVLDDPQHP 243
|
...
gi 495775764 239 RTR 241
Cdd:TIGR02323 244 YTQ 246
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
4-236 |
1.28e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 119.81 E-value: 1.28e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 4 IDVKNLVKKFHGQT---VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVgeitidTGKSISQQKglI 80
Cdd:PRK13642 5 LEVENLVFKYEKESdvnQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKI------DGELLTAEN--V 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 81 RRLRQHVGFVFQN-FNLFPHRTVLENIIEGpVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARAL 159
Cdd:PRK13642 77 WNLRRKIGMVFQNpDNQFVGATVEDDVAFG-MENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGII 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495775764 160 AMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKSLFANPQ 236
Cdd:PRK13642 156 ALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQlTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATSE 232
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
18-221 |
2.10e-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: 117.19 E-value: 2.10e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 18 VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSInlleqpeggtirVGEITIDTGKSisqqkglirRLRQHVGFVFQN---F 94
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSAL------------LGELEKLSGSV---------SVPGSIAYVSQEpwiQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 95 NlfphRTVLENIIegpvivKGEPKEEAtaRARELLAKVGL--------AGKETSYPRR---LSGGQQQRVAIARALAMRP 163
Cdd:cd03250 79 N----GTIRENIL------FGKPFDEE--RYEKVIKACALepdleilpDGDLTEIGEKginLSGGQKQRISLARAVYSDA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 164 DVILFDEPTSALDPElVGEVL--NTIRQLAQEKRTMVIVTHEMSFARDvADRAIFMDQGR 221
Cdd:cd03250 147 DIYLLDDPLSAVDAH-VGRHIfeNCILGLLLNNKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-224 |
2.45e-32 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 123.25 E-value: 2.45e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGEiTIdtgksisqqkglirrl 83
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGE-TV---------------- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 84 rqHVGFVFQNF-NLFPHRTVLENIIEGpvivkGEPKEEATARAreLLAKVGLAGKETSYP-RRLSGGQQQRVAIARALAM 161
Cdd:COG0488 379 --KIGYFDQHQeELDPDKTVLDELRDG-----APGGTEQEVRG--YLGRFLFSGDDAFKPvGVLSGGEKARLALAKLLLS 449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495775764 162 RPDVILFDEPTSALDPELVgEVLNTIrqLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVE 224
Cdd:COG0488 450 PPNVLLLDEPTNHLDIETL-EALEEA--LDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVRE 509
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
22-244 |
8.20e-32 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 119.08 E-value: 8.20e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 22 IDLEVEQGEVVAIIGPSGSGKT-TLLRSINLLEQPegGTIRVGEITIDtGKSISQQKGLIRR--LRQHVGFVFQN--FNL 96
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYP--GRVMAEKLEFN-GQDLQRISEKERRnlVGAEVAMIFQDpmTSL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 97 FPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGL---AGKETSYPRRLSGGQQQRVAIARALAMRPDVILFDEPTS 173
Cdd:PRK11022 103 NPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIpdpASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTT 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495775764 174 ALDPELVGEVLNTIRQLAQ-EKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFANPQQPRTRQFL 244
Cdd:PRK11022 183 ALDVTIQAQIIELLLELQQkENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAPRHPYTQALL 254
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-239 |
1.11e-31 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 116.53 E-value: 1.11e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 1 MSAIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIrvgeiTIDTgKSISQQKgLI 80
Cdd:PRK10895 1 MATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNI-----IIDD-EDISLLP-LH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 81 RRLRQHVGFVFQNFNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALA 160
Cdd:PRK10895 74 ARARRGIGYLPQEASIFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495775764 161 MRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFANPQQPR 239
Cdd:PRK10895 154 ANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKR 232
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
19-226 |
1.92e-31 |
|
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: 121.53 E-value: 1.92e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 19 LHGIDLEVEQGEVVAIIGPSGSGKTTLlrsINLLEQ---PEGGTIRVGEITIDTGKSISqqkglirrLRQHVGFVFQNFN 95
Cdd:TIGR01192 351 VFDVSFEAKAGQTVAIVGPTGAGKTTL---INLLQRvydPTVGQILIDGIDINTVTRES--------LRKSIATVFQDAG 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 96 LFpHRTVLENIIEGPVIVKGEPKEEATA----------RARELLAKVGLAGKetsyprRLSGGQQQRVAIARALAMRPDV 165
Cdd:TIGR01192 420 LF-NRSIRENIRLGREGATDEEVYEAAKaaaahdfilkRSNGYDTLVGERGN------RLSGGERQRLAIARAILKNAPI 492
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495775764 166 ILFDEPTSALDPELVGEVLNTIRQLAQEkRTMVIVTHEMSFARDvADRAIFMDQGRIVEQG 226
Cdd:TIGR01192 493 LVLDEATSALDVETEARVKNAIDALRKN-RTTFIIAHRLSTVRN-ADLVLFLDQGRLIEKG 551
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
10-222 |
4.69e-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: 113.30 E-value: 4.69e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 10 VKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVG--EITI-DTGKSISQQKGLIRRLRQH 86
Cdd:cd03215 7 VRGLSVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDgkPVTRrSPRDAIRAGIAYVPEDRKR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 87 VGfvfqnfnLFPHRTVLENIIegpvivkgepkeeatararellakvglagketsYPRRLSGGQQQRVAIARALAMRPDVI 166
Cdd:cd03215 87 EG-------LVLDLSVAENIA---------------------------------LSSLLSGGNQQKVVLARWLARDPRVL 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 495775764 167 LFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRI 222
Cdd:cd03215 127 ILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
15-202 |
5.31e-31 |
|
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: 119.77 E-value: 5.31e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 15 GQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGtirvgEITIDTGKSISQQKGLIRRLrqhVGFVFQNF 94
Cdd:TIGR02868 347 APPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQG-----EVTLDGVPVSSLDQDEVRRR---VSVCAQDA 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 95 NLFpHRTVLENIIEGpvivkgepKEEAT-ARARELLAKVGLA--------GKET---SYPRRLSGGQQQRVAIARALAMR 162
Cdd:TIGR02868 419 HLF-DTTVRENLRLA--------RPDATdEELWAALERVGLAdwlralpdGLDTvlgEGGARLSGGERQRLALARALLAD 489
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 495775764 163 PDVILFDEPTSALDPELVGEVLNTIRQlAQEKRTMVIVTH 202
Cdd:TIGR02868 490 APILLLDEPTEHLDAETADELLEDLLA-ALSGRTVVLITH 528
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
3-233 |
5.66e-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: 120.62 E-value: 5.66e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 3 AIDVKNLVKKFHGQT--VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGEITIDTGKSISqqkgli 80
Cdd:TIGR01846 455 AITFENIRFRYAPDSpeVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAW------ 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 81 rrLRQHVGFVFQNFNLFpHRTVLENIIEGPvivKGEPKEEATARARellakvgLAGKE---TSYPR-----------RLS 146
Cdd:TIGR01846 529 --LRRQMGVVLQENVLF-SRSIRDNIALCN---PGAPFEHVIHAAK-------LAGAHdfiSELPQgyntevgekgaNLS 595
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 147 GGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQeKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQG 226
Cdd:TIGR01846 596 GGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRNMREICR-GRTVIIIAHRLSTVRA-CDRIIVLEKGQIAESG 673
|
....*..
gi 495775764 227 PAKSLFA 233
Cdd:TIGR01846 674 RHEELLA 680
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-236 |
9.01e-31 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 114.44 E-value: 9.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 6 VKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGEITIdTGKSISQqkglIRRLRq 85
Cdd:COG4674 13 VEDLTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDL-TGLDEHE----IARLG- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 86 hVGFVFQNFNLFPHRTVLENIIegpVIVKGE----------PKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAI 155
Cdd:COG4674 87 -IGRKFQKPTVFEELTVFENLE---LALKGDrgvfaslfarLTAEERDRIEEVLETIGLTDKADRLAGLLSHGQKQWLEI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 156 ARALAMRPDVILFDEPTSALDP---ELVGEVLNTIRQlaqeKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLF 232
Cdd:COG4674 163 GMLLAQDPKLLLLDEPVAGMTDaetERTAELLKSLAG----KHSVVVVEHDMEFVRQIARKVTVLHQGSVLAEGSLDEVQ 238
|
....
gi 495775764 233 ANPQ 236
Cdd:COG4674 239 ADPR 242
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
18-234 |
9.01e-30 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 111.51 E-value: 9.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 18 VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSinLLEQPEGGTirvGEITIDtGKSISQQKgLIRRLRQHVGFVFQNFNLF 97
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGT--LCGDPRATS---GRIVFD-GKDITDWQ-TAKIMREAVAIVPEGRRVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 98 PHRTVLENIIEGPVIVKGEPKEEATARARELLAKvgLAGKETSYPRRLSGGQQQRVAIARALAMRPDVILFDEPTSALDP 177
Cdd:PRK11614 93 SRMTVEENLAMGGFFAERDQFQERIKWVYELFPR--LHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 495775764 178 ELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFAN 234
Cdd:PRK11614 171 IIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLAN 227
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
6-228 |
3.15e-29 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 110.16 E-value: 3.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 6 VKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSI--NLLEQPEGGtirvgEITIDtGKSISQ-------Q 76
Cdd:COG0396 3 IKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmgHPKYEVTSG-----SILLD-GEDILElspderaR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 77 KGLirrlrqhvGFVFQ---------NFNLFphRTVLENIIEGPVivkgePKEEATARARELLAKVGLAgkeTSYPRR--- 144
Cdd:COG0396 77 AGI--------FLAFQypveipgvsVSNFL--RTALNARRGEEL-----SAREFLKLLKEKMKELGLD---EDFLDRyvn 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 145 --LSGGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHemsFAR----DVADRAIFMD 218
Cdd:COG0396 139 egFSGGEKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITH---YQRildyIKPDFVHVLV 215
|
250
....*....|
gi 495775764 219 QGRIVEQGPA 228
Cdd:COG0396 216 DGRIVKSGGK 225
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
10-223 |
1.30e-28 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 112.80 E-value: 1.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 10 VKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVG--EITIdtgKSISQqkglirRLRQHV 87
Cdd:COG1129 259 VEGLSVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDgkPVRI---RSPRD------AIRAGI 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 88 GFVFQN---FNLFPHRTVLENII--------EGPVIvkgEPKEEAtARARELLAKVGLAGKETSYP-RRLSGGQQQRVAI 155
Cdd:COG1129 330 AYVPEDrkgEGLVLDLSIRENITlasldrlsRGGLL---DRRRER-ALAEEYIKRLRIKTPSPEQPvGNLSGGNQQKVVL 405
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495775764 156 ARALAMRPDVILFDEPTSALDpelVG---EVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIV 223
Cdd:COG1129 406 AKWLATDPKVLILDEPTRGID---VGakaEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRIV 473
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
2-202 |
3.43e-28 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 112.21 E-value: 3.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 2 SAIDVKNL-VKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLeQPEGGtirvGEITIDTGKSI---SQQK 77
Cdd:COG4178 361 GALALEDLtLRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGL-WPYGS----GRIARPAGARVlflPQRP 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 78 GLIR-RLRQHVgfvfqnfnLFPHrtvleniiegpvivkgEPKEEATARARELLAKVGLA------GKETSYPRRLSGGQQ 150
Cdd:COG4178 436 YLPLgTLREAL--------LYPA----------------TAEAFSDAELREALEAVGLGhlaerlDEEADWDQVLSLGEQ 491
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 495775764 151 QRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQlAQEKRTMVIVTH 202
Cdd:COG4178 492 QRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLRE-ELPGTTVISVGH 542
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
17-234 |
3.65e-28 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 112.06 E-value: 3.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 17 TVLHGIDLEVEQGEVVAIIGPSGSGKTTLLrsiNLLEQ-PEGGTIRVGEITIDtGKSISQQKglirrLRQHVGFVFQNFN 95
Cdd:TIGR00955 39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLM---NALAFrSPKGVKGSGSVLLN-GMPIDAKE-----MRAISAYVQQDDL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 96 LFPHRTVLENIIEGPVIVKGE--PKEEATARARELLAKVGL---AGKETSYPRR---LSGGQQQRVAIARALAMRPDVIL 167
Cdd:TIGR00955 110 FIPTLTVREHLMFQAHLRMPRrvTKKEKRERVDEVLQALGLrkcANTRIGVPGRvkgLSGGERKRLAFASELLTDPPLLF 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495775764 168 FDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMS---FarDVADRAIFMDQGRIVEQGP---AKSLFAN 234
Cdd:TIGR00955 190 CDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSselF--ELFDKIILMAEGRVAYLGSpdqAVPFFSD 260
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
16-228 |
4.00e-28 |
|
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: 111.67 E-value: 4.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 16 QTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRvgeitIDtGKSISQQKGliRRLRQHVGFVFQNFN 95
Cdd:TIGR01842 331 KPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVR-----LD-GADLKQWDR--ETFGKHIGYLPQDVE 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 96 LFPHrTVLENIIEGPVIVKGEPKEEAT--ARARELLAK--------VGLAGKEtsyprrLSGGQQQRVAIARALAMRPDV 165
Cdd:TIGR01842 403 LFPG-TVAENIARFGENADPEKIIEAAklAGVHELILRlpdgydtvIGPGGAT------LSGGQRQRIALARALYGDPKL 475
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495775764 166 ILFDEPTSALDPElvGE--VLNTIRQLAQEKRTMVIVTHEMSfARDVADRAIFMDQGRIVEQGPA 228
Cdd:TIGR01842 476 VVLDEPNSNLDEE--GEqaLANAIKALKARGITVVVITHRPS-LLGCVDKILVLQDGRIARFGER 537
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
4-226 |
4.94e-28 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 107.41 E-value: 4.94e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGeitidtGKSISQQKGliRRL 83
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLG------DKPISMLSS--RQL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 84 RQHVGFVFQnfnlfpHRTVLENIIEGPVIVKG------------EPKEEATARARELLAKVGLAGKETSyprRLSGGQQQ 151
Cdd:PRK11231 75 ARRLALLPQ------HHLTPEGITVRELVAYGrspwlslwgrlsAEDNARVNQAMEQTRINHLADRRLT---DLSGGQRQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495775764 152 RVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQG 226
Cdd:PRK11231 146 RAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQG 220
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
17-226 |
1.15e-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: 105.31 E-value: 1.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 17 TVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVgeitidTGKSISQqkglirrLRQHVGFVfqnfnl 96
Cdd:cd03220 36 WALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTV------RGRVSSL-------LGLGGGFN------ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 97 fPHRTVLENI-IEGpvIVKGEPKEEATARARELLAKVGLaGKETSYP-RRLSGGQQQRVAIARALAMRPDVILFDEPTSA 174
Cdd:cd03220 97 -PELTGRENIyLNG--RLLGLSRKEIDEKIDEIIEFSEL-GDFIDLPvKTYSSGMKARLAFAIATALEPDILLIDEVLAV 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 495775764 175 LDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQG 226
Cdd:cd03220 173 GDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
12-233 |
1.88e-27 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 106.24 E-value: 1.88e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 12 KFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIrvgeitIDTGKSISQQKGLIRRLRQHVGFVF 91
Cdd:PRK13638 10 RYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAV------LWQGKPLDYSKRGLLALRQQVATVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 92 QNfnlfPHRTVLENIIEGPVIVK----GEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPDVIL 167
Cdd:PRK13638 84 QD----PEQQIFYTDIDSDIAFSlrnlGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495775764 168 FDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFA 233
Cdd:PRK13638 160 LDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFA 225
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
18-222 |
2.11e-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: 104.86 E-value: 2.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 18 VLHGIDLEVEQGEVVAIIGPSGSGKTTLlrsINLLE---QPEGGTIRVgeitidTGKSISQQKGliRRLRQHVGFVFQNF 94
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTV---VALLEnfyQPQGGQVLL------DGKPISQYEH--KYLHSKVSLVGQEP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 95 NLFPhRTVLENIIEGpviVKGEPKEEATARARELLAKVGLAGKETSYPR-------RLSGGQQQRVAIARALAMRPDVIL 167
Cdd:cd03248 98 VLFA-RSLQDNIAYG---LQSCSFECVKEAAQKAHAHSFISELASGYDTevgekgsQLSGGQKQRVAIARALIRNPQVLI 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 495775764 168 FDEPTSALDPELVGEVLNTIRQlAQEKRTMVIVTHEMSFARDvADRAIFMDQGRI 222
Cdd:cd03248 174 LDEATSALDAESEQQVQQALYD-WPERRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-221 |
3.23e-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: 102.14 E-value: 3.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSInlleqpeggtirVGEITIDTGKSISQQKGLIRRL 83
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLI------------AGELEPDEGIVTWGSTVKIGYF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 84 RQhvgfvfqnfnlfphrtvleniiegpvivkgepkeeatararellakvglagketsyprrLSGGQQQRVAIARALAMRP 163
Cdd:cd03221 69 EQ-----------------------------------------------------------LSGGEKMRLALAKLLLENP 89
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 495775764 164 DVILFDEPTSALDPELVgEVLntIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGR 221
Cdd:cd03221 90 NLLLLDEPTNHLDLESI-EAL--EEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
4-227 |
3.28e-27 |
|
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: 104.11 E-value: 3.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 4 IDVKNLVKKF--HGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGEITIdtgKSISqqkglIR 81
Cdd:cd03244 3 IEFKNVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDI---SKIG-----LH 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 82 RLRQHVGFVFQNFNLFPHrTVLENIiegpvivkgEPKEEAT-ARARELLAKVGLAGKETSYPRRL-----------SGGQ 149
Cdd:cd03244 75 DLRSRISIIPQDPVLFSG-TIRSNL---------DPFGEYSdEELWQALERVGLKEFVESLPGGLdtvveeggenlSVGQ 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495775764 150 QQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQlAQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGP 227
Cdd:cd03244 145 RQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIRE-AFKDCTVLTIAHRLDTIID-SDRILVLDKGRVVEFDS 220
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
15-233 |
3.98e-27 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 109.44 E-value: 3.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 15 GQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGeitidtGKSISQQKglIRRLRQHVGFVFQNF 94
Cdd:TIGR01193 486 GSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLN------GFSLKDID--RHTLRQFINYLPQEP 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 95 NLFPHrTVLENIIEGpviVKGEPKEEATARARELLA--------KVGLAGKETSYPRRLSGGQQQRVAIARALAMRPDVI 166
Cdd:TIGR01193 558 YIFSG-SILENLLLG---AKENVSQDEIWAACEIAEikddienmPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVL 633
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495775764 167 LFDEPTSALDPELVGEVLNTIRQLaQEKrTMVIVTHEMSFARDVaDRAIFMDQGRIVEQGPAKSLFA 233
Cdd:TIGR01193 634 ILDESTSNLDTITEKKIVNNLLNL-QDK-TIIFVAHRLSVAKQS-DKIIVLDHGKIIEQGSHDELLD 697
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-226 |
5.76e-27 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 108.78 E-value: 5.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 4 IDVKNLVKKFHGQTVLHG-IDLEVEQGEVVAIIGPSGSGKTTLLrsiNLLEQ--PEGGTIRVGEITIdtgKSISQQKgli 80
Cdd:PRK11174 350 IEAEDLEILSPDGKTLAGpLNFTLPAGQRIALVGPSGAGKTSLL---NALLGflPYQGSLKINGIEL---RELDPES--- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 81 rrLRQHVGFVFQNFNLFpHRTVLENIIEGPVIVKGEPKEEATARAR--ELLAKV--GLAG--KETSypRRLSGGQQQRVA 154
Cdd:PRK11174 421 --WRKHLSWVGQNPQLP-HGTLRDNVLLGNPDASDEQLQQALENAWvsEFLPLLpqGLDTpiGDQA--AGLSVGQAQRLA 495
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495775764 155 IARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKrTMVIVTHEMSFARDVaDRAIFMDQGRIVEQG 226
Cdd:PRK11174 496 LARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQ-TTLMVTHQLEDLAQW-DQIWVMQDGQIVQQG 565
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-238 |
1.17e-26 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 105.19 E-value: 1.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 1 MSAIDVKNLVKKFHGQ----TVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGgtiRVGEITIDTGKSIS-- 74
Cdd:PRK09473 10 DALLDVKDLRVTFSTPdgdvTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANG---RIGGSATFNGREILnl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 75 QQKGLiRRLR-QHVGFVFQN--FNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGL--AGKE-TSYPRRLSGG 148
Cdd:PRK09473 87 PEKEL-NKLRaEQISMIFQDpmTSLNPYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMpeARKRmKMYPHEFSGG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 149 QQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVI-VTHEMSFARDVADRAIFMDQGRIVEQGP 227
Cdd:PRK09473 166 MRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIImITHDLGVVAGICDKVLVMYAGRTMEYGN 245
|
250
....*....|.
gi 495775764 228 AKSLFANPQQP 238
Cdd:PRK09473 246 ARDVFYQPSHP 256
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
6-229 |
4.53e-26 |
|
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: 100.68 E-value: 4.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 6 VKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEggtIRVGEITIDtGKSISQQKgLIRRLRQ 85
Cdd:cd03217 3 IKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYE---VTEGEILFK-GEDITDLP-PEERARL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 86 HVGFVFQNfnlfphrtvleniiegPVIVKGepkeeatARARELLAKVGLAgketsyprrLSGGQQQRVAIARALAMRPDV 165
Cdd:cd03217 78 GIFLAFQY----------------PPEIPG-------VKNADFLRYVNEG---------FSGGEKKRNEILQLLLLEPDL 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495775764 166 ILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTH-EMSFARDVADRAIFMDQGRIVEQGPAK 229
Cdd:cd03217 126 AILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHyQRLLDYIKPDRVHVLYDGRIVKSGDKE 190
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
16-224 |
6.26e-26 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 100.80 E-value: 6.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 16 QTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSI--NLLEQPEGGTIRVGEITIDTGKSIsqqkglirrlrqhvgfvfqn 93
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLagALKGTPVAGCVDVPDNQFGREASL-------------------- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 94 fnlfphrtvLENIiegpvivkgePKEEATARARELLAKVGLAgkeTSY-----PRRLSGGQQQRVAIARALAMRPDVILF 168
Cdd:COG2401 103 ---------IDAI----------GRKGDFKDAVELLNAVGLS---DAVlwlrrFKELSTGQKFRFRLALLLAERPKLLVI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 495775764 169 DEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVA-DRAIFMDQGRIVE 224
Cdd:COG2401 161 DEFCSHLDRQTAKRVARNLQKLARRAGiTLVVATHHYDVIDDLQpDLLIFVGYGGVPE 218
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-226 |
1.03e-25 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 104.87 E-value: 1.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGEITIDT-GKSISQQKGlirr 82
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKlDHKLAAQLG---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 83 lrqhVGFVFQNFNLFPHRTVLENIIEGPVIVK---GEPK---EEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIA 156
Cdd:PRK09700 82 ----IGIIYQELSVIDELTVLENLYIGRHLTKkvcGVNIidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 157 RALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQG 226
Cdd:PRK09700 158 KTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG 227
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
6-226 |
1.19e-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: 105.48 E-value: 1.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 6 VKNLVKKFH--GQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGEITIDTGksisqqkglIRRL 83
Cdd:TIGR01257 931 VKNLVKIFEpsGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETN---------LDAV 1001
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 84 RQHVGFVFQNFNLFPHRTVLENIIEGPVIvKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRP 163
Cdd:TIGR01257 1002 RQSLGMCPQHNILFHHLTVAEHILFYAQL-KGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDA 1080
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495775764 164 DVILFDEPTSALDPELVGEVLNTIRQLaQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQG 226
Cdd:TIGR01257 1081 KVVVLDEPTSGVDPYSRRSIWDLLLKY-RSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSG 1142
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
11-205 |
1.58e-25 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 104.58 E-value: 1.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 11 KKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSInlleqpeGGTIRVGEITidtGKSISQQKGLIRRLRQHVGFV 90
Cdd:PLN03211 76 RQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNAL-------AGRIQGNNFT---GTILANNRKPTKQILKRTGFV 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 91 FQNFNLFPHRTVLENIIEGPVI--VKGEPKEEATARARELLAKVGLAGKET-----SYPRRLSGGQQQRVAIARALAMRP 163
Cdd:PLN03211 146 TQDDILYPHLTVRETLVFCSLLrlPKSLTKQEKILVAESVISELGLTKCENtiignSFIRGISGGERKRVSIAHEMLINP 225
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 495775764 164 DVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMS 205
Cdd:PLN03211 226 SLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPS 267
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
7-231 |
2.51e-25 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 103.47 E-value: 2.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 7 KNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLeQPEGGTirVGEITID----TGKSI--SQQKGLI 80
Cdd:PRK13549 9 KNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPHGTY--EGEIIFEgeelQASNIrdTERAGIA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 81 rrlrqhvgFVFQNFNLFPHRTVLENIIEGPVIVKGE--PKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARA 158
Cdd:PRK13549 86 --------IIHQELALVKELSVLENIFLGNEITPGGimDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495775764 159 LAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSL 231
Cdd:PRK13549 158 LNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAGM 230
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
6-226 |
3.73e-25 |
|
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: 99.33 E-value: 3.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 6 VKNLVK-KFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGEITidtgkSISQQKGLIRRLr 84
Cdd:cd03267 23 LKSLFKrKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLV-----PWKRRKKFLRRI- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 85 qhvGFVFQnfnlfpHRTVLenIIEGPVI--------VKGEPKEEATARARELLAKVGLaGKETSYP-RRLSGGQQQRVAI 155
Cdd:cd03267 97 ---GVVFG------QKTQL--WWDLPVIdsfyllaaIYDLPPARFKKRLDELSELLDL-EELLDTPvRQLSLGQRMRAEI 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495775764 156 ARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVT-HEMSFARDVADRAIFMDQGRIVEQG 226
Cdd:cd03267 165 AAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTsHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
22-224 |
5.86e-25 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 102.95 E-value: 5.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 22 IDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGEITIDtgksisqqKGLIRRLRQHVGFVFQNFNLFPHrt 101
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVT--------ADNREAYRQLFSAVFSDFHLFDR-- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 102 vleniiegpviVKGEPKEEATARARELLAKVGLAGKeTSY------PRRLSGGQQQRVAIARALAMRPDVILFDEPTSAL 175
Cdd:COG4615 421 -----------LLGLDGEADPARARELLERLELDHK-VSVedgrfsTTDLSQGQRKRLALLVALLEDRPILVFDEWAADQ 488
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 495775764 176 DP--------ELVGEvlntirqLAQEKRTMVIVTHEMSFArDVADRAIFMDQGRIVE 224
Cdd:COG4615 489 DPefrrvfytELLPE-------LKARGKTVIAISHDDRYF-DLADRVLKMDYGKLVE 537
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
4-226 |
8.42e-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: 97.85 E-value: 8.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGtirvgEITIDtGKSISqqkgliRRL 83
Cdd:TIGR03740 1 LETKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSG-----EIIFD-GHPWT------RKD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 84 RQHVGFVFQNFNLFPHRTVLENIiEGPVIVKGEPKeeatARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRP 163
Cdd:TIGR03740 69 LHKIGSLIESPPLYENLTARENL-KVHTTLLGLPD----SRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHP 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495775764 164 DVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQG 226
Cdd:TIGR03740 144 KLLILDEPTNGLDPIGIQELRELIRSFPEQGITVILSSHILSEVQQLADHIGIISEGVLGYQG 206
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-227 |
1.16e-24 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 99.91 E-value: 1.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 1 MSAIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVgeitidTGKSISQQkglI 80
Cdd:PRK13536 39 TVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITV------LGVPVPAR---A 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 81 RRLRQHVGFVFQNFNLFPHRTVLENIIegpVIVK--GEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARA 158
Cdd:PRK13536 110 RLARARIGVVPQFDNLDLEFTVRENLL---VFGRyfGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARA 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 159 LAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGR-IVEQGP 227
Cdd:PRK13536 187 LINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRkIAEGRP 256
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
4-244 |
1.27e-24 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 98.71 E-value: 1.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 4 IDVKNLVKK-------FHGQTV--LHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGtirvgEITIDTGKsis 74
Cdd:PRK15112 5 LEVRNLSKTfryrtgwFRRQTVeaVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSG-----ELLIDDHP--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 75 QQKGLIRRLRQHVGFVFQN--FNLFPhRTVLENIIEGPVIVKGE-PKEEATARARELLAKVGLAGKETSY-PRRLSGGQQ 150
Cdd:PRK15112 77 LHFGDYSYRSQRIRMIFQDpsTSLNP-RQRISQILDFPLRLNTDlEPEQREKQIIETLRQVGLLPDHASYyPHMLAPGQK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 151 QRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLaQEKR--TMVIVTHEMSFARDVADRAIFMDQGRIVEQGPA 228
Cdd:PRK15112 156 QRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLEL-QEKQgiSYIYVTQHLGMMKHISDQVLVMHQGEVVERGST 234
|
250
....*....|....*.
gi 495775764 229 KSLFANPQQPRTRQFL 244
Cdd:PRK15112 235 ADVLASPLHELTKRLI 250
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
15-210 |
1.77e-24 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 97.09 E-value: 1.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 15 GQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIrvgeitIDTGKSISQQKGliRRLRQHVGFVFQNF 94
Cdd:PRK10247 19 DAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTL------LFEGEDISTLKP--EIYRQQVSYCAQTP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 95 NLFPHrTVLENIIEGPVIVKGEPKEEATARArelLAKVGLAgkETSYPRR---LSGGQQQRVAIARALAMRPDVILFDEP 171
Cdd:PRK10247 91 TLFGD-TVYDNLIFPWQIRNQQPDPAIFLDD---LERFALP--DTILTKNiaeLSGGEKQRISLIRNLQFMPKVLLLDEI 164
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 495775764 172 TSALDPELVGEVLNTIRQLAQEKRTMVI-VTH---EMSFARDV 210
Cdd:PRK10247 165 TSALDESNKHNVNEIIHRYVREQNIAVLwVTHdkdEINHADKV 207
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-234 |
9.17e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 97.08 E-value: 9.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 3 AIDVKNLVKKFH--------GQTV-------------LHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIR 61
Cdd:COG4586 1 IIEVENLSKTYRvyekepglKGALkglfrreyreveaVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 62 VGeitidtGKSISQQKgliRRLRQHVGFVF-QNFNLFPHRTVLE---------NIiegpvivkgePKEEATARARELLAK 131
Cdd:COG4586 81 VL------GYVPFKRR---KEFARRIGVVFgQRSQLWWDLPAIDsfrllkaiyRI----------PDAEYKKRLDELVEL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 132 VGLAGKETSYPRRLSGGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVT-HEMSFARDV 210
Cdd:COG4586 142 LDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTsHDMDDIEAL 221
|
250 260
....*....|....*....|....
gi 495775764 211 ADRAIFMDQGRIVEQGPAKSLFAN 234
Cdd:COG4586 222 CDRVIVIDHGRIIYDGSLEELKER 245
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
6-202 |
9.60e-24 |
|
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: 94.35 E-value: 9.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 6 VKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGeitidtGKSISQQKGLirrLRQ 85
Cdd:TIGR01189 3 ARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWN------GTPLAEQRDE---PHE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 86 HVGFVFQNFNLFPHRTVLENI-----IEGPvivkgepkeeATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALA 160
Cdd:TIGR01189 74 NILYLGHLPGLKPELSALENLhfwaaIHGG----------AQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWL 143
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 495775764 161 MRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTH 202
Cdd:TIGR01189 144 SRRPLWILDEPTTALDKAGVALLAGLLRAHLARGGIVLLTTH 185
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4-231 |
1.09e-23 |
|
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: 99.13 E-value: 1.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLeQPEGGTirVGEITIDtGKSIsQQKGLIRRL 83
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGV-YPHGTW--DGEIYWS-GSPL-KASNIRDTE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 84 RQHVGFVFQNFNLFPHRTVLENIIEGPVIVKGEPK---EEATARARELLAKVGLAGKETSYP-RRLSGGQQQRVAIARAL 159
Cdd:TIGR02633 77 RAGIVIIHQELTLVPELSVAENIFLGNEITLPGGRmayNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495775764 160 AMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSL 231
Cdd:TIGR02633 157 NKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTM 228
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
8-224 |
1.72e-23 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 98.44 E-value: 1.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 8 NLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGEITI---DTGKSISQQkglirrlr 84
Cdd:PRK11288 9 GIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrfaSTTAALAAG-------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 85 qhVGFVFQNFNLFPHRTVLENIIEGPVIVKGE--PKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMR 162
Cdd:PRK11288 81 --VAIIYQELHLVPEMTVAENLYLGQLPHKGGivNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495775764 163 PDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADR-AIFMDqGRIVE 224
Cdd:PRK11288 159 ARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAiTVFKD-GRYVA 220
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
4-231 |
2.62e-23 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 97.81 E-value: 2.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGeitidtGKSIS-------QQ 76
Cdd:PRK15439 12 LCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIG------GNPCArltpakaHQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 77 KGLIrrlrqhvgFVFQNFNLFPHRTVLENIIegpvivKGEPKEEAT-ARARELLAKVGLAGKETSYPRRLSGGQQQRVAI 155
Cdd:PRK15439 86 LGIY--------LVPQEPLLFPNLSVKENIL------FGLPKRQASmQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495775764 156 ARALaMRPDVIL-FDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSL 231
Cdd:PRK15439 152 LRGL-MRDSRILiLDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADL 227
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
19-233 |
3.63e-23 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 97.78 E-value: 3.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 19 LHGIDLEVEQGEVVAIIGPSGSGKTTLlrsINLLeqpeggT----IRVGEITIDtGKSISQQKglIRRLRQHVGFVFQNF 94
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTI---ANLL------TrfydIDEGEILLD-GHDLRDYT--LASLRNQVALVSQNV 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 95 NLFpHRTVLENIiegpvivkGEPKEEATARAR-ELLAKVGLA---------GKETSYPRR---LSGGQQQRVAIARALAM 161
Cdd:PRK11176 427 HLF-NDTIANNI--------AYARTEQYSREQiEEAARMAYAmdfinkmdnGLDTVIGENgvlLSGGQRQRIAIARALLR 497
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495775764 162 RPDVILFDEPTSALDPELVGEVLNTIRQLaQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKSLFA 233
Cdd:PRK11176 498 DSPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLSTIEK-ADEILVVEDGEIVERGTHAELLA 567
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
15-202 |
4.55e-23 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 93.01 E-value: 4.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 15 GQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGEITIDTGKSISQQkglirrlrQHVGfvFQNF 94
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEAC--------HYLG--HRNA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 95 nLFPHRTVLENIIEGPVIVKGEPKEEATArarelLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPDVILFDEPTSA 174
Cdd:PRK13539 84 -MKPALTVAENLEFWAAFLGGEELDIAAA-----LEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAA 157
|
170 180 190
....*....|....*....|....*....|
gi 495775764 175 LDPELVGEVLNTIR-QLAQEkrTMVIV-TH 202
Cdd:PRK13539 158 LDAAAVALFAELIRaHLAQG--GIVIAaTH 185
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
20-207 |
6.37e-23 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 92.56 E-value: 6.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 20 HGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGeitidtGKSISQQKGLIRRlrqhvgfvfqnfNLF-- 97
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQ------GEPIRRQRDEYHQ------------DLLyl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 98 -------PHRTVLENI-----IEGPVivkgepKEEATARArelLAKVGLAGKETSYPRRLSGGQQQRVAIAR-ALAMRPD 164
Cdd:PRK13538 80 ghqpgikTELTALENLrfyqrLHGPG------DDEALWEA---LAQVGLAGFEDVPVRQLSAGQQRRVALARlWLTRAPL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 495775764 165 VILfDEPTSALDPELVGEVLNTIRQLAqEKRTMVIVT--HEMSFA 207
Cdd:PRK13538 151 WIL-DEPFTAIDKQGVARLEALLAQHA-EQGGMVILTthQDLPVA 193
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
7-231 |
2.90e-22 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 92.36 E-value: 2.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 7 KNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVgeitidTGKSISQ--QKGLIRRlr 84
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWL------DGEHIQHyaSKEVARR-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 85 qhVGFVFQNFNLFPHRTVLENIIEG-----PVIVKGEPK-EEATARARELLAKVGLAGKETSyprRLSGGQQQRVAIARA 158
Cdd:PRK10253 83 --IGLLAQNATTPGDITVQELVARGryphqPLFTRWRKEdEEAVTKAMQATGITHLADQSVD---TLSGGQRQRAWIAMV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495775764 159 LAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEK-RTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSL 231
Cdd:PRK10253 158 LAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKgYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
16-234 |
2.94e-22 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 95.58 E-value: 2.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 16 QTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSInlleqpeggtirVGEITIDTGKSISqqkglirrLRQHVGFVFQNFN 95
Cdd:PLN03130 630 RPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAM------------LGELPPRSDASVV--------IRGTVAYVPQVSW 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 96 LFpHRTVLENIIEGPVI--VKGEPKEEATARARELLAKVGlaGKETSYPRR---LSGGQQQRVAIARALAMRPDVILFDE 170
Cdd:PLN03130 690 IF-NATVRDNILFGSPFdpERYERAIDVTALQHDLDLLPG--GDLTEIGERgvnISGGQKQRVSMARAVYSNSDVYIFDD 766
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495775764 171 PTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVaDRAIFMDQGRIVEQGPAKSLFAN 234
Cdd:PLN03130 767 PLSALDAHVGRQVFDKCIKDELRGKTRVLVTNQLHFLSQV-DRIILVHEGMIKEEGTYEELSNN 829
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
6-229 |
4.15e-22 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 94.32 E-value: 4.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 6 VKNL-VKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGEITIdTGKSISQqkglIRRL- 83
Cdd:COG3845 260 VENLsVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDI-TGLSPRE----RRRLg 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 84 -------RQHVGfvfqnfnLFPHRTVLENII----------EGPVIVKGepkeEATARARELLAKVGLAGKETSYP-RRL 145
Cdd:COG3845 335 vayipedRLGRG-------LVPDMSVAENLIlgryrrppfsRGGFLDRK----AIRAFAEELIEEFDVRTPGPDTPaRSL 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 146 SGGQQQRVAIARALAMRPDVILFDEPTSALDpelVG---EVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRI 222
Cdd:COG3845 404 SGGNQQKVILARELSRDPKLLIAAQPTRGLD---VGaieFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRI 480
|
....*..
gi 495775764 223 VEQGPAK 229
Cdd:COG3845 481 VGEVPAA 487
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
4-226 |
9.02e-22 |
|
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: 89.39 E-value: 9.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 4 IDVKNLVKKF--HGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIrvgeiTIDtGKSISQQKglIR 81
Cdd:cd03369 7 IEVENLSVRYapDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKI-----EID-GIDISTIP--LE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 82 RLRQHVGFVFQNFNLFPHrTVLENIiegpvivkgEPKEEATARarELLAkvglAGKETSYPRRLSGGQQQRVAIARALAM 161
Cdd:cd03369 79 DLRSSLTIIPQDPTLFSG-TIRSNL---------DPFDEYSDE--EIYG----ALRVSEGGLNLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495775764 162 RPDVILFDEPTSALDPELVGEVLNTIRQLAQeKRTMVIVTHEMSFARDVaDRAIFMDQGRIVEQG 226
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREEFT-NSTILTIAHRLRTIIDY-DKILVMDAGEVKEYD 205
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
4-202 |
3.29e-21 |
|
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: 87.93 E-value: 3.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVgeitidTGKSISQQKGLIRRL 83
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLL------NGGPLDFQRDSIARG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 84 RQHVGfvFQNfNLFPHRTVLENIiegpvivKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRP 163
Cdd:cd03231 75 LLYLG--HAP-GIKTTLSVLENL-------RFWHADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGR 144
|
170 180 190
....*....|....*....|....*....|....*....
gi 495775764 164 DVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTH 202
Cdd:cd03231 145 PLWILDEPTTALDKAGVARFAEAMAGHCARGGMVVLTTH 183
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
15-202 |
5.41e-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: 5.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 15 GQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIrvgeitidtgksisqqkglIRRLRQHVGFVfqnf 94
Cdd:cd03223 13 GRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI-------------------GMPEGEDLLFL---- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 95 nlfPHRTVLeniiegpvivkgepkeeATARARELLAkvglagketsYP--RRLSGGQQQRVAIARALAMRPDVILFDEPT 172
Cdd:cd03223 70 ---PQRPYL-----------------PLGTLREQLI----------YPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEAT 119
|
170 180 190
....*....|....*....|....*....|.
gi 495775764 173 SALDPelvgEVLNTIRQLAQEKRTMVI-VTH 202
Cdd:cd03223 120 SALDE----ESEDRLYQLLKELGITVIsVGH 146
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-225 |
1.06e-20 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 90.45 E-value: 1.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 1 MSAI-DVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIR-VGEITIDTGKSISQQKG 78
Cdd:PRK10762 1 MQALlQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILyLGKEVTFNGPKSSQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 79 lirrlrqhVGFVFQNFNLFPHRTVLENIIEGPVIVKGEPK---EEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAI 155
Cdd:PRK10762 81 --------IGIIHQELNLIPQLTIAENIFLGREFVNRFGRidwKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495775764 156 ARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADR-AIFMDQGRIVEQ 225
Cdd:PRK10762 153 AKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDvTVFRDGQFIAER 223
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
11-226 |
1.27e-20 |
|
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: 86.16 E-value: 1.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 11 KKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLL----EQPEGgTIRVGEITIDTGKSisqqkglirRLRQH 86
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRtegnVSVEG-DIHYNGIPYKEFAE---------KYPGE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 87 VGFVFQNFNLFPHRTVLENIiegpvivkgepkeEATARARellakvglaGKEtsYPRRLSGGQQQRVAIARALAMRPDVI 166
Cdd:cd03233 85 IIYVSEEDVHFPTLTVRETL-------------DFALRCK---------GNE--FVRGISGGERKRVSIAEALVSRASVL 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495775764 167 LFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTheMSFARDVA----DRAIFMDQGRIVEQG 226
Cdd:cd03233 141 CWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVS--LYQASDEIydlfDKVLVLYEGRQIYYG 202
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
1-245 |
1.66e-20 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 88.42 E-value: 1.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 1 MSAIDVKNLVKKF---HGQT-VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSInLLEQPEGGTIRVGEIT---IDTGK-S 72
Cdd:COG4170 1 MPLLDIRNLTIEIdtpQGRVkAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAI-CGITKDNWHVTADRFRwngIDLLKlS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 73 ISQQKGLIRRlrqHVGFVFQNFN--LFPHRTVLENIIEgpVI----VKG---EPKEEATARARELLAKVGLAGKE---TS 140
Cdd:COG4170 80 PRERRKIIGR---EIAMIFQEPSscLDPSAKIGDQLIE--AIpswtFKGkwwQRFKWRKKRAIELLHRVGIKDHKdimNS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 141 YPRRLSGGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQ-EKRTMVIVTHEMSFARDVADRAIFMDQ 219
Cdd:COG4170 155 YPHELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQlQGTSILLISHDLESISQWADTITVLYC 234
|
250 260
....*....|....*....|....*.
gi 495775764 220 GRIVEQGPAKSLFANPQQPRTRQFLE 245
Cdd:COG4170 235 GQTVESGPTEQILKSPHHPYTKALLR 260
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
19-233 |
3.39e-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: 89.62 E-value: 3.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 19 LHGIDLEVEQGEVVAIIGPSGSGKTTLLRSI-NLLEQPEGgtirvgEITIDTGKSISQQKGLIrrlrqhvgfvfQNfnlf 97
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALlAEMDKVEG------HVHMKGSVAYVPQQAWI-----------QN---- 712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 98 phRTVLENIIEGPVIvkGEPKEEATARARELLAKVGL--AGKETSYPRR---LSGGQQQRVAIARALAMRPDVILFDEPT 172
Cdd:TIGR00957 713 --DSLRENILFGKAL--NEKYYQQVLEACALLPDLEIlpSGDRTEIGEKgvnLSGGQKQRVSLARAVYSNADIYLFDDPL 788
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495775764 173 SALDPELVGEVL-NTIRQLAQEK-RTMVIVTHEMSFARDVaDRAIFMDQGRIVEQGPAKSLFA 233
Cdd:TIGR00957 789 SAVDAHVGKHIFeHVIGPEGVLKnKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLQ 850
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
15-231 |
4.16e-20 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 86.38 E-value: 4.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 15 GQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGEITIDTGKSisqqKGLIRRlrqhVGFVFQNF 94
Cdd:PRK10575 23 GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSS----KAFARK----VAYLPQQL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 95 NLFPHRTVLENIIEGPVI---VKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPDVILFDEP 171
Cdd:PRK10575 95 PAAEGMTVRELVAIGRYPwhgALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEP 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495775764 172 TSALDPELVGEVLNTIRQLAQEKRTMVI-VTHEMSFARDVADRAIFMDQGRIVEQGPAKSL 231
Cdd:PRK10575 175 TSALDIAHQVDVLALVHRLSQERGLTVIaVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
3-235 |
4.78e-20 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 88.62 E-value: 4.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 3 AIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGEITIDTGKsisqqkglIRR 82
Cdd:PRK10789 315 DVNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQ--------LDS 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 83 LRQHVGFVFQNFNLFPHrTVLENIIEGPVIVKGEPKEEAtarARelLAKVG------LAGKETSYPRR---LSGGQQQRV 153
Cdd:PRK10789 387 WRSRLAVVSQTPFLFSD-TVANNIALGRPDATQQEIEHV---AR--LASVHddilrlPQGYDTEVGERgvmLSGGQKQRI 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 154 AIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQeKRTMVIVTHEMSfARDVADRAIFMDQGRIVEQGPAKSLFA 233
Cdd:PRK10789 461 SIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGE-GRTVIISAHRLS-ALTEASEILVMQHGHIAQRGNHDQLAQ 538
|
..
gi 495775764 234 NP 235
Cdd:PRK10789 539 QS 540
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
2-231 |
6.95e-20 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 87.10 E-value: 6.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 2 SAIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTllrsinlleqpegGTIRVGEITIDTGKS-------IS 74
Cdd:NF000106 12 NAVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**R-------------GALPAHV*GPDAGRRpwrf*twCA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 75 QQKGLIRRLRQHVGFVFQNFNLFPHRTVLENIIEGPVIvkgePKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVA 154
Cdd:NF000106 79 NRRALRRTIG*HRPVR*GRRESFSGRENLYMIGR*LDL----SRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLD 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495775764 155 IARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSL 231
Cdd:NF000106 155 LAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
19-229 |
7.13e-20 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 85.28 E-value: 7.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 19 LHGIDLEVEQGEVVAIIGPSGSGKTTLLRSI-NLLEQPeggtirvGEITIDtGKSISQQKG--LIRR---LRQHV--GF- 89
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMaGLLPGQ-------GEILLN-GRPLSDWSAaeLARHrayLSQQQspPFa 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 90 --VFQNFNLFPHRtvleniiegpvivkGEPKEEATARARELLAKVGLAGKetsYPR---RLSGGQQQRVAIARAL----- 159
Cdd:COG4138 84 mpVFQYLALHQPA--------------GASSEAVEQLLAQLAEALGLEDK---LSRpltQLSGGEWQRVRLAAVLlqvwp 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495775764 160 AMRPD--VILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAK 229
Cdd:COG4138 147 TINPEgqLLLLDEPMNSLDVAQQAALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETA 218
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
14-232 |
1.62e-19 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 84.93 E-value: 1.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 14 HGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINlleqpegGTIRV--GEITIdTGKSISQQkglirrLRQH-VGFV 90
Cdd:PRK15056 18 NGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALM-------GFVRLasGKISI-LGQPTRQA------LQKNlVAYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 91 FQNFNL---FPhrTVLENIIE----GPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRP 163
Cdd:PRK15056 84 PQSEEVdwsFP--VLVEDVVMmgryGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQG 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495775764 164 DVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIfMDQGRIVEQGPAKSLF 232
Cdd:PRK15056 162 QVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTV-MVKGTVLASGPTETTF 229
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
3-234 |
2.03e-19 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 87.34 E-value: 2.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 3 AIDVKNLVKKFHGQT---VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSInlleqpeggtirVGEITIDTGKSISqqkgl 79
Cdd:PLN03232 614 AISIKNGYFSWDSKTskpTLSDINLEIPVGSLVAIVGGTGEGKTSLISAM------------LGELSHAETSSVV----- 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 80 irrLRQHVGFVFQNFNLFpHRTVLENIIEGPvivKGEPKE-----EATARAREL-------LAKVGLAGKEtsyprrLSG 147
Cdd:PLN03232 677 ---IRGSVAYVPQVSWIF-NATVRENILFGS---DFESERywraiDVTALQHDLdllpgrdLTEIGERGVN------ISG 743
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 148 GQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVaDRAIFMDQGRIVEQGP 227
Cdd:PLN03232 744 GQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLM-DRIILVSEGMIKEEGT 822
|
....*..
gi 495775764 228 AKSLFAN 234
Cdd:PLN03232 823 FAELSKS 829
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-190 |
2.35e-19 |
|
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: 86.53 E-value: 2.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGEiTIdtgksisqqkglirrl 83
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGE-TV---------------- 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 84 rqHVGFVFQNF-NLFPHRTVLENIIEG-PVIVKGepKEEATARAreLLAKVGLAGKETSYP-RRLSGGQQQRVAIARALA 160
Cdd:TIGR03719 386 --KLAYVDQSRdALDPNKTVWEEISGGlDIIKLG--KREIPSRA--YVGRFNFKGSDQQKKvGQLSGGERNRVHLAKTLK 459
|
170 180 190
....*....|....*....|....*....|
gi 495775764 161 MRPDVILFDEPTSALDpelvgevLNTIRQL 190
Cdd:TIGR03719 460 SGGNVLLLDEPTNDLD-------VETLRAL 482
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
7-224 |
3.01e-19 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 86.38 E-value: 3.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 7 KNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLrsiNLLeqpEG----GTIRvGEITIDTG----KSI--SQQ 76
Cdd:NF040905 5 RGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLM---KVL---SGvyphGSYE-GEILFDGEvcrfKDIrdSEA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 77 KGLIrrlrqhvgFVFQNFNLFPHRTVLENIIEGpvivkGEPK-------EEATARARELLAKVGLAGKETSYPRRLSGGQ 149
Cdd:NF040905 78 LGIV--------IIHQELALIPYLSIAENIFLG-----NERAkrgvidwNETNRRARELLAKVGLDESPDTLVTDIGVGK 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495775764 150 QQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVE 224
Cdd:NF040905 145 QQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGRTIE 219
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
19-220 |
4.11e-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: 81.91 E-value: 4.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 19 LHGIDLEVEQGEVVAIIGPSGSGKTTLLRSinLLEQPEGGTIRvGEITIDTgksisqqKGLIRRLRQHVGFVFQNFNLFP 98
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDV--LAGRKTAGVIT-GEILING-------RPLDKNFQRSTGYVEQQDVHSP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 99 HRTVLENIiegpvivkgepkeeatararELLAKVglagketsypRRLSGGQQQRVAIARALAMRPDVILFDEPTSALDPE 178
Cdd:cd03232 93 NLTVREAL--------------------RFSALL----------RGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQ 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 495775764 179 LVGEVLNTIRQLAQEKRTMVIVTHEMS---FARdvADRAIFMDQG 220
Cdd:cd03232 143 AAYNIVRFLKKLADSGQAILCTIHQPSasiFEK--FDRLLLLKRG 185
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
5-224 |
1.22e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 84.45 E-value: 1.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 5 DVKNLVKKFHGQtvLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVG--EITIDTG-KSISQQKGLIR 81
Cdd:PRK09700 267 EVRNVTSRDRKK--VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNgkDISPRSPlDAVKKGMAYIT 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 82 RLRQHVGFvFQNFNLFPHRTVLENI----IEGPVIVKGEPKEEATARARELLAKVGLAGKETSYpRRLSGGQQQRVAIAR 157
Cdd:PRK09700 345 ESRRDNGF-FPNFSIAQNMAISRSLkdggYKGAMGLFHEVDEQRTAENQRELLALKCHSVNQNI-TELSGGNQQKVLISK 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495775764 158 ALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVE 224
Cdd:PRK09700 423 WLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQ 489
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
15-227 |
3.00e-18 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 81.41 E-value: 3.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 15 GQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSI--NLLE--QPEGGTIRvGEITIDtGKSISQQKGL-IRRLR----- 84
Cdd:PRK13547 13 HRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALagDLTGggAPRGARVT-GDVTLN-GEPLAAIDAPrLARLRavlpq 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 85 -QHVGFVFQNFNL-----FPH--RTVLENIIEGPVIvkgepkeeatARARELLAKVGLAGKETSyprRLSGGQQQRVAIA 156
Cdd:PRK13547 91 aAQPAFAFSAREIvllgrYPHarRAGALTHRDGEIA----------WQALALAGATALVGRDVT---TLSGGELARVQFA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 157 RALAM---------RPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVI-VTHEMSFARDVADRAIFMDQGRIVEQG 226
Cdd:PRK13547 158 RVLAQlwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLaIVHDPNLAARHADRIAMLADGAIVAHG 237
|
.
gi 495775764 227 P 227
Cdd:PRK13547 238 A 238
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
4-178 |
3.60e-18 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 83.24 E-value: 3.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGEiTIdtgksisqqkglirrl 83
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGE-TV---------------- 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 84 rqHVGFVFQNF-NLFPHRTVLENIIEGPVIVK-GepKEEATARAreLLAKVGLAGKETSYP-RRLSGGQQQRVAIARALA 160
Cdd:PRK11819 388 --KLAYVDQSRdALDPNKTVWEEISGGLDIIKvG--NREIPSRA--YVGRFNFKGGDQQKKvGVLSGGERNRLHLAKTLK 461
|
170
....*....|....*...
gi 495775764 161 MRPDVILFDEPTSALDPE 178
Cdd:PRK11819 462 QGGNVLLLDEPTNDLDVE 479
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
5-223 |
4.16e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 83.04 E-value: 4.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 5 DVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGEITID---TGKSISQQKGLIR 81
Cdd:PRK11288 255 EVRLRLDGLKGPGLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDirsPRDAIRAGIMLCP 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 82 RLRQHVGFVfqnfnlfPHRTVLENI--------IEGPVIVKGePKEEATARARELLAKVGLAGKETSYpRRLSGGQQQRV 153
Cdd:PRK11288 335 EDRKAEGII-------PVHSVADNInisarrhhLRAGCLINN-RWEAENADRFIRSLNIKTPSREQLI-MNLSGGNQQKA 405
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495775764 154 AIARALAMRPDVILFDEPTSALDpelVG---EVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIV 223
Cdd:PRK11288 406 ILGRWLSEDMKVILLDEPTRGID---VGakhEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRIA 475
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
22-224 |
1.61e-17 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 81.17 E-value: 1.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 22 IDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGEITIDTGKsisqqkglIRRLRQHVGFVFQNFNLFPHrt 101
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQ--------PEDYRKLFSAVFTDFHLFDQ-- 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 102 vleniIEGPvivKGEPKEEATARA----RELLAKVGLAGKETSYPrRLSGGQQQRVAIARALAMRPDVILFDEPTSALDP 177
Cdd:PRK10522 412 -----LLGP---EGKPANPALVEKwlerLKMAHKLELEDGRISNL-KLSKGQKKRLALLLALAEERDILLLDEWAADQDP 482
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 495775764 178 ----ELVGEVLNTIRQLAQekrTMVIVTHEMSFArDVADRAIFMDQGRIVE 224
Cdd:PRK10522 483 hfrrEFYQVLLPLLQEMGK---TIFAISHDDHYF-IHADRLLEMRNGQLSE 529
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
15-220 |
7.24e-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: 76.60 E-value: 7.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 15 GQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSInlleqpeggtirVGEITIDTGK--------SISQQKGLIRRLRQH 86
Cdd:cd03290 13 GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAI------------LGEMQTLEGKvhwsnkneSEPSFEATRSRNRYS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 87 VGFVFQNFNLFpHRTVLENIIEGPVIVKGEPKeeATARARELLAKVGLA--GKETSYPRR---LSGGQQQRVAIARALAM 161
Cdd:cd03290 81 VAYAAQKPWLL-NATVEENITFGSPFNKQRYK--AVTDACSLQPDIDLLpfGDQTEIGERginLSGGQRQRICVARALYQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495775764 162 RPDVILFDEPTSALDPELVGEVLNT--IRQLAQEKRTMVIVTHEMSFARDvADRAIFMDQG 220
Cdd:cd03290 158 NTNIVFLDDPFSALDIHLSDHLMQEgiLKFLQDDKRTLVLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
3-223 |
8.06e-17 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 79.17 E-value: 8.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 3 AIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSInlleqpeggtirVGEITIDTGKSISQQKGLIRR 82
Cdd:PRK15064 319 ALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTL------------VGELEPDSGTVKWSENANIGY 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 83 LRQHVGFVFQNfnlfpHRTVLENIIEgpviVKGEPKEEATARAreLLAKVGLAGKETSYP-RRLSGGQQQRVAIARALAM 161
Cdd:PRK15064 387 YAQDHAYDFEN-----DLTLFDWMSQ----WRQEGDDEQAVRG--TLGRLLFSQDDIKKSvKVLSGGEKGRMLFGKLMMQ 455
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495775764 162 RPDVILFDEPTSALDPELVgEVLNTirQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIV 223
Cdd:PRK15064 456 KPNVLVMDEPTNHMDMESI-ESLNM--ALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVV 514
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
3-233 |
9.05e-17 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 78.99 E-value: 9.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 3 AIDVKNLVKKF-HGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLlrsINLLEqpegG--TIRVGEITIDtGKSISQQKGl 79
Cdd:PRK10790 340 RIDIDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTL---ASLLM----GyyPLTEGEIRLD-GRPLSSLSH- 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 80 iRRLRQHVGFVFQNFNLFPHrTVLENIIEGPVIvkgepKEEATARArelLAKVGLAGKETSYP-----------RRLSGG 148
Cdd:PRK10790 411 -SVLRQGVAMVQQDPVVLAD-TFLANVTLGRDI-----SEEQVWQA---LETVQLAELARSLPdglytplgeqgNNLSVG 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 149 QQQRVAIARALAMRPDVILFDEPTSALDP---ELVGEVLNTIRqlaqEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQ 225
Cdd:PRK10790 481 QKQLLALARVLVQTPQILILDEATANIDSgteQAIQQALAAVR----EHTTLVVIAHRLSTIVE-ADTILVLHRGQAVEQ 555
|
....*...
gi 495775764 226 GPAKSLFA 233
Cdd:PRK10790 556 GTHQQLLA 563
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
18-205 |
1.27e-16 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 76.64 E-value: 1.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 18 VLHGIDLeVEQGEVVAIIGPSGSGKTTLLRsinlleqpeggtIRVGEITIDTGKSISQQ--KGLIRRLRqhvGFVFQNFn 95
Cdd:cd03236 16 KLHRLPV-PREGQVLGLVGPNGIGKSTALK------------ILAGKLKPNLGKFDDPPdwDEILDEFR---GSELQNY- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 96 lfphrtvLENIIEGPV--IVKGE-----PKEeATARARELLAKVGLAGKETSYPRR-------------LSGGQQQRVAI 155
Cdd:cd03236 79 -------FTKLLEGDVkvIVKPQyvdliPKA-VKGKVGELLKKKDERGKLDELVDQlelrhvldrnidqLSGGELQRVAI 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 495775764 156 ARALAMRPDVILFDEPTSALDpelVGEVLN---TIRQLAQEKRTMVIVTHEMS 205
Cdd:cd03236 151 AAALARDADFYFFDEPSSYLD---IKQRLNaarLIRELAEDDNYVLVVEHDLA 200
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
8-244 |
1.96e-16 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 78.23 E-value: 1.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 8 NLVKKFHGQT---VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINllEQPEGGTIRV-GEITIDtgkSISQQKgLIRRL 83
Cdd:TIGR00956 63 RKLKKFRDTKtfdILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIA--SNTDGFHIGVeGVITYD---GITPEE-IKKHY 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 84 RQHVGFVFQNFNLFPHRTVLENI-----IEGPVI-VKGEPKEEATARAREL-LAKVGLA-GKET----SYPRRLSGGQQQ 151
Cdd:TIGR00956 137 RGDVVYNAETDVHFPHLTVGETLdfaarCKTPQNrPDGVSREEYAKHIADVyMATYGLShTRNTkvgnDFVRGVSGGERK 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 152 RVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVT-HEMS-FARDVADRAIFMDQGRIVEQGP-- 227
Cdd:TIGR00956 217 RVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVAiYQCSqDAYELFDKVIVLYEGYQIYFGPad 296
|
250 260
....*....|....*....|...
gi 495775764 228 -AKSLFAN-----PQQPRTRQFL 244
Cdd:TIGR00956 297 kAKQYFEKmgfkcPDRQTTADFL 319
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-223 |
2.63e-16 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 77.68 E-value: 2.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 1 MSAIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINlleqpeggtirvGEITIDTGKSISQQKGLI 80
Cdd:PRK11147 1 MSLISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILN------------GEVLLDDGRIIYEQDLIV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 81 RRLRQHvgfvfqnfnlfPHR----TVLENIIEG--------------PVIVKGEPKEEA-------------------TA 123
Cdd:PRK11147 69 ARLQQD-----------PPRnvegTVYDFVAEGieeqaeylkryhdiSHLVETDPSEKNlnelaklqeqldhhnlwqlEN 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 124 RARELLAKVGL-AGKETSyprRLSGGQQQRVAIARALAMRPDVILFDEPTSALDPElvgevlnTIRQLAQ----EKRTMV 198
Cdd:PRK11147 138 RINEVLAQLGLdPDAALS---SLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIE-------TIEWLEGflktFQGSII 207
|
250 260
....*....|....*....|....*
gi 495775764 199 IVTHEMSFARDVADRAIFMDQGRIV 223
Cdd:PRK11147 208 FISHDRSFIRNMATRIVDLDRGKLV 232
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
18-236 |
3.69e-16 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 77.51 E-value: 3.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 18 VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVgeitidTGKSISQQkGLiRRLRQHvgfvfqnFNLF 97
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRV------NGREIGAY-GL-RELRRQ-------FSMI 1389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 98 PHRTVLeniIEGPVIVKGEPKEEATA----RARELlakVGLAGKETSY-----PRRLSG------GQQQRVAIARALAMR 162
Cdd:PTZ00243 1390 PQDPVL---FDGTVRQNVDPFLEASSaevwAALEL---VGLRERVASEsegidSRVLEGgsnysvGQRQLMCMARALLKK 1463
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495775764 163 -PDVILFDEPTSALDPELVGEVLNTIRQlAQEKRTMVIVTHEMsfaRDVA--DRAIFMDQGRIVEQGPAKSLFANPQ 236
Cdd:PTZ00243 1464 gSGFILMDEATANIDPALDRQIQATVMS-AFSAYTVITIAHRL---HTVAqyDKIIVMDHGAVAEMGSPRELVMNRQ 1536
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
15-221 |
7.14e-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: 7.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 15 GQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVgeitidtgksisqQKGLirrlrqHVGFVFQNF 94
Cdd:TIGR03719 17 KKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARP-------------QPGI------KVGYLPQEP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 95 NLFPHRTVLENIIEGPVIVK-------------GEPKEEATARARE---------------LLAKVGLAGKETSYP---- 142
Cdd:TIGR03719 78 QLDPTKTVRENVEEGVAEIKdaldrfneisakyAEPDADFDKLAAEqaelqeiidaadawdLDSQLEIAMDALRCPpwda 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 143 --RRLSGGQQQRVAIARALAMRPDVILFDEPTSALDPELVG--EvlntiRQLAQEKRTMVIVTHEMSFARDVADRAIFMD 218
Cdd:TIGR03719 158 dvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAwlE-----RHLQEYPGTVVAVTHDRYFLDNVAGWILELD 232
|
...
gi 495775764 219 QGR 221
Cdd:TIGR03719 233 RGR 235
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
24-248 |
1.00e-15 |
|
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: 73.98 E-value: 1.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 24 LEVEQG-----EVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGEITID--TGKSISQQKGLIRRLRQHVGFVFQNFNL 96
Cdd:cd03237 15 LEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSykPQYIKADYEGTVRDLLSSITKDFYTHPY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 97 FPHRTV----LENIIEgpvivkgepkeeataraRELlakvglagketsypRRLSGGQQQRVAIARALAMRPDVILFDEPT 172
Cdd:cd03237 95 FKTEIAkplqIEQILD-----------------REV--------------PELSGGELQRVAIAACLSKDADIYLLDEPS 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495775764 173 SALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIfmdqgrIVEQGPAKSLFANPQQPRtRQFLEKFL 248
Cdd:cd03237 144 AYLDVEQRLMASKVIRRFAENnEKTAFVVEHDIIMIDYLADRLI------VFEGEPSVNGVANPPQSL-RSGMNRFL 213
|
|
| 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 495775764 3 AIDVKNLVKKFHGQ--TVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGgtirvGEITIDtGKSISQQkGLi 80
Cdd:PLN03130 1237 SIKFEDVVLRYRPElpPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELER-----GRILID-GCDISKF-GL- 1308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 81 RRLRQHVGFVFQN---------FNLFP---HRTV-LENIIEgpvivKGEPKEEATARARELLAKVGLAGKEtsyprrLSG 147
Cdd:PLN03130 1309 MDLRKVLGIIPQApvlfsgtvrFNLDPfneHNDAdLWESLE-----RAHLKDVIRRNSLGLDAEVSEAGEN------FSV 1377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 148 GQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRqlaQEKR--TMVIVTHEMSFARDvADRAIFMDQGRIVEQ 225
Cdd:PLN03130 1378 GQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIR---EEFKscTMLIIAHRLNTIID-CDRILVLDAGRVVEF 1453
|
....*....
gi 495775764 226 GPAKSLFAN 234
Cdd:PLN03130 1454 DTPENLLSN 1462
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
26-204 |
1.27e-15 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 75.62 E-value: 1.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 26 VEQGEVVAIIGPSGSGKTTLLRsinlleqpeggtIRVGEITIDTGKSISQ--QKGLIRRLRqhvGFVFQNFnlfphrtvL 103
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVK------------ILSGELIPNLGDYEEEpsWDEVLKRFR---GTELQNY--------F 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 104 ENIIEG--------------PVIVKGepkeeataRARELLAKVGLAGKETSYPRR-------------LSGGQQQRVAIA 156
Cdd:PRK13409 153 KKLYNGeikvvhkpqyvdliPKVFKG--------KVRELLKKVDERGKLDEVVERlglenildrdiseLSGGELQRVAIA 224
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 495775764 157 RALAMRPDVILFDEPTSALDpelVGEVLN---TIRQLAqEKRTMVIVTHEM 204
Cdd:PRK13409 225 AALLRDADFYFFDEPTSYLD---IRQRLNvarLIRELA-EGKYVLVVEHDL 271
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
27-204 |
2.37e-15 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 74.82 E-value: 2.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 27 EQGEVVAIIGPSGSGKTTllrSINLLEqpeggtirvGEITIDTGKSISQ--QKGLIRRlrqhvgfvFQNFNLFPHrtvLE 104
Cdd:COG1245 97 KKGKVTGILGPNGIGKST---ALKILS---------GELKPNLGDYDEEpsWDEVLKR--------FRGTELQDY---FK 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 105 NIIEG--------------PVIVKGEPKE--EAT---ARARELLAKVGLagkETSYPRR---LSGGQQQRVAIARALAMR 162
Cdd:COG1245 154 KLANGeikvahkpqyvdliPKVFKGTVREllEKVderGKLDELAEKLGL---ENILDRDiseLSGGELQRVAIAAALLRD 230
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 495775764 163 PDVILFDEPTSALDpelVGEVLN---TIRQLAQEKRTMVIVTHEM 204
Cdd:COG1245 231 ADFYFFDEPSSYLD---IYQRLNvarLIRELAEEGKYVLVVEHDL 272
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-241 |
4.37e-15 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 73.30 E-value: 4.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 1 MSAIDVKNLVKKFHGQ----TVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINlleqpeGGTIRVGEIT--------ID 68
Cdd:PRK15093 1 MPLLDIRNLTIEFKTSdgwvKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAIC------GVTKDNWRVTadrmrfddID 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 69 TGKSISQQKgliRRLRQH-VGFVFQNFN--LFPHRTVLENIIEG--PVIVKGEPKEEATARAR---ELLAKVGLAGKE-- 138
Cdd:PRK15093 75 LLRLSPRER---RKLVGHnVSMIFQEPQscLDPSERVGRQLMQNipGWTYKGRWWQRFGWRKRraiELLHRVGIKDHKda 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 139 -TSYPRRLSGGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADRAIF 216
Cdd:PRK15093 152 mRSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNtTILLISHDLQMLSQWADKINV 231
|
250 260
....*....|....*....|....*
gi 495775764 217 MDQGRIVEQGPAKSLFANPQQPRTR 241
Cdd:PRK15093 232 LYCGQTVETAPSKELVTTPHHPYTQ 256
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
10-222 |
5.39e-15 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 73.88 E-value: 5.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 10 VKKFHGQTVlHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGEITIDTgksISQQKGL------IRRL 83
Cdd:PRK10762 260 VDNLSGPGV-NDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVT---RSPQDGLangivyISED 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 84 RQHVGFVF-----QNFNLfphrTVLENIIEGPVIVKGEPKEEATARARELL--------AKVGLagketsyprrLSGGQQ 150
Cdd:PRK10762 336 RKRDGLVLgmsvkENMSL----TALRYFSRAGGSLKHADEQQAVSDFIRLFniktpsmeQAIGL----------LSGGNQ 401
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495775764 151 QRVAIARALAMRPDVILFDEPTSALDpelVG---EVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRI 222
Cdd:PRK10762 402 QKVAIARGLMTRPKVLILDEPTRGVD---VGakkEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
3-228 |
5.68e-15 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 74.01 E-value: 5.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 3 AIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRV-GEiTIDTGkSISqqkglir 81
Cdd:NF033858 266 AIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLfGQ-PVDAG-DIA------- 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 82 rLRQHVGFVFQNFNLFPHRTVLENIiegpvivkgE--------PKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRV 153
Cdd:NF033858 337 -TRRRVGYMSQAFSLYGELTVRQNL---------ElharlfhlPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRL 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 154 AIARALAMRPDVILFDEPTSALDP-------ELVGEvlntirqLAQEKR-TMVIVTHEMSFA-RdvADRAIFMDQGRIVE 224
Cdd:NF033858 407 SLAVAVIHKPELLILDEPTSGVDPvardmfwRLLIE-------LSREDGvTIFISTHFMNEAeR--CDRISLMHAGRVLA 477
|
....*
gi 495775764 225 QG-PA 228
Cdd:NF033858 478 SDtPA 482
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
15-233 |
9.79e-15 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 73.24 E-value: 9.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 15 GQTV-LHGIDLEVEQGEVVAIIGPSGSGKTTLL------RSInlleqpEGGTIRVgeitidTGKSISQqkgliRRLRQHV 87
Cdd:NF033858 12 GKTVaLDDVSLDIPAGCMVGLIGPDGVGKSSLLsliagaRKI------QQGRVEV------LGGDMAD-----ARHRRAV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 88 G----FVFQNF--NLFPHRTVLENIiegpvivkGEPKEEATARARELLAKVGL-------AGKetsyprrLSGGQQQRVA 154
Cdd:NF033858 75 CpriaYMPQGLgkNLYPTLSVFENLdffg-rlfGQDAAERRRRIDELLRATGLapfadrpAGK-------LSGGMKQKLG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 155 IARALAMRPDVILFDEPTSALDP-------ELVgevlNTIRqlaQEKRTM-VIV-THEMSFARDVaDRAIFMDQGRIVEQ 225
Cdd:NF033858 147 LCCALIHDPDLLILDEPTTGVDPlsrrqfwELI----DRIR---AERPGMsVLVaTAYMEEAERF-DWLVAMDAGRVLAT 218
|
....*...
gi 495775764 226 GPAKSLFA 233
Cdd:NF033858 219 GTPAELLA 226
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
25-230 |
1.66e-14 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 70.73 E-value: 1.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 25 EVEQGEVVAIIGPSGSGKTTLLRSI-NLLEQPeggtirvGEITIDtGKSISQ--QKGLIRR---LRQHVG--F---VFQN 93
Cdd:PRK03695 18 EVRAGEILHLVGPNGAGKSTLLARMaGLLPGS-------GSIQFA-GQPLEAwsAAELARHrayLSQQQTppFampVFQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 94 FNLFPHrtvleniiegpvivKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARA-LAMRPDV------I 166
Cdd:PRK03695 90 LTLHQP--------------DKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVvLQVWPDInpagqlL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495775764 167 LFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKS 230
Cdd:PRK03695 156 LLDEPMNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDE 219
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
3-224 |
2.84e-14 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 71.91 E-value: 2.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 3 AIDVKNLVKKFHGQtvlhgidleVEQGEVVAIIGPSGSGKTTLLRSinLLEQ--PEGGTIRVGeitidtgksisqQKGLI 80
Cdd:PRK11147 328 QIDGKQLVKDFSAQ---------VQRGDKIALIGPNGCGKTTLLKL--MLGQlqADSGRIHCG------------TKLEV 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 81 RRLRQHvgfvfqNFNLFPHRTVLENIIEGpvivkgepKEEAT--ARARELLakvglagketSY-------PRR------- 144
Cdd:PRK11147 385 AYFDQH------RAELDPEKTVMDNLAEG--------KQEVMvnGRPRHVL----------GYlqdflfhPKRamtpvka 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 145 LSGGQQQRVAIARaLAMRP-DVILFDEPTSALDPELVgEVLNTIrqLAQEKRTMVIVTHEMSFARD-VADRAIFMDQGRI 222
Cdd:PRK11147 441 LSGGERNRLLLAR-LFLKPsNLLILDEPTNDLDVETL-ELLEEL--LDSYQGTVLLVSHDRQFVDNtVTECWIFEGNGKI 516
|
..
gi 495775764 223 VE 224
Cdd:PRK11147 517 GR 518
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
24-215 |
3.38e-14 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 71.38 E-value: 3.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 24 LEVE-----QGEVVAIIGPSGSGKTTLLRSINLLEQPEGG----TIRVG----EITIDTGKSISQqkgLIRRLRQHVGFV 90
Cdd:PRK13409 355 LEVEggeiyEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGevdpELKISykpqYIKPDYDGTVED---LLRSITDDLGSS 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 91 FQNFNLFpHRTVLENIIEGPVivkgepkeeatararellakvglagketsypRRLSGGQQQRVAIARALAMRPDVILFDE 170
Cdd:PRK13409 432 YYKSEII-KPLQLERLLDKNV-------------------------------KDLSGGELQRVAIAACLSRDADLYLLDE 479
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 495775764 171 PTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADRAI 215
Cdd:PRK13409 480 PSAHLDVEQRLAVAKAIRRIAEEREaTALVVDHDIYMIDYISDRLM 525
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
26-220 |
3.84e-14 |
|
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: 71.58 E-value: 3.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 26 VEQGEVVAIIGPSGSGKTTLLRSINlleqpeggtirvGEITIDTGKSISQQKGLIRRLRQhvgfVFQNFNLFPHRTVLEN 105
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLT------------GDTTVTSGDATVAGKSILTNISD----VHQNMGYCPQFDAIDD 2025
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 106 IIEGP------VIVKGEPKEEATARARELLAKVGLagkeTSYPRRL----SGGQQQRVAIARALAMRPDVILFDEPTSAL 175
Cdd:TIGR01257 2026 LLTGRehlylyARLRGVPAEEIEKVANWSIQSLGL----SLYADRLagtySGGNKRKLSTAIALIGCPPLVLLDEPTTGM 2101
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 495775764 176 DPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQG 220
Cdd:TIGR01257 2102 DPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
4-190 |
4.30e-14 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 71.20 E-value: 4.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLrSINLLEQPEGGTirvGEITIdtgksISQQKG---LI 80
Cdd:PRK10938 261 IVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLL-SLITGDHPQGYS---NDLTL-----FGRRRGsgeTI 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 81 RRLRQHVGFVFQNFNLfPHR---TVLENIIEG---PVIVKGEPKEEATARARELLAKVGLAGKETSYP-RRLSGGQQQRV 153
Cdd:PRK10938 332 WDIKKHIGYVSSSLHL-DYRvstSVRNVILSGffdSIGIYQAVSDRQQKLAQQWLDILGIDKRTADAPfHSLSWGQQRLA 410
|
170 180 190
....*....|....*....|....*....|....*..
gi 495775764 154 AIARALAMRPDVILFDEPTSALDPelvgevLNtiRQL 190
Cdd:PRK10938 411 LIVRALVKHPTLLILDEPLQGLDP------LN--RQL 439
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
18-220 |
5.24e-14 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 71.29 E-value: 5.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 18 VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSinLLEQPEGGTIRVGEITIDTGKsisQQKGLIRRlrqhVGFVFQNFNLF 97
Cdd:TIGR00956 778 ILNNVDGWVKPGTLTALMGASGAGKTTLLNV--LAERVTTGVITGGDRLVNGRP---LDSSFQRS----IGYVQQQDLHL 848
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 98 PHRTVLENII-----EGPVIVKGEPKEEATARARELL-------AKVGLAGKEtsyprrLSGGQQQRVAIARALAMRPDV 165
Cdd:TIGR00956 849 PTSTVRESLRfsaylRQPKSVSKSEKMEYVEEVIKLLemesyadAVVGVPGEG------LNVEQRKRLTIGVELVAKPKL 922
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 495775764 166 ILF-DEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMS---FARdvADRAIFMDQG 220
Cdd:TIGR00956 923 LLFlDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQPSailFEE--FDRLLLLQKG 979
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
18-178 |
2.12e-13 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 67.18 E-value: 2.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 18 VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGEITIDTGKsisqqkglirRLRqHVGFVFQNFNLF 97
Cdd:PRK13543 26 VFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGD----------RSR-FMAYLGHLPGLK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 98 PHRTVLENIiegpVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPDVILFDEPTSALDP 177
Cdd:PRK13543 95 ADLSTLENL----HFLCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL 170
|
.
gi 495775764 178 E 178
Cdd:PRK13543 171 E 171
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
25-215 |
2.27e-13 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 69.04 E-value: 2.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 25 EVEQGEVVAIIGPSGSGKTTLLRsinlleqpeggtIRVGEITIDTGKSISQQKglIRRLRQHV-----GFVfqnfnlfph 99
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAK------------ILAGVLKPDEGEVDEDLK--ISYKPQYIspdydGTV--------- 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 100 RTVLENIIEGPVivkGEPKEEAtararELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPDVILFDEPTSALDPEL 179
Cdd:COG1245 419 EEFLRSANTDDF---GSSYYKT-----EIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQ 490
|
170 180 190
....*....|....*....|....*....|....*..
gi 495775764 180 VGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAI 215
Cdd:COG1245 491 RLAVAKAIRRFAENrGKTAMVVDHDIYLIDYISDRLM 527
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
4-204 |
6.91e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 66.29 E-value: 6.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRvgeitidtgksisqqkgliRRL 83
Cdd:PRK09544 5 VSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK-------------------RNG 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 84 RQHVGFVFQNFNLFPhrtVLENIIEGPVIVKGEPKEEATARArelLAKVGlAGKETSYP-RRLSGGQQQRVAIARALAMR 162
Cdd:PRK09544 66 KLRIGYVPQKLYLDT---TLPLTVNRFLRLRPGTKKEDILPA---LKRVQ-AGHLIDAPmQKLSGGETQRVLLARALLNR 138
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 495775764 163 PDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVI-VTHEM 204
Cdd:PRK09544 139 PQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLmVSHDL 181
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
18-234 |
8.13e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 67.69 E-value: 8.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 18 VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGtirvgEITIDtgksisqqkglirrlrqhvGFVFQNFNLF 97
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKG-----RIMID-------------------DCDVAKFGLT 1306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 98 PHRTVLENIIEGPVIVKG------EPKEE--------ATARA--RELLAK--VGLAGKETSYPRRLSGGQQQRVAIARAL 159
Cdd:PLN03232 1307 DLRRVLSIIPQSPVLFSGtvrfniDPFSEhndadlweALERAhiKDVIDRnpFGLDAEVSEGGENFSVGQRQLLSLARAL 1386
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495775764 160 AMRPDVILFDEPTSALDPELVGEVLNTIRqlaQEKR--TMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKSLFAN 234
Cdd:PLN03232 1387 LRRSKILVLDEATASVDVRTDSLIQRTIR---EEFKscTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSR 1459
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
7-231 |
9.20e-13 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 67.06 E-value: 9.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 7 KNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIrvgeitIDTGKSIsQQKGLIRRLRQH 86
Cdd:PRK10982 2 SNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSI------LFQGKEI-DFKSSKEALENG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 87 VGFVFQNFNLFPHRTVLENI------IEGPVIVKGEPKEEATARARELLAKVGLAGKETSyprrLSGGQQQRVAIARALA 160
Cdd:PRK10982 75 ISMVHQELNLVLQRSVMDNMwlgrypTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVAT----LSVSQMQMIEIAKAFS 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495775764 161 MRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSL 231
Cdd:PRK10982 151 YNAKIVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGL 221
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
4-228 |
9.97e-13 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 65.82 E-value: 9.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSInlLEQPeGGTIRVGEITIDtGKSISQqkgLIRRL 83
Cdd:CHL00131 8 LEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVI--AGHP-AYKILEGDILFK-GESILD---LEPEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 84 RQHVGfVFQNFNlFPhrtvleniIEGPVI---------------VKGEPKEEATARARELLAKVGLAGKETSYPRR---- 144
Cdd:CHL00131 81 RAHLG-IFLAFQ-YP--------IEIPGVsnadflrlaynskrkFQGLPELDPLEFLEIINEKLKLVGMDPSFLSRnvne 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 145 -LSGGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHemsFAR--D--VADRAIFMDQ 219
Cdd:CHL00131 151 gFSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITH---YQRllDyiKPDYVHVMQN 227
|
....*....
gi 495775764 220 GRIVEQGPA 228
Cdd:CHL00131 228 GKIIKTGDA 236
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
19-226 |
1.81e-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: 1.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 19 LHGIDLEVEQGEVVAIIGPSGSGKTTLLRSInlleqpeggtirvgeitIDTGKSISQQKGLIRRLRQHVGFVFQnfnlfp 98
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEG-----------------LYASGKARLISFLPKFSRNKLIFIDQ------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 99 hrtvLENIIegpvivkgepkeeatararellaKVGLA----GKETSyprRLSGGQQQRVAIARALAMRPD--VILFDEPT 172
Cdd:cd03238 68 ----LQFLI-----------------------DVGLGyltlGQKLS---TLSGGELQRVKLASELFSEPPgtLFILDEPS 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 173 SALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFArDVADRAIFM------DQGRIVEQG 226
Cdd:cd03238 118 TGLHQQDINQLLEVIKGLIDLGNTVILIEHNLDVL-SSADWIIDFgpgsgkSGGKVVFSG 176
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
4-226 |
1.96e-12 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 64.81 E-value: 1.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEqpeggtirvgEITIDTGKSISQQKGLIR-- 81
Cdd:PRK09580 2 LSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRE----------DYEVTGGTVEFKGKDLLEls 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 82 ---RLRQHVGFVFQNFNLFP---HRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRR-----LSGGQQ 150
Cdd:PRK09580 72 pedRAGEGIFMAFQYPVEIPgvsNQFFLQTALNAVRSYRGQEPLDRFDFQDLMEEKIALLKMPEDLLTRsvnvgFSGGEK 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495775764 151 QRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVA-DRAIFMDQGRIVEQG 226
Cdd:PRK09580 152 KRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYQRILDYIKpDYVHVLYQGRIVKSG 228
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
14-220 |
5.77e-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: 64.11 E-value: 5.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 14 HGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIR-VGEItidtgkSISQQKGLIrrlrqhvgfvfq 92
Cdd:cd03291 48 VGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKhSGRI------SFSSQFSWI------------ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 93 nfnlFPHrTVLENIIEG--------PVIVKGEPKEEATARARE----LLAKVGLAgketsyprrLSGGQQQRVAIARALA 160
Cdd:cd03291 110 ----MPG-TIKENIIFGvsydeyryKSVVKACQLEEDITKFPEkdntVLGEGGIT---------LSGGQRARISLARAVY 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 161 MRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARdVADRAIFMDQG 220
Cdd:cd03291 176 KDADLYLLDSPFGYLDVFTEKEIFESCVCKLMANKTRILVTSKMEHLK-KADKILILHEG 234
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
18-235 |
7.77e-12 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 64.80 E-value: 7.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 18 VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSinLLEQPEggtIRVGEITIDtgKSIS---QQKGLIrrlrqhvgfvfqnf 94
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQS--LLSQFE---ISEGRVWAE--RSIAyvpQQAWIM-------------- 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 95 nlfpHRTVLENIIEGpvivkgepKEEATA------RARELLAKVGL--AGKETSYPRR---LSGGQQQRVAIARALAMRP 163
Cdd:PTZ00243 734 ----NATVRGNILFF--------DEEDAArladavRVSQLEADLAQlgGGLETEIGEKgvnLSGGQKARVSLARAVYANR 801
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495775764 164 DVILFDEPTSALDPElVGE-VLNTIRQLAQEKRTMVIVTHEMSFArDVADRAIFMDQGRIVEQGPAKSLFANP 235
Cdd:PTZ00243 802 DVYLLDDPLSALDAH-VGErVVEECFLGALAGKTRVLATHQVHVV-PRADYVVALGDGRVEFSGSSADFMRTS 872
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
4-212 |
1.25e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 61.89 E-value: 1.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 4 IDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGEITIDTGKSISQQKglirrl 83
Cdd:PRK13540 2 LDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQ------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 84 rqhVGFVFQNFNLFPHRTVLENIIEgpvivkgEPKEEATARARELLAKVGLAGKETSYP-RRLSGGQQQRVAIARALAMR 162
Cdd:PRK13540 76 ---LCFVGHRSGINPYLTLRENCLY-------DIHFSPGAVGITELCRLFSLEHLIDYPcGLLSSGQKRQVALLRLWMSK 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 495775764 163 PDVILFDEPTSALDpELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVAD 212
Cdd:PRK13540 146 AKLWLLDEPLVALD-ELSLLTIITKIQEHRAKGGAVLLTSHQDLPLNKAD 194
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
10-221 |
1.35e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 63.60 E-value: 1.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 10 VKKFHGQ--TVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVgeitidtgksisqQKGLirrlrqHV 87
Cdd:PRK11819 12 VSKVVPPkkQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARP-------------APGI------KV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 88 GFVFQNFNLFPHRTVLENIIEGPVIVK-------------GEPKEE---------------ATARARELLAKVGLAGKET 139
Cdd:PRK11819 73 GYLPQEPQLDPEKTVRENVEEGVAEVKaaldrfneiyaayAEPDADfdalaaeqgelqeiiDAADAWDLDSQLEIAMDAL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 140 SYP------RRLSGGQQQRVAIARALAMRPDVILFDEPTSALDPELVG--EvlntiRQLAQEKRTMVIVTHEMSFARDVA 211
Cdd:PRK11819 153 RCPpwdakvTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAwlE-----QFLHDYPGTVVAVTHDRYFLDNVA 227
|
250
....*....|
gi 495775764 212 DRAIFMDQGR 221
Cdd:PRK11819 228 GWILELDRGR 237
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
22-222 |
1.57e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 63.53 E-value: 1.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 22 IDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGEITIdTGKSISQqkglirRLRQhvGFVF-----QNFNL 96
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEI-NALSTAQ------RLAR--GLVYlpedrQSSGL 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 97 FPHRTVLENIIEGPVIVKG---EPKEEAtARARELLAKVGLAGKETSYP-RRLSGGQQQRVAIARALAMRPDVILFDEPT 172
Cdd:PRK15439 353 YLDAPLAWNVCALTHNRRGfwiKPAREN-AVLERYRRALNIKFNHAEQAaRTLSGGNQQKVLIAKCLEASPQLLIVDEPT 431
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 495775764 173 SALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRI 222
Cdd:PRK15439 432 RGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
19-247 |
1.67e-11 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 63.37 E-value: 1.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 19 LHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRV-GEITIdtgksISQQKGLIRRLrqhvgfvfqnfnlf 97
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIkGSAAL-----IAISSGLNGQL-------------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 98 phrTVLENiIEGPVIVKGEPKEEatarARELLAKV---GLAGKETSYP-RRLSGGQQQRVAIARALAMRPDVILFDEPTS 173
Cdd:PRK13545 101 ---TGIEN-IELKGLMMGLTKEK----IKEIIPEIiefADIGKFIYQPvKTYSSGMKSRLGFAISVHINPDILVIDEALS 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495775764 174 ALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFANpqqprTRQFLEKF 247
Cdd:PRK13545 173 VGDQTFTKKCLDKMNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDH-----YDEFLKKY 241
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
22-222 |
1.93e-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: 63.31 E-value: 1.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 22 IDLEVEQGEVVAIIGPSGSGKTTLLRSI-NLLEQPEGGTIRVGEITIDT---GKSISQQKGLIRRLRQHVGFVfqnfnlf 97
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQALfGAYPGKFEGNVFINGKPVDIrnpAQAIRAGIAMVPEDRKRHGIV------- 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 98 PHRTVLENIIEGPV-IVKGEPKEEATARARELLAKVGLAGKETSYP----RRLSGGQQQRVAIARALAMRPDVILFDEPT 172
Cdd:TIGR02633 352 PILGVGKNITLSVLkSFCFKMRIDAAAELQIIGSAIQRLKVKTASPflpiGRLSGGNQQKAVLAKMLLTNPRVLILDEPT 431
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 495775764 173 SALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRI 222
Cdd:TIGR02633 432 RGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
28-216 |
2.23e-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: 60.08 E-value: 2.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 28 QGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIrvgeITIDTGKSISQQKGLIRRLRQHVGfvfqnfnlfphrtvlenii 107
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGV----IYIDGEDILEEVLDQLLLIIVGGK------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 108 egpvivkgepkeeatararellakvglagketsyPRRLSGGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVL--- 184
Cdd:smart00382 58 ----------------------------------KASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLlle 103
|
170 180 190
....*....|....*....|....*....|....*
gi 495775764 185 ---NTIRQLAQEKRTMVIVTHEMSFARDVADRAIF 216
Cdd:smart00382 104 elrLLLLLKSEKNLTVILTTNDEKDLGPALLRRRF 138
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
2-222 |
2.47e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 63.02 E-value: 2.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 2 SAIDVKNLVKKfhgqtVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSI-NLLEQPEGGTIRVG--EITIDT-GKSISQQK 77
Cdd:PRK13549 266 TAWDPVNPHIK-----RVDDVSFSLRRGEILGIAGLVGAGRTELVQCLfGAYPGRWEGEIFIDgkPVKIRNpQQAIAQGI 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 78 GLIRRLRQHVGFVF-----QNFNLfphrTVLENIIEGPVIvkGEPKEEATARARELLAKVglagkETSYPR----RLSGG 148
Cdd:PRK13549 341 AMVPEDRKRDGIVPvmgvgKNITL----AALDRFTGGSRI--DDAAELKTILESIQRLKV-----KTASPElaiaRLSGG 409
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495775764 149 QQQRVAIARALAMRPDVILFDEPTSALDpelVG---EVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRI 222
Cdd:PRK13549 410 NQQKAVLAKCLLLNPKILILDEPTRGID---VGakyEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
29-227 |
5.38e-11 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 62.17 E-value: 5.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 29 GEVVAIIGPSGSGKTTLLRSinLLEQPEGGTIRvGEITI-------DTGKSISqqkglirrlrqhvGFVFQNFNLFPHRT 101
Cdd:PLN03140 906 GVLTALMGVSGAGKTTLMDV--LAGRKTGGYIE-GDIRIsgfpkkqETFARIS-------------GYCEQNDIHSPQVT 969
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 102 VLENIIEG-----PVIVKGEPKEEATARARELL-------AKVGLAGKETsyprrLSGGQQQRVAIARALAMRPDVILFD 169
Cdd:PLN03140 970 VRESLIYSaflrlPKEVSKEEKMMFVDEVMELVeldnlkdAIVGLPGVTG-----LSTEQRKRLTIAVELVANPSIIFMD 1044
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 170 EPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSF-ARDVADRAIFMDQ-GRIVEQGP 227
Cdd:PLN03140 1045 EPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSIdIFEAFDELLLMKRgGQVIYSGP 1104
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
25-248 |
5.77e-11 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 59.51 E-value: 5.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 25 EVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIRVGEITIdtgkSISQQKglirrlrqhvgfvfqnfnlfphrtvle 104
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITP----VYKPQY--------------------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 105 niiegpvivkgepkeeatararellakvglagketsypRRLSGGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVL 184
Cdd:cd03222 70 --------------------------------------IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAA 111
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495775764 185 NTIRQLAQE-KRTMVIVTHEMSFARDVADRAIfmdqgrIVEQGPAKSLFANPQQPrTRQFLEKFL 248
Cdd:cd03222 112 RAIRRLSEEgKKTALVVEHDLAVLDYLSDRIH------VFEGEPGVYGIASQPKG-TREGINRFL 169
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
18-233 |
6.35e-11 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 62.27 E-value: 6.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 18 VLHGIDLEVEQGEVVAIIGPSGSGKTTL-LRSINLLEQPEGgtirvgEITIDtGKSISQqKGLiRRLRQHVGFVFQNFNL 96
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLtLGLFRINESAEG------EIIID-GLNIAK-IGL-HDLRFKITIIPQDPVL 1371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 97 FPHrTVLENIieGPVivkGEPKEEATARARELlakVGLAGKETSYPRRL-----------SGGQQQRVAIARALAMRPDV 165
Cdd:TIGR00957 1372 FSG-SLRMNL--DPF---SQYSDEEVWWALEL---AHLKTFVSALPDKLdhecaeggenlSVGQRQLVCLARALLRKTKI 1442
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495775764 166 ILFDEPTSALDPELVGEVLNTIRQlAQEKRTMVIVTHEMSFARDVAdRAIFMDQGRIVEQGPAKSLFA 233
Cdd:TIGR00957 1443 LVLDEATAAVDLETDNLIQSTIRT-QFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNLLQ 1508
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1-233 |
9.86e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 61.18 E-value: 9.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 1 MSAIDVKNLVKKFHGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINlleqpeggtirvGEITIDTGKSISQQKGLI 80
Cdd:PRK10938 1 MSSLQISQGTFRLSDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALA------------GELPLLSGERQSQFSHIT 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 81 R----RLRQHVGFVFQNFN---LFPH-----RTVLENIIEGpvivkgepkEEATARARELLAKVGLagkETSYPRR---L 145
Cdd:PRK10938 69 RlsfeQLQKLVSDEWQRNNtdmLSPGeddtgRTTAEIIQDE---------VKDPARCEQLAQQFGI---TALLDRRfkyL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 146 SGGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQ 225
Cdd:PRK10938 137 STGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAET 216
|
250
....*....|...
gi 495775764 226 GP-----AKSLFA 233
Cdd:PRK10938 217 GEreeilQQALVA 229
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
4-189 |
1.20e-10 |
|
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: 61.46 E-value: 1.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 4 IDVKNLVKKF--HGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEggtirvGEITID--TGKSISQQKgl 79
Cdd:TIGR01271 1218 MDVQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE------GEIQIDgvSWNSVTLQT-- 1289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 80 irrLRQHVGFVFQNFNLFPHrTVLENIiegpvivkgEPKEEATARARELLA-KVGLAGKETSYPRR-----------LSG 147
Cdd:TIGR01271 1290 ---WRKAFGVIPQKVFIFSG-TFRKNL---------DPYEQWSDEEIWKVAeEVGLKSVIEQFPDKldfvlvdggyvLSN 1356
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 495775764 148 GQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQ 189
Cdd:TIGR01271 1357 GHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQ 1398
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
18-223 |
1.48e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 60.57 E-value: 1.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 18 VLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSI--NLLEQPEGGTIRVG--EITIDT-GKSISQQKGLIRRLRQHVGFVFQ 92
Cdd:NF040905 275 VVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVfgRSYGRNISGTVFKDgkEVDVSTvSDAIDAGLAYVTEDRKGYGLNLI 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 93 ----------NFNLFPHRTVLENIIEgpVIVKGEPKEEATARARELLAKVGlagketsyprRLSGGQQQRVAIARALAMR 162
Cdd:NF040905 355 ddikrnitlaNLGKVSRRGVIDENEE--IKVAEEYRKKMNIKTPSVFQKVG----------NLSGGNQQKVVLSKWLFTD 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495775764 163 PDVILFDEPTSALDpelVG---EVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIV 223
Cdd:NF040905 423 PDVLILDEPTRGID---VGakyEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMNEGRIT 483
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
14-220 |
1.87e-10 |
|
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: 60.69 E-value: 1.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 14 HGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIR-VGEItidtgkSISQQKGLIrrlrqhvgfvfq 92
Cdd:TIGR01271 437 YVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKhSGRI------SFSPQTSWI------------ 498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 93 nfnlFPHrTVLENIIEG--------PVIVKGEPKEEATARARELLAKVGLAGKETsyprrLSGGQQQRVAIARALAMRPD 164
Cdd:TIGR01271 499 ----MPG-TIKDNIIFGlsydeyryTSVIKACQLEEDIALFPEKDKTVLGEGGIT-----LSGGQRARISLARAVYKDAD 568
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 495775764 165 VILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDvADRAIFMDQG 220
Cdd:TIGR01271 569 LYLLDSPFTHLDVVTEKEIFESCLCKLMSNKTRILVTSKLEHLKK-ADKILLLHEG 623
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
145-224 |
2.44e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 60.13 E-value: 2.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 145 LSGGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGR--- 221
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLvag 471
|
...
gi 495775764 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 495775764 134 LAGKETSyprRLSGGQQQRVAIARALAMRPDVILFDEPTSALDPE---LVGEVLNTIRqlAQEKRTMVIVTHEMSFAR 208
Cdd:PTZ00265 572 LVGSNAS---KLSGGQKQRISIARAIIRNPKILILDEATSSLDNKseyLVQKTINNLK--GNENRITIIIAHRLSTIR 644
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
121-222 |
8.17e-10 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 58.36 E-value: 8.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 121 ATARARELLAKVGLAGKETSYP-RRLSGGQQQRVAIARALAMRPDVILFDEPTSALDpelvgevLNTIRQLAQE----KR 195
Cdd:PRK15064 131 AEARAGELLLGVGIPEEQHYGLmSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLD-------INTIRWLEDVlnerNS 203
|
90 100 110
....*....|....*....|....*....|.
gi 495775764 196 TMVIVTHEMSFARDV----ADraifMDQGRI 222
Cdd:PRK15064 204 TMIIISHDRHFLNSVcthmAD----LDYGEL 230
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
4-189 |
1.44e-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: 57.17 E-value: 1.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 4 IDVKNLVKKF--HGQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGgtirvgEITIDtgkSISQQKGLIR 81
Cdd:cd03289 3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEG------DIQID---GVSWNSVPLQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 82 RLRQHVGFVFQNFNLF--PHRTVLENiiegpvivKGEPKEEATARAREllaKVGLAGKETSYPRRL-----------SGG 148
Cdd:cd03289 74 KWRKAFGVIPQKVFIFsgTFRKNLDP--------YGKWSDEEIWKVAE---EVGLKSVIEQFPGQLdfvlvdggcvlSHG 142
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 495775764 149 QQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQ 189
Cdd:cd03289 143 HKQLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQ 183
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
141-205 |
2.18e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 57.35 E-value: 2.18e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495775764 141 YPRRLSGGQQQRVAIARALAMRPDVILFDEPTSALDP---ELVGEVLNTIRQLAQekRTMVIVTHEMS 205
Cdd:PTZ00265 1355 YGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSnseKLIEKTIVDIKDKAD--KTIITIAHRIA 1420
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
4-233 |
1.14e-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: 54.14 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 4 IDVKNLVKKFHG--QTVLHGIDLEVEQGEVVAIIGPSGSGKTTL----LRSINLLEqpeggtirvGEITIDtGKSISqqK 77
Cdd:cd03288 20 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIFD---------GKIVID-GIDIS--K 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 78 GLIRRLRQHVGFVFQN---------FNLFPHRTVLEN-------IIEGPVIVKGEPKeeatararellakvGLAGKETSY 141
Cdd:cd03288 88 LPLHTLRSRLSIILQDpilfsgsirFNLDPECKCTDDrlwealeIAQLKNMVKSLPG--------------GLDAVVTEG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 142 PRRLSGGQQQRVAIARALAMRPDVILFDEPTSALDPElVGEVLNTIRQLAQEKRTMVIVTHEMSFARDvADRAIFMDQGR 221
Cdd:cd03288 154 GENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMA-TENILQKVVMTAFADRTVVTIAHRVSTILD-ADLVLVLSRGI 231
|
250
....*....|..
gi 495775764 222 IVEQGPAKSLFA 233
Cdd:cd03288 232 LVECDTPENLLA 243
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
121-210 |
4.86e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 53.33 E-value: 4.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 121 ATARARELLAKVGLAGK-ETSYPRRLSGGQQQRVAIARALAMRPDVILFDEPTSALDpelVGEVLNTIRQLAQEKRTMVI 199
Cdd:PLN03073 320 AEARAASILAGLSFTPEmQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD---LHAVLWLETYLLKWPKTFIV 396
|
90
....*....|.
gi 495775764 200 VTHEMSFARDV 210
Cdd:PLN03073 397 VSHAREFLNTV 407
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
29-202 |
1.51e-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: 49.67 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 29 GEVVAIIGPSGSGKTTLLRSINLLEqpeggtirvgeitidTGKSISQQKGLIRRLRQHVGFVFQNFNLFPHRtvleniie 108
Cdd:cd03227 21 GSLTIITGPNGSGKSTILDAIGLAL---------------GGAQSATRRRSGVKAGCIVAAVSAELIFTRLQ-------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 109 gpvivkgepkeeatararellakvglagketsyprrLSGGQQQRVAIARALA----MRPDVILFDEPTSALDPELVGEVL 184
Cdd:cd03227 78 ------------------------------------LSGGEKELSALALILAlaslKPRPLYILDEIDRGLDPRDGQALA 121
|
170
....*....|....*...
gi 495775764 185 NTIRQLAQEKRTMVIVTH 202
Cdd:cd03227 122 EAILEHLVKGAQVIVITH 139
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
23-248 |
1.68e-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: 51.16 E-value: 1.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 23 DLEVE-QGEVVAIIGPSGSGKTTLLRSINLL-----------------EQPEGGTIRVgEITIDTGKSISQQKGLIRRLR 84
Cdd:COG3593 16 DLSIElSDDLTVLVGENNSGKSSILEALRLLlgpsssrkfdeedfylgDDPDLPEIEI-ELTFGSLLSRLLRLLLKEEDK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 85 QHVGFVFQNFN--LFPHRTVLENIIEGPVIVKGEPKE---EATARARELLAK---VGLAGKETSYPRRLSGGQQQRVAIA 156
Cdd:COG3593 95 EELEEALEELNeeLKEALKALNELLSEYLKELLDGLDlelELSLDELEDLLKslsLRIEDGKELPLDRLGSGFQRLILLA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 157 RALAM-------RPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIfmdqgRIVEQGPAK 229
Cdd:COG3593 175 LLSALaelkrapANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTHSPHLLSEVPLENI-----RRLRRDSGG 249
|
250 260
....*....|....*....|.
gi 495775764 230 SLFA--NPQQPRTRQFLEKFL 248
Cdd:COG3593 250 TTSTklIDLDDEDLRKLLRYL 270
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
4-202 |
1.96e-07 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 50.01 E-value: 1.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 4 IDVKNLvKKFHGQTVlhgIDLEveqGEVVAIIGPSGSGKTTLLRSINLL---EQPEGGTIRVGEITIDTGK-------SI 73
Cdd:COG0419 5 LRLENF-RSYRDTET---IDFD---DGLNLIVGPNGAGKSTILEAIRYAlygKARSRSKLRSDLINVGSEEasvelefEH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 74 SQQKGLIRRlRQHVGFVFQNFNLFPHRTVLENIIEGPVIVK-----GEPKEEATARARELLAKVGLAGK------ETSYP 142
Cdd:COG0419 78 GGKRYRIER-RQGEFAEFLEAKPSERKEALKRLLGLEIYEElkerlKELEEALESALEELAELQKLKQEilaqlsGLDPI 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 143 RRLSGGQQQRVAIARALAMrpdviLFDepTSALDPELVGEVLNTIRQLAqekrtmvIVTH 202
Cdd:COG0419 157 ETLSGGERLRLALADLLSL-----ILD--FGSLDEERLERLLDALEELA-------IITH 202
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
31-212 |
2.66e-07 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 49.53 E-value: 2.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 31 VVAIIGPSGSGKTTLLRSINLL---EQPEGGTIRVGEITIDTGKSISQQKGLIRRLRQHVGF-VFQNFNlfphrtVLENI 106
Cdd:cd03240 24 LTLIVGQNGAGKTTIIEALKYAltgELPPNSKGGAHDPKLIREGEVRAQVKLAFENANGKKYtITRSLA------ILENV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 107 IegpvIVKGEpkEEATARAREllakvglagketsyPRRLSGGQQQ------RVAIARALAMRPDVILFDEPTSALDPELV 180
Cdd:cd03240 98 I----FCHQG--ESNWPLLDM--------------RGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENI 157
|
170 180 190
....*....|....*....|....*....|....
gi 495775764 181 GEVLNTI--RQLAQEKRTMVIVTHEMSFaRDVAD 212
Cdd:cd03240 158 EESLAEIieERKSQKNFQLIVITHDEEL-VDAAD 190
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
123-224 |
2.68e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 50.94 E-value: 2.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 123 ARARELLAKVGLAGKETSYP-RRLSGGQQQRVAIARALAMRPDVILFDEPTSALDpelVGEVLNTIRQLAQEKRTMVIVT 201
Cdd:PRK10636 127 SRAASLLHGLGFSNEQLERPvSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLD---LDAVIWLEKWLKSYQGTLILIS 203
|
90 100
....*....|....*....|...
gi 495775764 202 HEMSFARDVADRAIFMDQGRIVE 224
Cdd:PRK10636 204 HDRDFLDPIVDKIIHIEQQSLFE 226
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
21-222 |
2.87e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 51.01 E-value: 2.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 21 GIDLEVEqgevVAIIGPSGSGKTTLLRSINLLEQPEGGTI-RVGEITIDTgksISQQKglIRRLRQHVGFVFQNFNLFPh 99
Cdd:PLN03073 531 GIDLDSR----IAMVGPNGIGKSTILKLISGELQPSSGTVfRSAKVRMAV---FSQHH--VDGLDLSSNPLLYMMRCFP- 600
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 100 rtvleniiegpvivkGEPKEeataRARELLAKVGLAGKETSYPR-RLSGGQQQRVAIARALAMRPDVILFDEPTSALDPE 178
Cdd:PLN03073 601 ---------------GVPEQ----KLRAHLGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLD 661
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 495775764 179 LVgEVLntIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRI 222
Cdd:PLN03073 662 AV-EAL--IQGLVLFQGGVLMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
19-247 |
5.11e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 49.43 E-value: 5.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 19 LHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTI-RVGEITIdtgksISQQKGLIRRLrqhvgfvfqnfnlf 97
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVdRNGEVSV-----IAISAGLSGQL-------------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 98 phrTVLENIiEGPVIVKGEPKEEATARARELLAKVGLaGKETSYP-RRLSGGQQQRVAIARALAMRPDVILFDEPTSALD 176
Cdd:PRK13546 101 ---TGIENI-EFKMLCMGFKRKEIKAMTPKIIEFSEL-GEFIYQPvKKYSSGMRAKLGFSINITVNPDILVIDEALSVGD 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495775764 177 PELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKSLFanpqqPRTRQFLEKF 247
Cdd:PRK13546 176 QTFAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVL-----PKYEAFLNDF 241
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
15-205 |
8.14e-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: 49.36 E-value: 8.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 15 GQTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIrvgeiTIDT-GK--SISQQKGLIRR-LRQHVGF- 89
Cdd:TIGR00954 464 GDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRL-----TKPAkGKlfYVPQRPYMTLGtLRDQIIYp 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 90 --VFQNFNLFPHRTVLENIIEG---PVIVKGEPKEEATARARELLakvglagketsyprrlSGGQQQRVAIARALAMRPD 164
Cdd:TIGR00954 539 dsSEDMKRRGLSDKDLEQILDNvqlTHILEREGGWSAVQDWMDVL----------------SGGEKQRIAMARLFYHKPQ 602
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 495775764 165 VILFDEPTSALDPELVGEvlntIRQLAQEKR-TMVIVTHEMS 205
Cdd:TIGR00954 603 FAILDECTSAVSVDVEGY----MYRLCREFGiTLFSVSHRKS 640
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
16-222 |
2.50e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 47.86 E-value: 2.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 16 QTVLHGIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEGGTIrvgeitidtgksisqqkGLIRRLRqhVGFVFQnfn 95
Cdd:PRK10636 325 RIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI-----------------GLAKGIK--LGYFAQ--- 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 96 lfpHRTVLENIIEGPV--IVKGEPKEeATARARELLAKVGLAG-KETSYPRRLSGGQQQRVAIARALAMRPDVILFDEPT 172
Cdd:PRK10636 383 ---HQLEFLRADESPLqhLARLAPQE-LEQKLRDYLGGFGFQGdKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPT 458
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 495775764 173 SALDPELvgevlntiRQLAQE-----KRTMVIVTHEMSFARDVADRAIFMDQGRI 222
Cdd:PRK10636 459 NHLDLDM--------RQALTEalidfEGALVVVSHDRHLLRSTTDDLYLVHDGKV 505
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
19-226 |
2.86e-06 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 46.87 E-value: 2.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 19 LHGIDLEVEQGEVVAIIGPSGSGKTTL-------------LRSINLLEQPEGGTIRVGEITIDTGKS--IS-QQKGLIRR 82
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLafdtiyaegqrryVESLSAYARQFLGQMDKPDVDSIEGLSpaIAiDQKTTSRN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 83 LRQHVGFVFQNFNLFphRTVLENIiegpvivkgepkeeaTARAR-ELLAKVGLA----GKETSyprRLSGGQQQRVAIAR 157
Cdd:cd03270 91 PRSTVGTVTEIYDYL--RLLFARV---------------GIRERlGFLVDVGLGyltlSRSAP---TLSGGEAQRIRLAT 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495775764 158 ALAMRPDVIL--FDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARdVADRAIFM------DQGRIVEQG 226
Cdd:cd03270 151 QIGSGLTGVLyvLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIR-AADHVIDIgpgagvHGGEIVAQG 226
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
19-227 |
7.12e-06 |
|
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: 46.07 E-value: 7.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 19 LHGIDLEVEQGEVVAIIGPSGSGKTTLLRSI------NLL----EQPEGGTIRVGEITIDTGKSISQQ------------ 76
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLINDTlypalaRRLhlkkEQPGNHDRIEGLEHIDKVIVIDQSpigrtprsnpat 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 77 -KGLIRRLRQhvgfVF------QNFNlfphRTVLENIIEGPVI--VKGEPKEEA---------TARARELLAKVGLA--- 135
Cdd:cd03271 91 yTGVFDEIRE----LFcevckgKRYN----RETLEVRYKGKSIadVLDMTVEEAleffenipkIARKLQTLCDVGLGyik 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 136 -GKETSyprRLSGGQQQRVAIARALAMR---PDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARdVA 211
Cdd:cd03271 163 lGQPAT---TLSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIK-CA 238
|
250 260
....*....|....*....|..
gi 495775764 212 DRAIFMDQ------GRIVEQGP 227
Cdd:cd03271 239 DWIIDLGPeggdggGQVVASGT 260
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
145-232 |
1.36e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 45.98 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 145 LSGGQQQRVAIARALAMRPDVILF--DEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHE---MSFArdvadraifmdq 219
Cdd:PRK00635 477 LSGGEQERTALAKHLGAELIGITYilDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDeqmISLA------------ 544
|
90
....*....|...
gi 495775764 220 GRIVEQGPAKSLF 232
Cdd:PRK00635 545 DRIIDIGPGAGIF 557
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
145-204 |
2.46e-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: 2.46e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495775764 145 LSGGQQQRVAIARALAMR---PDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEM 204
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNL 892
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
142-202 |
2.22e-04 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 41.61 E-value: 2.22e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495775764 142 PRRLSGGQQQ---RVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTH 202
Cdd:pfam13304 234 AFELSDGTKRllaLLAALLSALPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTH 297
|
|
| ABC_ATPase |
pfam09818 |
ATPase of the ABC class; This is the C-terminal ATPase domain from bacterial ABC class ATPases. ... |
146-241 |
2.47e-04 |
|
ATPase of the ABC class; This is the C-terminal ATPase domain from bacterial ABC class ATPases. This entry also includes MRB1590 from Trypanosoma brucei brucei has a central ATPase domain homologous to this domain.
Pssm-ID: 462914 Cd Length: 282 Bit Score: 41.43 E-value: 2.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 146 SGGQQQRVAIARALAMRPDVILFDEPTSA--------LDPELVG---EVLNTIRQLAQEKR-----TMVIVTHEMSFARD 209
Cdd:pfam09818 159 SGSTSQAANIMEALEAGASLLLIDEDTSAtnfmirdeRMQALVSkdkEPITPFVDRVRSLYddlgvSTILVVGGSGDYLD 238
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 495775764 210 VADRAIFMDQGR----------IVEQGPAKSLFANPQQPRTR 241
Cdd:pfam09818 239 VADTVILMDEYRpsdvteeakeIAEELPTGRYEEASKFGPPR 280
|
|
| 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 495775764 13 FHGQTVlhgidlEVEQGEVVAIIGPSGSGKTTLLRSINLL 52
Cdd:pfam13555 12 FDGHTI------PIDPRGNTLLTGPSGSGKSTLLDAIQTL 45
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
10-202 |
3.83e-04 |
|
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: 40.33 E-value: 3.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 10 VKKFHGQTVLHGIDLE-VEQGEVVAIIGPSGSGKTTLLRSINLleQPEGGTIRVGEiTIDTGKSISQQKGLIRrlrqhVG 88
Cdd:cd03279 8 LKNFGPFREEQVIDFTgLDNNGLFLICGPTGAGKSTILDAITY--ALYGKTPRYGR-QENLRSVFAPGEDTAE-----VS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 89 FVFQNFNLFpHRtvleniiegpviVKGEPKEEATARARELLAKVGLAGKETSYP-RRLSGGQQQRVAIARALAM------ 161
Cdd:cd03279 80 FTFQLGGKK-YR------------VERSRGLDYDQFTRIVLLPQGEFDRFLARPvSTLSGGETFLASLSLALALsevlqn 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 495775764 162 ----RPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTH 202
Cdd:cd03279 147 rggaRLEALFIDEGFGTLDPEALEAVATALELIRTENRMVGVISH 191
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
145-227 |
6.90e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.58 E-value: 6.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 145 LSGGQQQRVAIARAL---AMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARdVADraifmdqgR 221
Cdd:PRK00635 810 LSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNMHVVK-VAD--------Y 880
|
....*.
gi 495775764 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 |
1.50e-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: 39.61 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 145 LSGGQQQRVAIARALAMRPDVILF--DEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARdVADRAIFMDQ--- 219
Cdd:TIGR00630 489 LSGGEAQRIRLATQIGSGLTGVLYvlDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEDTIR-AADYVIDIGPgag 567
|
90 100
....*....|....*....|
gi 495775764 220 ---GRIVEQGPAKSLFANPQ 236
Cdd:TIGR00630 568 ehgGEVVASGTPEEILANPD 587
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
143-246 |
1.65e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 39.44 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 143 RRLSGGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIvtheMSFAR------DVADRAIF 216
Cdd:PLN03140 335 RGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEATVL----MSLLQpapetfDLFDDIIL 410
|
90 100 110
....*....|....*....|....*....|....*...
gi 495775764 217 MDQGRIVEQGPAKSL--------FANPQQPRTRQFLEK 246
Cdd:PLN03140 411 LSEGQIVYQGPRDHIleffescgFKCPERKGTADFLQE 448
|
|
| MobB |
COG1763 |
Molybdopterin-guanine dinucleotide biosynthesis protein [Coenzyme transport and metabolism]; ... |
31-46 |
1.94e-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: 1.94e-03
|
| YejR |
COG0523 |
Zinc metallochaperone YeiR/ZagA and related GTPases, G3E family [General function prediction ... |
39-68 |
2.16e-03 |
|
Zinc metallochaperone YeiR/ZagA and related GTPases, G3E family [General function prediction only];
Pssm-ID: 440289 [Multi-domain] Cd Length: 318 Bit Score: 38.62 E-value: 2.16e-03
10 20 30
....*....|....*....|....*....|....*
gi 495775764 39 GSGKTTLLRsiNLLEQPEGGTIRV-----GEITID 68
Cdd:COG0523 14 GAGKTTLLN--HLLANPEGRRIAVivnefGEVGID 46
|
|
| NACHT |
COG5635 |
Predicted NTPase, NACHT family domain [Signal transduction mechanisms]; |
8-62 |
2.21e-03 |
|
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
Pssm-ID: 444362 [Multi-domain] Cd Length: 935 Bit Score: 39.02 E-value: 2.21e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 495775764 8 NLVKKFHGQTVLHGIDLeveQGEVVAIIGPSGSGKTTLLRSI--NLLEQPEGGTIRV 62
Cdd:COG5635 162 NLLERIESLKRLELLEA---KKKRLLILGEPGSGKTTLLRYLalELAERYLDAEDPI 215
|
|
| Udk |
COG0572 |
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ... |
31-49 |
2.51e-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: 2.51e-03
|
| BMS1 |
cd01882 |
Bms1, an essential GTPase, promotes assembly of preribosomal RNA processing complexes; Bms1 is ... |
31-72 |
2.87e-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: 38.09 E-value: 2.87e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 495775764 31 VVAIIGPSGSGKTTLLRSinLLEQPEGGTIRV--GEITIDTGKS 72
Cdd:cd01882 41 VVVVVGPPGVGKSTLIRS--LIKRYTKQNLSDikGPITIVTGKK 82
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
28-71 |
4.05e-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: 37.14 E-value: 4.05e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 495775764 28 QGEVVAIIGPSGSGKTTLlrsINLLeQPEgGTIRVGEITIDTGK 71
Cdd:pfam03193 105 KGKTTVLAGQSGVGKSTL---LNAL-LPE-LDLRTGEISEKLGR 143
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
136-201 |
4.63e-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: 37.24 E-value: 4.63e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 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 |
5.49e-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: 5.49e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 495775764 145 LSGGQQQR---VAIARALAM----------RPDVILFDEPTSALDPELVGEVLNTIRQ 189
Cdd:pfam13558 33 LSGGEKQLlayLPLAAALAAqygsaegrppAPRLVFLDEAFAKLDEENIRTALELLRA 90
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
28-71 |
5.78e-03 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 36.99 E-value: 5.78e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 495775764 28 QGEVVAIIGPSGSGKTTLlrsINLLeQPEGGtIRVGEITIDTGK 71
Cdd:cd01854 84 KGKTSVLVGQSGVGKSTL---LNAL-LPELV-LATGEISEKLGR 122
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
23-52 |
5.81e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 37.60 E-value: 5.81e-03
10 20 30
....*....|....*....|....*....|
gi 495775764 23 DLEVEQGEVVAIIGPSGSGKTTLLRSINLL 52
Cdd:COG4637 15 DLELPLGPLTVLIGANGSGKSNLLDALRFL 44
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
145-212 |
5.88e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 37.70 E-value: 5.88e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495775764 145 LSGGQQQRVAIARALAMRPD---VILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMsfarDV---AD 212
Cdd:COG0178 827 LSGGEAQRVKLASELSKRSTgktLYILDEPTTGLHFHDIRKLLEVLHRLVDKGNTVVVIEHNL----DViktAD 896
|
|
| TrwB_TraG_TraD_VirD4 |
cd01127 |
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are ... |
32-69 |
6.14e-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: 6.14e-03
10 20 30
....*....|....*....|....*....|....*...
gi 495775764 32 VAIIGPSGSGKTTLLRSINLLEQPEGGTIrvgeITIDT 69
Cdd:cd01127 2 TLVLGTTGSGKTTSIVIPLLDQAARGGSV----IITDP 35
|
|
| CobW-like |
cd03112 |
cobalamin synthesis protein CobW; The function of this protein family is unknown. The amino ... |
39-78 |
6.74e-03 |
|
cobalamin synthesis protein CobW; The function of this protein family is unknown. The amino acid sequence of YjiA protein in E. coli contains several conserved motifs that characterizes it as a P-loop GTPase. YijA gene is among the genes significantly induced in response to DNA-damage caused by mitomycin. YijA gene is a homologue of the CobW gene which encodes the cobalamin synthesis protein/P47K.
Pssm-ID: 349766 Cd Length: 198 Bit Score: 36.73 E-value: 6.74e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 495775764 39 GSGKTTLLRsiNLLEQPEGGTIRV-----GEITIDtGKSISQQKG 78
Cdd:cd03112 10 GAGKTTLLN--HILSEQHGKRIAVivnefGEVGID-AALLADSGG 51
|
|
| PEPCK_HprK |
cd00820 |
Phosphoenolpyruvate carboxykinase (PEPCK), a critical gluconeogenic enzyme, catalyzes the ... |
15-45 |
6.83e-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: 6.83e-03
10 20 30
....*....|....*....|....*....|.
gi 495775764 15 GQTVLHGIDLEVEQGEVVAIIGPSGSGKTTL 45
Cdd:cd00820 1 GTTSLHGVLVDVYGKVGVLITGDSGIGKTEL 31
|
|
| COG4938 |
COG4938 |
Predicted ATPase [General function prediction only]; |
1-202 |
7.11e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443965 [Multi-domain] Cd Length: 277 Bit Score: 36.87 E-value: 7.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 1 MSAIDVKNLvKKFhgqtvlhgIDLEVEQGEVVAIIGPSGSGKTTLLRSINLLEQPEG--------GTIRVGEITIDTGKS 72
Cdd:COG4938 1 IKSISIKNF-GPF--------KEAELELKPLTLLIGPNGSGKSTLIQALLLLLQSNFiylpaersGPARLYPSLVRELSD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 73 I----------SQQKGLIRRLRQHVGFVFQNFNLFphrtvLENIIEGPVIVKGEPKEEatararELLAKVGLAGKETSyP 142
Cdd:COG4938 72 LgsrgeytadfLAELENLEILDDKSKELLEQVEEW-----LEKIFPGKVEVDASSDLV------RLVFRPSGNGKRIP-L 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495775764 143 RRLSGGQQQRVAIARALAMRP---DVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTH 202
Cdd:COG4938 140 SNVGSGVSELLPILLALLSAAkpgSLLIIEEPEAHLHPKAQSALAELLAELANSGVQVIIETH 202
|
|
| ExeA |
COG3267 |
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ... |
26-54 |
7.44e-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: 36.69 E-value: 7.44e-03
10 20 30
....*....|....*....|....*....|
gi 495775764 26 VEQGE-VVAIIGPSGSGKTTLLRSinLLEQ 54
Cdd:COG3267 39 LAQGGgFVVLTGEVGTGKTTLLRR--LLER 66
|
|
| AAA_33 |
pfam13671 |
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ... |
31-92 |
7.51e-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: 35.75 E-value: 7.51e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495775764 31 VVAIIGPSGSGKTTLLRsiNLLEQPegGTIRVGE------ITIDTGKSISQQKGLIRRLRQHVGFVFQ 92
Cdd:pfam13671 1 LILLVGLPGSGKSTLAR--RLLEEL--GAVRLSSdderkrLFGEGRPSISYYTDATDRTYERLHELAR 64
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
31-52 |
7.79e-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: 36.98 E-value: 7.79e-03
|
| RepA_RSF1010_like |
cd01125 |
Hexameric Replicative Helicase RepA of plasmid RSF1010 and related proteins; This family ... |
29-141 |
8.30e-03 |
|
Hexameric Replicative Helicase RepA of plasmid RSF1010 and related proteins; This family includes the homo-hexameric replicative helicase RepA encoded by plasmid RSF1010. RSF1010 is found in most Gram-negative bacteria and some Gram-positive bacteria . The RepA protein of Plasmid RSF1010 is a 5'-3' DNA helicase which can utilize ATP, dATP, GTP and dGTP (and CTP and dCTP to a lesser extent).
Pssm-ID: 410870 Cd Length: 238 Bit Score: 36.59 E-value: 8.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495775764 29 GEVVAIIGPSGSGKTTLLRSI--------NLLEQPEGGTIRV----GEitidtgksiSQQKGLIRRLRQHVGFVFQNFNL 96
Cdd:cd01125 1 GTLGMLVGPPGSGKSFLALDLavavatgrDWLGERRVKQGRVvylaAE---------DPRDGLRRRLKAIGAHLGDEDAA 71
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 495775764 97 FPHRTVLENIIEGPVIVKGEPKEEATARAREL---------LAKVGLAGKETSY 141
Cdd:cd01125 72 LAENLVIENLRGKPVSIDAEAPELERIIEELEgvrliiidtLARVLHGGDENDA 125
|
|
| |
