|
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: 507.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 1 MSAIEVKSLVKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDAGRSLGPQKGLI 80
Cdd:PRK11264 1 MSAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLSQQKGLI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 81 RQLRQHVGFVFQNFNLFPHRTVLENIIEGPVIVKGEDKQESMARARELLAKVGLSGKENSYPRRLSGGQQQRVAIARALA 160
Cdd:PRK11264 81 RQLRQHVGFVFQNFNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 161 MRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGEAKALFASPQQPRT 240
Cdd:PRK11264 161 MRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPRT 240
|
250
....*....|
gi 1879798416 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 |
2.48e-163 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 451.37 E-value: 2.48e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 4 IEVKSLVKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDAGRSLgpqkglIRQL 83
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKD------INKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 84 RQHVGFVFQNFNLFPHRTVLENIIEGPVIVKGEDKQESMARARELLAKVGLSGKENSYPRRLSGGQQQRVAIARALAMRP 163
Cdd:COG1126 76 RRKVGMVFQQFNLFPHLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 164 DVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGEAKALFASPQQPRTRQF 243
Cdd:COG1126 156 KVMLFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHERTRAF 235
|
....
gi 1879798416 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 |
1.62e-133 |
|
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: 374.94 E-value: 1.62e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 4 IEVKSLVKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDAgrslgpQKGLIRQL 83
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTD------DKKNINEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 84 RQHVGFVFQNFNLFPHRTVLENIIEGPVIVKGEDKQESMARARELLAKVGLSGKENSYPRRLSGGQQQRVAIARALAMRP 163
Cdd:cd03262 75 RQKVGMVFQQFNLFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNP 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1879798416 164 DVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRI 222
Cdd:cd03262 155 KVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
3-244 |
2.36e-129 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 366.05 E-value: 2.36e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 3 AIEVKSLVKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTID--AGRSLGPQKGLI 80
Cdd:COG4598 8 ALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRlkPDRDGELVPADR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 81 RQL---RQHVGFVFQNFNLFPHRTVLENIIEGPVIVKGEDKQESMARARELLAKVGLSGKENSYPRRLSGGQQQRVAIAR 157
Cdd:COG4598 88 RQLqriRTRLGMVFQSFNLWSHMTVLENVIEAPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIAR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 158 ALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGEAKALFASPQQ 237
Cdd:COG4598 168 ALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVFGNPKS 247
|
....*..
gi 1879798416 238 PRTRQFL 244
Cdd:COG4598 248 ERLRQFL 254
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
4-245 |
5.77e-110 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 316.26 E-value: 5.77e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 4 IEVKSLVKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDAGRSLgpqkglIRQL 83
Cdd:PRK09493 2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVD------ERLI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 84 RQHVGFVFQNFNLFPHRTVLENIIEGPVIVKGEDKQESMARARELLAKVGLSGKENSYPRRLSGGQQQRVAIARALAMRP 163
Cdd:PRK09493 76 RQEAGMVFQQFYLFPHLTALENVMFGPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 164 DVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGEAKALFASPQQPRTRQF 243
Cdd:PRK09493 156 KLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEF 235
|
..
gi 1879798416 244 LE 245
Cdd:PRK09493 236 LQ 237
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
4-244 |
1.13e-100 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 296.22 E-value: 1.13e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 4 IEVKSLVKKFHGQ----TVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDA--GRSLgpqk 77
Cdd:COG1135 2 IELENLSKTFPTKggpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTAlsEREL---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 78 gliRQLRQHVGFVFQNFNLFPHRTVLENIiEGPVIVKGEDKQESMARARELLAKVGLSGKENSYPRRLSGGQQQRVAIAR 157
Cdd:COG1135 78 ---RAARRKIGMIFQHFNLLSSRTVAENV-ALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIAR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 158 ALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGEAKALFASPQ 236
Cdd:COG1135 154 ALANNPKVLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQ 233
|
....*...
gi 1879798416 237 QPRTRQFL 244
Cdd:COG1135 234 SELTRRFL 241
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1-244 |
7.38e-99 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 288.45 E-value: 7.38e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 1 MSaIEVKSLVKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDAGRSLGPQKglI 80
Cdd:COG4161 1 MS-IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDFSQKPSEKA--I 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 81 RQLRQHVGFVFQNFNLFPHRTVLENIIEGPVIVKGEDKQESMARARELLAKVGLSGKENSYPRRLSGGQQQRVAIARALA 160
Cdd:COG4161 78 RLLRQKVGMVFQQYNLWPHLTVMENLIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 161 MRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGEAkALFASPQQPRT 240
Cdd:COG4161 158 MEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDA-SHFTQPQTEAF 236
|
....
gi 1879798416 241 RQFL 244
Cdd:COG4161 237 AHYL 240
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
3-244 |
2.87e-97 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 284.21 E-value: 2.87e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 3 AIEVKSlVKKFHGQT-VLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDAGRSLGPQKglIR 81
Cdd:PRK11124 2 SIQLNG-INCFYGAHqALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSKTPSDKA--IR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 82 QLRQHVGFVFQNFNLFPHRTVLENIIEGPVIVKGEDKQESMARARELLAKVGLSGKENSYPRRLSGGQQQRVAIARALAM 161
Cdd:PRK11124 79 ELRRNVGMVFQQYNLWPHLTVQQNLIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 162 RPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGEAKAlFASPQQPRTR 241
Cdd:PRK11124 159 EPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASC-FTQPQTEAFK 237
|
...
gi 1879798416 242 QFL 244
Cdd:PRK11124 238 NYL 240
|
|
| ectoine_ehuA |
TIGR03005 |
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ... |
4-248 |
1.89e-94 |
|
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: 277.48 E-value: 1.89e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 4 IEVKSLVKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRV-GDVTID----AGRSLGPQKG 78
Cdd:TIGR03005 1 VRFSDVTKRFGILTVLDGLNFSVAAGEKVALIGPSGSGKSTILRILMTLEPIDEGQIQVeGEQLYHmpgrNGPLVPADEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 79 LIRQLRQHVGFVFQNFNLFPHRTVLENIIEGPVIVKGEDKQESMARARELLAKVGLSGKENSYPRRLSGGQQQRVAIARA 158
Cdd:TIGR03005 81 HLRQMRNKIGMVFQSFNLFPHKTVLDNVTEAPVLVLGMARAEAEKRAMELLDMVGLADKADHMPAQLSGGQQQRVAIARA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 159 LAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGEAKALFASPQQ 237
Cdd:TIGR03005 161 LAMRPKVMLFDEVTSALDPELVGEVLNVIRRLASEhDLTMLLVTHEMGFAREFADRVCFFDKGRIVEQGKPDEIFRQPKE 240
|
250
....*....|.
gi 1879798416 238 PRTRQFLEKFL 248
Cdd:TIGR03005 241 ERTREFLSKVI 251
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
4-236 |
3.32e-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: 265.98 E-value: 3.32e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 4 IEVKSLVKKFHGQ----TVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVG--DVTIDAGRSLgpqk 77
Cdd:cd03258 2 IELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDgtDLTLLSGKEL---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 78 gliRQLRQHVGFVFQNFNLFPHRTVLENIiEGPVIVKGEDKQESMARARELLAKVGLSGKENSYPRRLSGGQQQRVAIAR 157
Cdd:cd03258 78 ---RKARRRIGMIFQHFNLLSSRTVFENV-ALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIAR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 158 ALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADRAIFMDQGRIVEQGEAKALFASPQ 236
Cdd:cd03258 154 ALANNPKVLLCDEATSALDPETTQSILALLRDINRELGlTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-225 |
5.99e-90 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 264.98 E-value: 5.99e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 1 MSA-IEVKSLVKKFH----GQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTI----DAGR 71
Cdd:COG1136 1 MSPlLELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDIsslsEREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 72 SLgpqkglIRqlRQHVGFVFQNFNLFPHRTVLENIiEGPVIVKGEDKQESMARARELLAKVGLSGKENSYPRRLSGGQQQ 151
Cdd:COG1136 81 AR------LR--RRHIGFVFQFFNLLPELTALENV-ALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1879798416 152 RVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEK-RTMVIVTHEMSFARdVADRAIFMDQGRIVEQ 225
Cdd:COG1136 152 RVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELgTTIVMVTHDPELAA-RADRVIRLRDGRIVSD 225
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-222 |
4.40e-89 |
|
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: 262.43 E-value: 4.40e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 4 IEVKSLVKKFHGQ----TVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIdagRSLGPqKGL 79
Cdd:cd03255 1 IELKNLSKTYGGGgekvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDI---SKLSE-KEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 80 IRQLRQHVGFVFQNFNLFPHRTVLENIiEGPVIVKGEDKQESMARARELLAKVGLSGKENSYPRRLSGGQQQRVAIARAL 159
Cdd:cd03255 77 AAFRRRHIGFVFQSFNLLPDLTALENV-ELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1879798416 160 AMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEK-RTMVIVTHEMSFARDvADRAIFMDQGRI 222
Cdd:cd03255 156 ANDPKIILADEPTGNLDSETGKEVMELLRELNKEAgTTIVVVTHDPELAEY-ADRIIELRDGKI 218
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
4-244 |
3.76e-87 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 259.13 E-value: 3.76e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 4 IEVKSLVKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDAGRSLGPQ-----KG 78
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGQlkvadKN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 79 LIRQLRQHVGFVFQNFNLFPHRTVLENIIEGPVIVKGEDKQESMARARELLAKVGLSGK-ENSYPRRLSGGQQQRVAIAR 157
Cdd:PRK10619 86 QLRLLRTRLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERaQGKYPVHLSGGQQQRVSIAR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 158 ALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGEAKALFASPQQ 237
Cdd:PRK10619 166 ALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQS 245
|
....*..
gi 1879798416 238 PRTRQFL 244
Cdd:PRK10619 246 PRLQQFL 252
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-241 |
4.23e-86 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 259.65 E-value: 4.23e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 1 MSAIEVKSLVKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDAgrsLGPQKgli 80
Cdd:COG3842 3 MPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTG---LPPEK--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 81 rqlRqHVGFVFQNFNLFPHRTVLENIIEGPViVKGEDKQESMARARELLAKVGLSGKENSYPRRLSGGQQQRVAIARALA 160
Cdd:COG3842 77 ---R-NVGMVFQDYALFPHLTVAENVAFGLR-MRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 161 MRPDVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGEAKALFaspQQPR 239
Cdd:COG3842 152 PEPRVLLLDEPLSALDAKLREEMREELRRLQRElGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIY---ERPA 228
|
..
gi 1879798416 240 TR 241
Cdd:COG3842 229 TR 230
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-245 |
2.39e-85 |
|
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: 262.92 E-value: 2.39e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 4 IEVKSLVKKF-----HGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDAGRslgpqKG 78
Cdd:COG1123 261 LEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLS-----RR 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 79 LIRQLRQHVGFVFQNFN--LFPHRTVLENIIEGPVIVKGEDKQESMARARELLAKVGLSGK-ENSYPRRLSGGQQQRVAI 155
Cdd:COG1123 336 SLRELRRRVQMVFQDPYssLNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLPPDlADRYPHELSGGQRQRVAI 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 156 ARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGEAKALFAS 234
Cdd:COG1123 416 ARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFAN 495
|
250
....*....|.
gi 1879798416 235 PQQPRTRQFLE 245
Cdd:COG1123 496 PQHPYTRALLA 506
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
3-244 |
1.12e-83 |
|
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: 249.51 E-value: 1.12e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 3 AIEVKSLVKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDAGRslgpQKGLiRQ 82
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLS----EKEL-YE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 83 LRQHVGFVFQNFNLFPHRTVLENI----IEGPVIvkgeDKQESMARARELLAKVGLSGKENSYPRRLSGGQQQRVAIARA 158
Cdd:COG1127 80 LRRRIGMLFQGGALFDSLTVFENVafplREHTDL----SEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 159 LAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGEAKALFASPqQ 237
Cdd:COG1127 156 LALDPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASD-D 234
|
....*..
gi 1879798416 238 PRTRQFL 244
Cdd:COG1127 235 PWVRQFL 241
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-233 |
3.44e-82 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 245.32 E-value: 3.44e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 4 IEVKSLVKKFHGQT-VLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDAGRslgpqkglIRQ 82
Cdd:COG1122 1 IELENLSFSYPGGTpALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKN--------LRE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 83 LRQHVGFVFQN-FN-LFpHRTVLENIIEGPVIvKGEDKQESMARARELLAKVGLSGKENSYPRRLSGGQQQRVAIARALA 160
Cdd:COG1122 73 LRRKVGLVFQNpDDqLF-APTVEEDVAFGPEN-LGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1879798416 161 MRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGEAKALFA 233
Cdd:COG1122 151 MEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFS 223
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
3-244 |
1.12e-80 |
|
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: 242.20 E-value: 1.12e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 3 AIEVKSLVKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDaGRSLGPQKGLIRQ 82
Cdd:TIGR00972 1 AIEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMNDLVPGVRIEGKVLFD-GQDIYDKKIDVVE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 83 LRQHVGFVFQNFNLFPhRTVLENIIEGPVIVKGEDKQESMARARELLAKVGL----SGKENSYPRRLSGGQQQRVAIARA 158
Cdd:TIGR00972 80 LRRRVGMVFQKPNPFP-MSIYDNIAYGPRLHGIKDKKELDEIVEESLKKAALwdevKDRLHDSALGLSGGQQQRLCIARA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 159 LAMRPDVILFDEPTSALDPELVGEVLNTIRQLAqEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGEAKALFASPQQP 238
Cdd:TIGR00972 159 LAVEPEVLLLDEPTSALDPIATGKIEELIQELK-KKYTIVIVTHNMQQAARISDRTAFFYDGELVEYGPTEQIFTNPKEK 237
|
....*.
gi 1879798416 239 RTRQFL 244
Cdd:TIGR00972 238 RTEDYI 243
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
2-231 |
1.64e-80 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 241.88 E-value: 1.64e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 2 SAIEVKSLVKKFHGQT-VLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDA--GRSLgpqkg 78
Cdd:COG3638 1 PMLELRNLSKRYPGGTpALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTAlrGRAL----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 79 liRQLRQHVGFVFQNFNLFPHRTVLENIIEG-----PV------IVKGEDKQesmaRARELLAKVGLSGKENSYPRRLSG 147
Cdd:COG3638 76 --RRLRRRIGMIFQQFNLVPRLSVLTNVLAGrlgrtSTwrsllgLFPPEDRE----RALEALERVGLADKAYQRADQLSG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 148 GQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVT-HEMSFARDVADRAIFMDQGRIVEQG 226
Cdd:COG3638 150 GQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNlHQVDLARRYADRIIGLRDGRVVFDG 229
|
....*
gi 1879798416 227 EAKAL 231
Cdd:COG3638 230 PPAEL 234
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
4-243 |
3.13e-80 |
|
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: 240.87 E-value: 3.13e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 4 IEVKSLVKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDAGRslgpQKGLIRqL 83
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLS----EAELYR-L 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 84 RQHVGFVFQNFNLFPHRTVLENIiEGPVIVKGEDKQESM-ARARELLAKVGLSGKENSYPRRLSGGQQQRVAIARALAMR 162
Cdd:cd03261 76 RRRMGMLFQSGALFDSLTVFENV-AFPLREHTRLSEEEIrEIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 163 PDVILFDEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADRAIFMDQGRIVEQGEAKALFASpQQPRTR 241
Cdd:cd03261 155 PELLLYDEPTAGLDPIASGVIDDLIRSLKKELGlTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRAS-DDPLVR 233
|
..
gi 1879798416 242 QF 243
Cdd:cd03261 234 QF 235
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-244 |
4.46e-79 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 241.59 E-value: 4.46e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 1 MSaIEVKSLVKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVtiDAGRSLGPQKgli 80
Cdd:COG1118 1 MS-IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGR--DLFTNLPPRE--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 81 rqlRqHVGFVFQNFNLFPHRTVLENIIEGPViVKGEDKQESMARARELLAKVGLSGKENSYPRRLSGGQQQRVAIARALA 160
Cdd:COG1118 75 ---R-RVGFVFQHYALFPHMTVAENIAFGLR-VRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 161 MRPDVILFDEPTSALD----PELVGEVLNTIRQLaqeKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGEAKALFASPQ 236
Cdd:COG1118 150 VEPEVLLLDEPFGALDakvrKELRRWLRRLHDEL---GGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPA 226
|
....*...
gi 1879798416 237 QPRTRQFL 244
Cdd:COG1118 227 TPFVARFL 234
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
4-228 |
1.52e-78 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 236.10 E-value: 1.52e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 4 IEVKSLVKKF-HGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIdagRSLGPQKglIRQ 82
Cdd:COG2884 2 IRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDL---SRLKRRE--IPY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 83 LRQHVGFVFQNFNLFPHRTVLENIiEGPVIVKGEDKQESMARARELLAKVGLSGKENSYPRRLSGGQQQRVAIARALAMR 162
Cdd:COG2884 77 LRRRIGVVFQDFRLLPDRTVYENV-ALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNR 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1879798416 163 PDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGEA 228
Cdd:COG2884 156 PELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLVRDEAR 221
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-224 |
3.39e-78 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 236.52 E-value: 3.39e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 1 MSAIEVKSLVKKFH----GQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDagrslGPq 76
Cdd:COG1116 5 APALELRGVSKRFPtgggGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVT-----GP- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 77 kglirqlRQHVGFVFQNFNLFPHRTVLENIIEGPVIvKGEDKQESMARARELLAKVGLSGKENSYPRRLSGGQQQRVAIA 156
Cdd:COG1116 79 -------GPDRGVVFQEPALLPWLTVLDNVALGLEL-RGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 157 RALAMRPDVILFDEPTSALDP----ELVGEVLntiRQLAQEKRTMVIVTHemsfarDV------ADRAIFMDQ--GRIVE 224
Cdd:COG1116 151 RALANDPEVLLMDEPFGALDAltreRLQDELL---RLWQETGKTVLFVTH------DVdeavflADRVVVLSArpGRIVE 221
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-245 |
4.58e-78 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 235.34 E-value: 4.58e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 4 IEVKSLVKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDAGRslgpqkgliRQL 83
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDP---------AEV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 84 RQHVGFVFQNFNLFPHRTVLENIIegpVI--VKGEDKQESMARARELLAKVGLSGKENSYPRRLSGGQQQRVAIARALAM 161
Cdd:COG1131 72 RRRIGYVPQEPALYPDLTVRENLR---FFarLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLH 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 162 RPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGEAKALfaspqqprTR 241
Cdd:COG1131 149 DPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL--------KA 220
|
....
gi 1879798416 242 QFLE 245
Cdd:COG1131 221 RLLE 224
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
4-244 |
3.33e-76 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 234.31 E-value: 3.33e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 4 IEVKSLVKKFHGQ----TVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDAgrsLGPqKGL 79
Cdd:PRK11153 2 IELKNISKVFPQGgrtiHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTA---LSE-KEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 80 iRQLRQHVGFVFQNFNLFPHRTVLENIIEgPVIVKGEDKQESMARARELLAKVGLSGKENSYPRRLSGGQQQRVAIARAL 159
Cdd:PRK11153 78 -RKARRQIGMIFQHFNLLSSRTVFDNVAL-PLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 160 AMRPDVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGEAKALFASPQQP 238
Cdd:PRK11153 156 ASNPKVLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHP 235
|
....*.
gi 1879798416 239 RTRQFL 244
Cdd:PRK11153 236 LTREFI 241
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-221 |
6.32e-75 |
|
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: 225.14 E-value: 6.32e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 4 IEVKSLVKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDAGRslgpqkGLIRQL 83
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLE------DELPPL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 84 RQHVGFVFQNFNLFPHRTVLENIIEGpvivkgedkqesmararellakvglsgkensyprrLSGGQQQRVAIARALAMRP 163
Cdd:cd03229 75 RRRIGMVFQDFALFPHLTVLENIALG-----------------------------------LSGGQQQRVALARALAMDP 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1879798416 164 DVILFDEPTSALDPELVGEVLNTIRQL-AQEKRTMVIVTHEMSFARDVADRAIFMDQGR 221
Cdd:cd03229 120 DVLLLDEPTSALDPITRREVRALLKSLqAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-245 |
1.39e-74 |
|
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: 226.99 E-value: 1.39e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 3 AIEVKSLVKKF----HGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGdvtidaGRSLGPQKG 78
Cdd:COG1124 1 MLEVRNLSVSYgqggRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFD------GRPVTRRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 79 liRQLRQHVGFVFQN----FNlfPHRTVLENIIEgPVIVKGEDKQEsmARARELLAKVGLSGKE-NSYPRRLSGGQQQRV 153
Cdd:COG1124 75 --KAFRRRVQMVFQDpyasLH--PRHTVDRILAE-PLRIHGLPDRE--ERIAELLEQVGLPPSFlDRYPHQLSGGQRQRV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 154 AIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQL-AQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGEAKALF 232
Cdd:COG1124 148 AIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLrEERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLL 227
|
250
....*....|...
gi 1879798416 233 ASPQQPRTRQFLE 245
Cdd:COG1124 228 AGPKHPYTRELLA 240
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-231 |
1.21e-73 |
|
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: 224.37 E-value: 1.21e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 4 IEVKSLVKKF-HGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIdagRSLGPQKglIRQ 82
Cdd:cd03256 1 IEVENLSKTYpNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDI---NKLKGKA--LRQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 83 LRQHVGFVFQNFNLFPHRTVLENIIEG-----------PVIVKGEDKQesmaRARELLAKVGLSGKENSYPRRLSGGQQQ 151
Cdd:cd03256 76 LRRQIGMIFQQFNLIERLSVLENVLSGrlgrrstwrslFGLFPKEEKQ----RALAALERVGLLDKAYQRADQLSGGQQQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 152 RVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEK-RTMVIVTHEMSFARDVADRAIFMDQGRIVEQGEAKA 230
Cdd:cd03256 152 RVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEgITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAE 231
|
.
gi 1879798416 231 L 231
Cdd:cd03256 232 L 232
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-226 |
3.93e-73 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 222.01 E-value: 3.93e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 4 IEVKSLVKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDagrSLGPQKGlirql 83
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVT---GVPPERR----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 84 rqHVGFVFQNFNLFPHRTVLENIIEGPViVKGEDKQESMARARELLAKVGLSGKENSYPRRLSGGQQQRVAIARALAMRP 163
Cdd:cd03259 73 --NIGMVFQDYALFPHLTVAENIAFGLK-LRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1879798416 164 DVILFDEPTSALDPELVGEVLNTIRQL-AQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQG 226
Cdd:cd03259 150 SLLLLDEPLSALDAKLREELREELKELqRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
4-244 |
6.87e-73 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 224.58 E-value: 6.87e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 4 IEVKSLVKKF-HGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIdagRSLGPQkglirQ 82
Cdd:COG1125 2 IEFENVTKRYpDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDI---RDLDPV-----E 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 83 LRQHVGFVFQNFNLFPHRTVLENIiegpVIV---KGEDKQESMARARELLAKVGLSGKE--NSYPRRLSGGQQQRVAIAR 157
Cdd:COG1125 74 LRRRIGYVIQQIGLFPHMTVAENI----ATVprlLGWDKERIRARVDELLELVGLDPEEyrDRYPHELSGGQQQRVGVAR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 158 ALAMRPDVILFDEPTSALDP----ELVGEVLNTIRQLaqeKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGEAKALFA 233
Cdd:COG1125 150 ALAADPPILLMDEPFGALDPitreQLQDELLRLQREL---GKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILA 226
|
250
....*....|.
gi 1879798416 234 SPQQPRTRQFL 244
Cdd:COG1125 227 NPANDFVADFV 237
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-225 |
6.92e-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: 221.58 E-value: 6.92e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 4 IEVKSLVKKFHG----QTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGdvtidaGRSlgpqkgl 79
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVD------GEP------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 80 IRQLRQHVGFVFQNFNLFPHRTVLENIIEGPVIvKGEDKQESMARARELLAKVGLSGKENSYPRRLSGGQQQRVAIARAL 159
Cdd:cd03293 68 VTGPGPDRGYVFQQDALLPWLTVLDNVALGLEL-QGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARAL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1879798416 160 AMRPDVILFDEPTSALDP---ELVGEVLntIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQ--GRIVEQ 225
Cdd:cd03293 147 AVDPDVLLLDEPFSALDAltrEQLQEEL--LDIWRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRIVAE 215
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-235 |
9.64e-73 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 225.72 E-value: 9.64e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 1 MSAIEVKSLVKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDagrSLGPQKgli 80
Cdd:COG3839 1 MASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVT---DLPPKD--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 81 RqlrqHVGFVFQNFNLFPHRTVLENiIEGPVIVKGEDKQESMARARELLAKVGLSGKENSYPRRLSGGQQQRVAIARALA 160
Cdd:COG3839 75 R----NIAMVFQSYALYPHMTVYEN-IAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 161 MRPDVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHE----MSFardvADRAIFMDQGRIVEQGEAKALFASP 235
Cdd:COG3839 150 REPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRlGTTTIYVTHDqveaMTL----ADRIAVMNDGRIQQVGTPEELYDRP 225
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-244 |
3.02e-72 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 221.06 E-value: 3.02e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 2 SAIEVKSLVKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLL--EQPE---SGTIRVGDVTIdagrsLGPQ 76
Cdd:COG1117 10 PKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndLIPGarvEGEILLDGEDI-----YDPD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 77 KGLIrQLRQHVGFVFQNFNLFPHrTVLENIIEGPVIVKGEDKQESMARARELLAKVGL----SGKENSYPRRLSGGQQQR 152
Cdd:COG1117 85 VDVV-ELRRRVGMVFQKPNPFPK-SIYDNVAYGLRLHGIKSKSELDEIVEESLRKAALwdevKDRLKKSALGLSGGQQQR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 153 VAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAqEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGEAKALF 232
Cdd:COG1117 163 LCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELK-KDYTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIF 241
|
250
....*....|..
gi 1879798416 233 ASPQQPRTRQFL 244
Cdd:COG1117 242 TNPKDKRTEDYI 253
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
16-221 |
1.79e-71 |
|
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: 217.72 E-value: 1.79e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 16 QTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDAGRslgpqkglIRQLRQHVGFVFQNFN 95
Cdd:cd03225 14 RPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLS--------LKELRRKVGLVFQNPD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 96 L-FPHRTVLENIIEGPVIvKGEDKQESMARARELLAKVGLSGKENSYPRRLSGGQQQRVAIARALAMRPDVILFDEPTSA 174
Cdd:cd03225 86 DqFFGPTVEEEVAFGLEN-LGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAG 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1879798416 175 LDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGR 221
Cdd:cd03225 165 LDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
4-226 |
1.45e-70 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 215.83 E-value: 1.45e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 4 IEVKSLVKKFHGQ----TVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVgdvtidAGRSLGPQKGL 79
Cdd:cd03257 2 LEVKNLSVSFPTGggsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIF------DGKDLLKLSRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 80 IRQLR-QHVGFVFQN--FNLFPHRTVLENIIEGPVIVKGEDKQESMARAR-ELLAKVGLSGK-ENSYPRRLSGGQQQRVA 154
Cdd:cd03257 76 LRKIRrKEIQMVFQDpmSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVlLLLVGVGLPEEvLNRYPHELSGGQRQRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1879798416 155 IARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEK-RTMVIVTHEMSFARDVADRAIFMDQGRIVEQG 226
Cdd:cd03257 156 IARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELgLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-231 |
2.08e-70 |
|
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: 215.51 E-value: 2.08e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 4 IEVKSLVKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDAGRSLGPQKGLIRqL 83
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGAPDEGEVLLDGKDIYDLDVDVLE-L 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 84 RQHVGFVFQNFNLFPhRTVLENIIEGPVIVKGEDKQESMARARELLAKVGLSG--KENSYPRRLSGGQQQRVAIARALAM 161
Cdd:cd03260 80 RRRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALWDevKDRLHALGLSGGQQQRLCLARALAN 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 162 RPDVILFDEPTSALDPELVGEVLNTIRQLAQEkRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGEAKAL 231
Cdd:cd03260 159 EPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-241 |
4.53e-69 |
|
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: 215.30 E-value: 4.53e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 4 IEVKSLVKKFHGQ----TVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSI-NLLEQP--ESGTIRVGDVTIdagRSLGPQ 76
Cdd:COG0444 2 LEVRNLKVYFPTRrgvvKAVDGVSFDVRRGETLGLVGESGSGKSTLARAIlGLLPPPgiTSGEILFDGEDL---LKLSEK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 77 KglIRQLR-QHVGFVFQN----FNlfPHRTVLENIIEGPVIVKGEDKQESMARARELLAKVGLSGKE---NSYPRRLSGG 148
Cdd:COG0444 79 E--LRKIRgREIQMIFQDpmtsLN--PVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLPDPErrlDRYPHELSGG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 149 QQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADRAIFMDQGRIVEQGE 227
Cdd:COG0444 155 MRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGlAILFITHDLGVVAEIADRVAVMYAGRIVEEGP 234
|
250
....*....|....
gi 1879798416 228 AKALFASPQQPRTR 241
Cdd:COG0444 235 VEELFENPRHPYTR 248
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
4-246 |
3.90e-68 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 210.23 E-value: 3.90e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 4 IEVKSLVKKF-HGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIdagRSLGPQkglirQ 82
Cdd:cd03295 1 IEFENVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDI---REQDPV-----E 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 83 LRQHVGFVFQNFNLFPHRTVLENIIEGPVIvKGEDKQESMARARELLAKVGLSGKE--NSYPRRLSGGQQQRVAIARALA 160
Cdd:cd03295 73 LRRKIGYVIQQIGLFPHMTVEENIALVPKL-LKWPKEKIRERADELLALVGLDPAEfaDRYPHELSGGQQQRVGVARALA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 161 MRPDVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGEAKALFASPQQPR 239
Cdd:cd03295 152 ADPPLLLMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDF 231
|
....*..
gi 1879798416 240 TRQFLEK 246
Cdd:cd03295 232 VAEFVGA 238
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
16-247 |
1.11e-67 |
|
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: 210.39 E-value: 1.11e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 16 QTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDAGrslgpQKGLIRQLRQHVGFVFQnfn 95
Cdd:TIGR04521 18 KKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAK-----KKKKLKDLRKKVGLVFQ--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 96 lFPH-----RTVLENIIEGPVIVkGEDKQESMARARELLAKVGLSG--KENSyPRRLSGGQQQRVAIARALAMRPDVILF 168
Cdd:TIGR04521 90 -FPEhqlfeETVYKDIAFGPKNL-GLSEEEAEERVKEALELVGLDEeyLERS-PFELSGGQMRRVAIAGVLAMEPEVLIL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 169 DEPTSALDPELVGEVLNTIRQLAQEK-RTMVIVTHEMSFARDVADRAIFMDQGRIVEQGEAKALFASPqqprtrQFLEKF 247
Cdd:TIGR04521 167 DEPTAGLDPKGRKEILDLFKRLHKEKgLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDV------DELEKI 240
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-230 |
3.59e-67 |
|
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: 207.29 E-value: 3.59e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 2 SAIEVKSLVKKFHGQ----TVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVgdvtidAGRSLGP-- 75
Cdd:COG4181 7 PIIELRGLTKTVGTGagelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRL------AGQDLFAld 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 76 QKGLIRQLRQHVGFVFQNFNLFPHRTVLENIIEgPVIVKGEDkqESMARARELLAKVGLSGKENSYPRRLSGGQQQRVAI 155
Cdd:COG4181 81 EDARARLRARHVGFVFQSFQLLPTLTALENVML-PLELAGRR--DARARARALLERVGLGHRLDHYPAQLSGGEQQRVAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1879798416 156 ARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDvADRAIFMDQGRIVEQGEAKA 230
Cdd:COG4181 158 ARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGtTLVLVTHDPALAAR-CDRVLRLRAGRLVEDTAATA 232
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
4-231 |
9.65e-67 |
|
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: 206.77 E-value: 9.65e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 4 IEVKSLVKKF-HGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGtirvgDVTIDaGRSLGPQKGL-IR 81
Cdd:TIGR02315 2 LEVENLSKVYpNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSG-----SILLE-GTDITKLRGKkLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 82 QLRQHVGFVFQNFNLFPHRTVLENIIEGPVIVKG-----------EDKQesmaRARELLAKVGLSGKENSYPRRLSGGQQ 150
Cdd:TIGR02315 76 KLRRRIGMIFQHYNLIERLTVLENVLHGRLGYKPtwrsllgrfseEDKE----RALSALERVGLADKAYQRADQLSGGQQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 151 QRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVT-HEMSFARDVADRAIFMDQGRIVEQGEAK 229
Cdd:TIGR02315 152 QRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINlHQVDLAKKYADRIVGLKAGEIVFDGAPS 231
|
..
gi 1879798416 230 AL 231
Cdd:TIGR02315 232 EL 233
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
1-235 |
2.86e-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: 210.34 E-value: 2.86e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 1 MSAIEVKSLVKKF-----------------------HGQTV-LHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPE 56
Cdd:COG4175 1 MPKIEVRNLYKIFgkrperalklldqgkskdeilekTGQTVgVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 57 SGTIRVGDVTIdagRSLGPQKglIRQLRQH-VGFVFQNFNLFPHRTVLENIiEGPVIVKGEDKQESMARARELLAKVGLS 135
Cdd:COG4175 81 AGEVLIDGEDI---TKLSKKE--LRELRRKkMSMVFQHFALLPHRTVLENV-AFGLEIQGVPKAERRERAREALELVGLA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 136 GKENSYPRRLSGGQQQRVAIARALAMRPDVILFDEPTSALDP----ELVGEVLntirQL-AQEKRTMVIVTHEMSFARDV 210
Cdd:COG4175 155 GWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDPlirrEMQDELL----ELqAKLKKTIVFITHDLDEALRL 230
|
250 260
....*....|....*....|....*
gi 1879798416 211 ADRAIFMDQGRIVEQGEAKALFASP 235
Cdd:COG4175 231 GDRIAIMKDGRIVQIGTPEEILTNP 255
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
3-244 |
6.75e-66 |
|
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: 204.50 E-value: 6.75e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 3 AIEVKSLVKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVG--DVTidagrSLGPQKgli 80
Cdd:cd03296 2 SIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGgeDAT-----DVPVQE--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 81 rqlRQhVGFVFQNFNLFPHRTVLENIIEGPVIVKGE---DKQESMARARELLAKVGLSGKENSYPRRLSGGQQQRVAIAR 157
Cdd:cd03296 74 ---RN-VGFVFQHYALFRHMTVFDNVAFGLRVKPRSerpPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALAR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 158 ALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADRAIFMDQGRIVEQGEAKALFASPQ 236
Cdd:cd03296 150 ALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHvTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPA 229
|
....*...
gi 1879798416 237 QPRTRQFL 244
Cdd:cd03296 230 SPFVYSFL 237
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
7-245 |
1.92e-65 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 204.41 E-value: 1.92e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 7 KSLVKKFHGQTV-LHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDAGRslgpqKGLIRQLRQ 85
Cdd:cd03294 27 KEEILKKTGQTVgVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMS-----RKELRELRR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 86 H-VGFVFQNFNLFPHRTVLENIIEGpVIVKGEDKQESMARARELLAKVGLSGKENSYPRRLSGGQQQRVAIARALAMRPD 164
Cdd:cd03294 102 KkISMVFQSFALLPHRTVLENVAFG-LEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPD 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 165 VILFDEPTSALDPELVGEVLNTIRQL-AQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGEAKALFASPQQPRTRQF 243
Cdd:cd03294 181 ILLMDEAFSALDPLIRREMQDELLRLqAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREF 260
|
..
gi 1879798416 244 LE 245
Cdd:cd03294 261 FR 262
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-233 |
8.93e-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: 202.66 E-value: 8.93e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 4 IEVKSLVKKFHGQT--VLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRV-GDVTIDAGRslgpqkglI 80
Cdd:TIGR04520 1 IEVENVSFSYPESEkpALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVdGLDTLDEEN--------L 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 81 RQLRQHVGFVFQN-FNLFPHRTV-------LENIiegpvivkGEDKQESMARARELLAKVGLSGKENSYPRRLSGGQQQR 152
Cdd:TIGR04520 73 WEIRKKVGMVFQNpDNQFVGATVeddvafgLENL--------GVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 153 VAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQL-AQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGEAKAL 231
Cdd:TIGR04520 145 VAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLnKEEGITVISITHDMEEAVL-ADRVIVMNKGKIVAEGTPREI 223
|
..
gi 1879798416 232 FA 233
Cdd:TIGR04520 224 FS 225
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-237 |
1.12e-64 |
|
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: 209.37 E-value: 1.12e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 3 AIEVKSLVKKFHGQT--VLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLeQPESGTIRvGDVTIDaGRSLGPQKGLI 80
Cdd:COG1123 4 LLEVRDLSVRYPGGDvpAVDGVSLTIAPGETVALVGESGSGKSTLALALMGL-LPHGGRIS-GEVLLD-GRDLLELSEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 81 RqlRQHVGFVFQNF--NLFPHrTVLENIIEGPVIvKGEDKQESMARARELLAKVGLSGKENSYPRRLSGGQQQRVAIARA 158
Cdd:COG1123 81 R--GRRIGMVFQDPmtQLNPV-TVGDQIAEALEN-LGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 159 LAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEK-RTMVIVTHEMSFARDVADRAIFMDQGRIVEQGEAKALFASPQQ 237
Cdd:COG1123 157 LALDPDLLIADEPTTALDVTTQAEILDLLRELQRERgTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQA 236
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-248 |
8.74e-64 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 198.61 E-value: 8.74e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 4 IEVKSLVKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDAgrsLGPQKglirql 83
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITN---LPPHK------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 84 rQHVGFVFQNFNLFPHRTVLENIIEGpVIVKGEDKQESMARARELLAKVGLSGKENSYPRRLSGGQQQRVAIARALAMRP 163
Cdd:cd03300 72 -RPVNTVFQNYALFPHLTVFENIAFG-LRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 164 DVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGEAKALFaspQQPRTRq 242
Cdd:cd03300 150 KVLLLDEPLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIY---EEPANR- 225
|
....*.
gi 1879798416 243 FLEKFL 248
Cdd:cd03300 226 FVADFI 231
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
1-247 |
7.88e-63 |
|
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: 200.26 E-value: 7.88e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 1 MSAIEVKSLVKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDAgrsLGPQKgli 80
Cdd:TIGR03265 2 SPYLSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITR---LPPQK--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 81 rqlrQHVGFVFQNFNLFPHRTVLENIIEGpVIVKGEDKQESMARARELLAKVGLSGKENSYPRRLSGGQQQRVAIARALA 160
Cdd:TIGR03265 76 ----RDYGIVFQSYALFPNLTVADNIAYG-LKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 161 MRPDVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGEAKALFaspQQPR 239
Cdd:TIGR03265 151 TSPGLLLLDEPLSALDARVREHLRTEIRQLQRRlGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIY---RHPA 227
|
....*...
gi 1879798416 240 TRqFLEKF 247
Cdd:TIGR03265 228 TP-FVADF 234
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4-222 |
1.15e-61 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 192.72 E-value: 1.15e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 4 IEVKSLVKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDAGRslgpqkglIRQL 83
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMP--------PPEW 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 84 RQHVGFVFQNFNLFPHrTVLENIIEGPVIvkgEDKQESMARARELLAKVGLSGKENSYP-RRLSGGQQQRVAIARALAMR 162
Cdd:COG4619 73 RRQVAYVPQEPALWGG-TVRDNLPFPFQL---RERKFDRERALELLERLGLPPDILDKPvERLSGGERQRLALIRALLLQ 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1879798416 163 PDVILFDEPTSALDPELVGEVLNTIRQLAQEK-RTMVIVTHEMSFARDVADRAIFMDQGRI 222
Cdd:COG4619 149 PDVLLLDEPTSALDPENTRRVEELLREYLAEEgRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
4-244 |
1.20e-61 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 193.43 E-value: 1.20e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 4 IEVKSLVKKFHGQTvLHgIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDAgrsLGPQKglirql 83
Cdd:COG3840 2 LRLDDLTYRYGDFP-LR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTA---LPPAE------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 84 RQhVGFVFQNFNLFPHRTVLENIIEGpvIVKG-----EDKQesmaRARELLAKVGLSGKENSYPRRLSGGQQQRVAIARA 158
Cdd:COG3840 71 RP-VSMLFQENNLFPHLTVAQNIGLG--LRPGlkltaEQRA----QVEQALERVGLAGLLDRLPGQLSGGQRQRVALARC 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 159 LAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGEAKALFASPQQ 237
Cdd:COG3840 144 LVRKRPILLLDEPFSALDPALRQEMLDLVDELCRErGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPP 223
|
....*..
gi 1879798416 238 PRTRQFL 244
Cdd:COG3840 224 PALAAYL 230
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
4-250 |
2.27e-61 |
|
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: 193.15 E-value: 2.27e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 4 IEVKSLVKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDAGRslgpqkgliRQL 83
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEP---------REA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 84 RQHVGFVFQNFNLFPHRTVLENI-IEGPVivKGEDKQESMARARELLAKVGLSGKENSYPRRLSGGQQQRVAIARALAMR 162
Cdd:COG4555 73 RRQIGVLPDERGLYDRLTVRENIrYFAEL--YGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 163 PDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGEAKALfaspQQPRTRQ 242
Cdd:COG4555 151 PKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL----REEIGEE 226
|
....*...
gi 1879798416 243 FLEKFLMQ 250
Cdd:COG4555 227 NLEDAFVA 234
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
4-241 |
9.46e-61 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 194.18 E-value: 9.46e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 4 IEVKSLVKKF---------HGQTV--LHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVG--DVTIDAG 70
Cdd:COG4608 8 LEVRDLKKHFpvrgglfgrTVGVVkaVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDgqDITGLSG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 71 RSLgpqkgliRQLRQHVGFVFQN----FNlfPHRTVLENIIEGPVIVKGEDKQESMARARELLAKVGLSgKE--NSYPRR 144
Cdd:COG4608 88 REL-------RPLRRRMQMVFQDpyasLN--PRMTVGDIIAEPLRIHGLASKAERRERVAELLELVGLR-PEhaDRYPHE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 145 LSGGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIV 223
Cdd:COG4608 158 FSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDElGLTYLFISHDLSVVRHISDRVAVMYLGKIV 237
|
250
....*....|....*...
gi 1879798416 224 EQGEAKALFASPQQPRTR 241
Cdd:COG4608 238 EIAPRDELYARPLHPYTQ 255
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-222 |
1.59e-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: 1.59e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 4 IEVKSLVKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDAGRslgpqkgliRQL 83
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEP---------EEV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 84 RQHVGFVFQNFNLFPHRTVLENIiegpvivkgedkqesmararellakvglsgkensyprRLSGGQQQRVAIARALAMRP 163
Cdd:cd03230 72 KRRIGYLPEEPSLYENLTVRENL-------------------------------------KLSGGMKQRLALAQALLHDP 114
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1879798416 164 DVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRI 222
Cdd:cd03230 115 ELLILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-232 |
1.59e-60 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 191.03 E-value: 1.59e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 3 AIEVKSLVKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIdagRSLGPqkgliRQ 82
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDL---ASLSR-----RE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 83 LRQHVGFVFQ----NFNL----------FPHRTVLeniiegpvivkGEDKQESMARARELLAKVGLSGKENSYPRRLSGG 148
Cdd:COG1120 73 LARRIAYVPQeppaPFGLtvrelvalgrYPHLGLF-----------GRPSAEDREAVEEALERTGLEHLADRPVDELSGG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 149 QQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEK-RTMVIVTHEMSFARDVADRAIFMDQGRIVEQGE 227
Cdd:COG1120 142 ERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERgRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGP 221
|
....*
gi 1879798416 228 AKALF 232
Cdd:COG1120 222 PEEVL 226
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-236 |
2.09e-60 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 190.34 E-value: 2.09e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 4 IEVKSLVKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDAgrsLGPQK----GL 79
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITG---LPPHEiarlGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 80 IRqlrqhvgfVFQNFNLFPHRTVLENIIEGPVIVKGE---------DKQESMARARELLAKVGLSGKENSYPRRLSGGQQ 150
Cdd:cd03219 78 GR--------TFQIPRLFPELTVLENVMVAAQARTGSglllararrEEREARERAEELLERVGLADLADRPAGELSYGQQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 151 QRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGEAKA 230
Cdd:cd03219 150 RRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDE 229
|
....*.
gi 1879798416 231 LFASPQ 236
Cdd:cd03219 230 VRNNPR 235
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-236 |
4.73e-60 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 189.86 E-value: 4.73e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 1 MSAIEVKSLVKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDAgrsLGP----Q 76
Cdd:COG0411 2 DPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITG---LPPhriaR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 77 KGLIRqlrqhvgfVFQNFNLFPHRTVLENIIEGPVIVKGE--------------DKQESMARARELLAKVGLSGKENSYP 142
Cdd:COG0411 79 LGIAR--------TFQNPRLFPELTVLENVLVAAHARLGRgllaallrlprarrEEREARERAEELLERVGLADRADEPA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 143 RRLSGGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGR 221
Cdd:COG0411 151 GNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDErGITILLIEHDMDLVMGLADRIVVLDFGR 230
|
250
....*....|....*
gi 1879798416 222 IVEQGEAKALFASPQ 236
Cdd:COG0411 231 VIAEGTPAEVRADPR 245
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
6-217 |
4.83e-60 |
|
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: 188.21 E-value: 4.83e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 6 VKSLVKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDAGRSLgpQKGLIRqlRQ 85
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSK--KASKFR--RE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 86 HVGFVFQNFNLFPHRTVLENIIEGPVIVKGeDKQESMARARELLAKVGLSGKENSYPRRLSGGQQQRVAIARALAMRPDV 165
Cdd:TIGR03608 77 KLGYLFQNFALIENETVEENLDLGLKYKKL-SKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1879798416 166 ILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFArDVADRAIFM 217
Cdd:TIGR03608 156 ILADEPTGSLDPKNRDEVLDLLLELNDEGKTIIIVTHDPEVA-KQADRVIEL 206
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
3-233 |
6.18e-59 |
|
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: 198.13 E-value: 6.18e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 3 AIEVKSLVKKFHGQT--VLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIdagRSLGPqkgli 80
Cdd:COG2274 473 DIELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDL---RQIDP----- 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 81 RQLRQHVGFVFQNFNLFpHRTVLENIIEGpvivkgeDKQESMARARELLAKVGLSGKENSYP-----------RRLSGGQ 149
Cdd:COG2274 545 ASLRRQIGVVLQDVFLF-SGTIRENITLG-------DPDATDEEIIEAARLAGLHDFIEALPmgydtvvgeggSNLSGGQ 616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 150 QQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQeKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGEAK 229
Cdd:COG2274 617 RQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK-GRTVIIIAHRLSTIRL-ADRIIVLDKGRIVEDGTHE 694
|
....
gi 1879798416 230 ALFA 233
Cdd:COG2274 695 ELLA 698
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-222 |
1.05e-57 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 183.75 E-value: 1.05e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 1 MSAIEVKSLVKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIdagrslgpqkgli 80
Cdd:COG1121 4 MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPP------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 81 RQLRQHVGFVFQNFNL---FPhRTVLE----------NIIEGPvivKGEDKQesmaRARELLAKVGLSGKENSYPRRLSG 147
Cdd:COG1121 71 RRARRRIGYVPQRAEVdwdFP-ITVRDvvlmgrygrrGLFRRP---SRADRE----AVDEALERVGLEDLADRPIGELSG 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1879798416 148 GQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRI 222
Cdd:COG1121 143 GQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLV 217
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
10-231 |
2.69e-57 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 181.86 E-value: 2.69e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 10 VKKFHGQT-VLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDAGRSlgpqkglIRQLRQHVG 88
Cdd:cd03224 6 LNAGYGKSqILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPP-------HERARAGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 89 FVFQNFNLFPHRTVLENIIEGPVIVKGEDKQESMARARELLAKvgLSGKENSYPRRLSGGQQQRVAIARALAMRPDVILF 168
Cdd:cd03224 79 YVPEGRRIFPELTVEENLLLGAYARRRAKRKARLERVYELFPR--LKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1879798416 169 DEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGEAKAL 231
Cdd:cd03224 157 DEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-248 |
1.43e-56 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 184.13 E-value: 1.43e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 1 MSaIEVKSLVKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVG--DVTIDAGRSlgpqkg 78
Cdd:PRK10851 1 MS-IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHgtDVSRLHARD------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 79 lirqlrQHVGFVFQNFNLFPHRTVLENIIEGPVIVKGEDKQESMA---RARELLAKVGLSGKENSYPRRLSGGQQQRVAI 155
Cdd:PRK10851 74 ------RKVGFVFQHYALFRHMTVFDNIAFGLTVLPRRERPNAAAikaKVTQLLEMVQLAHLADRYPAQLSGGQKQRVAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 156 ARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGeakalfaS 234
Cdd:PRK10851 148 ARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAG-------T 220
|
250
....*....|....*...
gi 1879798416 235 PQQ----PRTRQFLEkFL 248
Cdd:PRK10851 221 PDQvwrePATRFVLE-FM 237
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-226 |
4.95e-56 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 178.22 E-value: 4.95e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 4 IEVKSLVKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVG--DVTidagrSLGPQKglir 81
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGgrDVT-----DLPPKD---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 82 qlrQHVGFVFQNFNLFPHRTVLENIiEGPVIVKGEDKQESMARARELLAKVGLSGKENSYPRRLSGGQQQRVAIARALAM 161
Cdd:cd03301 72 ---RDIAMVFQNYALYPHMTVYDNI-AFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVR 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1879798416 162 RPDVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQG 226
Cdd:cd03301 148 EPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRlGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
4-248 |
1.29e-55 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 181.84 E-value: 1.29e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 4 IEVKSLVKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVG--DVTidagrslgpqKGLIR 81
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDgeDVT----------HRSIQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 82 QlrQHVGFVFQNFNLFPHRTVLENIIEGpVIVKGEDKQESMARARELLAKVGLSGKENSYPRRLSGGQQQRVAIARALAM 161
Cdd:PRK11432 77 Q--RDICMVFQSYALFPHMSLGENVGYG-LKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALIL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 162 RPDVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGEAKALFaspQQPRT 240
Cdd:PRK11432 154 KPKVLLFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELY---RQPAS 230
|
....*...
gi 1879798416 241 RqFLEKFL 248
Cdd:PRK11432 231 R-FMASFM 237
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
19-221 |
3.07e-55 |
|
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: 176.28 E-value: 3.07e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 19 LHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVgdvtidAGRSLGPQKG-LIRQLRQHVGFVFQNFNLF 97
Cdd:TIGR02673 18 LHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRI------AGEDVNRLRGrQLPLLRRRIGVVFQDFRLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 98 PHRTVLENIIEgPVIVKGEDKQESMARARELLAKVGLSGKENSYPRRLSGGQQQRVAIARALAMRPDVILFDEPTSALDP 177
Cdd:TIGR02673 92 PDRTVYENVAL-PLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLADEPTGNLDP 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1879798416 178 ELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGR 221
Cdd:TIGR02673 171 DLSERILDLLKRLNKRGTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
19-245 |
5.82e-55 |
|
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: 184.50 E-value: 5.82e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 19 LHGIDLEVQKGEVVAIIGPSGSGKTTLLRSI-NLLEQpeSGTIRVGDVTIDAGRslgpQKGLiRQLRQHVGFVFQN-FN- 95
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALlRLIPS--EGEIRFDGQDLDGLS----RRAL-RPLRRRMQVVFQDpFGs 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 96 LFPHRTVLENIIEGPVIVK-GEDKQESMARARELLAKVGLSGK-ENSYPRRLSGGQQQRVAIARALAMRPDVILFDEPTS 173
Cdd:COG4172 375 LSPRMTVGQIIAEGLRVHGpGLSAAERRARVAEALEEVGLDPAaRHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTS 454
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1879798416 174 ALDPELVGEVLNTIRQLaQEKR--TMVIVTHEMSFARDVADRAIFMDQGRIVEQGEAKALFASPQQPRTRQFLE 245
Cdd:COG4172 455 ALDVSVQAQILDLLRDL-QREHglAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDAPQHPYTRALLA 527
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
15-221 |
8.18e-55 |
|
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: 173.72 E-value: 8.18e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 15 GQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIdagRSLGPqkgliRQLRQHVGFVFQNF 94
Cdd:cd03228 14 PKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDL---RDLDL-----ESLRKNIAYVPQDP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 95 NLFpHRTVLENIiegpvivkgedkqesmararellakvglsgkensyprrLSGGQQQRVAIARALAMRPDVILFDEPTSA 174
Cdd:cd03228 86 FLF-SGTIRENI--------------------------------------LSGGQRQRIAIARALLRDPPILILDEATSA 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1879798416 175 LDPELVGEVLNTIRQLAQEkRTMVIVTHEMSFARDvADRAIFMDQGR 221
Cdd:cd03228 127 LDPETEALILEALRALAKG-KTVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
4-222 |
1.35e-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: 174.90 E-value: 1.35e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 4 IEVKSLVKKF-HGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDagrslGPQKGLIRQ 82
Cdd:cd03292 1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVS-----DLRGRAIPY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 83 LRQHVGFVFQNFNLFPHRTVLENIIEgPVIVKGEDKQESMARARELLAKVGLSGKENSYPRRLSGGQQQRVAIARALAMR 162
Cdd:cd03292 76 LRRKIGVVFQDFRLLPDRNVYENVAF-ALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNS 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 163 PDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRI 222
Cdd:cd03292 155 PTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
4-244 |
1.41e-54 |
|
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: 175.22 E-value: 1.41e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 4 IEVKSLVKKFhGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVG--DVTidagrSLGPQKglir 81
Cdd:cd03299 1 LKVENLSKDW-KEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNgkDIT-----NLPPEK---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 82 qlrQHVGFVFQNFNLFPHRTVLENIIEGpVIVKGEDKQESMARARELLAKVGLSGKENSYPRRLSGGQQQRVAIARALAM 161
Cdd:cd03299 71 ---RDISYVPQNYALFPHMTVYKNIAYG-LKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 162 RPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVI-VTHEMSFARDVADRAIFMDQGRIVEQGEAKALFASPQQPRT 240
Cdd:cd03299 147 NPKILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLhVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFV 226
|
....
gi 1879798416 241 RQFL 244
Cdd:cd03299 227 AEFL 230
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
11-246 |
2.77e-54 |
|
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 178.51 E-value: 2.77e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 11 KKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIdagRSLGPQKgLIRQLRQHVGFV 90
Cdd:TIGR01186 1 KKTGGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENI---MKQSPVE-LREVRRKKIGMV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 91 FQNFNLFPHRTVLENIIEGPVIVkGEDKQESMARARELLAKVGLSGKENSYPRRLSGGQQQRVAIARALAMRPDVILFDE 170
Cdd:TIGR01186 77 FQQFALFPHMTILQNTSLGPELL-GWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDE 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1879798416 171 PTSALDPELVGEVLNTIRQL-AQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGEAKALFASPQQPRTRQFLEK 246
Cdd:TIGR01186 156 AFSALDPLIRDSMQDELKKLqATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIGK 232
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-245 |
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 1879798416 1 MSAIEVKSLVKKFHG----QTVLHGIDLEVQKGEVVAIIGPSGSGKT-TLLRSINLLeqPESGTIRVGDVTIDaGRSLG- 74
Cdd:COG4172 4 MPLLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILRLL--PDPAAHPSGSILFD-GQDLLg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 75 -PQKGLiRQLR-QHVGFVFQ------NfnlfPHRTVLENIIEGPVIVKGEDKQESMARARELLAKVGLSGKE---NSYPR 143
Cdd:COG4172 81 lSEREL-RRIRgNRIAMIFQepmtslN----PLHTIGKQIAEVLRLHRGLSGAAARARALELLERVGIPDPErrlDAYPH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 144 RLSGGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRT-MVIVTHEMSFARDVADRAIFMDQGRI 222
Cdd:COG4172 156 QLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMaLLLITHDLGVVRRFADRVAVMRQGEI 235
|
250 260
....*....|....*....|...
gi 1879798416 223 VEQGEAKALFASPQQPRTRQFLE 245
Cdd:COG4172 236 VEQGPTAELFAAPQHPYTRKLLA 258
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-221 |
8.07e-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: 8.07e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 5 EVKSLVKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIdagrslgpQKGLIRQLR 84
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDI--------AKLPLEELR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 85 QHVGFVFQnfnlfphrtvleniiegpvivkgedkqesmararellakvglsgkensyprrLSGGQQQRVAIARALAMRPD 164
Cdd:cd00267 73 RRIGYVPQ----------------------------------------------------LSGGQRQRVALARALLLNPD 100
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1879798416 165 VILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGR 221
Cdd:cd00267 101 LLLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-236 |
1.79e-53 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 172.47 E-value: 1.79e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 1 MSAIEVKSLVKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDAgrsLGPQkgli 80
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITG---LPPH---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 81 RQLRQHVGFVFQNFNLFPHRTVLENIIEGPVIVKGEDK-QESMARAREL---LAKvglsgKENSYPRRLSGGQQQRVAIA 156
Cdd:COG0410 74 RIARLGIGYVPEGRRIFPSLTVEENLLLGAYARRDRAEvRADLERVYELfprLKE-----RRRQRAGTLSGGEQQMLAIG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 157 RALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGEAKALFASPQ 236
Cdd:COG0410 149 RALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPE 228
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
19-236 |
1.86e-53 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 174.44 E-value: 1.86e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 19 LHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDAGRSlgpQKGLiRQLRQHVGFVFQnfnlFP 98
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKK---NKKL-KPLRKKVGIVFQ----FP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 99 H-----RTVLENIIEGPvIVKGEDKQESMARARELLAKVGLSGK--ENSyPRRLSGGQQQRVAIARALAMRPDVILFDEP 171
Cdd:PRK13634 95 EhqlfeETVEKDICFGP-MNFGVSEEDAKQKAREMIELVGLPEEllARS-PFELSGGQMRRVAIAGVLAMEPEVLVLDEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1879798416 172 TSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADRAIFMDQGRIVEQGEAKALFASPQ 236
Cdd:PRK13634 173 TAGLDPKGRKEMMEMFYKLHKEKGlTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
3-245 |
3.21e-53 |
|
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: 180.35 E-value: 3.21e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 3 AIEVKSLVKKFHGQT--VLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIdagRSLGPQkgli 80
Cdd:COG4987 333 SLELEDVSFRYPGAGrpVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDL---RDLDED---- 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 81 rQLRQHVGFVFQNFNLFpHRTVLENIIEGpvivkgeDKQESMARARELLAKVGLSGKENSYP-----------RRLSGGQ 149
Cdd:COG4987 406 -DLRRRIAVVPQRPHLF-DTTLRENLRLA-------RPDATDEELWAALERVGLGDWLAALPdgldtwlgeggRRLSGGE 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 150 QQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEkRTMVIVTHEMSfARDVADRAIFMDQGRIVEQGEAK 229
Cdd:COG4987 477 RRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAG-RTVLLITHRLA-GLERMDRILVLEDGRIVEQGTHE 554
|
250
....*....|....*.
gi 1879798416 230 ALFAspQQPRTRQFLE 245
Cdd:COG4987 555 ELLA--QNGRYRQLYQ 568
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-226 |
4.48e-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: 169.54 E-value: 4.48e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 5 EVKSLVKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDagrSLGPqkgliRQLR 84
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLA---SLSP-----KELA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 85 QHVGFVFQnfnlfphrtvleniiegpvivkgedkqesmarareLLAKVGLSGKENSYPRRLSGGQQQRVAIARALAMRPD 164
Cdd:cd03214 73 RKIAYVPQ-----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPP 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1879798416 165 VILFDEPTSALDPELVGEVLNTIRQLAQEK-RTMVIVTHEMSFARDVADRAIFMDQGRIVEQG 226
Cdd:cd03214 118 ILLLDEPTSHLDIAHQIELLELLRRLARERgKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
4-227 |
4.93e-53 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 173.73 E-value: 4.93e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 4 IEVKSLVKKFHGQT-----VLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIR----------------- 61
Cdd:PRK13651 3 IKVKNIVKIFNKKLptelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEwifkdeknkkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 62 -VGDVTIDAGRSLGPQKglIRQLRQHVGFVFQ--NFNLFpHRTVLENIIEGPVIVkGEDKQESMARARELLAKVGLsgkE 138
Cdd:PRK13651 83 vLEKLVIQKTRFKKIKK--IKEIRRRVGVVFQfaEYQLF-EQTIEKDIIFGPVSM-GVSKEEAKKRAAKYIELVGL---D 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 139 NSY----PRRLSGGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRA 214
Cdd:PRK13651 156 ESYlqrsPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRT 235
|
250
....*....|...
gi 1879798416 215 IFMDQGRIVEQGE 227
Cdd:PRK13651 236 IFFKDGKIIKDGD 248
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
15-226 |
6.27e-53 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 179.98 E-value: 6.27e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 15 GQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLlrsINLLE---QPESGTIRVGDVTIdagRSLGPQkglirQLRQHVGFVF 91
Cdd:COG1132 352 DRPVLKDISLTIPPGETVALVGPSGSGKSTL---VNLLLrfyDPTSGRILIDGVDI---RDLTLE-----SLRRQIGVVP 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 92 QNFNLFpHRTVLENIIEGpvivkgeDKQESMARARELLAKVGLSGKENSYP-----------RRLSGGQQQRVAIARALA 160
Cdd:COG1132 421 QDTFLF-SGTIRENIRYG-------RPDATDEEVEEAAKAAQAHEFIEALPdgydtvvgergVNLSGGQRQRIAIARALL 492
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1879798416 161 MRPDVILFDEPTSALDPELVGEVLNTIRQLAQEkRTMVIVTHEMSFARDvADRAIFMDQGRIVEQG 226
Cdd:COG1132 493 KDPPILILDEATSALDTETEALIQEALERLMKG-RTTIVIAHRLSTIRN-ADRILVLDDGRIVEQG 556
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
4-235 |
6.58e-53 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 175.14 E-value: 6.58e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 4 IEVKSLVKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDagrSLGPQKglirql 83
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIT---HVPAEN------ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 84 rQHVGFVFQNFNLFPHRTVLENIIEGpVIVKGEDKQESMARARELLAKVGLSGKENSYPRRLSGGQQQRVAIARALAMRP 163
Cdd:PRK09452 86 -RHVNTVFQSYALFPHMTVFENVAFG-LRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1879798416 164 DVILFDEPTSALDPELVGEVLNTIRQLaQEKR--TMVIVTHEMSFARDVADRAIFMDQGRIVEQGEAKALFASP 235
Cdd:PRK09452 164 KVLLLDESLSALDYKLRKQMQNELKAL-QRKLgiTFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEP 236
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
10-244 |
9.59e-53 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 173.61 E-value: 9.59e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 10 VKK--FHGQ-TV--LHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRvgdvtIDAGRSLGPQKGLIRQLR 84
Cdd:PRK11308 17 VKRglFKPErLVkaLDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELY-----YQGQDLLKADPEAQKLLR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 85 QHVGFVFQN--FNLFPHRTVlENIIEGPVIVKGE-DKQESMARARELLAKVGLSGKE-NSYPRRLSGGQQQRVAIARALA 160
Cdd:PRK11308 92 QKIQIVFQNpyGSLNPRKKV-GQILEEPLLINTSlSAAERREKALAMMAKVGLRPEHyDRYPHMFSGGQRQRIAIARALM 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 161 MRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRT-MVIVTHEMSFARDVADRAIFMDQGRIVEQGEAKALFASPQQPR 239
Cdd:PRK11308 171 LDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLsYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPRHPY 250
|
....*
gi 1879798416 240 TRQFL 244
Cdd:PRK11308 251 TQALL 255
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
22-226 |
9.61e-53 |
|
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: 170.17 E-value: 9.61e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 22 IDLEVqKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDAGR---SLGPQkglirqlRQHVGFVFQNFNLFP 98
Cdd:cd03297 17 IDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRkkiNLPPQ-------QRKIGLVFQQYALFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 99 HRTVLENIIEG-PVIVKGEDKQesmaRARELLAKVGLSGKENSYPRRLSGGQQQRVAIARALAMRPDVILFDEPTSALDP 177
Cdd:cd03297 89 HLNVRENLAFGlKRKRNREDRI----SVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDR 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1879798416 178 ELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQG 226
Cdd:cd03297 165 ALRLQLLPELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
19-173 |
4.99e-52 |
|
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: 165.90 E-value: 4.99e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 19 LHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDAGRslgpqkglIRQLRQHVGFVFQNFNLFP 98
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDE--------RKSLRKEIGYVFQDPQLFP 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1879798416 99 HRTVLENIIEGpVIVKGEDKQESMARARELLAKVGLSGKEN----SYPRRLSGGQQQRVAIARALAMRPDVILFDEPTS 173
Cdd:pfam00005 73 RLTVRENLRLG-LLLKGLSKREKDARAEEALEKLGLGDLADrpvgERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
15-234 |
6.03e-52 |
|
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: 176.87 E-value: 6.03e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 15 GQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIdagRSLGPQkglirQLRQHVGFVFQNF 94
Cdd:COG4988 349 GRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDL---SDLDPA-----SWRRQIAWVPQNP 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 95 NLFpHRTVLENIIEGpvivkgeDKQESMARARELLAKVGLSGKENSYP-----------RRLSGGQQQRVAIARALAMRP 163
Cdd:COG4988 421 YLF-AGTIRENLRLG-------RPDASDEELEAALEAAGLDEFVAALPdgldtplgeggRGLSGGQAQRLALARALLRDA 492
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1879798416 164 DVILFDEPTSALDPELVGEVLNTIRQLAQEkRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGEAKALFAS 234
Cdd:COG4988 493 PLLLLDEPTAHLDAETEAEILQALRRLAKG-RTVILITHRLALLAQ-ADRILVLDDGRIVEQGTHEELLAK 561
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
22-235 |
1.11e-51 |
|
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: 171.44 E-value: 1.11e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 22 IDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTI---DAGRSLGPQkglirqlRQHVGFVFQNFNLFP 98
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLqdsARGIFLPPH-------RRRIGYVFQEARLFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 99 HRTVLENIIEGPVIVKGEDKQESMARARELLakvGLSGKENSYPRRLSGGQQQRVAIARALAMRPDVILFDEPTSALDPE 178
Cdd:COG4148 91 HLSVRGNLLYGRKRAPRAERRISFDEVVELL---GIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1879798416 179 LVGEVLNTIRQLAQEKRT-MVIVTHEMSFARDVADRAIFMDQGRIVEQGEAKALFASP 235
Cdd:COG4148 168 RKAEILPYLERLRDELDIpILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP 225
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
4-237 |
6.84e-51 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 167.50 E-value: 6.84e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 4 IEVKSLVKKFHGQT--VLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGdvtidaGRSLGPQKglIR 81
Cdd:PRK13635 6 IRVEHISFRYPDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVG------GMVLSEET--VW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 82 QLRQHVGFVFQN-FNLFPHRTV-------LENIiegpvivkGEDKQESMARARELLAKVGLSGKENSYPRRLSGGQQQRV 153
Cdd:PRK13635 78 DVRRQVGMVFQNpDNQFVGATVqddvafgLENI--------GVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 154 AIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVI-VTHEMSFARDvADRAIFMDQGRIVEQGEAKALF 232
Cdd:PRK13635 150 AIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLsITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIF 228
|
....*
gi 1879798416 233 ASPQQ 237
Cdd:PRK13635 229 KSGHM 233
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
18-247 |
1.59e-50 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 174.53 E-value: 1.59e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 18 VLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVgdvtidAGRSLGPQKG--LIRQLRQHVGFVFQNFN 95
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRV------AGQDVATLDAdaLAQLRREHFGFIFQRYH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 96 LFPHRTVLENIiEGPVIVKGEDKQESMARARELLAKVGLSGKENSYPRRLSGGQQQRVAIARALAMRPDVILFDEPTSAL 175
Cdd:PRK10535 97 LLSHLTAAQNV-EVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGAL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 176 DPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDvADRAIFMDQGRIV--------EQGEAKALFASPQQPRTRQFLEKF 247
Cdd:PRK10535 176 DSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQ-AERVIEIRDGEIVrnppaqekVNVAGGTEPVVNTASGWRQFVSGF 254
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
5-226 |
2.06e-50 |
|
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: 163.86 E-value: 2.06e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 5 EVKSLVKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVgdvtidAGRSlgpqkglIRQLR 84
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRV------FGKP-------LEKER 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 85 QHVGFVFQNFNL---FPhRTVLENIIEGPVIVKG---EDKQESMARARELLAKVGLSGKENSYPRRLSGGQQQRVAIARA 158
Cdd:cd03235 68 KRIGYVPQRRSIdrdFP-ISVRDVVLMGLYGHKGlfrRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1879798416 159 LAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDqGRIVEQG 226
Cdd:cd03235 147 LVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLN-RTVVASG 213
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
4-239 |
3.95e-50 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 165.25 E-value: 3.95e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 4 IEVKSLVKKF-HGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDAGRslgpqKGLIrQ 82
Cdd:PRK13639 2 LETRDLKYSYpDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDK-----KSLL-E 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 83 LRQHVGFVFQNFN--LFPhRTVLENIIEGPVIVkGEDKQESMARARELLAKVGLSGKENSYPRRLSGGQQQRVAIARALA 160
Cdd:PRK13639 76 VRKTVGIVFQNPDdqLFA-PTVEEDVAFGPLNL-GLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1879798416 161 MRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGEAKALFASPQQPR 239
Cdd:PRK13639 154 MKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIETIR 232
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
7-222 |
6.62e-49 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 160.27 E-value: 6.62e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 7 KSLVKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRV-GDVTIDAGRSlgpQKGLIRqlRQ 85
Cdd:NF038007 9 KCYITKTIKTKVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLaGKEVTNLSYS---QKIILR--RE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 86 HVGFVFQNFNLFPHRTVLENIiEGPVIVKGEDKQESMARARELLAKVGLSGKENSYPRRLSGGQQQRVAIARALAMRPDV 165
Cdd:NF038007 84 LIGYIFQSFNLIPHLSIFDNV-ALPLKYRGVAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSNPAL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1879798416 166 ILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSfARDVADRAIFMDQGRI 222
Cdd:NF038007 163 LLADEPTGNLDSKNARAVLQQLKYINQKGTTIIMVTHSDE-ASTYGNRIINMKDGKL 218
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-231 |
1.25e-48 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 166.73 E-value: 1.25e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 3 AIEVKSLVKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIdagRSLGPQKGLirq 82
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPV---RFRSPRDAQ--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 83 lRQHVGFVFQNFNLFPHRTVLENI------IEGPVIvkgeDKQESMARARELLAKVGLSGKENSYPRRLSGGQQQRVAIA 156
Cdd:COG1129 78 -AAGIAIIHQELNLVPNLSVAENIflgrepRRGGLI----DWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1879798416 157 RALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGEAKAL 231
Cdd:COG1129 153 RALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
14-223 |
3.92e-48 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 157.80 E-value: 3.92e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 14 HGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDAgrslgpqkgliRQLRQHVGFVFQN 93
Cdd:cd03226 11 KGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA-----------KERRKSIGYVMQD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 94 --FNLFpHRTVLENIIEGpvivkGEDKQESMARARELLAKVGLSGKENSYPRRLSGGQQQRVAIARALAMRPDVILFDEP 171
Cdd:cd03226 80 vdYQLF-TDSVREELLLG-----LKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1879798416 172 TSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIV 223
Cdd:cd03226 154 TSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
4-244 |
2.94e-47 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 157.24 E-value: 2.94e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 4 IEVKSLVKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDAGRSLGPQKGLIrQL 83
Cdd:PRK14239 6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNPEVTITGSIVYNGHNIYSPRTDTV-DL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 84 RQHVGFVFQNFNLFPHrTVLENIIEGPVIVKGEDKQ------ESMARARELLAKVGLSGKENSYPrrLSGGQQQRVAIAR 157
Cdd:PRK14239 85 RKEIGMVFQQPNPFPM-SIYENVVYGLRLKGIKDKQvldeavEKSLKGASIWDEVKDRLHDSALG--LSGGQQQRVCIAR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 158 ALAMRPDVILFDEPTSALDPELVGEVLNTIRQLaQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGEAKALFASPQQ 237
Cdd:PRK14239 162 VLATSPKIILLDEPTSALDPISAGKIEETLLGL-KDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPKH 240
|
....*..
gi 1879798416 238 PRTRQFL 244
Cdd:PRK14239 241 KETEDYI 247
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-244 |
1.37e-46 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 156.41 E-value: 1.37e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 3 AIEVKSLVKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIdAGRSLGPQKGLIrQ 82
Cdd:PRK14271 21 AMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLL-GGRSIFNYRDVL-E 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 83 LRQHVGFVFQNFNLFPhRTVLENIIEGPVIVKGEDKQESMARARELLAKVGL----SGKENSYPRRLSGGQQQRVAIARA 158
Cdd:PRK14271 99 FRRRVGMLFQRPNPFP-MSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLwdavKDRLSDSPFRLSGGQQQLLCLART 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 159 LAMRPDVILFDEPTSALDPELVGEVLNTIRQLAqEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGEAKALFASPQQP 238
Cdd:PRK14271 178 LAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLA-DRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHA 256
|
....*.
gi 1879798416 239 RTRQFL 244
Cdd:PRK14271 257 ETARYV 262
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
34-235 |
1.80e-46 |
|
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: 157.27 E-value: 1.80e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 34 IIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIdagrSLGPQKglirqlRQHVGFVFQNFNLFPHRTVLENIIEgPVIV 113
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDV----TNVPPH------LRHINMVFQSYALFPHMTVEENVAF-GLKM 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 114 KGEDKQESMARARELLAKVGLSGKENSYPRRLSGGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLaQE 193
Cdd:TIGR01187 70 RKVPRAEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTI-QE 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1879798416 194 KR--TMVIVTHEMSFARDVADRAIFMDQGRIVEQGEAKALFASP 235
Cdd:TIGR01187 149 QLgiTFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEP 192
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
15-207 |
1.91e-46 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 152.96 E-value: 1.91e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 15 GQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDAGRslgpqKGLIRqLRQHVGFVFQNF 94
Cdd:TIGR01166 4 GPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDYSR-----KGLLE-RRQRVGLVFQDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 95 N--LFpHRTVLENIIEGPVIVKGEDkQESMARARELLAKVGLSGKENSYPRRLSGGQQQRVAIARALAMRPDVILFDEPT 172
Cdd:TIGR01166 78 DdqLF-AADVDQDVAFGPLNLGLSE-AEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPT 155
|
170 180 190
....*....|....*....|....*....|....*
gi 1879798416 173 SALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFA 207
Cdd:TIGR01166 156 AGLDPAGREQMLAILRRLRAEGMTVVISTHDVDLA 190
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4-203 |
2.15e-46 |
|
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: 153.40 E-value: 2.15e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 4 IEVKSLVKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDAGRSlgpqkglirQL 83
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARE---------DY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 84 RQHVGFVFQNFNLFPHRTVLENIIegpVIVKGEDKQESMARARELLAKVGLSGKENSYPRRLSGGQQQRVAIARALAMRP 163
Cdd:COG4133 74 RRRLAYLGHADGLKPELTVRENLR---FWAALYGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1879798416 164 DVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHE 203
Cdd:COG4133 151 PLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQ 190
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
14-226 |
2.36e-46 |
|
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: 153.42 E-value: 2.36e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 14 HGQTVLHgIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDAgrsLGPQkglirqlRQHVGFVFQN 93
Cdd:cd03298 10 YGEQPMH-FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTA---APPA-------DRPVSMLFQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 94 FNLFPHRTVLENIIEG--PVIVKGEDKQESMARArelLAKVGLSGKENSYPRRLSGGQQQRVAIARALAMRPDVILFDEP 171
Cdd:cd03298 79 NNLFAHLTVEQNVGLGlsPGLKLTAEDRQAIEVA---LARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1879798416 172 TSALDPELVGEVLNTIRQL-AQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQG 226
Cdd:cd03298 156 FAALDPALRAEMLDLVLDLhAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
4-235 |
2.83e-46 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 156.55 E-value: 2.83e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 4 IEVKSLVKKFHGQT-----VLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDAGRSLGPQKG 78
Cdd:PRK13631 22 LRVKNLYCVFDEKQenelvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNHELIT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 79 LIRQ--------LRQHVGFVFQ--NFNLFpHRTVLENIIEGPVIVkGEDKQESMARARELLAKVGLsgkENSY----PRR 144
Cdd:PRK13631 102 NPYSkkiknfkeLRRRVSMVFQfpEYQLF-KDTIEKDIMFGPVAL-GVKKSEAKKLAKFYLNKMGL---DDSYlersPFG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 145 LSGGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVE 224
Cdd:PRK13631 177 LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILK 256
|
250
....*....|.
gi 1879798416 225 QGEAKALFASP 235
Cdd:PRK13631 257 TGTPYEIFTDQ 267
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-244 |
2.87e-46 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 155.02 E-value: 2.87e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 1 MSAIEVKSLVKKFHG----QTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDagrslGPq 76
Cdd:COG4525 1 MSMLTVRHVSVRYPGggqpQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVT-----GP- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 77 kGLIRqlrqhvGFVFQNFNLFPHRTVLENIIEGPVIvKGEDKQESMARARELLAKVGLSGKENSYPRRLSGGQQQRVAIA 156
Cdd:COG4525 75 -GADR------GVVFQKDALLPWLNVLDNVAFGLRL-RGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 157 RALAMRPDVILFDEPTSALDP---ELVGEVLNTIRQLAQekRTMVIVTHEMSFARDVADRAIFMD--QGRIVE------- 224
Cdd:COG4525 147 RALAADPRFLLMDEPFGALDAltrEQMQELLLDVWQRTG--KGVFLITHSVEEALFLATRLVVMSpgPGRIVErleldfs 224
|
250 260
....*....|....*....|....*
gi 1879798416 225 ----QGE-AKALFASPQQPRTRQFL 244
Cdd:COG4525 225 rrflAGEdARAIKSDPAFIALREEL 249
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-244 |
1.47e-45 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 152.69 E-value: 1.47e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 1 MSAIEVKSLVKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSIN-LLEQPESGTIRvGDVTIdAGRSLGPQKGL 79
Cdd:PRK14267 2 KFAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNrLLELNEEARVE-GEVRL-FGRNIYSPDVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 80 IRQLRQHVGFVFQNFNLFPHRTVLENIIEG---PVIVKGedKQESMARARELLAKVGL----SGKENSYPRRLSGGQQQR 152
Cdd:PRK14267 80 PIEVRREVGMVFQYPNPFPHLTIYDNVAIGvklNGLVKS--KKELDERVEWALKKAALwdevKDRLNDYPSNLSGGQRQR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 153 VAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEkRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGEAKALF 232
Cdd:PRK14267 158 LVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVF 236
|
250
....*....|..
gi 1879798416 233 ASPQQPRTRQFL 244
Cdd:PRK14267 237 ENPEHELTEKYV 248
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-226 |
2.68e-45 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 151.12 E-value: 2.68e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 4 IEVKSLVKKFHG--QTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGdvtidaGRSLGPQkglIR 81
Cdd:cd03263 1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYIN------GYSIRTD---RK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 82 QLRQHVGFVFQNFNLFPHRTVLENI-IEGpvIVKGEDKQESMARARELLAKVGLSGKENSYPRRLSGGQQQRVAIARALA 160
Cdd:cd03263 72 AARQSLGYCPQFDALFDELTVREHLrFYA--RLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1879798416 161 MRPDVILFDEPTSALDPELVGEVLNTIRQLaQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQG 226
Cdd:cd03263 150 GGPSVLLLDEPTSGLDPASRRAIWDLILEV-RKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIG 214
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
2-231 |
3.49e-45 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 152.09 E-value: 3.49e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 2 SAIEVKSLVKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLL----EQPESGTIRVGDVTIDAGRSLGPqk 77
Cdd:PRK09984 3 TIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgdKSAGSHIELLGRTVQREGRLARD-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 78 glIRQLRQHVGFVFQNFNLFPHRTVLENIIEGPVivkGED----------KQESMARARELLAKVGLSGKENSYPRRLSG 147
Cdd:PRK09984 81 --IRKSRANTGYIFQQFNLVNRLSVLENVLIGAL---GSTpfwrtcfswfTREQKQRALQALTRVGMVHFAHQRVSTLSG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 148 GQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVT-HEMSFARDVADRAIFMDQGRIVEQG 226
Cdd:PRK09984 156 GQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTlHQVDYALRYCERIVALRQGHVFYDG 235
|
....*
gi 1879798416 227 EAKAL 231
Cdd:PRK09984 236 SSQQF 240
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-234 |
3.64e-45 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 152.96 E-value: 3.64e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 3 AIEVKSLVKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGdvtidaGRSLGPQKglirq 82
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWD------GEPLDPED----- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 83 lRQHVGFVFQNFNLFPHRTVLEniiegpVIV-----KGEDKQESMARARELLAKVGLSGKENSYPRRLSGGQQQRVAIAR 157
Cdd:COG4152 70 -RRRIGYLPEERGLYPKMKVGE------QLVylarlKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 158 ALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQG---EAKALFAS 234
Cdd:COG4152 143 ALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGsvdEIRRQFGR 222
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
5-244 |
6.49e-45 |
|
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: 150.37 E-value: 6.49e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 5 EVKSLVKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDagrSLGPQkgliRQLR 84
Cdd:TIGR03410 2 EVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDIT---KLPPH----ERAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 85 QHVGFVFQNFNLFPHRTVLENIIEGpVIVKGEDKQESMARARELlakvglsgkensYP-------RR---LSGGQQQRVA 154
Cdd:TIGR03410 75 AGIAYVPQGREIFPRLTVEENLLTG-LAALPRRSRKIPDEIYEL------------FPvlkemlgRRggdLSGGQQQQLA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 155 IARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADRAIFMDQGRIVEQGEAKALfa 233
Cdd:TIGR03410 142 IARALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGmAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL-- 219
|
250
....*....|.
gi 1879798416 234 spQQPRTRQFL 244
Cdd:TIGR03410 220 --DEDKVRRYL 228
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
19-232 |
6.99e-45 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 152.12 E-value: 6.99e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 19 LHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDAgrslgpQKGLIRQLRQHVGFVFQ--NFNL 96
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITD------KKVKLSDIRKKVGLVFQypEYQL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 97 FpHRTVLENIIEGPVIVkGEDKQESMARARELLAKVGLSG---KENSyPRRLSGGQQQRVAIARALAMRPDVILFDEPTS 173
Cdd:PRK13637 97 F-EETIEKDIAFGPINL-GLSEEEIENRVKRAMNIVGLDYedyKDKS-PFELSGGQKRRVAIAGVVAMEPKILILDEPTA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 174 ALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGEAKALF 232
Cdd:PRK13637 174 GLDPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVF 233
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
4-232 |
9.30e-45 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 151.39 E-value: 9.30e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 4 IEVKSLVKKFHG------QTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDV-TIDAGRslgpq 76
Cdd:PRK13633 5 IKCKNVSYKYESneesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLdTSDEEN----- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 77 kglIRQLRQHVGFVFQNfnlfPHRTVLENIIEGPVIVKGE----DKQESMARARELLAKVGLSGKENSYPRRLSGGQQQR 152
Cdd:PRK13633 80 ---LWDIRNKAGMVFQN----PDNQIVATIVEEDVAFGPEnlgiPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 153 VAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDvADRAIFMDQGRIVEQGEAKAL 231
Cdd:PRK13633 153 VAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGiTIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEI 231
|
.
gi 1879798416 232 F 232
Cdd:PRK13633 232 F 232
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
19-232 |
1.11e-44 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 151.44 E-value: 1.11e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 19 LHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDAGRslgpQKGLIRQLRQHVGFVFQnfnlFP 98
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTS----KNKDIKQIRKKVGLVFQ----FP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 99 H-----RTVLENIIEGPVIVkGEDKQESMARARELLAKVGLSgkENSY---PRRLSGGQQQRVAIARALAMRPDVILFDE 170
Cdd:PRK13649 95 EsqlfeETVLKDVAFGPQNF-GVSQEEAEALAREKLALVGIS--ESLFeknPFELSGGQMRRVAIAGILAMEPKILVLDE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1879798416 171 PTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGEAKALF 232
Cdd:PRK13649 172 PTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIF 233
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-226 |
1.96e-44 |
|
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: 148.50 E-value: 1.96e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 4 IEVKSLVKKFHGQTVLHGIDLEVQKGeVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDAGRSlgpqkglirQL 83
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQ---------KL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 84 RQHVGFVFQNFNLFPHRTVLEnIIEGPVIVKGEDKQESMARARELLAKVGLSGKENSYPRRLSGGQQQRVAIARALAMRP 163
Cdd:cd03264 71 RRRIGYLPQEFGVYPNFTVRE-FLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1879798416 164 DVILFDEPTSALDPELVGEVLNTIRQLAQEkRTMVIVTHEMSFARDVADRAIFMDQGRIVEQG 226
Cdd:cd03264 150 SILIVDEPTAGLDPEERIRFRNLLSELGED-RIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
22-238 |
2.91e-44 |
|
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: 152.19 E-value: 2.91e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 22 IDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDAGRslgpQKGLIRQLRQHVGFVFQNFNLFPHRT 101
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSR----KGIFLPPEKRRIGYVFQEARLFPHLS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 102 VLENIIEGPVIVKGEDKQESMARARELLakvGLSGKENSYPRRLSGGQQQRVAIARALAMRPDVILFDEPTSALDPELVG 181
Cdd:TIGR02142 92 VRGNLRYGMKRARPSERRISFERVIELL---GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKY 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1879798416 182 EVLNTIRQLAQEKRT-MVIVTHEMSFARDVADRAIFMDQGRIVEQGEAKALFASPQQP 238
Cdd:TIGR02142 169 EILPYLERLHAEFGIpILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLP 226
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-226 |
3.45e-44 |
|
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: 147.75 E-value: 3.45e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 4 IEVKSLVKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVgdvtidagrsLGPQKGLIRQL 83
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITF----------DGKSYQKNIEA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 84 RQHVGFVFQNFNLFPHRTVLENIIEGPVIVKGEDKqesmaRARELLAKVGLSGKENSYPRRLSGGQQQRVAIARALAMRP 163
Cdd:cd03268 71 LRRIGALIEAPGFYPNLTARENLRLLARLLGIRKK-----RIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNP 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1879798416 164 DVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQG 226
Cdd:cd03268 146 DLLILDEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-221 |
5.61e-44 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 147.97 E-value: 5.61e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 1 MSA-IEVKSLVKKF--HGQ-----TVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRV--GDVTIDAG 70
Cdd:COG4778 1 MTTlLEVENLSKTFtlHLQggkrlPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWVDLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 71 RsLGPQKglIRQLRQH-VGFVFQNFNLFPHRTVLENIIEgPVIVKGEDKQESMARARELLAKVGLsgkensyPRRL---- 145
Cdd:COG4778 81 Q-ASPRE--ILALRRRtIGYVSQFLRVIPRVSALDVVAE-PLLERGVDREEARARARELLARLNL-------PERLwdlp 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 146 ----SGGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGR 221
Cdd:COG4778 150 patfSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
6-222 |
6.93e-44 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 148.67 E-value: 6.93e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 6 VKSLVKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDagrslgpqkglirQLRQ 85
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLA-------------EARE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 86 HVGFVFQNFNLFPHRTVLENIIEGpviVKGEDKqesmARARELLAKVGLSGKENSYPRRLSGGQQQRVAIARALAMRPDV 165
Cdd:PRK11247 82 DTRLMFQDARLLPWKKVIDNVGLG---LKGQWR----DAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1879798416 166 ILFDEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADRAIFMDQGRI 222
Cdd:PRK11247 155 LLLDEPLGALDALTRIEMQDLIESLWQQHGfTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
19-237 |
7.63e-44 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 149.54 E-value: 7.63e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 19 LHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDAGrslgPQKGLIRQLRQHVGFVFQnfnlFP 98
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHK----TKDKYIRPVRKRIGMVFQ----FP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 99 HRTVLENIIEGPVIVK----GEDKQESMARARELLAKVGLSGK-ENSYPRRLSGGQQQRVAIARALAMRPDVILFDEPTS 173
Cdd:PRK13646 95 ESQLFEDTVEREIIFGpknfKMNLDEVKNYAHRLLMDLGFSRDvMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1879798416 174 ALDPELVGEVLNTIRQLAQEK-RTMVIVTHEMSFARDVADRAIFMDQGRIVEQGEAKALFASPQQ 237
Cdd:PRK13646 175 GLDPQSKRQVMRLLKSLQTDEnKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKDKKK 239
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-246 |
1.07e-43 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 148.60 E-value: 1.07e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 2 SAIEVKSLVKKFHGQT--VLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDagrslgpqKGL 79
Cdd:PRK13632 6 VMIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITIS--------KEN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 80 IRQLRQHVGFVFQN-FNLFPHRTV-------LENiiegpvivKGEDKQESMARARELLAKVGLSGKENSYPRRLSGGQQQ 151
Cdd:PRK13632 78 LKEIRKKIGIIFQNpDNQFIGATVeddiafgLEN--------KKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 152 RVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARdVADRAIFMDQGRIVEQGEAKA 230
Cdd:PRK13632 150 RVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTrKKTLISITHDMDEAI-LADKVIVFSEGKLIAQGKPKE 228
|
250
....*....|....*.
gi 1879798416 231 LFASpqqprtRQFLEK 246
Cdd:PRK13632 229 ILNN------KEILEK 238
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-244 |
1.10e-43 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 148.14 E-value: 1.10e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 1 MSAIEVKSLVKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSIN-LLEQPESGTIRvGDVTIDaGRSLGpqKGL 79
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNrLIELYPEARVS-GEVYLD-GQDIF--KMD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 80 IRQLRQHVGFVFQNFNLFPHRTVLENIIEGPVIVK-GEDKQESMARARELLAKVGL----SGKENSYPRRLSGGQQQRVA 154
Cdd:PRK14247 77 VIELRRRVQMVFQIPNPIPNLSIFENVALGLKLNRlVKSKKELQERVRWALEKAQLwdevKDRLDAPAGKLSGGQQQRLC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 155 IARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEkRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGEAKALFAS 234
Cdd:PRK14247 157 IARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTN 235
|
250
....*....|
gi 1879798416 235 PQQPRTRQFL 244
Cdd:PRK14247 236 PRHELTEKYV 245
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-234 |
2.28e-43 |
|
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: 147.15 E-value: 2.28e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 1 MSAIEVKSLVKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGtirvGDVTIdagrsLGPQKGL- 79
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYG----NDVRL-----FGERRGGe 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 80 -IRQLRQHVGFV----FQNFNlfPHRTVLEniiegpVIVKG-----------EDKQEsmARARELLAKVGLSGKENSYPR 143
Cdd:COG1119 72 dVWELRKRIGLVspalQLRFP--RDETVLD------VVLSGffdsiglyrepTDEQR--ERARELLELLGLAHLADRPFG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 144 RLSGGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRI 222
Cdd:COG1119 142 TLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEgAPTLVLVTHHVEEIPPGITHVLLLKDGRV 221
|
250
....*....|..
gi 1879798416 223 VEQGEAKALFAS 234
Cdd:COG1119 222 VAAGPKEEVLTS 233
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
3-226 |
2.55e-43 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 147.23 E-value: 2.55e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 3 AIEVKSLVKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDagrSLGPQKgLIRQ 82
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLA---DWSPAE-LARR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 83 ---LRQH--VGFVFqnfnlfphrTVLEnIIEGPVIVKGEDKQESMARARELLAKVGLSGKENSYPRRLSGGQQQRVAIAR 157
Cdd:PRK13548 78 ravLPQHssLSFPF---------TVEE-VVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLAR 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1879798416 158 ALA------MRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVI-VTHEMSFARDVADRAIFMDQGRIVEQG 226
Cdd:PRK13548 148 VLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIvVLHDLNLAARYADRIVLLHQGRLVADG 223
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-229 |
3.09e-43 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 152.87 E-value: 3.09e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 3 AIEVKSLVKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGD--VTI----DAgRSLGpq 76
Cdd:COG3845 5 ALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGkpVRIrsprDA-IALG-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 77 kglirqlrqhVGFVFQNFNLFPHRTVLENIIEG--PVIVKGEDKQESMARARELLAKVGLSGKENSYPRRLSGGQQQRVA 154
Cdd:COG3845 82 ----------IGMVHQHFMLVPNLTVAENIVLGlePTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1879798416 155 IARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGEAK 229
Cdd:COG3845 152 ILKALYRGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTA 226
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-226 |
7.88e-43 |
|
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: 144.35 E-value: 7.88e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 4 IEVKSLVKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGdvtidaGRSLGPQKglirql 83
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFD------GKPLDIAA------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 84 RQHVGFVFQNFNLFPHRTVLENIIEGPVIvKGEDKQESMARARELLAKVGLSGKENSYPRRLSGGQQQRVAIARALAMRP 163
Cdd:cd03269 69 RNRIGYLPEERGLYPKMKVIDQLVYLAQL-KGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDP 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1879798416 164 DVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQG 226
Cdd:cd03269 148 ELLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-244 |
1.52e-42 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 145.56 E-value: 1.52e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 1 MSAIEVKSLVKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPEsGTIRVGDVTIDAGRSLGPQKGLI 80
Cdd:PRK14258 5 IPAIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELE-SEVRVEGRVEFFNQNIYERRVNL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 81 RQLRQHVGFVFQNFNLFPhRTVLENIIEGPVIV------KGEDKQESMARARELLAKVglSGKENSYPRRLSGGQQQRVA 154
Cdd:PRK14258 84 NRLRRQVSMVHPKPNLFP-MSVYDNVAYGVKIVgwrpklEIDDIVESALKDADLWDEI--KHKIHKSALDLSGGQQQRLC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 155 IARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLA-QEKRTMVIVTHEMSFARDVADRAIFMDQ-----GRIVEQGEA 228
Cdd:PRK14258 161 IARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLT 240
|
250
....*....|....*.
gi 1879798416 229 KALFASPQQPRTRQFL 244
Cdd:PRK14258 241 KKIFNSPHDSRTREYV 256
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
3-226 |
1.83e-42 |
|
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: 143.88 E-value: 1.83e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 3 AIEVKSLVKKFHGQT--VLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIdagRSLGPQkgli 80
Cdd:cd03245 2 RIEFRNVSFSYPNQEipALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDI---RQLDPA---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 81 rQLRQHVGFVFQNFNLFpHRTVLENIIEGPVIVKGEDKQESMARA--RELLAK--------VGLSGkensypRRLSGGQQ 150
Cdd:cd03245 75 -DLRRNIGYVPQDVTLF-YGTLRDNITLGAPLADDERILRAAELAgvTDFVNKhpngldlqIGERG------RGLSGGQR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1879798416 151 QRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKrTMVIVTHEMSFArDVADRAIFMDQGRIVEQG 226
Cdd:cd03245 147 QAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDK-TLIIITHRPSLL-DLVDRIIVMDSGRIVADG 220
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-233 |
3.69e-42 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 144.87 E-value: 3.69e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 1 MSAIEVKSLVKKFHGQT---VLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGtirvgDVTIDaGRSLGPQK 77
Cdd:PRK13650 2 SNIIEVKNLTFKYKEDQekyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESG-----QIIID-GDLLTEEN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 78 glIRQLRQHVGFVFQN-FNLFPHRTV-------LENiiegpvivKGEDKQESMARARELLAKVGLSGKENSYPRRLSGGQ 149
Cdd:PRK13650 76 --VWDIRHKIGMVFQNpDNQFVGATVeddvafgLEN--------KGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 150 QQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVI-VTHEMSfarDVA--DRAIFMDQGRIVEQG 226
Cdd:PRK13650 146 KQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVIsITHDLD---EVAlsDRVLVMKNGQVESTS 222
|
....*..
gi 1879798416 227 EAKALFA 233
Cdd:PRK13650 223 TPRELFS 229
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-226 |
6.62e-42 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 143.33 E-value: 6.62e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 4 IEVKSLVKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDAgrsLGPQKgLIRQ- 82
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAA---WSPWE-LARRr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 83 --LRQH--VGFVFqnfnlfphrTVLENIIEGpVIVKGEDKQESMARARELLAKVGLSGKENSYPRRLSGGQQQRVAIARA 158
Cdd:COG4559 78 avLPQHssLAFPF---------TVEEVVALG-RAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARV 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1879798416 159 LA-------MRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQG 226
Cdd:COG4559 148 LAqlwepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQG 222
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-223 |
9.63e-42 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 140.26 E-value: 9.63e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 4 IEVKSLVKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIdagRSLGPQKGLirql 83
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEV---SFASPRDAR---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 84 RQHVGFVFQnfnlfphrtvleniiegpvivkgedkqesmararellakvglsgkensyprrLSGGQQQRVAIARALAMRP 163
Cdd:cd03216 74 RAGIAMVYQ----------------------------------------------------LSVGERQMVEIARALARNA 101
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 164 DVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIV 223
Cdd:cd03216 102 RLLILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
4-231 |
1.25e-41 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 141.74 E-value: 1.25e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 4 IEVKSLVKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVG--DVTIDAgrslgpqkgliR 81
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAghDVVREP-----------R 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 82 QLRQHVGFVFQNFNLFPHRTVLENI-IEGPVI-VKGEDKQEsmaRARELLAKVGLSGKENSYPRRLSGGQQQRVAIARAL 159
Cdd:cd03265 70 EVRRRIGIVFQDLSVDDELTGWENLyIHARLYgVPGAERRE---RIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1879798416 160 AMRPDVILFDEPTSALDPELVGEVLNTIRQL-AQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGEAKAL 231
Cdd:cd03265 147 VHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLkEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
1-245 |
1.29e-41 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 143.05 E-value: 1.29e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 1 MSA-IEVKSLVKKFHGQT---------VLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIdag 70
Cdd:COG4167 1 MSAlLEVRNLSKTFKYRTglfrrqqfeAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKL--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 71 rslgpQKGLIRQLRQHVGFVFQNFN--LFPHRTVLEnIIEGPVIVKGE-DKQESMARARELLAKVGLSGKE-NSYPRRLS 146
Cdd:COG4167 78 -----EYGDYKYRCKHIRMIFQDPNtsLNPRLNIGQ-ILEEPLRLNTDlTAEEREERIFATLRLVGLLPEHaNFYPHMLS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 147 GGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLaQEKR--TMVIVTHEMSFARDVADRAIFMDQGRIVE 224
Cdd:COG4167 152 SGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLEL-QEKLgiSYIYVSQHLGIVKHISDKVLVMHQGEVVE 230
|
250 260
....*....|....*....|.
gi 1879798416 225 QGEAKALFASPQQPRTRQFLE 245
Cdd:COG4167 231 YGKTAEVFANPQHEVTKRLIE 251
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
19-232 |
2.53e-41 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 142.95 E-value: 2.53e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 19 LHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDagrSLGPQKGlIRQLRQHVGFVFQnfnlFP 98
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVS---STSKQKE-IKPVRKKVGVVFQ----FP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 99 H-----RTVLENIIEGPVIVkGEDKQESMARARELLAKVGLSGK--ENSyPRRLSGGQQQRVAIARALAMRPDVILFDEP 171
Cdd:PRK13643 94 EsqlfeETVLKDVAFGPQNF-GIPKEKAEKIAAEKLEMVGLADEfwEKS-PFELSGGQMRRVAIAGILAMEPEVLVLDEP 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1879798416 172 TSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGEAKALF 232
Cdd:PRK13643 172 TAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
23-226 |
2.95e-41 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 140.38 E-value: 2.95e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 23 DLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIdagRSLGPQkglirqlRQHVGFVFQNFNLFPHRTV 102
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSH---TGLAPY-------QRPVSMLFQENNLFAHLTV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 103 LENIIEG--PVIVKGEDKQESMARAREllaKVGLSGKENSYPRRLSGGQQQRVAIARALAMRPDVILFDEPTSALDPELV 180
Cdd:TIGR01277 88 RQNIGLGlhPGLKLNAEQQEKVVDAAQ---QVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1879798416 181 GEVLNTIRQLAQEK-RTMVIVTHEMSFARDVADRAIFMDQGRIVEQG 226
Cdd:TIGR01277 165 EEMLALVKQLCSERqRTLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
3-239 |
3.91e-41 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 149.25 E-value: 3.91e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 3 AIEVKSLVKKFHGQT--VLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIdagRSLGPQkgli 80
Cdd:TIGR03375 463 EIEFRNVSFAYPGQEtpALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDI---RQIDPA---- 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 81 rQLRQHVGFVFQNFNLFpHRTVLENIIEGPVIVkgEDkqESMARARELlakVGLSGKENSYP-----------RRLSGGQ 149
Cdd:TIGR03375 536 -DLRRNIGYVPQDPRLF-YGTLRDNIALGAPYA--DD--EEILRAAEL---AGVTEFVRRHPdgldmqigergRSLSGGQ 606
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 150 QQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKrTMVIVTHEMSFArDVADRAIFMDQGRIVEQGEAK 229
Cdd:TIGR03375 607 RQAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLAGK-TLVLVTHRTSLL-DLVDRIIVMDNGRIVADGPKD 684
|
250
....*....|
gi 1879798416 230 ALFASPQQPR 239
Cdd:TIGR03375 685 QVLEALRKGR 694
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
23-231 |
5.03e-41 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 140.49 E-value: 5.03e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 23 DLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTidaGRSLGPQkglirqlRQHVGFVFQNFNLFPHRTV 102
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD---HTTTPPS-------RRPVSMLFQENNLFSHLTV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 103 LENIIEG--PVIVKGEDKQESMaraRELLAKVGLSGKENSYPRRLSGGQQQRVAIARALAMRPDVILFDEPTSALDPELV 180
Cdd:PRK10771 89 AQNIGLGlnPGLKLNAAQREKL---HAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALR 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1879798416 181 GEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADRAIFMDQGRIVEQGEAKAL 231
Cdd:PRK10771 166 QEMLTLVSQVCQERQlTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDEL 217
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-225 |
5.06e-41 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 143.83 E-value: 5.06e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 1 MSAIEVKSLVKKFHGQT-VLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTID----AGRSlgp 75
Cdd:PRK11650 1 MAGLKLQAVRKSYDGKTqVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNelepADRD--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 76 qkglirqlrqhVGFVFQNFNLFPHRTVLENIIEGPVIvKGEDKQESMARARELLAKVGLSGKENSYPRRLSGGQQQRVAI 155
Cdd:PRK11650 78 -----------IAMVFQNYALYPHMSVRENMAYGLKI-RGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAM 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1879798416 156 ARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIvEQ 225
Cdd:PRK11650 146 GRAIVREPAVFLFDEPLSNLDAKLRVQMRLEIQRLHRRlKTTSLYVTHDQVEAMTLADRVVVMNGGVA-EQ 215
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
4-244 |
7.73e-41 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 143.82 E-value: 7.73e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 4 IEVKSLVKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIrvgdvTIDagrslGPQKGLIRQL 83
Cdd:PRK11607 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQI-----MLD-----GVDLSHVPPY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 84 RQHVGFVFQNFNLFPHRTVLENIIEGpviVKGED--KQESMARARELLAKVGLSGKENSYPRRLSGGQQQRVAIARALAM 161
Cdd:PRK11607 90 QRPINMMFQSYALFPHMTVEQNIAFG---LKQDKlpKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 162 RPDVILFDEPTSALDPELVGEV-LNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGEAKALFASPQQPRT 240
Cdd:PRK11607 167 RPKLLLLDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYS 246
|
....
gi 1879798416 241 RQFL 244
Cdd:PRK11607 247 AEFI 250
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-236 |
8.25e-41 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 140.16 E-value: 8.25e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 1 MSAIEVKSLVKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDA----GRSlgpQ 76
Cdd:COG1137 1 MMTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHlpmhKRA---R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 77 KGLirqlrqhvGFVFQNFNLFPHRTVLENI---IEgpviVKGEDKQESMARARELLAKVGLSGKENSYPRRLSGGQQQRV 153
Cdd:COG1137 78 LGI--------GYLPQEASIFRKLTVEDNIlavLE----LRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 154 AIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQekRTM-VIVT-HEMSFARDVADRAIFMDQGRIVEQGEAKAL 231
Cdd:COG1137 146 EIARALATNPKFILLDEPFAGVDPIAVADIQKIIRHLKE--RGIgVLITdHNVRETLGICDRAYIISEGKVLAEGTPEEI 223
|
....*
gi 1879798416 232 FASPQ 236
Cdd:COG1137 224 LNNPL 228
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
19-247 |
1.77e-40 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 140.73 E-value: 1.77e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 19 LHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDAGRSlgpQKGLiRQLRQHVGFVFQnfnlFP 98
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETG---NKNL-KKLRKKVSLVFQ----FP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 99 H-----RTVLENIIEGPVIVkGEDKQESMARARELLAKVGLSGK-ENSYPRRLSGGQQQRVAIARALAMRPDVILFDEPT 172
Cdd:PRK13641 95 EaqlfeNTVLKDVEFGPKNF-GFSEDEAKEKALKWLKKVGLSEDlISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 173 SALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGEAKALFASPQ--------QPRTRQFL 244
Cdd:PRK13641 174 AGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKEwlkkhyldEPATSRFA 253
|
...
gi 1879798416 245 EKF 247
Cdd:PRK13641 254 SKL 256
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
3-236 |
2.08e-40 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 140.26 E-value: 2.08e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 3 AIEVKSLVKKFH-GQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVgdvtidAGRSLGPQKglIR 81
Cdd:PRK13647 4 IIEVEDLHFRYKdGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKV------MGREVNAEN--EK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 82 QLRQHVGFVFQNFN--LFPhRTVLENIIEGPVIVkGEDKQESMARARELLAKVGLSGKENSYPRRLSGGQQQRVAIARAL 159
Cdd:PRK13647 76 WVRSKVGLVFQDPDdqVFS-STVWDDVAFGPVNM-GLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1879798416 160 AMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGeAKALFASPQ 236
Cdd:PRK13647 154 AMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEG-DKSLLTDED 229
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
14-234 |
2.82e-40 |
|
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: 138.51 E-value: 2.82e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 14 HGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIdagRSLGpqkglIRQLRQHVGFVFQN 93
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDI---RDIS-----RKSLRSMIGVVLQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 94 FNLFPhRTVLENIIEGPVIVKGEDKQESM--ARARELLAK--------VGLSGKensyprRLSGGQQQRVAIARALAMRP 163
Cdd:cd03254 86 TFLFS-GTIMENIRLGRPNATDEEVIEAAkeAGAHDFIMKlpngydtvLGENGG------NLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1879798416 164 DVILFDEPTSALDPELVGEVLNTIRQLaQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGEAKALFAS 234
Cdd:cd03254 159 KILILDEATSNIDTETEKLIQEALEKL-MKGRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEGTHDELLAK 227
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
14-233 |
2.92e-40 |
|
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: 138.52 E-value: 2.92e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 14 HGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIdagRSLGpqkglIRQLRQHVGFVFQN 93
Cdd:cd03251 13 DGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDV---RDYT-----LASLRRQIGLVSQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 94 FNLFpHRTVLENIIEGpviVKGEDKQESMARARELLAKVGLSGKENSYPR-------RLSGGQQQRVAIARALAMRPDVI 166
Cdd:cd03251 85 VFLF-NDTVAENIAYG---RPGATREEVEEAARAANAHEFIMELPEGYDTvigergvKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1879798416 167 LFDEPTSALDPELVGEVLNTIRQLaQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGEAKALFA 233
Cdd:cd03251 161 ILDEATSALDTESERLVQAALERL-MKNRTTFVIAHRLSTIEN-ADRIVVLEDGKIVERGTHEELLA 225
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
11-231 |
5.99e-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: 139.83 E-value: 5.99e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 11 KKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVG--DVTIDAgrslgpqkgliRQLRQHVG 88
Cdd:TIGR01188 1 KVYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAgyDVVREP-----------RKVRRSIG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 89 FVFQNFNLFPHRTVLENIiEGPVIVKGEDKQESMARARELLAKVGLSGKENSYPRRLSGGQQQRVAIARALAMRPDVILF 168
Cdd:TIGR01188 70 IVPQYASVDEDLTGRENL-EMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1879798416 169 DEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGEAKAL 231
Cdd:TIGR01188 149 DEPTTGLDPRTRRAIWDYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEEL 211
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-227 |
6.12e-40 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 144.17 E-value: 6.12e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 4 IEVKSLVKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQ--PESGTI-----------------RVGD 64
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIiyhvalcekcgyverpsKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 65 VTIDAGRSL--------GPQKGLIRQLRQHVGFVFQ-NFNLFPHRTVLENIIEG-PVIvkGEDKQESMARARELLAKVGL 134
Cdd:TIGR03269 81 PCPVCGGTLepeevdfwNLSDKLRRRIRKRIAIMLQrTFALYGDDTVLDNVLEAlEEI--GYEGKEAVGRAVDLIEMVQL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 135 SGKENSYPRRLSGGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADR 213
Cdd:TIGR03269 159 SHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGiSMVLTSHWPEVIEDLSDK 238
|
250
....*....|....
gi 1879798416 214 AIFMDQGRIVEQGE 227
Cdd:TIGR03269 239 AIWLENGEIKEEGT 252
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
15-233 |
9.52e-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: 137.36 E-value: 9.52e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 15 GQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVG-----DVTIDAgrslgpqkglirqLRQHVGF 89
Cdd:cd03253 13 GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDgqdirEVTLDS-------------LRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 90 VFQNFNLFpHRTVLENIIEGPVIVKGEDKQESMARAR---ELLA-------KVGLSGkensypRRLSGGQQQRVAIARAL 159
Cdd:cd03253 80 VPQDTVLF-NDTIGYNIRYGRPDATDEEVIEAAKAAQihdKIMRfpdgydtIVGERG------LKLSGGEKQRVAIARAI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1879798416 160 AMRPDVILFDEPTSALDPELVGEVLNTIRQLAQeKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGEAKALFA 233
Cdd:cd03253 153 LKNPPILLLDEATSALDTHTEREIQAALRDVSK-GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEELLA 224
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
21-233 |
9.71e-40 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 143.79 E-value: 9.71e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 21 GIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGT--IRVGDVTIDAGRSLGPQKGlirQLRQHVGFVFQNFNLFP 98
Cdd:TIGR03269 302 NVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEvnVRVGDEWVDMTKPGPDGRG---RAKRYIGILHQEYDLYP 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 99 HRTVLENIIEGpvIVKGEDKQESMARARELLAKVGLSGKE-----NSYPRRLSGGQQQRVAIARALAMRPDVILFDEPTS 173
Cdd:TIGR03269 379 HRTVLDNLTEA--IGLELPDELARMKAVITLKMVGFDEEKaeeilDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTG 456
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1879798416 174 ALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGEAKALFA 233
Cdd:TIGR03269 457 TMDPITKVDVTHSILKAREEmEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIVE 517
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
19-220 |
9.81e-40 |
|
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: 137.21 E-value: 9.81e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 19 LHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDAGrslGPQKGLirqlrqhvgfVFQNFNLFP 98
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEP---GPDRMV----------VFQNYSLLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 99 HRTVLENI-IEGPVIVKGEDKQESMARARELLAKVGLSGKENSYPRRLSGGQQQRVAIARALAMRPDVILFDEPTSALDP 177
Cdd:TIGR01184 68 WLTVRENIaLAVDRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1879798416 178 ELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADRAIFMDQG 220
Cdd:TIGR01184 148 LTRGNLQEELMQIWEEHRvTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
14-227 |
1.09e-39 |
|
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: 1.09e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 14 HGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPE---SGTIRVGDVTIDAgrsLGPQkglirqlRQHVGFV 90
Cdd:COG4136 12 GGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTA---LPAE-------QRRIGIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 91 FQNFNLFPHRTVLENIIEG-PVIVKGEDKQesmARARELLAKVGLSGKENSYPRRLSGGQQQRVAIARALAMRPDVILFD 169
Cdd:COG4136 82 FQDDLLFPHLSVGENLAFAlPPTIGRAQRR---ARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1879798416 170 EPTSALDPELVGEVLNTIRQLAQEKRT-MVIVTHemsfarDVADRAifmDQGRIVEQGE 227
Cdd:COG4136 159 EPFSKLDAALRAQFREFVFEQIRQRGIpALLVTH------DEEDAP---AAGRVLDLGN 208
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
15-235 |
1.45e-39 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 138.20 E-value: 1.45e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 15 GQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDvtIDAGrslGPQKglIRQLRQHVGFVFQNF 94
Cdd:PRK13644 14 GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSG--IDTG---DFSK--LQGIRKLVGIVFQNP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 95 NL-FPHRTVLENIIEGP--VIVKGEDKQESMARArelLAKVGLSGKENSYPRRLSGGQQQRVAIARALAMRPDVILFDEP 171
Cdd:PRK13644 87 ETqFVGRTVEEDLAFGPenLCLPPIEIRKRVDRA---LAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEV 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1879798416 172 TSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGEAKALFASP 235
Cdd:PRK13644 164 TSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGEPENVLSDV 226
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
8-224 |
1.54e-39 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 137.90 E-value: 1.54e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 8 SLVKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVgdvtidAGRSLGPQKGL-IRQLRQH 86
Cdd:PRK10419 17 GLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSW------RGEPLAKLNRAqRKAFRRD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 87 VGFVFQN----FNlfPHRTVLENIIEGPVIVKGEDKQESMARARELLAKVGLS-GKENSYPRRLSGGQQQRVAIARALAM 161
Cdd:PRK10419 91 IQMVFQDsisaVN--PRKTVREIIREPLRHLLSLDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQLQRVCLARALAV 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1879798416 162 RPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRT-MVIVTHEMSFARDVADRAIFMDQGRIVE 224
Cdd:PRK10419 169 EPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTaCLFITHDLRLVERFCQRVMVMDNGQIVE 232
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
19-245 |
2.55e-39 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 137.22 E-value: 2.55e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 19 LHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIdAGRSLGPQKGLIRQLRQHVGFVFQNFNLFP 98
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPGFRVEGKVTF-HGKNLYAPDVDPVEVRRRIGMVFQKPNPFP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 99 hRTVLENIIEGPVI--VKG---EDKQESMARA------RELLAKVGLSgkensyprrLSGGQQQRVAIARALAMRPDVIL 167
Cdd:PRK14243 105 -KSIYDNIAYGARIngYKGdmdELVERSLRQAalwdevKDKLKQSGLS---------LSGGQQQRLCIARAIAVQPEVIL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 168 FDEPTSALDPELVGEVLNTIRQLaQEKRTMVIVTHEMSFARDVADRAIFMD---------QGRIVEQGEAKALFASPQQP 238
Cdd:PRK14243 175 MDEPCSALDPISTLRIEELMHEL-KEQYTIIIVTHNMQQAARVSDMTAFFNveltegggrYGYLVEFDRTEKIFNSPQQQ 253
|
....*..
gi 1879798416 239 RTRQFLE 245
Cdd:PRK14243 254 ATRDYVS 260
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
15-233 |
2.93e-39 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 136.13 E-value: 2.93e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 15 GQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLlrsINLLEQ---PESGTIRVGDVTIdagRSLGpqkglIRQLRQHVGFVF 91
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTV---VSLLERfydPTSGEILLDGVDI---RDLN-----LRWLRSQIGLVS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 92 QNFNLFPhRTVLENIIEG--PVIVKGEDKQESMARARELLAK--------VGLSGKEnsyprrLSGGQQQRVAIARALAM 161
Cdd:cd03249 84 QEPVLFD-GTIAENIRYGkpDATDEEVEEAAKKANIHDFIMSlpdgydtlVGERGSQ------LSGGQKQRIAIARALLR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1879798416 162 RPDVILFDEPTSALDPELVGEVLNTIRQLAqEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGEAKALFA 233
Cdd:cd03249 157 NPKILLLDEATSALDAESEKLVQEALDRAM-KGRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGTHDELMA 226
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
4-222 |
5.27e-39 |
|
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: 133.50 E-value: 5.27e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 4 IEVKSLVKKFHG--QTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIdagRSLGPqkgliR 81
Cdd:cd03246 1 LEVENVSFRYPGaePPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADI---SQWDP-----N 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 82 QLRQHVGFVFQNFNLFPHrTVLENIiegpvivkgedkqesmararellakvglsgkensyprrLSGGQQQRVAIARALAM 161
Cdd:cd03246 73 ELGDHVGYLPQDDELFSG-SIAENI--------------------------------------LSGGQRQRLGLARALYG 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1879798416 162 RPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARdVADRAIFMDQGRI 222
Cdd:cd03246 114 NPRILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLA-SADRILVLEDGRV 173
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
4-243 |
8.56e-39 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 136.13 E-value: 8.56e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 4 IEVKSLVKKF-HGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDAGRslgpqKGLIrQ 82
Cdd:PRK13636 6 LKVEELNYNYsDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSR-----KGLM-K 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 83 LRQHVGFVFQ--NFNLFPhRTVLENIIEGPVIVkGEDKQESMARARELLAKVGLSGKENSYPRRLSGGQQQRVAIARALA 160
Cdd:PRK13636 80 LRESVGMVFQdpDNQLFS-ASVYQDVSFGAVNL-KLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 161 MRPDVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGEAKALFASPQQPR 239
Cdd:PRK13636 158 MEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAEKEMLR 237
|
....
gi 1879798416 240 TRQF 243
Cdd:PRK13636 238 KVNL 241
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-236 |
1.70e-38 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 137.47 E-value: 1.70e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 1 MSAIEVKSLVKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDagrSLGPQKgli 80
Cdd:PRK11000 1 MASVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMN---DVPPAE--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 81 rqlrQHVGFVFQNFNLFPHRTVLENIIEGpVIVKGEDKQESMARARELLAKVGLSGKENSYPRRLSGGQQQRVAIARALA 160
Cdd:PRK11000 75 ----RGVGMVFQSYALYPHLSVAENMSFG-LKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1879798416 161 MRPDVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGEAKALFASPQ 236
Cdd:PRK11000 150 AEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRlGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPA 226
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-235 |
1.85e-38 |
|
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: 133.82 E-value: 1.85e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 4 IEVKSLVKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDagrslgpQKGLIRQL 83
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDIT-------KLPMHKRA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 84 RQHVGFVFQNFNLFPHRTVLENII---EgpviVKGEDKQESMARARELLAKVGLSGKENSYPRRLSGGQQQRVAIARALA 160
Cdd:cd03218 74 RLGIGYLPQEASIFRKLTVEENILavlE----IRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1879798416 161 MRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGEAKALFASP 235
Cdd:cd03218 150 TNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANE 224
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
15-241 |
7.44e-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: 7.44e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 15 GQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDAGRSlgpqkgliRQLRQHVGFVFQNF 94
Cdd:COG4618 344 KRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDR--------EELGRHIGYLPQDV 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 95 NLFPHrTVLENI--IEGPvivkgeDKQE-----SMARARELLAK--------VGLSGkensypRRLSGGQQQRVAIARAL 159
Cdd:COG4618 416 ELFDG-TIAENIarFGDA------DPEKvvaaaKLAGVHEMILRlpdgydtrIGEGG------ARLSGGQRQRIGLARAL 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 160 AMRPDVILFDEPTSALDPElvGE--VLNTIRQLAQEKRTMVIVTHEMSFARdVADRAIFMDQGRIVEQGEAKALFASPQQ 237
Cdd:COG4618 483 YGDPRLVVLDEPNSNLDDE--GEaaLAAAIRALKARGATVVVITHRPSLLA-AVDKLLVLRDGRVQAFGPRDEVLARLAR 559
|
....
gi 1879798416 238 PRTR 241
Cdd:COG4618 560 PAAA 563
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
4-207 |
1.26e-37 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 131.44 E-value: 1.26e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 4 IEVKSLVKKF----HGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVgdvtidAGRSLGPQKGL 79
Cdd:PRK10584 7 VEVHHLKKSVgqgeHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSL------VGQPLHQMDEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 80 IR-QLR-QHVGFVFQNFNLFPHRTVLENIiEGPVIVKGEDKQESMARARELLAKVGLSGKENSYPRRLSGGQQQRVAIAR 157
Cdd:PRK10584 81 ARaKLRaKHVGFVFQSFMLIPTLNALENV-ELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALAR 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1879798416 158 ALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFA 207
Cdd:PRK10584 160 AFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREhGTTLILVTHDLQLA 210
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
3-224 |
1.51e-37 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 132.13 E-value: 1.51e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 3 AIEVKSLVKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDagrslGPqkGLIRq 82
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVE-----GP--GAER- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 83 lrqhvGFVFQNFNLFPHRTVLENIIEGpVIVKGEDKQESMARARELLAKVGLSGKENSYPRRLSGGQQQRVAIARALAMR 162
Cdd:PRK11248 73 -----GVVFQNEGLLPWRNVQDNVAFG-LQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAAN 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1879798416 163 PDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMV-IVTHEMSFARDVADRAIFM--DQGRIVE 224
Cdd:PRK11248 147 PQLLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVlLITHDIEEAVFMATELVLLspGPGRVVE 211
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
18-225 |
1.52e-37 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 131.48 E-value: 1.52e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 18 VLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIrvgdvtIDAGRSLGPQKGLIR-QLRQH-VGFVFQNFN 95
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDV------IFNGQPMSKLSSAAKaELRNQkLGFIYQFHH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 96 LFPHRTVLENIIEgPVIVKGEDKQESMARARELLAKVGLSGKENSYPRRLSGGQQQRVAIARALAMRPDVILFDEPTSAL 175
Cdd:PRK11629 98 LLPDFTALENVAM-PLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1879798416 176 DPELVGEVLNTIRQLAQEKRT-MVIVTHEMSFARDVaDRAIFMDQGRIVEQ 225
Cdd:PRK11629 177 DARNADSIFQLLGELNRLQGTaFLVVTHDLQLAKRM-SRQLEMRDGRLTAE 226
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
15-235 |
1.62e-37 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 138.94 E-value: 1.62e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 15 GQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTirvgdVTIDaGRSLgpqKGL-IRQLRQHVGFVFQN 93
Cdd:TIGR03797 465 GPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGS-----VFYD-GQDL---AGLdVQAVRRQLGVVLQN 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 94 FNLFPHrTVLENIIEGPVIvkgedkqeSMARARELLAKVGLSGKENSYP-----------RRLSGGQQQRVAIARALAMR 162
Cdd:TIGR03797 536 GRLMSG-SIFENIAGGAPL--------TLDEAWEAARMAGLAEDIRAMPmgmhtviseggGTLSGGQRQRLLIARALVRK 606
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1879798416 163 PDVILFDEPTSALDPELVGEVLNTIRQLaqeKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGEAKALFASP 235
Cdd:TIGR03797 607 PRILLFDEATSALDNRTQAIVSESLERL---KVTRIVIAHRLSTIRN-ADRIYVLDAGRVVQQGTYDELMARE 675
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
21-241 |
1.73e-37 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 134.06 E-value: 1.73e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 21 GIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIrvgdvtIDAGRSL-GPQKGLIRQLRQHVGFVFQN--FNLF 97
Cdd:PRK15079 39 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEV------AWLGKDLlGMKDDEWRAVRSDIQMIFQDplASLN 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 98 PHRTVLENIIEGPVIVKGE-DKQESMARARELLAKVGL-SGKENSYPRRLSGGQQQRVAIARALAMRPDVILFDEPTSAL 175
Cdd:PRK15079 113 PRMTIGEIIAEPLRTYHPKlSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSAL 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1879798416 176 DPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADRAIFMDQGRIVEQGEAKALFASPQQPRTR 241
Cdd:PRK15079 193 DVSIQAQVVNLLQQLQREMGlSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPYTK 259
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
14-226 |
2.38e-37 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 129.98 E-value: 2.38e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 14 HGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSIN--LLEQPESGTIRVGdvtidaGRSLGPQKglirqLRQHVGFVF 91
Cdd:cd03213 20 SGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLIN------GRPLDKRS-----FRKIIGYVP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 92 QNFNLFPHRTVleniiegpvivkgedkQESMARARELlakvglsgkensypRRLSGGQQQRVAIARALAMRPDVILFDEP 171
Cdd:cd03213 89 QDDILHPTLTV----------------RETLMFAAKL--------------RGLSGGERKRVSIALELVSNPSLLFLDEP 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1879798416 172 TSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMS---FArdVADRAIFMDQGRIVEQG 226
Cdd:cd03213 139 TSGLDSSSALQVMSLLRRLADTGRTIICSIHQPSseiFE--LFDKLLLLSQGRVIYFG 194
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
16-244 |
3.19e-37 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 131.32 E-value: 3.19e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 16 QTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDAGRSLGPQKGLirQLRQHVGFVFQNFN 95
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDIFQIDAI--KLRKEVGMVFQQPN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 96 LFPHRTVLENIIEgPVIVKG-EDKQESMARARELLAKVGL----SGKENSYPRRLSGGQQQRVAIARALAMRPDVILFDE 170
Cdd:PRK14246 101 PFPHLSIYDNIAY-PLKSHGiKEKREIKKIVEECLRKVGLwkevYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDE 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1879798416 171 PTSALDPELVGEVLNTIRQLAQEKrTMVIVTHEMSFARDVADRAIFMDQGRIVEQGEAKALFASPQQPRTRQFL 244
Cdd:PRK14246 180 PTSMIDIVNSQAIEKLITELKNEI-AIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKYV 252
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
4-226 |
1.70e-36 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 129.43 E-value: 1.70e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 4 IEVKSLVKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVgdvtidAGRSLG--PQKGLIR 81
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLV------DGLDVAttPSRELAK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 82 Q---LRQHVGFVFQ-------NFNLFPHRtvleniiegpvivKG----EDKQEsMARARELLakvGLSGKENSYPRRLSG 147
Cdd:COG4604 76 RlaiLRQENHINSRltvrelvAFGRFPYS-------------KGrltaEDREI-IDEAIAYL---DLEDLADRYLDELSG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 148 GQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEK-RTMVIVTHEMSFARDVADRAIFMDQGRIVEQG 226
Cdd:COG4604 139 GQRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELgKTVVIVLHDINFASCYADHIVAMKDGRVVAQG 218
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-234 |
1.76e-36 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 130.70 E-value: 1.76e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 2 SAIEVKSLVKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIdagrslgPQKGliR 81
Cdd:PRK13537 6 APIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPV-------PSRA--R 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 82 QLRQHVGFVFQNFNLFPHRTVLENI-IEGPVIvkGEDKQESMARARELLAKVGLSGKENSYPRRLSGGQQQRVAIARALA 160
Cdd:PRK13537 77 HARQRVGVVPQFDNLDPDFTVRENLlVFGRYF--GLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1879798416 161 MRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGEAKALFAS 234
Cdd:PRK13537 155 NDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIES 228
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-217 |
2.64e-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: 134.34 E-value: 2.64e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 2 SAIEVKSLVKKFHGQT-VLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDAGRSlgpqkgli 80
Cdd:TIGR02857 320 SSLEFSGVSVAYPGRRpALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADA-------- 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 81 RQLRQHVGFVFQNFNLFPhRTVLENIIEGPVIVKGEDKQESMARA--RELLAKV--GLSGKENSYPRRLSGGQQQRVAIA 156
Cdd:TIGR02857 392 DSWRDQIAWVPQHPFLFA-GTIAENIRLARPDASDAEIREALERAglDEFVAALpqGLDTPIGEGGAGLSGGQAQRLALA 470
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1879798416 157 RALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQeKRTMVIVTHEMSFARDvADRAIFM 217
Cdd:TIGR02857 471 RAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ-GRTVLLVTHRLALAAL-ADRIVVL 529
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
18-226 |
2.92e-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: 128.16 E-value: 2.92e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 18 VLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLeQPESGTIRvGDVTIDaGRSLGPQkglirQLRQHVGFVFQNFNLF 97
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGR-VEGGGTTS-GQILFN-GQPRKPD-----QFQKCVAYVRQDDILL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 98 PHRTVLE-----NIIEGPVIVKgeDKQESMARARELLAKVGLSGKENSYPRRLSGGQQQRVAIARALAMRPDVILFDEPT 172
Cdd:cd03234 94 PGLTVREtltytAILRLPRKSS--DAIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1879798416 173 SALDPELVGEVLNTIRQLAQEKRTMVIVTHE-MSFARDVADRAIFMDQGRIVEQG 226
Cdd:cd03234 172 SGLDSFTALNLVSTLSQLARRNRIVILTIHQpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
4-236 |
3.97e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 128.72 E-value: 3.97e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 4 IEVKSLVKKFHGQT--VLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDAGRslgpqkglIR 81
Cdd:PRK13648 8 IVFKNVSFQYQSDAsfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDN--------FE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 82 QLRQHVGFVFQN-FNLFPHRTV-------LENIIegpviVKGEDKQEsmaRARELLAKVGLSGKENSYPRRLSGGQQQRV 153
Cdd:PRK13648 80 KLRKHIGIVFQNpDNQFVGSIVkydvafgLENHA-----VPYDEMHR---RVSEALKQVDMLERADYEPNALSGGQKQRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 154 AIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVI-VTHEMSFARDvADRAIFMDQGRIVEQGEAKALF 232
Cdd:PRK13648 152 AIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIIsITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIF 230
|
....
gi 1879798416 233 ASPQ 236
Cdd:PRK13648 231 DHAE 234
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
19-234 |
7.13e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 128.97 E-value: 7.13e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 19 LHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDAGRSLGPQkglIRQLRQHVGFVFQ--NFNL 96
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKIKE---VKRLRKEIGLVFQfpEYQL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 97 FpHRTVLENIIEGPVIVkGEDKQESMARARELLAKVGLSGK-ENSYPRRLSGGQQQRVAIARALAMRPDVILFDEPTSAL 175
Cdd:PRK13645 104 F-QETIEKDIAFGPVNL-GENKQEAYKKVPELLKLVQLPEDyVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGL 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 176 DPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGEAKALFAS 234
Cdd:PRK13645 182 DPKGEEDFINLFERLNKEyKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN 241
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
10-242 |
9.21e-36 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 129.99 E-value: 9.21e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 10 VKKFHGQTVLHgIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGD---VTIDAGRSLGPQKglirqlrQH 86
Cdd:PRK11144 6 FKQQLGDLCLT-VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlFDAEKGICLPPEK-------RR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 87 VGFVFQNFNLFPHRTVLENIIEGpviVKGEDKQEsmarareLLAKVGLSGKE---NSYPRRLSGGQQQRVAIARALAMRP 163
Cdd:PRK11144 78 IGYVFQDARLFPHYKVRGNLRYG---MAKSMVAQ-------FDKIVALLGIEpllDRYPGSLSGGEKQRVAIGRALLTAP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 164 DVILFDEPTSALDPELVGEVLNTIRQLAQEKRT-MVIVTHEMSFARDVADRAIFMDQGRIVEQGEAKALFASPQ----QP 238
Cdd:PRK11144 148 ELLLMDEPLASLDLPRKRELLPYLERLAREINIpILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSAmrpwLP 227
|
....
gi 1879798416 239 RTRQ 242
Cdd:PRK11144 228 KEEQ 231
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-235 |
1.73e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 127.61 E-value: 1.73e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 1 MSAIEVKSLVKKFHGQT-VLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVgdvtidagRSLGPQKGL 79
Cdd:PRK13652 1 MHLIETRDLCYSYSGSKeALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLI--------RGEPITKEN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 80 IRQLRQHVGFVFQNFN--LFPhRTVLENIIEGPvIVKGEDKQESMARARELLAKVGLSGKENSYPRRLSGGQQQRVAIAR 157
Cdd:PRK13652 73 IREVRKFVGLVFQNPDdqIFS-PTVEQDIAFGP-INLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1879798416 158 ALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGEAKALFASP 235
Cdd:PRK13652 151 VIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
15-234 |
2.05e-35 |
|
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: 126.06 E-value: 2.05e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 15 GQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDV---TIDAGrslgpqkglirQLRQHVGFVF 91
Cdd:cd03252 14 GPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHdlaLADPA-----------WLRRQVGVVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 92 QNFNLFpHRTVLENIIEGPVIVKGEDKQE--SMARARELLAKVGLsGKENSYPRR---LSGGQQQRVAIARALAMRPDVI 166
Cdd:cd03252 83 QENVLF-NRSIRDNIALADPGMSMERVIEaaKLAGAHDFISELPE-GYDTIVGEQgagLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1879798416 167 LFDEPTSALDPELVGEVLNTIRQLAqEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGEAKALFAS 234
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDIC-AGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLAE 226
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
15-247 |
2.07e-35 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 132.26 E-value: 2.07e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 15 GQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDAGRSlgpqkgliRQLRQHVGFVFQNF 94
Cdd:PRK11160 352 PQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSE--------AALRQAISVVSQRV 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 95 NLFPHrTVLENIIEGpvivkgeDKQESMARARELLAKVGLSG-KENSYP---------RRLSGGQQQRVAIARALAMRPD 164
Cdd:PRK11160 424 HLFSA-TLRDNLLLA-------APNASDEALIEVLQQVGLEKlLEDDKGlnawlgeggRQLSGGEQRRLGIARALLHDAP 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 165 VILFDEPTSALDPELVGEVLNTIRQLAQEKrTMVIVTHEMSfARDVADRAIFMDQGRIVEQGEAKALFAspQQPRTRQFL 244
Cdd:PRK11160 496 LLLLDEPTEGLDAETERQILELLAEHAQNK-TVLMITHRLT-GLEQFDRICVMDNGQIIEQGTHQELLA--QQGRYYQLK 571
|
...
gi 1879798416 245 EKF 247
Cdd:PRK11160 572 QRL 574
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
24-244 |
2.52e-35 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 129.77 E-value: 2.52e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 24 LEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVtiDAGRSLGPQKGLIRqlRQHVGFVFQNFNLFPHRTVL 103
Cdd:PRK10070 49 LAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGV--DIAKISDAELREVR--RKKIAMVFQSFALMPHMTVL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 104 ENIIEGpVIVKGEDKQESMARARELLAKVGLSGKENSYPRRLSGGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEV 183
Cdd:PRK10070 125 DNTAFG-MELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1879798416 184 LNTIRQL-AQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGEAKALFASPQQPRTRQFL 244
Cdd:PRK10070 204 QDELVKLqAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFF 265
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-230 |
2.56e-35 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 126.74 E-value: 2.56e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 4 IEVKSLVKKFHGQTV-----LHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTI----DAGRSlg 74
Cdd:COG1101 2 LELKNLSKTFNPGTVnekraLDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVtklpEYKRA-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 75 pqkglirqlrQHVGFVFQNFNL--FPHRTVLENII------EGPVIVKGEDKQEsMARARELLAKVGLsGKENsyprR-- 144
Cdd:COG1101 80 ----------KYIGRVFQDPMMgtAPSMTIEENLAlayrrgKRRGLRRGLTKKR-RELFRELLATLGL-GLEN----Rld 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 145 -----LSGGQQQrvaiARALAM----RPDVILFDEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADRA 214
Cdd:COG1101 144 tkvglLSGGQRQ----ALSLLMatltKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNlTTLMVTHNMEQALDYGNRL 219
|
250
....*....|....*...
gi 1879798416 215 IFMDQGRIVE--QGEAKA 230
Cdd:COG1101 220 IMMHEGRIILdvSGEEKK 237
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-226 |
4.16e-35 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 125.87 E-value: 4.16e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 1 MSA--IEVKSLVKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIdAGRS--LGPQ 76
Cdd:PRK11300 1 MSQplLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHI-EGLPghQIAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 77 KGLIRqlrqhvgfVFQNFNLFPHRTVLEN------------IIEG----PVIVKGEdkQESMARARELLAKVGLSGKENS 140
Cdd:PRK11300 80 MGVVR--------TFQHVRLFREMTVIENllvaqhqqlktgLFSGllktPAFRRAE--SEALDRAATWLERVGLLEHANR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 141 YPRRLSGGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMV-IVTHEMSFARDVADRAIFMDQ 219
Cdd:PRK11300 150 QAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVlLIEHDMKLVMGISDRIYVVNQ 229
|
....*..
gi 1879798416 220 GRIVEQG 226
Cdd:PRK11300 230 GTPLANG 236
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-222 |
4.66e-35 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 130.96 E-value: 4.66e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 6 VKSLVKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVgdvtidagrslgpQKGLirqlrq 85
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI-------------PKGL------ 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 86 HVGFVFQNFNLFPHRTVLENIIEG----------------------PVIVKGEDKQESM---------ARARELLAKVGL 134
Cdd:COG0488 62 RIGYLPQEPPLDDDLTVLDTVLDGdaelraleaeleeleaklaepdEDLERLAELQEEFealggweaeARAEEILSGLGF 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 135 SGKENSYP-RRLSGGQQQRVAIARALAMRPDVILFDEPTSALDpelvgevLNTIR----QLAQEKRTMVIVTHEMSFARD 209
Cdd:COG0488 142 PEEDLDRPvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLD-------LESIEwleeFLKNYPGTVLVVSHDRYFLDR 214
|
250
....*....|...
gi 1879798416 210 VADRAIFMDQGRI 222
Cdd:COG0488 215 VATRILELDRGKL 227
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
19-226 |
5.12e-35 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 131.24 E-value: 5.12e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 19 LHGIDLEVQKGEVVAIIGPSGSGKTTLlrsINLLEQ---PESGTIRVGDVTIdagRSLGpqkglIRQLRQHVGFVFQNFN 95
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTL---INLLQRvfdPQSGRILIDGTDI---RTVT-----RASLRRNIAVVFQDAG 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 96 LFpHRTVLENIIEGpvivKGEDKQESMARARELLAKVG-LSGKENSYP-------RRLSGGQQQRVAIARALAMRPDVIL 167
Cdd:PRK13657 420 LF-NRSIEDNIRVG----RPDATDEEMRAAAERAQAHDfIERKPDGYDtvvgergRQLSGGERQRLAIARALLKDPPILI 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1879798416 168 FDEPTSALDPEL---VGEVLNTIRQlaqeKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQG 226
Cdd:PRK13657 495 LDEATSALDVETeakVKAALDELMK----GRTTFIIAHRLSTVRN-ADRILVFDNGRVVESG 551
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
4-226 |
5.19e-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: 5.19e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 4 IEVKSLVKKFHGQT----VLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDvtIDAGRSlgPqkgl 79
Cdd:cd03266 2 ITADALTKRFRDVKktvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDG--FDVVKE--P---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 80 iRQLRQHVGFVFQNFNLFPHRTVLENIiEGPVIVKGEDKQESMARARELLAKVGLSGKENSYPRRLSGGQQQRVAIARAL 159
Cdd:cd03266 74 -AEARRRLGFVSDSTGLYDRLTARENL-EYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1879798416 160 AMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQG 226
Cdd:cd03266 152 VHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
15-233 |
6.65e-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: 130.99 E-value: 6.65e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 15 GQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIdagrslgpQKGLIRQLRQHVGFVFQNF 94
Cdd:TIGR02203 344 DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDL--------ADYTLASLRRQVALVSQDV 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 95 NLFpHRTVLENIiegpviVKGEDKQESMARARELLAKVGLSGKENSYPR-----------RLSGGQQQRVAIARALAMRP 163
Cdd:TIGR02203 416 VLF-NDTIANNI------AYGRTEQADRAEIERALAAAYAQDFVDKLPLgldtpigengvLLSGGQRQRLAIARALLKDA 488
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 164 DVILFDEPTSALDPELVGEVLNTIRQLAQEkRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGEAKALFA 233
Cdd:TIGR02203 489 PILILDEATSALDNESERLVQAALERLMQG-RTTLVIAHRLSTIEK-ADRIVVMDDGRIVERGTHNELLA 556
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
16-244 |
2.12e-34 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 129.05 E-value: 2.12e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 16 QTVLHGIDLEVQKGEVVAIIGPSGSGKT-TLLRSINLLEQPE----SGTIRVgdvtidAGRSL--GPQKGLiRQLR-QHV 87
Cdd:PRK15134 22 RTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRF------HGESLlhASEQTL-RGVRgNKI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 88 GFVFQN--FNLFPHRTVLENIIEGPVIVKGEDKQESMARARELLAKVGL---SGKENSYPRRLSGGQQQRVAIARALAMR 162
Cdd:PRK15134 95 AMIFQEpmVSLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIrqaAKRLTDYPHQLSGGERQRVMIAMALLTR 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 163 PDVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGEAKALFASPQQPRTR 241
Cdd:PRK15134 175 PELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAPTHPYTQ 254
|
...
gi 1879798416 242 QFL 244
Cdd:PRK15134 255 KLL 257
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
15-223 |
2.17e-34 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 123.06 E-value: 2.17e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 15 GQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDAGRSlgpqkGLIRQLRQHVGFVFQNF 94
Cdd:PRK10908 14 GRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKN-----REVPFLRRQIGMIFQDH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 95 NLFPHRTVLENIiEGPVIVKGEDKQESMARARELLAKVGLSGKENSYPRRLSGGQQQRVAIARALAMRPDVILFDEPTSA 174
Cdd:PRK10908 89 HLLMDRTVYDNV-AIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGN 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1879798416 175 LDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIV 223
Cdd:PRK10908 168 LDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
13-213 |
5.48e-34 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 121.19 E-value: 5.48e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 13 FHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGdvtidAGRSLG--PQKG-LIRQL----RQ 85
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRA-----GGARVAyvPQRSeVPDSLpltvRD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 86 HVGFvfqnfNLFPHRTVLENIiegpvivKGEDKqesmARARELLAKVGLSGKENSYPRRLSGGQQQRVAIARALAMRPDV 165
Cdd:NF040873 77 LVAM-----GRWARRGLWRRL-------TRDDR----AAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADL 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1879798416 166 ILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDvADR 213
Cdd:NF040873 141 LLLDEPTTGLDAESRERIIALLAEEHARGATVVVVTHDLELVRR-ADP 187
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-224 |
6.71e-34 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 127.49 E-value: 6.71e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 4 IEVKSLVKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGdVTIdagrslgpqkglirql 83
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLG-ETV---------------- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 84 rqHVGFVFQNF-NLFPHRTVLENIIEGpvivkGEDKQESMARAreLLAKVGLSGKE-NSYPRRLSGGQQQRVAIARALAM 161
Cdd:COG0488 379 --KIGYFDQHQeELDPDKTVLDELRDG-----APGGTEQEVRG--YLGRFLFSGDDaFKPVGVLSGGEKARLALAKLLLS 449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1879798416 162 RPDVILFDEPTSALDPELVgEVLNTIrqLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVE 224
Cdd:COG0488 450 PPNVLLLDEPTNHLDIETL-EALEEA--LDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVRE 509
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
22-245 |
1.44e-33 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 122.18 E-value: 1.44e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 22 IDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDAgrslgPQKGLIRQLRQHVGFVFQNFNLFPHRT 101
Cdd:PRK11831 26 ISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPA-----MSRSRLYTVRKRMSMLFQSGALFTDMN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 102 VLEN--------------IIEGPVIVKgedkqesmararelLAKVGLSGKENSYPRRLSGGQQQRVAIARALAMRPDVIL 167
Cdd:PRK11831 101 VFDNvayplrehtqlpapLLHSTVMMK--------------LEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIM 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1879798416 168 FDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGEAKALFASPqQPRTRQFLE 245
Cdd:PRK11831 167 FDEPFVGQDPITMGVLVKLISELNSAlGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANP-DPRVRQFLD 244
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-236 |
1.88e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 122.22 E-value: 1.88e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 2 SAIEVK--SLVKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVgdVTIDaGRSLGPQKgl 79
Cdd:PRK13640 4 NIVEFKhvSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSK--ITVD-GITLTAKT-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 80 IRQLRQHVGFVFQN-FNLFPHRTV-------LENiiegpvivKGEDKQESMARARELLAKVGLSGKENSYPRRLSGGQQQ 151
Cdd:PRK13640 79 VWDIREKVGIVFQNpDNQFVGATVgddvafgLEN--------RAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 152 RVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFArDVADRAIFMDQGRIVEQGEAKA 230
Cdd:PRK13640 151 RVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNlTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVE 229
|
....*.
gi 1879798416 231 LFASPQ 236
Cdd:PRK13640 230 IFSKVE 235
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
20-244 |
2.88e-33 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 120.96 E-value: 2.88e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 20 HGIDLEVQKGEVVAIIGPSGSGKTtlLRSINLLEQPESGTIRV-GDVTIDaGRSLGPQkglirQLR-QHVGFVFQN---- 93
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKS--LTCAAALGILPAGVRQTaGRVLLD-GKPVAPC-----ALRgRKIATIMQNprsa 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 94 FNlfPHRTVLENIIEgpvIVKGEDKQESMARARELLAKVGLSGKE---NSYPRRLSGGQQQRVAIARALAMRPDVILFDE 170
Cdd:PRK10418 92 FN--PLHTMHTHARE---TCLALGKPADDATLTAALEAVGLENAArvlKLYPFEMSGGMLQRMMIALALLCEAPFIIADE 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1879798416 171 PTSALDPELVGEVLNTIRQLAQEKRT-MVIVTHEMSFARDVADRAIFMDQGRIVEQGEAKALFASPQQPRTRQFL 244
Cdd:PRK10418 167 PTTDLDVVAQARILDLLESIVQKRALgMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLV 241
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
16-226 |
3.59e-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: 118.57 E-value: 3.59e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 16 QTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDAgrslgpqkgLIRQLRQHVGFVFQNFN 95
Cdd:cd03247 15 QQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSD---------LEKALSSLISVLNQRPY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 96 LFpHRTVLENIiegpvivkgedkqesmararellakvglsgkensyPRRLSGGQQQRVAIARALAMRPDVILFDEPTSAL 175
Cdd:cd03247 86 LF-DTTLRNNL-----------------------------------GRRFSGGERQRLALARILLQDAPIVLLDEPTVGL 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1879798416 176 DPELVGEVLNTIRQLAQEKrTMVIVTHEMSfARDVADRAIFMDQGRIVEQG 226
Cdd:cd03247 130 DPITERQLLSLIFEVLKDK-TLIWITHHLT-GIEHMDKILFLENGKIIMQG 178
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
7-245 |
8.48e-33 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 124.82 E-value: 8.48e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 7 KSLVKKFHGQ-TVLHGIDLEVQKGEVVAIIGPSGSGKTT----LLRSINlleqpesgtiRVGDVTIDAGrslgPQKGLIR 81
Cdd:PRK15134 289 KGILKRTVDHnVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN----------SQGEIWFDGQ----PLHNLNR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 82 Q----LRQHVGFVFQNFN--LFPHRTVLENIIEG-PVIVKGEDKQESMARARELLAKVGLSGK-ENSYPRRLSGGQQQRV 153
Cdd:PRK15134 355 RqllpVRHRIQVVFQDPNssLNPRLNVLQIIEEGlRVHQPTLSAAQREQQVIAVMEEVGLDPEtRHRYPAEFSGGQRQRI 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 154 AIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVI-VTHEMSFARDVADRAIFMDQGRIVEQGEAKALF 232
Cdd:PRK15134 435 AIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLfISHDLHVVRALCHQVIVLRQGEVVEQGDCERVF 514
|
250
....*....|...
gi 1879798416 233 ASPQQPRTRQFLE 245
Cdd:PRK15134 515 AAPQQEYTRQLLA 527
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
22-244 |
1.57e-32 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 121.00 E-value: 1.57e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 22 IDLEVQKGEVVAIIGPSGSGKT-TLLRSINLLEQPesgtirvGDVTIDA----GRSLgpQKGLIRQLRQHVG----FVFQ 92
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYP-------GRVMAEKlefnGQDL--QRISEKERRNLVGaevaMIFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 93 N--FNLFPHRTVLENIIEGPVIVKGEDKQESMARARELLAKVGLSGKE---NSYPRRLSGGQQQRVAIARALAMRPDVIL 167
Cdd:PRK11022 97 DpmTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPAsrlDVYPHQLSGGMSQRVMIAMAIACRPKLLI 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1879798416 168 FDEPTSALDPELVGEVLNTIRQLAQ-EKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGEAKALFASPQQPRTRQFL 244
Cdd:PRK11022 177 ADEPTTALDVTIQAQIIELLLELQQkENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAPRHPYTQALL 254
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
18-221 |
1.63e-32 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 117.57 E-value: 1.63e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 18 VLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSInLLE-QPESGTIRVGdvtidaGR-SLGPQKGLIrqlrqhvgfvfQNfn 95
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSAL-LGElEKLSGSVSVP------GSiAYVSQEPWI-----------QN-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 96 lfphRTVLENIIEGpvivKGEDKQ--ESMARA------RELLAK-----VGLSGkensypRRLSGGQQQRVAIARALAMR 162
Cdd:cd03250 80 ----GTIRENILFG----KPFDEEryEKVIKAcalepdLEILPDgdlteIGEKG------INLSGGQKQRISLARAVYSD 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1879798416 163 PDVILFDEPTSALDPElVGEVL--NTIRQLAQEKRTMVIVTHEMSFARDvADRAIFMDQGR 221
Cdd:cd03250 146 ADIYLLDDPLSAVDAH-VGRHIfeNCILGLLLNNKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
6-244 |
1.66e-32 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 119.26 E-value: 1.66e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 6 VKSLVKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTI----RVGDVTIDAGRSLGPQKGLir 81
Cdd:PRK11701 9 VRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVhyrmRDGQLRDLYALSEAERRRL-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 82 qLRQHVGFVFQNF--NLFPHRTVLENIIEGPVIVKGEDKQESMARARELLAKVGL-SGKENSYPRRLSGGQQQRVAIARA 158
Cdd:PRK11701 87 -LRTEWGFVHQHPrdGLRMQVSAGGNIGERLMAVGARHYGDIRATAGDWLERVEIdAARIDDLPTTFSGGMQQRLQIARN 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 159 LAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADRAIFMDQGRIVEQGEAKALFASPQQ 237
Cdd:PRK11701 166 LVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGlAVVIVTHDLAVARLLAHRLLVMKQGRVVESGLTDQVLDDPQH 245
|
....*..
gi 1879798416 238 PRTrQFL 244
Cdd:PRK11701 246 PYT-QLL 251
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
22-244 |
2.14e-32 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 124.20 E-value: 2.14e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 22 IDLEVQKGEVVAIIGPSGSGKT-TLLRSINLLEQpESGTIRVGDV--------TIDAGRSLGPQKGLIRQlrQHVGFVFQ 92
Cdd:PRK10261 35 LSFSLQRGETLAIVGESGSGKSvTALALMRLLEQ-AGGLVQCDKMllrrrsrqVIELSEQSAAQMRHVRG--ADMAMIFQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 93 N--FNLFPHRTVLENIIEGPVIVKGEDKQESMARARELLAKVGLSGKE---NSYPRRLSGGQQQRVAIARALAMRPDVIL 167
Cdd:PRK10261 112 EpmTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQtilSRYPHQLSGGMRQRVMIAMALSCRPAVLI 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1879798416 168 FDEPTSALDPELVGEVLNTIRQLAQEKRTMVI-VTHEMSFARDVADRAIFMDQGRIVEQGEAKALFASPQQPRTRQFL 244
Cdd:PRK10261 192 ADEPTTALDVTIQAQILQLIKVLQKEMSMGVIfITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAPQHPYTRALL 269
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-229 |
2.21e-32 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 118.26 E-value: 2.21e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 1 MS-AIEVKSLVKKFHGQ----------------------TVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPES 57
Cdd:COG1134 1 MSsMIEVENVSKSYRLYhepsrslkelllrrrrtrreefWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 58 GTIRV-GDVT--IDAGrslgpqkglirqlrqhVGFVfqnfnlfPHRTVLENIIEGPVIVkGEDKQESMARARELLAKVGL 134
Cdd:COG1134 81 GRVEVnGRVSalLELG----------------AGFH-------PELTGRENIYLNGRLL-GLSRKEIDEKFDEIVEFAEL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 135 SGKENSYPRRLSGGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRA 214
Cdd:COG1134 137 GDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGAVRRLCDRA 216
|
250
....*....|....*
gi 1879798416 215 IFMDQGRIVEQGEAK 229
Cdd:COG1134 217 IWLEKGRLVMDGDPE 231
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-235 |
2.47e-32 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 121.87 E-value: 2.47e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 1 MSAIEVKSLVKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDAGRSlgpqkgli 80
Cdd:PRK09536 1 MPMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSA-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 81 RQLRQHVGFVFQNFNL---FPHRTVLEnIIEGPVIVKGEDKQESMARA-RELLAKVGLSGKENSYPRRLSGGQQQRVAIA 156
Cdd:PRK09536 73 RAASRRVASVPQDTSLsfeFDVRQVVE-MGRTPHRSRFDTWTETDRAAvERAMERTGVAQFADRPVTSLSGGERQRVLLA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1879798416 157 RALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGEAKALFASP 235
Cdd:PRK09536 152 RALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTAD 230
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-239 |
4.23e-32 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 117.69 E-value: 4.23e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 1 MSAIEVKSLVKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIdagrSLGPqkgLI 80
Cdd:PRK10895 1 MATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDI----SLLP---LH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 81 RQLRQHVGFVFQNFNLFPHRTVLENIIEGPVIVKGEDKQESMARARELLAKVGLSGKENSYPRRLSGGQQQRVAIARALA 160
Cdd:PRK10895 74 ARARRGIGYLPQEASIFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1879798416 161 MRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGEAKALFASPQQPR 239
Cdd:PRK10895 154 ANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKR 232
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
17-234 |
6.94e-32 |
|
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: 122.62 E-value: 6.94e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 17 TVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRsinLLEQ---PESGTIRVG-----DVTIDAgrslgpqkglirqLRQHVG 88
Cdd:COG5265 372 PILKGVSFEVPAGKTVAIVGPSGAGKSTLAR---LLFRfydVTSGRILIDgqdirDVTQAS-------------LRAAIG 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 89 FVFQNFNLFpHRTVLENIIEG-PvivkGEDKQESMARARelLA---------------KVGLSGkensypRRLSGGQQQR 152
Cdd:COG5265 436 IVPQDTVLF-NDTIAYNIAYGrP----DASEEEVEAAAR--AAqihdfieslpdgydtRVGERG------LKLSGGEKQR 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 153 VAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEkRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGEAKALF 232
Cdd:COG5265 503 VAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARG-RTTLVIAHRLSTIVD-ADEILVLEAGRIVERGTHAELL 580
|
..
gi 1879798416 233 AS 234
Cdd:COG5265 581 AQ 582
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
4-241 |
7.09e-32 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 117.24 E-value: 7.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 4 IEVKSLVKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDvtidagRSLGPQKGLI--- 80
Cdd:TIGR02323 4 LQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIM------RSGAELELYQlse 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 81 ----RQLRQHVGFVFQNFNLFPHRTVLE--NIIEGPVIVKGEDKQESMARARELLAKVGLS-GKENSYPRRLSGGQQQRV 153
Cdd:TIGR02323 78 aerrRLMRTEWGFVHQNPRDGLRMRVSAgaNIGERLMAIGARHYGNIRATAQDWLEEVEIDpTRIDDLPRAFSGGMQQRL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 154 AIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADRAIFMDQGRIVEQGEAKALF 232
Cdd:TIGR02323 158 QIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGlAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQVL 237
|
....*....
gi 1879798416 233 ASPQQPRTR 241
Cdd:TIGR02323 238 DDPQHPYTQ 246
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
10-222 |
7.39e-32 |
|
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: 115.22 E-value: 7.39e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 10 VKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDAGRSLGPQK---GLIRQLRQH 86
Cdd:cd03215 7 VRGLSVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRagiAYVPEDRKR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 87 VGfvfqnfnLFPHRTVLENIIegpvivkgedkqesmararellakvglsgkensYPRRLSGGQQQRVAIARALAMRPDVI 166
Cdd:cd03215 87 EG-------LVLDLSVAENIA---------------------------------LSSLLSGGNQQKVVLARWLARDPRVL 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1879798416 167 LFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRI 222
Cdd:cd03215 127 ILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
19-226 |
1.40e-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: 121.92 E-value: 1.40e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 19 LHGIDLEVQKGEVVAIIGPSGSGKTTLlrsINLLEQ---PESGTIRVGDVTIDAGRSlgpqkgliRQLRQHVGFVFQNFN 95
Cdd:TIGR01192 351 VFDVSFEAKAGQTVAIVGPTGAGKTTL---INLLQRvydPTVGQILIDGIDINTVTR--------ESLRKSIATVFQDAG 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 96 LFpHRTVLENIIEGPvivKGEDKQESMARARELLAKVGLSGKENSYP-------RRLSGGQQQRVAIARALAMRPDVILF 168
Cdd:TIGR01192 420 LF-NRSIRENIRLGR---EGATDEEVYEAAKAAAAHDFILKRSNGYDtlvgergNRLSGGERQRLAIARAILKNAPILVL 495
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1879798416 169 DEPTSALDPELVGEVLNTIRQLAQEkRTMVIVTHEMSFARDvADRAIFMDQGRIVEQG 226
Cdd:TIGR01192 496 DEATSALDVETEARVKNAIDALRKN-RTTFIIAHRLSTVRN-ADLVLFLDQGRLIEKG 551
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
22-244 |
1.62e-31 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 121.89 E-value: 1.62e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 22 IDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDagrSLGPQKglIRQLRQHVGFVFQN--FNLFPH 99
Cdd:PRK10261 343 VSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRID---TLSPGK--LQALRRDIQFIFQDpyASLDPR 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 100 RTVLENIIEgPVIVKG-EDKQESMARARELLAKVGLSGKEN-SYPRRLSGGQQQRVAIARALAMRPDVILFDEPTSALDP 177
Cdd:PRK10261 418 QTVGDSIME-PLRVHGlLPGKAAAARVAWLLERVGLLPEHAwRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDV 496
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1879798416 178 ELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGEAKALFASPQQPRTRQFL 244
Cdd:PRK10261 497 SIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLM 564
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
16-235 |
5.88e-31 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 120.60 E-value: 5.88e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 16 QTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTirvgdVTIDAGRslgpqkglIRQ-----LRQHVGFV 90
Cdd:TIGR00958 494 VPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQ-----VLLDGVP--------LVQydhhyLHRQVALV 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 91 FQNFNLFpHRTVLENIIEGpviVKGEDKQESMARARELLAKVGLSGKENSYPR-------RLSGGQQQRVAIARALAMRP 163
Cdd:TIGR00958 561 GQEPVLF-SGSVRENIAYG---LTDTPDEEIMAAAKAANAHDFIMEFPNGYDTevgekgsQLSGGQKQRIAIARALVRKP 636
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1879798416 164 DVILFDEPTSALDPElvgevlntIRQLAQE-----KRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGEAKALFASP 235
Cdd:TIGR00958 637 RVLILDEATSALDAE--------CEQLLQEsrsraSRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
4-236 |
9.17e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 115.19 E-value: 9.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 4 IEVKSLVKKFHGQT---VLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSIN-LLEQPEsgtirvGDVTIDAGRSLGPQkgl 79
Cdd:PRK13642 5 LEVENLVFKYEKESdvnQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDgLFEEFE------GKVKIDGELLTAEN--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 80 IRQLRQHVGFVFQN-FNLFPHRTVLENIIEGpVIVKGEDKQESMARARELLAKVGLSGKENSYPRRLSGGQQQRVAIARA 158
Cdd:PRK13642 76 VWNLRRKIGMVFQNpDNQFVGATVEDDVAFG-MENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1879798416 159 LAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDvADRAIFMDQGRIVEQGEAKALFASPQ 236
Cdd:PRK13642 155 IALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQlTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATSE 232
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
18-234 |
6.61e-30 |
|
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: 117.54 E-value: 6.61e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 18 VLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDAgrsLGPQkglirQLRQHVGFVFQNFNLF 97
Cdd:TIGR01846 472 VLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAI---ADPA-----WLRRQMGVVLQENVLF 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 98 pHRTVLENIIEGPvivKGEDKQESMARARELLAKVGLSGKENSYPRR-------LSGGQQQRVAIARALAMRPDVILFDE 170
Cdd:TIGR01846 544 -SRSIRDNIALCN---PGAPFEHVIHAAKLAGAHDFISELPQGYNTEvgekganLSGGQRQRIAIARALVGNPRILIFDE 619
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1879798416 171 PTSALDPELVGEVLNTIRQLAQeKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGEAKALFAS 234
Cdd:TIGR01846 620 ATSALDYESEALIMRNMREICR-GRTVIIIAHRLSTVRA-CDRIIVLEKGQIAESGRHEELLAL 681
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
10-223 |
7.50e-30 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 116.27 E-value: 7.50e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 10 VKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDAGRslgpqkglIRQ-LRQHVG 88
Cdd:COG1129 259 VEGLSVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRS--------PRDaIRAGIA 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 89 FVFQN---FNLFPHRTVLENII--------EGPVIvkgeDKQESMARARELLAKVGLSGKENSYP-RRLSGGQQQRVAIA 156
Cdd:COG1129 331 YVPEDrkgEGLVLDLSIRENITlasldrlsRGGLL----DRRRERALAEEYIKRLRIKTPSPEQPvGNLSGGNQQKVVLA 406
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 157 RALAMRPDVILFDEPTSALDpelVG---EVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIV 223
Cdd:COG1129 407 KWLATDPKVLILDEPTRGID---VGakaEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRIV 473
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
17-226 |
1.05e-29 |
|
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: 110.70 E-value: 1.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 17 TVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRV-GDVT--IDAGrslgpqkglirqlrqhVGFVfqn 93
Cdd:cd03220 36 WALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVrGRVSslLGLG----------------GGFN--- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 94 fnlfPHRTVLENI-IEGpvIVKGEDKQESMARARELlakVGLSGKENSY--P-RRLSGGQQQRVAIARALAMRPDVILFD 169
Cdd:cd03220 97 ----PELTGRENIyLNG--RLLGLSRKEIDEKIDEI---IEFSELGDFIdlPvKTYSSGMKARLAFAIATALEPDILLID 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1879798416 170 EPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQG 226
Cdd:cd03220 168 EVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
15-202 |
1.35e-29 |
|
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: 115.92 E-value: 1.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 15 GQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDAGRSlgpqkgliRQLRQHVGFVFQNF 94
Cdd:TIGR02868 347 APPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQ--------DEVRRRVSVCAQDA 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 95 NLFpHRTVLENIIEGPVIVKGEDKQESMARAR--ELLAKV--GLSGKENSYPRRLSGGQQQRVAIARALAMRPDVILFDE 170
Cdd:TIGR02868 419 HLF-DTTVRENLRLARPDATDEELWAALERVGlaDWLRALpdGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDE 497
|
170 180 190
....*....|....*....|....*....|..
gi 1879798416 171 PTSALDPELVGEVLNTIRQlAQEKRTMVIVTH 202
Cdd:TIGR02868 498 PTEHLDAETADELLEDLLA-ALSGRTVVLITH 528
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-235 |
1.42e-29 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 116.10 E-value: 1.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 4 IEVKSLVKKFHGQTVLHG-IDLEVQKGEVVAIIGPSGSGKTTLLrsiNLLEQ--PESGTIRVGDVTIdagRSLGPQkgli 80
Cdd:PRK11174 350 IEAEDLEILSPDGKTLAGpLNFTLPAGQRIALVGPSGAGKTSLL---NALLGflPYQGSLKINGIEL---RELDPE---- 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 81 rQLRQHVGFVFQNFNLFpHRTVLENIIEGPVIVKGEDKQESMARAR--ELLAKV--GLSG--KENSypRRLSGGQQQRVA 154
Cdd:PRK11174 420 -SWRKHLSWVGQNPQLP-HGTLRDNVLLGNPDASDEQLQQALENAWvsEFLPLLpqGLDTpiGDQA--AGLSVGQAQRLA 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 155 IARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKrTMVIVTHEMSFARDVaDRAIFMDQGRIVEQGEAKALFAS 234
Cdd:PRK11174 496 LARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQ-TTLMVTHQLEDLAQW-DQIWVMQDGQIVQQGDYAELSQA 573
|
.
gi 1879798416 235 P 235
Cdd:PRK11174 574 G 574
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
15-233 |
2.52e-29 |
|
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: 115.61 E-value: 2.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 15 GQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDAGRslgpqkglIRQLRQHVGFVFQNF 94
Cdd:TIGR01193 486 GSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDID--------RHTLRQFINYLPQEP 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 95 NLFPHrTVLENIIEGpviVKGEDKQESMARARELLA--------KVGLSGKENSYPRRLSGGQQQRVAIARALAMRPDVI 166
Cdd:TIGR01193 558 YIFSG-SILENLLLG---AKENVSQDEIWAACEIAEikddienmPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVL 633
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1879798416 167 LFDEPTSALDPELVGEVLNTIRQLaQEKrTMVIVTHEMSFARDVaDRAIFMDQGRIVEQGEAKALFA 233
Cdd:TIGR01193 634 ILDESTSNLDTITEKKIVNNLLNL-QDK-TIIFVAHRLSVAKQS-DKIIVLDHGKIIEQGSHDELLD 697
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
5-226 |
3.12e-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: 3.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 5 EVKSLVKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSI--NLLEQPESGTIRVG--DVTidagrSLGP----Q 76
Cdd:COG0396 2 EIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmgHPKYEVTSGSILLDgeDIL-----ELSPderaR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 77 KGLirqlrqhvGFVFQ---------NFNLFphRTVLENIIEGPVivkgeDKQESMARARELLAKVGLSgkeNSYPRR--- 144
Cdd:COG0396 77 AGI--------FLAFQypveipgvsVSNFL--RTALNARRGEEL-----SAREFLKLLKEKMKELGLD---EDFLDRyvn 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 145 --LSGGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHemsFAR----DVADRAIFMD 218
Cdd:COG0396 139 egFSGGEKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITH---YQRildyIKPDFVHVLV 215
|
....*...
gi 1879798416 219 QGRIVEQG 226
Cdd:COG0396 216 DGRIVKSG 223
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
4-226 |
3.81e-29 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 115.14 E-value: 3.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 4 IEVKSLVKKFHGQ--------TVLHGIDLEVQKGEVVAIIGPSGSGKTTLLrsiNLLEQ-PESGTIRVGDVTIDaGRSLG 74
Cdd:TIGR00955 18 GSWKQLVSRLRGCfcrerprkHLLKNVSGVAKPGELLAVMGSSGAGKTTLM---NALAFrSPKGVKGSGSVLLN-GMPID 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 75 PqkgliRQLRQHVGFVFQNFNLFPHRTVLENIIEGPVIVKGED--KQESMARARELLAKVGLS-------GKENSYpRRL 145
Cdd:TIGR00955 94 A-----KEMRAISAYVQQDDLFIPTLTVREHLMFQAHLRMPRRvtKKEKRERVDEVLQALGLRkcantriGVPGRV-KGL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 146 SGGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMS---FarDVADRAIFMDQGRI 222
Cdd:TIGR00955 168 SGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSselF--ELFDKIILMAEGRV 245
|
....
gi 1879798416 223 VEQG 226
Cdd:TIGR00955 246 AYLG 249
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
14-202 |
8.32e-29 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 113.75 E-value: 8.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 14 HGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDvtidAGRSLG-PQK------GLIRQLrqh 86
Cdd:COG4178 374 DGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPA----GARVLFlPQRpylplgTLREAL--- 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 87 vgfvfqnfnLFPHrtvleniiegpvivkgEDKQESMARARELLAKVGLS------GKENSYPRRLSGGQQQRVAIARALA 160
Cdd:COG4178 447 ---------LYPA----------------TAEAFSDAELREALEAVGLGhlaerlDEEADWDQVLSLGEQQRLAFARLLL 501
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1879798416 161 MRPDVILFDEPTSALDPELVGEVLNTIRQlAQEKRTMVIVTH 202
Cdd:COG4178 502 HKPDWLFLDEATSALDEENEAALYQLLRE-ELPGTTVISVGH 542
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
16-228 |
9.44e-29 |
|
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: 113.60 E-value: 9.44e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 16 QTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDA--GRSLGPqkglirqlrqHVGFVFQN 93
Cdd:TIGR01842 331 KPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQwdRETFGK----------HIGYLPQD 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 94 FNLFPHrTVLENIIEGPVIVKGEDKQES--MARARELLAK--------VGLSGKEnsyprrLSGGQQQRVAIARALAMRP 163
Cdd:TIGR01842 401 VELFPG-TVAENIARFGENADPEKIIEAakLAGVHELILRlpdgydtvIGPGGAT------LSGGQRQRIALARALYGDP 473
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1879798416 164 DVILFDEPTSALDPElvGE--VLNTIRQLAQEKRTMVIVTHEMSfARDVADRAIFMDQGRIVEQGEA 228
Cdd:TIGR01842 474 KLVVLDEPNSNLDEE--GEqaLANAIKALKARGITVVVITHRPS-LLGCVDKILVLQDGRIARFGER 537
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
16-226 |
1.38e-28 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 108.56 E-value: 1.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 16 QTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDAgrsLGPqkgliRQLRQHVGFVFQnfn 95
Cdd:PRK11231 15 KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISM---LSS-----RQLARRLALLPQ--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 96 lfpHRTVLENIIEGPVIVKG------------EDKQESMARARELLAKVGLSGKENSyprRLSGGQQQRVAIARALAMRP 163
Cdd:PRK11231 84 ---HHLTPEGITVRELVAYGrspwlslwgrlsAEDNARVNQAMEQTRINHLADRRLT---DLSGGQRQRAFLAMVLAQDT 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1879798416 164 DVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQG 226
Cdd:PRK11231 158 PVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQG 220
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-229 |
1.98e-28 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 112.57 E-value: 1.98e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 4 IEVKSLVKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDagrSLGPQkgLIRQL 83
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYN---KLDHK--LAAQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 84 rqHVGFVFQNFNLFPHRTVLENIIEGPVIVKGE------DKQESMARARELLAKVGLSGKENSYPRRLSGGQQQRVAIAR 157
Cdd:PRK09700 81 --GIGIIYQELSVIDELTVLENLYIGRHLTKKVcgvniiDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAK 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1879798416 158 ALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGEAK 229
Cdd:PRK09700 159 TLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVS 230
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-226 |
2.45e-28 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 107.90 E-value: 2.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 5 EVKSLVKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGdvtidaGRSLgpqkgliRQLR 84
Cdd:COG4674 12 YVEDLTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFG------GTDL-------TGLD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 85 QH------VGFVFQNFNLFPHRTVLENIIegpvIVKGEDK-----------QESMARARELLAKVGLSGKENSYPRRLSG 147
Cdd:COG4674 79 EHeiarlgIGRKFQKPTVFEELTVFENLE----LALKGDRgvfaslfarltAEERDRIEEVLETIGLTDKADRLAGLLSH 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 148 GQQQRVAIARALAMRPDVILFDEPTSALDP---ELVGEVLNTIRQlaqeKRTMVIVTHEMSFARDVADRAIFMDQGRIVE 224
Cdd:COG4674 155 GQKQWLEIGMLLAQDPKLLLLDEPVAGMTDaetERTAELLKSLAG----KHSVVVVEHDMEFVRQIARKVTVLHQGSVLA 230
|
..
gi 1879798416 225 QG 226
Cdd:COG4674 231 EG 232
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
18-234 |
4.73e-28 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 106.89 E-value: 4.73e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 18 VLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDAGRSlgpqkglIRQLRQHVGFVFQNFNLF 97
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQT-------AKIMREAVAIVPEGRRVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 98 PHRTVLENIIEGPVIVKGEDKQESMARARELLAKvgLSGKENSYPRRLSGGQQQRVAIARALAMRPDVILFDEPTSALDP 177
Cdd:PRK11614 93 SRMTVEENLAMGGFFAERDQFQERIKWVYELFPR--LHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1879798416 178 ELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGEAKALFAS 234
Cdd:PRK11614 171 IIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLAN 227
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-221 |
1.39e-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: 102.91 E-value: 1.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 4 IEVKSLVKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTidagrslgpqkglirql 83
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTV----------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 84 rqhvgfvfqnfnlfphrtvleniiegpvivkgedkqesmararellaKVGlsgkensYPRRLSGGQQQRVAIARALAMRP 163
Cdd:cd03221 64 -----------------------------------------------KIG-------YFEQLSGGEKMRLALAKLLLENP 89
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1879798416 164 DVILFDEPTSALDPELVgEVLntIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGR 221
Cdd:cd03221 90 NLLLLDEPTNHLDLESI-EAL--EEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-231 |
2.18e-27 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 107.61 E-value: 2.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 1 MSAIEVKSLVKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVtidagrslgPQKGLI 80
Cdd:PRK13536 39 TVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGV---------PVPARA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 81 RQLRQHVGFVFQNFNLFPHRTVLENIIegpVIVK--GEDKQESMARARELLAKVGLSGKENSYPRRLSGGQQQRVAIARA 158
Cdd:PRK13536 110 RLARARIGVVPQFDNLDLEFTVRENLL---VFGRyfGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARA 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1879798416 159 LAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGEAKAL 231
Cdd:PRK13536 187 LINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHAL 259
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
11-234 |
3.25e-27 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 109.58 E-value: 3.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 11 KKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSInlleqpeSGTIRVGDVTidaGRSLGPQKGLIRQLRQHVGFV 90
Cdd:PLN03211 76 RQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNAL-------AGRIQGNNFT---GTILANNRKPTKQILKRTGFV 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 91 FQNFNLFPHRTVLENIIEGPVI--VKGEDKQESMARARELLAKVGLSGKEN-----SYPRRLSGGQQQRVAIARALAMRP 163
Cdd:PLN03211 146 TQDDILYPHLTVRETLVFCSLLrlPKSLTKQEKILVAESVISELGLTKCENtiignSFIRGISGGERKRVSIAHEMLINP 225
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1879798416 164 DVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHE-MSFARDVADRAIFMDQGRIVEQG---EAKALFAS 234
Cdd:PLN03211 226 SLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQpSSRVYQMFDSVLVLSEGRCLFFGkgsDAMAYFES 300
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
4-226 |
2.01e-26 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 102.19 E-value: 2.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 4 IEVKSLVKKF--HGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIdagRSLGPQKglir 81
Cdd:cd03244 3 IEFKNVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDI---SKIGLHD---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 82 qLRQHVGFVFQNFNLFPHrTVLENIieGPvivkgeDKQESMARARELLAKVGLSGKENSYPRRL-----------SGGQQ 150
Cdd:cd03244 76 -LRSRISIIPQDPVLFSG-TIRSNL--DP------FGEYSDEELWQALERVGLKEFVESLPGGLdtvveeggenlSVGQR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1879798416 151 QRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQlAQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQG 226
Cdd:cd03244 146 QLLCLARALLRKSKILVLDEATASVDPETDALIQKTIRE-AFKDCTVLTIAHRLDTIID-SDRILVLDKGRVVEFD 219
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
12-233 |
3.81e-26 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 102.78 E-value: 3.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 12 KFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIrvgdvtIDAGRSLGPQKGLIRQLRQHVGFVF 91
Cdd:PRK13638 10 RYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAV------LWQGKPLDYSKRGLLALRQQVATVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 92 QNfnlfPHRTVLENIIEGPVIVK----GEDKQESMARARELLAKVGLSGKENSYPRRLSGGQQQRVAIARALAMRPDVIL 167
Cdd:PRK13638 84 QD----PEQQIFYTDIDSDIAFSlrnlGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1879798416 168 FDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGEAKALFA 233
Cdd:PRK13638 160 LDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFA 225
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1-224 |
5.11e-26 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 105.76 E-value: 5.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 1 MSAIEVKSLVKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVT---------IDAGr 71
Cdd:PRK11288 2 SPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEmrfasttaaLAAG- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 72 slgpqkglirqlrqhVGFVFQNFNLFPHRTVLENIIEGPVIVKGE--DKQESMARARELLAKVGLSGKENSYPRRLSGGQ 149
Cdd:PRK11288 81 ---------------VAIIYQELHLVPEMTVAENLYLGQLPHKGGivNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1879798416 150 QQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADR-AIFMDqGRIVE 224
Cdd:PRK11288 146 RQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAiTVFKD-GRYVA 220
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
4-244 |
5.21e-26 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 102.18 E-value: 5.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 4 IEVKSLVKK-------FHGQTV--LHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDAG---- 70
Cdd:PRK15112 5 LEVRNLSKTfryrtgwFRRQTVeaVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGdysy 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 71 RSlgpqkglirqlrQHVGFVFQN--FNLFPhRTVLENIIEGPVIVKGE-DKQESMARARELLAKVGL-SGKENSYPRRLS 146
Cdd:PRK15112 85 RS------------QRIRMIFQDpsTSLNP-RQRISQILDFPLRLNTDlEPEQREKQIIETLRQVGLlPDHASYYPHMLA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 147 GGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLaQEKR--TMVIVTHEMSFARDVADRAIFMDQGRIVE 224
Cdd:PRK15112 152 PGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLEL-QEKQgiSYIYVTQHLGMMKHISDQVLVMHQGEVVE 230
|
250 260
....*....|....*....|
gi 1879798416 225 QGEAKALFASPQQPRTRQFL 244
Cdd:PRK15112 231 RGSTADVLASPLHELTKRLI 250
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
22-224 |
5.64e-26 |
|
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: 105.65 E-value: 5.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 22 IDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDAGRslgpqkglIRQLRQHVGFVFQNFNLFPHrt 101
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADN--------REAYRQLFSAVFSDFHLFDR-- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 102 vleniiegpviVKGEDKQESMARARELLAKVGLSGK---ENSY--PRRLSGGQQQRVAIARALAMRPDVILFDEPTSALD 176
Cdd:COG4615 421 -----------LLGLDGEADPARARELLERLELDHKvsvEDGRfsTTDLSQGQRKRLALLVALLEDRPILVFDEWAADQD 489
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1879798416 177 P--------ELVGEvlntirqLAQEKRTMVIVTHEMSFArDVADRAIFMDQGRIVE 224
Cdd:COG4615 490 PefrrvfytELLPE-------LKARGKTVIAISHDDRYF-DLADRVLKMDYGKLVE 537
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-238 |
8.71e-26 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 102.88 E-value: 8.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 1 MSAIEVKSLVKKFHGQ----TVLHGIDLEVQKGEVVAIIGPSGSGKT-TLLRSINLLEQpeSGTIRvGDVTIDAGRSLG- 74
Cdd:PRK09473 10 DALLDVKDLRVTFSTPdgdvTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAA--NGRIG-GSATFNGREILNl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 75 PQKGLIRQLRQHVGFVFQN--FNLFPHRTVLENIIEGPVIVKGEDKQESMARARELLAKVGL---SGKENSYPRRLSGGQ 149
Cdd:PRK09473 87 PEKELNKLRAEQISMIFQDpmTSLNPYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMpeaRKRMKMYPHEFSGGM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 150 QQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVI-VTHEMSFARDVADRAIFMDQGRIVEQGEA 228
Cdd:PRK09473 167 RQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIImITHDLGVVAGICDKVLVMYAGRTMEYGNA 246
|
250
....*....|
gi 1879798416 229 KALFASPQQP 238
Cdd:PRK09473 247 RDVFYQPSHP 256
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
4-227 |
1.35e-25 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 100.17 E-value: 1.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 4 IEVKSLVKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIrvgdvtIDAGRSLGpqkgliRQL 83
Cdd:TIGR03740 1 LETKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEI------IFDGHPWT------RKD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 84 RQHVGFVFQNFNLFPHRTVLENIiegPVIVKGEDKQESmaRARELLAKVGLSGKENSYPRRLSGGQQQRVAIARALAMRP 163
Cdd:TIGR03740 69 LHKIGSLIESPPLYENLTARENL---KVHTTLLGLPDS--RIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHP 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1879798416 164 DVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGE 227
Cdd:TIGR03740 144 KLLILDEPTNGLDPIGIQELRELIRSFPEQGITVILSSHILSEVQQLADHIGIISEGVLGYQGK 207
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
4-227 |
1.44e-25 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 104.36 E-value: 1.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 4 IEVKSLVKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVtidagrslgPQKGLIRQL 83
Cdd:PRK15439 12 LCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGN---------PCARLTPAK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 84 RQHVG--FVFQNFNLFPHRTVLENIIEGPvivkgEDKQESMARARELLAKVGLSGKENSYPRRLSGGQQQRVAIARALaM 161
Cdd:PRK15439 83 AHQLGiyLVPQEPLLFPNLSVKENILFGL-----PKRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGL-M 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1879798416 162 RPDVIL-FDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGE 227
Cdd:PRK15439 157 RDSRILiLDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGK 223
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
16-224 |
2.12e-25 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 99.65 E-value: 2.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 16 QTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSI--NLLEQPESGTIRVGDVTIDagrslgpqkglirqlrqhvgfvfqn 93
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLagALKGTPVAGCVDVPDNQFG------------------------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 94 fnlfPHRTVLENIiegpvivkgeDKQESMARARELLAKVGLSGKEN--SYPRRLSGGQQQRVAIARALAMRPDVILFDEP 171
Cdd:COG2401 98 ----REASLIDAI----------GRKGDFKDAVELLNAVGLSDAVLwlRRFKELSTGQKFRFRLALLLAERPKLLVIDEF 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1879798416 172 TSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVA-DRAIFMDQGRIVE 224
Cdd:COG2401 164 CSHLDRQTAKRVARNLQKLARRAGiTLVVATHHYDVIDDLQpDLLIFVGYGGVPE 218
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
15-202 |
2.12e-25 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 98.97 E-value: 2.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 15 GQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDAGRSlgpqkglirQLRQHVGFVFQNF 94
Cdd:TIGR01189 12 ERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRD---------EPHENILYLGHLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 95 NLFPHRTVLENIIEGPVIVKGEDKQesmarARELLAKVGLSGKENSYPRRLSGGQQQRVAIARALAMRPDVILFDEPTSA 174
Cdd:TIGR01189 83 GLKPELSALENLHFWAAIHGGAQRT-----IEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTA 157
|
170 180
....*....|....*....|....*...
gi 1879798416 175 LDPELVGEVLNTIRQLAQEKRTMVIVTH 202
Cdd:TIGR01189 158 LDKAGVALLAGLLRAHLARGGIVLLTTH 185
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
6-226 |
3.60e-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: 103.94 E-value: 3.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 6 VKSLVKKFH--GQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDAGrslgpqkglIRQL 83
Cdd:TIGR01257 931 VKNLVKIFEpsGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETN---------LDAV 1001
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 84 RQHVGFVFQNFNLFPHRTVLENIIEGPVIvKGEDKQESMARARELLAKVGLSGKENSYPRRLSGGQQQRVAIARALAMRP 163
Cdd:TIGR01257 1002 RQSLGMCPQHNILFHHLTVAEHILFYAQL-KGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDA 1080
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1879798416 164 DVILFDEPTSALDPELVGEVLNTIRQLaQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQG 226
Cdd:TIGR01257 1081 KVVVLDEPTSGVDPYSRRSIWDLLLKY-RSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSG 1142
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
6-226 |
7.29e-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: 98.56 E-value: 7.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 6 VKSLVK-KFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDvtidagrsLGPQKGLIRQLR 84
Cdd:cd03267 23 LKSLFKrKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG--------LVPWKRRKKFLR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 85 QhVGFVFQnfnlfpHRTVLenIIEGPVI--------VKGEDKQESMARARELLAKVGLSGKENSYPRRLSGGQQQRVAIA 156
Cdd:cd03267 95 R-IGVVFG------QKTQL--WWDLPVIdsfyllaaIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIA 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1879798416 157 RALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVT-HEMSFARDVADRAIFMDQGRIVEQG 226
Cdd:cd03267 166 AALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTsHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
15-210 |
1.25e-24 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 97.48 E-value: 1.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 15 GQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDAgrsLGPQkglirQLRQHVGFVFQNF 94
Cdd:PRK10247 19 DAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDIST---LKPE-----IYRQQVSYCAQTP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 95 NLFPHrTVLENIIeGPVIVKGedKQESMARARELLAKVGLSgkENSYPRR---LSGGQQQRVAIARALAMRPDVILFDEP 171
Cdd:PRK10247 91 TLFGD-TVYDNLI-FPWQIRN--QQPDPAIFLDDLERFALP--DTILTKNiaeLSGGEKQRISLIRNLQFMPKVLLLDEI 164
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1879798416 172 TSALDPELVGEVLNTIRQLAQEKRTMVI-VTH---EMSFARDV 210
Cdd:PRK10247 165 TSALDESNKHNVNEIIHRYVREQNIAVLwVTHdkdEINHADKV 207
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
4-212 |
1.76e-24 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 101.16 E-value: 1.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 4 IEVKSLVKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLeQPeSGTIRvGDVTIDaGRSLgpQKGLIRQL 83
Cdd:PRK13549 6 LEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YP-HGTYE-GEIIFE-GEEL--QASNIRDT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 84 -RQHVGFVFQNFNLFPHRTVLENIIEGPVIVKGE--DKQESMARARELLAKVGLSGKENSYPRRLSGGQQQRVAIARALA 160
Cdd:PRK13549 80 eRAGIAIIHQELALVKELSVLENIFLGNEITPGGimDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALN 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1879798416 161 MRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVAD 212
Cdd:PRK13549 160 KQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISD 211
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
20-207 |
3.07e-24 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 96.03 E-value: 3.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 20 HGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDAGRS--------LGPQKGLIRQLrqhvgfvf 91
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDeyhqdllyLGHQPGIKTEL-------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 92 qnfnlfphrTVLENI-----IEGPVivkgedKQESMARArelLAKVGLSGKENSYPRRLSGGQQQRVAIAR-ALAMRPDV 165
Cdd:PRK13538 90 ---------TALENLrfyqrLHGPG------DDEALWEA---LAQVGLAGFEDVPVRQLSAGQQRRVALARlWLTRAPLW 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1879798416 166 ILfDEPTSALDPELVGEVLNTIRQLAqEKRTMVIVT--HEMSFA 207
Cdd:PRK13538 152 IL-DEPFTAIDKQGVARLEALLAQHA-EQGGMVILTthQDLPVA 193
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
4-226 |
3.21e-24 |
|
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: 95.67 E-value: 3.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 4 IEVKSLVKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPE--SGTIRVGDVTIDAgrsLGPQKglir 81
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEvtEGEILFKGEDITD---LPPEE---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 82 QLRQHVGFVFQNfnlfPHRtvleniIEGpviVKGEDkqesmarareLLAKVGLSgkensyprrLSGGQQQRVAIARALAM 161
Cdd:cd03217 74 RARLGIFLAFQY----PPE------IPG---VKNAD----------FLRYVNEG---------FSGGEKKRNEILQLLLL 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1879798416 162 RPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTH-EMSFARDVADRAIFMDQGRIVEQG 226
Cdd:cd03217 122 EPDLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHyQRLLDYIKPDRVHVLYDGRIVKSG 187
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4-231 |
1.64e-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: 98.36 E-value: 1.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 4 IEVKSLVKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSInlleqpeSGTIRVGDVTID---AGRSLGPQKglI 80
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKIL-------SGVYPHGTWDGEiywSGSPLKASN--I 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 81 RQL-RQHVGFVFQNFNLFPHRTVLENIIEGPVIV-KGE--DKQESMARARELLAKVGLSGKENSYP-RRLSGGQQQRVAI 155
Cdd:TIGR02633 73 RDTeRAGIVIIHQELTLVPELSVAENIFLGNEITlPGGrmAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1879798416 156 ARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGEAKAL 231
Cdd:TIGR02633 153 AKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTM 228
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
19-233 |
2.88e-23 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 98.17 E-value: 2.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 19 LHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIdagrslgpQKGLIRQLRQHVGFVFQNFNLFp 98
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDL--------RDYTLASLRNQVALVSQNVHLF- 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 99 HRTVLENI------------IEgpvivkgedKQESMARARELLAKV--GLSG--KENSYprRLSGGQQQRVAIARALAMR 162
Cdd:PRK11176 430 NDTIANNIayarteqysreqIE---------EAARMAYAMDFINKMdnGLDTviGENGV--LLSGGQRQRIAIARALLRD 498
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1879798416 163 PDVILFDEPTSALDPELVGEVLNTIRQLaQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGEAKALFA 233
Cdd:PRK11176 499 SPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLSTIEK-ADEILVVEDGEIVERGTHAELLA 567
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
18-222 |
3.10e-23 |
|
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: 94.07 E-value: 3.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 18 VLHGIDLEVQKGEVVAIIGPSGSGKTTLlrsINLLE---QPESGTIRVGDVTIDAGRSlgpqkgliRQLRQHVGFVFQNF 94
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTV---VALLEnfyQPQGGQVLLDGKPISQYEH--------KYLHSKVSLVGQEP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 95 NLFPhRTVLENIIEGpviVKGEDKQESMARARELLAKVGLSGKENSYPR-------RLSGGQQQRVAIARALAMRPDVIL 167
Cdd:cd03248 98 VLFA-RSLQDNIAYG---LQSCSFECVKEAAQKAHAHSFISELASGYDTevgekgsQLSGGQKQRVAIARALIRNPQVLI 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1879798416 168 FDEPTSALDPELVGEVLNTIRQlAQEKRTMVIVTHEMSFARDvADRAIFMDQGRI 222
Cdd:cd03248 174 LDEATSALDAESEQQVQQALYD-WPERRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
15-202 |
5.10e-23 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 92.63 E-value: 5.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 15 GQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDAGRS------LGPQKGLIRQLrqhvg 88
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVaeachyLGHRNAMKPAL----- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 89 fvfqnfnlfphrTVLENIIEGPVIVKGEDkqesmARARELLAKVGLSGKENSYPRRLSGGQQQRVAIARALAMRPDVILF 168
Cdd:PRK13539 89 ------------TVAENLEFWAAFLGGEE-----LDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWIL 151
|
170 180 190
....*....|....*....|....*....|....*.
gi 1879798416 169 DEPTSALDPELVGEVLNTIR-QLAQEkrTMVIV-TH 202
Cdd:PRK13539 152 DEPTAALDAAAVALFAELIRaHLAQG--GIVIAaTH 185
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-226 |
9.59e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 94.38 E-value: 9.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 3 AIEVKSLVKKFH--------GQTV-------------LHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIR 61
Cdd:COG4586 1 IIEVENLSKTYRvyekepglKGALkglfrreyreveaVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 62 VGDVTidagrslgPQKGLIRQLRQhVGFVF-QNFNLFPHRTVLEN------IIEgpviVKGEDKQESMARARELLakvGL 134
Cdd:COG4586 81 VLGYV--------PFKRRKEFARR-IGVVFgQRSQLWWDLPAIDSfrllkaIYR----IPDAEYKKRLDELVELL---DL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 135 SGKENSYPRRLSGGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVT-HEMSfarDV--- 210
Cdd:COG4586 145 GELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTsHDMD---DIeal 221
|
250
....*....|....*.
gi 1879798416 211 ADRAIFMDQGRIVEQG 226
Cdd:COG4586 222 CDRVIVIDHGRIIYDG 237
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
11-226 |
3.77e-22 |
|
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: 90.40 E-value: 3.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 11 KKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSI-NLLEQPES--GTIRVGDVTIdagrslgpqKGLIRQLRQHV 87
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALaNRTEGNVSveGDIHYNGIPY---------KEFAEKYPGEI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 88 GFVFQNFNLFPHRTVleniiegpvivkgedkqesmaraRELLaKVGLSGKENSYPRRLSGGQQQRVAIARALAMRPDVIL 167
Cdd:cd03233 86 IYVSEEDVHFPTLTV-----------------------RETL-DFALRCKGNEFVRGISGGERKRVSIAEALVSRASVLC 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1879798416 168 FDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTheMSFARDVA----DRAIFMDQGRIVEQG 226
Cdd:cd03233 142 WDNSTRGLDSSTALEILKCIRTMADVLKTTTFVS--LYQASDEIydlfDKVLVLYEGRQIYYG 202
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
15-235 |
5.08e-22 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 91.39 E-value: 5.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 15 GQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDAGRSlgpqKGLIRQlrqhVGFVFQNF 94
Cdd:PRK10575 23 GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSS----KAFARK----VAYLPQQL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 95 NLFPHRTVLENIIEGPVI---VKGEDKQESMARARELLAKVGLSGKENSYPRRLSGGQQQRVAIARALAMRPDVILFDEP 171
Cdd:PRK10575 95 PAAEGMTVRELVAIGRYPwhgALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEP 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1879798416 172 TSALDPELVGEVLNTIRQLAQEKRTMVI-VTHEMSFARDVADRAIFMDQGRIVEQGEAKALFASP 235
Cdd:PRK10575 175 TSALDIAHQVDVLALVHRLSQERGLTVIaVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGE 239
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
5-223 |
5.88e-22 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 93.94 E-value: 5.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 5 EVKSL-VKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDAgrsLGPQKglIRQL 83
Cdd:COG3845 259 EVENLsVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITG---LSPRE--RRRL 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 84 --------RQHVGfvfqnfnLFPHRTVLENII----EGPVIVKG--EDKQESMARARELLAKVGL-SGKENSYPRRLSGG 148
Cdd:COG3845 334 gvayipedRLGRG-------LVPDMSVAENLIlgryRRPPFSRGgfLDRKAIRAFAEELIEEFDVrTPGPDTPARSLSGG 406
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1879798416 149 QQQRVAIARALAMRPDVILFDEPTSALDpelVG---EVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIV 223
Cdd:COG3845 407 NQQKVILARELSRDPKLLIAAQPTRGLD---VGaieFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRIV 481
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
2-231 |
1.19e-21 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 92.11 E-value: 1.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 2 SAIEVKSLVKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTtllrsinlleqpeSGTIRVGDVTIDAGRS-------LG 74
Cdd:NF000106 12 NAVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**-------------RGALPAHV*GPDAGRRpwrf*twCA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 75 PQKGLIRQLRQHVGFVFQNFNLFPHRtvlENIIegpVIVKGED--KQESMARARELLAKVGLSGKENSYPRRLSGGQQQR 152
Cdd:NF000106 79 NRRALRRTIG*HRPVR*GRRESFSGR---ENLY---MIGR*LDlsRKDARARADELLERFSLTEAAGRAAAKYSGGMRRR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1879798416 153 VAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGEAKAL 231
Cdd:NF000106 153 LDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
4-226 |
1.58e-21 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 89.01 E-value: 1.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 4 IEVKSLVKKF--HGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIdagrSLGPqkglIR 81
Cdd:cd03369 7 IEVENLSVRYapDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDI----STIP----LE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 82 QLRQHVGFVFQNFNLFPHrTVLENiiegpviVKGEDKQESmaraRELLAKVGLS-GKENsyprrLSGGQQQRVAIARALA 160
Cdd:cd03369 79 DLRSSLTIIPQDPTLFSG-TIRSN-------LDPFDEYSD----EEIYGALRVSeGGLN-----LSQGQRQLLCLARALL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1879798416 161 MRPDVILFDEPTSALDPELVGEVLNTIRQLAQeKRTMVIVTHEMSFARDVaDRAIFMDQGRIVEQG 226
Cdd:cd03369 142 KRPRVLVLDEATASIDYATDALIQKTIREEFT-NSTILTIAHRLRTIIDY-DKILVMDAGEVKEYD 205
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
17-231 |
2.94e-21 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 89.66 E-value: 2.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 17 TVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIdagrslgpQKGLIRQLRQHVGFVFQNFNL 96
Cdd:PRK10253 21 TVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHI--------QHYASKEVARRIGLLAQNATT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 97 FPHRTVLENIIEG-----PVIVKGEdKQESMARARELLAkVGLSGKENSYPRRLSGGQQQRVAIARALAMRPDVILFDEP 171
Cdd:PRK10253 93 PGDITVQELVARGryphqPLFTRWR-KEDEEAVTKAMQA-TGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1879798416 172 TSALDPELVGEVLNTIRQLAQEK-RTMVIVTHEMSFARDVADRAIFMDQGRIVEQGEAKAL 231
Cdd:PRK10253 171 TTWLDISHQIDLLELLSELNREKgYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-225 |
1.02e-20 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 90.45 E-value: 1.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 1 MSAI-EVKSLVKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIR-VGDVTIDAGRSLGPQKG 78
Cdd:PRK10762 1 MQALlQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILyLGKEVTFNGPKSSQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 79 lirqlrqhVGFVFQNFNLFPHRTVLENIIEGPVIVK---GEDKQESMARARELLAKVGLSGKENSYPRRLSGGQQQRVAI 155
Cdd:PRK10762 81 --------IGIIHQELNLIPQLTIAENIFLGREFVNrfgRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1879798416 156 ARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADR-AIFMDQGRIVEQ 225
Cdd:PRK10762 153 AKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDvTVFRDGQFIAER 223
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-178 |
1.13e-20 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 90.38 E-value: 1.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 4 IEVKSLVKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDvTIdagrslgpqkglirql 83
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGE-TV---------------- 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 84 rqHVGFVFQNF-NLFPHRTVLENIIEG-PVIVKGedKQESMARAreLLAKVGLSGKENSYP-RRLSGGQQQRVAIARALA 160
Cdd:TIGR03719 386 --KLAYVDQSRdALDPNKTVWEEISGGlDIIKLG--KREIPSRA--YVGRFNFKGSDQQKKvGQLSGGERNRVHLAKTLK 459
|
170
....*....|....*...
gi 1879798416 161 MRPDVILFDEPTSALDPE 178
Cdd:TIGR03719 460 SGGNVLLLDEPTNDLDVE 477
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
5-224 |
1.19e-20 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 90.23 E-value: 1.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 5 EVKSLVKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLrsiNLLeqpeSGtirV-------GDVTIDagrslgpqk 77
Cdd:NF040905 3 EMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLM---KVL----SG---VyphgsyeGEILFD--------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 78 GLIRQLR-----QHVGFVF--QNFNLFPHRTVLENIIEGPVIVKGE--DKQESMARARELLAKVGLsgKENsyPRRLSG- 147
Cdd:NF040905 64 GEVCRFKdirdsEALGIVIihQELALIPYLSIAENIFLGNERAKRGviDWNETNRRARELLAKVGL--DES--PDTLVTd 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 148 ---GQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVE 224
Cdd:NF040905 140 igvGKQQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGRTIE 219
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
15-202 |
1.56e-20 |
|
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: 85.28 E-value: 1.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 15 GQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIrvgdvtidagrslgpqkglIRQLRQHVGFVfqnf 94
Cdd:cd03223 13 GRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI-------------------GMPEGEDLLFL---- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 95 nlfPHRtvleniiegPVIVKGedkqesmaRARELLAkvglsgkensYP--RRLSGGQQQRVAIARALAMRPDVILFDEPT 172
Cdd:cd03223 70 ---PQR---------PYLPLG--------TLREQLI----------YPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEAT 119
|
170 180 190
....*....|....*....|....*....|.
gi 1879798416 173 SALDPelvgEVLNTIRQLAQEKRTMVI-VTH 202
Cdd:cd03223 120 SALDE----ESEDRLYQLLKELGITVIsVGH 146
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
4-202 |
1.65e-20 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 86.01 E-value: 1.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 4 IEVKSLVKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVgdvtidAGRSLGPQKGLIRQL 83
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLL------NGGPLDFQRDSIARG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 84 RQHVGfvFQNfNLFPHRTVLENIiegpvivKGEDKQESMARARELLAKVGLSGKENSYPRRLSGGQQQRVAIARALAMRP 163
Cdd:cd03231 75 LLYLG--HAP-GIKTTLSVLENL-------RFWHADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGR 144
|
170 180 190
....*....|....*....|....*....|....*....
gi 1879798416 164 DVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTH 202
Cdd:cd03231 145 PLWILDEPTTALDKAGVARFAEAMAGHCARGGMVVLTTH 183
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
5-224 |
2.99e-20 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 89.07 E-value: 2.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 5 EVKSLVKKFHGQtvLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDAGRSLGPQK---GLIR 81
Cdd:PRK09700 267 EVRNVTSRDRKK--VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKkgmAYIT 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 82 QLRQHVGFvFQNFNLFPHRTVLENIIEGPV-----IVKGEDKQESMARARELLAKVGLSGKENSypRRLSGGQQQRVAIA 156
Cdd:PRK09700 345 ESRRDNGF-FPNFSIAQNMAISRSLKDGGYkgamgLFHEVDEQRTAENQRELLALKCHSVNQNI--TELSGGNQQKVLIS 421
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1879798416 157 RALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVE 224
Cdd:PRK09700 422 KWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQ 489
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
19-233 |
4.18e-20 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 89.23 E-value: 4.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 19 LHGIDLEVQKGEVVAIIGPSGSGKTTLLRSinLLEQPESGTirvGDVTIDAGRSLGPQKGLIrqlrqhvgfvfQNfnlfp 98
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSA--LLAEMDKVE---GHVHMKGSVAYVPQQAWI-----------QN----- 712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 99 hRTVLENIIEGPVIvkGEDKQESMARARELLAKVGL--SGKENSYPRR---LSGGQQQRVAIARALAMRPDVILFDEPTS 173
Cdd:TIGR00957 713 -DSLRENILFGKAL--NEKYYQQVLEACALLPDLEIlpSGDRTEIGEKgvnLSGGQKQRVSLARAVYSNADIYLFDDPLS 789
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1879798416 174 ALDPELVGEVL-NTIRQLAQEK-RTMVIVTHEMSFARDVaDRAIFMDQGRIVEQGEAKALFA 233
Cdd:TIGR00957 790 AVDAHVGKHIFeHVIGPEGVLKnKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLQ 850
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
19-220 |
1.21e-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: 83.45 E-value: 1.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 19 LHGIDLEVQKGEVVAIIGPSGSGKTTLLrsiNLLEQPESGTIRVGDVTIDaGRSLGPQkglirqLRQHVGFVFQNFNLFP 98
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLL---DVLAGRKTAGVITGEILIN-GRPLDKN------FQRSTGYVEQQDVHSP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 99 HRTVLENIiegpvivkgedkqesmararELLAKVglsgkensypRRLSGGQQQRVAIARALAMRPDVILFDEPTSALDPE 178
Cdd:cd03232 93 NLTVREAL--------------------RFSALL----------RGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQ 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1879798416 179 LVGEVLNTIRQLAQEKRTMVIVTHEMS---FARdvADRAIFMDQG 220
Cdd:cd03232 143 AAYNIVRFLKKLADSGQAILCTIHQPSasiFEK--FDRLLLLKRG 185
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
14-235 |
1.61e-19 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 87.08 E-value: 1.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 14 HGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDAGRslgpqkglIRQLRQHVGFVFQN 93
Cdd:PRK10789 326 TDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQ--------LDSWRSRLAVVSQT 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 94 FNLFPHrTVLENIIEGpvivKGEDKQESMARARELlAKVG------LSGKENSYPRR---LSGGQQQRVAIARALAMRPD 164
Cdd:PRK10789 398 PFLFSD-TVANNIALG----RPDATQQEIEHVARL-ASVHddilrlPQGYDTEVGERgvmLSGGQKQRISIARALLLNAE 471
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1879798416 165 VILFDEPTSALDPELVGEVLNTIRQLAQeKRTMVIVTHEMSfARDVADRAIFMDQGRIVEQGEAKALFASP 235
Cdd:PRK10789 472 ILILDDALSAVDGRTEHQILHNLRQWGE-GRTVIISAHRLS-ALTEASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
22-231 |
1.71e-19 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 86.95 E-value: 1.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 22 IDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDAGRslgpqkglIRQLRQHVGFVFQNFNLFPHrt 101
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQ--------PEDYRKLFSAVFTDFHLFDQ-- 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 102 vleniiegpvIVKGEDKQESMARARELLAKVGLSGK---ENSYPR--RLSGGQQQRVAIARALAMRPDVILFDEPTSALD 176
Cdd:PRK10522 412 ----------LLGPEGKPANPALVEKWLERLKMAHKlelEDGRISnlKLSKGQKKRLALLLALAEERDILLLDEWAADQD 481
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1879798416 177 PELVGEVLNTIRQLAQEK-RTMVIVTHEMSFArDVADRAIFMDQGRIVE-QGEAKAL 231
Cdd:PRK10522 482 PHFRREFYQVLLPLLQEMgKTIFAISHDDHYF-IHADRLLEMRNGQLSElTGEERDA 537
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
16-234 |
1.98e-19 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 87.10 E-value: 1.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 16 QTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLrSINLLEQPesgTIRVGDVTIDAGRSLGPQKGLIrqlrqhvgfvfqnFN 95
Cdd:PLN03130 630 RPTLSNINLDVPVGSLVAIVGSTGEGKTSLI-SAMLGELP---PRSDASVVIRGTVAYVPQVSWI-------------FN 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 96 lfphRTVLENIIEGPVI--VKGEDKQESMARAREL-------LAKVGLSGKEnsyprrLSGGQQQRVAIARALAMRPDVI 166
Cdd:PLN03130 693 ----ATVRDNILFGSPFdpERYERAIDVTALQHDLdllpggdLTEIGERGVN------ISGGQKQRVSMARAVYSNSDVY 762
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1879798416 167 LFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVaDRAIFMDQGRIVEQGEAKALFAS 234
Cdd:PLN03130 763 IFDDPLSALDAHVGRQVFDKCIKDELRGKTRVLVTNQLHFLSQV-DRIILVHEGMIKEEGTYEELSNN 829
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
4-178 |
3.32e-19 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 86.33 E-value: 3.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 4 IEVKSLVKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDvTIdagrslgpqkglirql 83
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGE-TV---------------- 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 84 rqHVGFVFQNF-NLFPHRTVLENIIEGPVIVK-GedKQESMARAreLLAKVGLSGKENSYP-RRLSGGQQQRVAIARALA 160
Cdd:PRK11819 388 --KLAYVDQSRdALDPNKTVWEEISGGLDIIKvG--NREIPSRA--YVGRFNFKGGDQQKKvGVLSGGERNRLHLAKTLK 461
|
170
....*....|....*...
gi 1879798416 161 MRPDVILFDEPTSALDPE 178
Cdd:PRK11819 462 QGGNVLLLDEPTNDLDVE 479
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
18-245 |
6.21e-19 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 84.19 E-value: 6.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 18 VLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSI-NLLEQpesgtirvgDVTIDAGR---------SLGPQKGliRQL-RQH 86
Cdd:COG4170 22 AVDRVSLTLNEGEIRGLVGESGSGKSLIAKAIcGITKD---------NWHVTADRfrwngidllKLSPRER--RKIiGRE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 87 VGFVFQNFN--LFPHRTVLENIIEgpVI----VKG---EDKQESMARARELLAKVGLSGKE---NSYPRRLSGGQQQRVA 154
Cdd:COG4170 91 IAMIFQEPSscLDPSAKIGDQLIE--AIpswtFKGkwwQRFKWRKKRAIELLHRVGIKDHKdimNSYPHELTEGECQKVM 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 155 IARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQ-EKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGEAKALFA 233
Cdd:COG4170 169 IAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQlQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILK 248
|
250
....*....|..
gi 1879798416 234 SPQQPRTRQFLE 245
Cdd:COG4170 249 SPHHPYTKALLR 260
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
19-234 |
6.93e-19 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 85.80 E-value: 6.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 19 LHGIDLEVQKGEVVAIIGPSGSGKTTLLRSInLLEQPESGTirvGDVTIDAGRSLGPQkglirqlrqhVGFVFqnfnlfp 98
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAM-LGELSHAET---SSVVIRGSVAYVPQ----------VSWIF------- 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 99 HRTVLENIIEGpvivkGEDKQESMARARELLAkvgLSGKENSYPRR-----------LSGGQQQRVAIARALAMRPDVIL 167
Cdd:PLN03232 692 NATVRENILFG-----SDFESERYWRAIDVTA---LQHDLDLLPGRdlteigergvnISGGQKQRVSMARAVYSNSDIYI 763
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1879798416 168 FDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVaDRAIFMDQGRIVEQGEAKALFAS 234
Cdd:PLN03232 764 FDDPLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLM-DRIILVSEGMIKEEGTFAELSKS 829
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
19-229 |
1.42e-18 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 81.81 E-value: 1.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 19 LHGIDLEVQKGEVVAIIGPSGSGKTTLLRSI-NLLeqPESGTIRVgdvtidAGRSLG--PQKGLIRQ---LRQHV--GF- 89
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMaGLL--PGQGEILL------NGRPLSdwSAAELARHrayLSQQQspPFa 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 90 --VFQNFNLFPHRtvleniiegpvivkGEDKQESMARARELLAKVGLSGKensYPR---RLSGGQQQRVAIARAL----- 159
Cdd:COG4138 84 mpVFQYLALHQPA--------------GASSEAVEQLLAQLAEALGLEDK---LSRpltQLSGGEWQRVRLAAVLlqvwp 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1879798416 160 AMRPD--VILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGEAK 229
Cdd:COG4138 147 TINPEgqLLLLDEPMNSLDVAQQAALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETA 218
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
3-223 |
1.04e-17 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 81.86 E-value: 1.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 3 AIEVKSLVKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSInlleqpesgtirVGDVTIDAGRSLGPQKGLIRQ 82
Cdd:PRK15064 319 ALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTL------------VGELEPDSGTVKWSENANIGY 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 83 LRQHVGFVFQNfnlfpHRTVLENIIEgpviVKGEDKQESMARAreLLAKVGLSGKE-NSYPRRLSGGQQQRVAIARALAM 161
Cdd:PRK15064 387 YAQDHAYDFEN-----DLTLFDWMSQ----WRQEGDDEQAVRG--TLGRLLFSQDDiKKSVKVLSGGEKGRMLFGKLMMQ 455
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1879798416 162 RPDVILFDEPTSALDPELVgEVLNTirQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIV 223
Cdd:PRK15064 456 KPNVLVMDEPTNHMDMESI-ESLNM--ALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVV 514
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
5-242 |
1.87e-17 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 81.11 E-value: 1.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 5 EVKSLVKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVT---------IDAGRSLGP 75
Cdd:PRK11288 255 EVRLRLDGLKGPGLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPidirsprdaIRAGIMLCP 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 76 QKglirqlRQHVGFVfqnfnlfPHRTVLENI--------IEGPVIVKGEDKQESMARARELLAKVGLSGKENSypRRLSG 147
Cdd:PRK11288 335 ED------RKAEGII-------PVHSVADNInisarrhhLRAGCLINNRWEAENADRFIRSLNIKTPSREQLI--MNLSG 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 148 GQQQRVAIARALAMRPDVILFDEPTSALDpelVG---EVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVe 224
Cdd:PRK11288 400 GNQQKAILGRWLSEDMKVILLDEPTRGID---VGakhEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRIA- 475
|
250 260
....*....|....*....|....
gi 1879798416 225 qGEAKALFASPQQ------PRTRQ 242
Cdd:PRK11288 476 -GELAREQATERQalslalPRTSA 498
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
15-226 |
2.60e-17 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 78.72 E-value: 2.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 15 GQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSI--NLLEQPESGTIRV-GDVTIDaGRSL----GPQKGLIRQ-LRQH 86
Cdd:PRK13547 13 HRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALagDLTGGGAPRGARVtGDVTLN-GEPLaaidAPRLARLRAvLPQA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 87 V--GFVFQNFNL-----FPHrtvleniiegpVIVKGEDKQESMARARELLAKVGLSGKENSYPRRLSGGQQQRVAIARAL 159
Cdd:PRK13547 92 AqpAFAFSAREIvllgrYPH-----------ARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1879798416 160 AM---------RPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVI-VTHEMSFARDVADRAIFMDQGRIVEQG 226
Cdd:PRK13547 161 AQlwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLaIVHDPNLAARHADRIAMLADGAIVAHG 237
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
5-222 |
3.18e-17 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 80.43 E-value: 3.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 5 EVKSLVKKFHGQTVlHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDAgRSlgPQKGL----- 79
Cdd:PRK10762 255 EVRLKVDNLSGPGV-NDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVT-RS--PQDGLangiv 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 80 -IRQLRQHVGFVF-----QNFNLfphrTVLENIIEGPVIVKGEDKQESMARARELL--------AKVGLsgkensyprrL 145
Cdd:PRK10762 331 yISEDRKRDGLVLgmsvkENMSL----TALRYFSRAGGSLKHADEQQAVSDFIRLFniktpsmeQAIGL----------L 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 146 SGGQQQRVAIARALAMRPDVILFDEPTSALDpelVG---EVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRI 222
Cdd:PRK10762 397 SGGNQQKVAIARGLMTRPKVLILDEPTRGVD---VGakkEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
27-204 |
4.96e-17 |
|
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: 79.83 E-value: 4.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 27 QKGEVVAIIGPSGSGKTTllrSINLLeqpeSGTIR--VGDVTIDAGrslgpQKGLIRQlrqhvgfvFQNFNLFPHrtvLE 104
Cdd:COG1245 97 KKGKVTGILGPNGIGKST---ALKIL----SGELKpnLGDYDEEPS-----WDEVLKR--------FRGTELQDY---FK 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 105 NIIEG--------------PVIVKGedkqesmaRARELLAKVGLSGK----------ENSYPRR---LSGGQQQRVAIAR 157
Cdd:COG1245 154 KLANGeikvahkpqyvdliPKVFKG--------TVRELLEKVDERGKldelaeklglENILDRDiseLSGGELQRVAIAA 225
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1879798416 158 ALAMRPDVILFDEPTSALDpelVGEVLN---TIRQLAQEKRTMVIVTHEM 204
Cdd:COG1245 226 ALLRDADFYFFDEPSSYLD---IYQRLNvarLIRELAEEGKYVLVVEHDL 272
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
14-234 |
1.04e-16 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 77.23 E-value: 1.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 14 HGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDagrslgpqkgliRQLRQH-VGFVFQ 92
Cdd:PRK15056 18 NGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR------------QALQKNlVAYVPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 93 NFNL---FPhrTVLENIIE----GPVIVKGEDKQESMARARELLAKVGLSGKENSYPRRLSGGQQQRVAIARALAMRPDV 165
Cdd:PRK15056 86 SEEVdwsFP--VLVEDVVMmgryGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQV 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1879798416 166 ILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIfMDQGRIVEQGEAKALFAS 234
Cdd:PRK15056 164 ILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTV-MVKGTVLASGPTETTFTA 231
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
3-224 |
1.32e-16 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 78.84 E-value: 1.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 3 AIEVKSLVKKFHGQtvlhgidleVQKGEVVAIIGPSGSGKTTLLRSinLLEQ--PESGTIRVGdvtidagrslgpQKGLI 80
Cdd:PRK11147 328 QIDGKQLVKDFSAQ---------VQRGDKIALIGPNGCGKTTLLKL--MLGQlqADSGRIHCG------------TKLEV 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 81 RQLRQHvgfvfqNFNLFPHRTVLENIIEGpvivkgedKQESM--ARARELLakvglsgkenSY-------PRR------- 144
Cdd:PRK11147 385 AYFDQH------RAELDPEKTVMDNLAEG--------KQEVMvnGRPRHVL----------GYlqdflfhPKRamtpvka 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 145 LSGGQQQRVAIARaLAMRP-DVILFDEPTSALDPELVgEVLNTIrqLAQEKRTMVIVTHEMSFARD-VADRAIFMDQGRI 222
Cdd:PRK11147 441 LSGGERNRLLLAR-LFLKPsNLLILDEPTNDLDVETL-ELLEEL--LDSYQGTVLLVSHDRQFVDNtVTECWIFEGNGKI 516
|
..
gi 1879798416 223 VE 224
Cdd:PRK11147 517 GR 518
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
25-240 |
1.50e-16 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 78.29 E-value: 1.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 25 EVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRvGDVTIdagrSLGPQKglirqlrqhvgfvfqnfnlfphrtvLE 104
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVD-EDLKI----SYKPQY-------------------------IS 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 105 NIIEGPVI-----VKGEDKQESMARArELLAKVGLSGKENSYPRRLSGGQQQRVAIARALAMRPDVILFDEPTSALDPEL 179
Cdd:COG1245 412 PDYDGTVEeflrsANTDDFGSSYYKT-EIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQ 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1879798416 180 VGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDqGRIVEQGEAKalfaSPQQPRT 240
Cdd:COG1245 491 RLAVAKAIRRFAENrGKTAMVVDHDIYLIDYISDRLMVFE-GEPGVHGHAS----GPMDMRE 547
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
15-221 |
1.69e-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: 78.44 E-value: 1.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 15 GQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRvgdvtidagrslgPQKGLirqlrqHVGFVFQNF 94
Cdd:TIGR03719 17 KKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEAR-------------PQPGI------KVGYLPQEP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 95 NLFPHRTVLENIIEGPVIVKG--------------EDKQ-----ESMARARELLAKVGLSGKENSYPR------------ 143
Cdd:TIGR03719 78 QLDPTKTVRENVEEGVAEIKDaldrfneisakyaePDADfdklaAEQAELQEIIDAADAWDLDSQLEIamdalrcppwda 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 144 ---RLSGGQQQRVAIARALAMRPDVILFDEPTSALDPELVG--EvlntiRQLAQEKRTMVIVTHEMSFARDVADRAIFMD 218
Cdd:TIGR03719 158 dvtKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAwlE-----RHLQEYPGTVVAVTHDRYFLDNVAGWILELD 232
|
...
gi 1879798416 219 QGR 221
Cdd:TIGR03719 233 RGR 235
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
26-204 |
1.83e-16 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 78.31 E-value: 1.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 26 VQKGEVVAIIGPSGSGKTTllrSINLLeqpeSGTIR------VGDVTIDAgrslgpqkgLIRQLRqhvGFVFQNFnlfph 99
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTT---AVKIL----SGELIpnlgdyEEEPSWDE---------VLKRFR---GTELQNY----- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 100 rtvLENIIEG--------------PVIVKGedkqesmaRARELLAKVGLSGK----------ENSYPRR---LSGGQQQR 152
Cdd:PRK13409 152 ---FKKLYNGeikvvhkpqyvdliPKVFKG--------KVRELLKKVDERGKldevverlglENILDRDiseLSGGELQR 220
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1879798416 153 VAIARALAMRPDVILFDEPTSALDpelVGEVLN---TIRQLAqEKRTMVIVTHEM 204
Cdd:PRK13409 221 VAIAAALLRDADFYFFDEPTSYLD---IRQRLNvarLIRELA-EGKYVLVVEHDL 271
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
25-245 |
2.00e-16 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 75.91 E-value: 2.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 25 EVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIdagrSLGPQ------KGLIRQLrqhvgfvfqnfnlfp 98
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV----SYKPQyikadyEGTVRDL--------------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 99 hrtvLENIIEGpvivKGEDKQESMararELLAKVGLSGKENSYPRRLSGGQQQRVAIARALAMRPDVILFDEPTSALDPE 178
Cdd:cd03237 82 ----LSSITKD----FYTHPYFKT----EIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVE 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 179 LVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDqGRIVEQGEAkalfASPQQPRT--RQFLE 245
Cdd:cd03237 150 QRLMASKVIRRFAENnEKTAFVVEHDIIMIDYLADRLIVFE-GEPSVNGVA----NPPQSLRSgmNRFLK 214
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
3-236 |
2.59e-16 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 78.24 E-value: 2.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 3 AIEVKSLVKKFHGQ--TVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIdagRSLGpqkglI 80
Cdd:PLN03130 1237 SIKFEDVVLRYRPElpPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDI---SKFG-----L 1308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 81 RQLRQHVGFVFQN---------FNLFP---HRTVleniiegpvivkgeDKQESMARA----------RELLAKVGLSGkE 138
Cdd:PLN03130 1309 MDLRKVLGIIPQApvlfsgtvrFNLDPfneHNDA--------------DLWESLERAhlkdvirrnsLGLDAEVSEAG-E 1373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 139 NsyprrLSGGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRqlaQEKR--TMVIVTHEMSFARDvADRAIF 216
Cdd:PLN03130 1374 N-----FSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIR---EEFKscTMLIIAHRLNTIID-CDRILV 1444
|
250 260
....*....|....*....|
gi 1879798416 217 MDQGRIVEqgeakalFASPQ 236
Cdd:PLN03130 1445 LDAGRVVE-------FDTPE 1457
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
18-205 |
2.64e-16 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 75.87 E-value: 2.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 18 VLHGIDLeVQKGEVVAIIGPSGSGKTTLLRsinlleqpesgtIRVGDVTIDAGRSLGPQ--KGLIRQLRqhvGFVFQNFn 95
Cdd:cd03236 16 KLHRLPV-PREGQVLGLVGPNGIGKSTALK------------ILAGKLKPNLGKFDDPPdwDEILDEFR---GSELQNY- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 96 lfphrtvLENIIEG--------------PVIVKGedkqesmaRARELLAKVGLSGKENSYPRR-------------LSGG 148
Cdd:cd03236 79 -------FTKLLEGdvkvivkpqyvdliPKAVKG--------KVGELLKKKDERGKLDELVDQlelrhvldrnidqLSGG 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 149 QQQRVAIARALAMRPDVILFDEPTSALDpelVGEVLN---TIRQLAQEKRTMVIVTHEMS 205
Cdd:cd03236 144 ELQRVAIAAALARDADFYFFDEPSSYLD---IKQRLNaarLIRELAEDDNYVLVVEHDLA 200
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
15-220 |
3.85e-16 |
|
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: 74.67 E-value: 3.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 15 GQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDagrSLGPQKGLIRQlRQHVGFVFQNF 94
Cdd:cd03290 13 GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNES---EPSFEATRSRN-RYSVAYAAQKP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 95 NLFpHRTVLENIIEGPVIVKgeDKQESMARARELLAKVGL--SGKENSYPRR---LSGGQQQRVAIARALAMRPDVILFD 169
Cdd:cd03290 89 WLL-NATVEENITFGSPFNK--QRYKAVTDACSLQPDIDLlpFGDQTEIGERginLSGGQRQRICVARALYQNTNIVFLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1879798416 170 EPTSALDPELVGEVLNT--IRQLAQEKRTMVIVTHEMSFARDvADRAIFMDQG 220
Cdd:cd03290 166 DPFSALDIHLSDHLMQEgiLKFLQDDKRTLVLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
4-215 |
4.96e-16 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 76.77 E-value: 4.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 4 IEVKSLVKKFHG--QTVLHGidlEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIrVGDVTIdagrSLGPQKglir 81
Cdd:PRK13409 341 VEYPDLTKKLGDfsLEVEGG---EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV-DPELKI----SYKPQY---- 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 82 qlrqhvgfvfqnfnlfphrtvLENIIEGPVivkgEDKQESMARA-------RELLAKVGLSGKENSYPRRLSGGQQQRVA 154
Cdd:PRK13409 409 ---------------------IKPDYDGTV----EDLLRSITDDlgssyykSEIIKPLQLERLLDKNVKDLSGGELQRVA 463
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1879798416 155 IARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADRAI 215
Cdd:PRK13409 464 IAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREaTALVVDHDIYMIDYISDRLM 525
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
17-244 |
6.35e-16 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 77.07 E-value: 6.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 17 TVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINL-LEQPESGtiRVGDVTIDagrSLGPQKgLIRQLRQHVGFVFQNFN 95
Cdd:TIGR00956 75 DILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASnTDGFHIG--VEGVITYD---GITPEE-IKKHYRGDVVYNAETDV 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 96 LFPHRTVLENI-----IEGPVI-VKGEDKQESMARAREL-LAKVGLSGKENS-----YPRRLSGGQQQRVAIARALAMRP 163
Cdd:TIGR00956 149 HFPHLTVGETLdfaarCKTPQNrPDGVSREEYAKHIADVyMATYGLSHTRNTkvgndFVRGVSGGERKRVSIAEASLGGA 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 164 DVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVT-HEMS-FARDVADRAIFMDQGRIVEQG---EAKALFAS---- 234
Cdd:TIGR00956 229 KIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVAiYQCSqDAYELFDKVIVLYEGYQIYFGpadKAKQYFEKmgfk 308
|
250
....*....|.
gi 1879798416 235 -PQQPRTRQFL 244
Cdd:TIGR00956 309 cPDRQTTADFL 319
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
4-237 |
1.11e-15 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 75.82 E-value: 1.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 4 IEVKSLVKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLrSINLLEQPESGTirvGDVTIdagrsLGPQKG---LI 80
Cdd:PRK10938 261 IVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLL-SLITGDHPQGYS---NDLTL-----FGRRRGsgeTI 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 81 RQLRQHVGFVFQNFNLfPHR---TVLENIIEGPVIVKG-----EDKQESMARarELLAKVGLSGKENSYP-RRLSGGQQQ 151
Cdd:PRK10938 332 WDIKKHIGYVSSSLHL-DYRvstSVRNVILSGFFDSIGiyqavSDRQQKLAQ--QWLDILGIDKRTADAPfHSLSWGQQR 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 152 RVAIARALAMRPDVILFDEPTSALDPelvgevLNtiRQLAQEkrtmvivthemsfardvadraiFMDQgrIVEQGEAKAL 231
Cdd:PRK10938 409 LALIVRALVKHPTLLILDEPLQGLDP------LN--RQLVRR----------------------FVDV--LISEGETQLL 456
|
....*.
gi 1879798416 232 FASPQQ 237
Cdd:PRK10938 457 FVSHHA 462
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
14-234 |
1.74e-15 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 75.52 E-value: 1.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 14 HGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLlrsINLLE---QPESGTIRvgdvtIDaGRSLGpqkGLIRQ-LRQHVGF 89
Cdd:PRK10790 352 DDNLVLQNINLSVPSRGFVALVGHTGSGKSTL---ASLLMgyyPLTEGEIR-----LD-GRPLS---SLSHSvLRQGVAM 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 90 VFQNFNLFPHrTVLENIIEGPVIvkgedkqeSMARARELLAKVGLSGKENSYP-----------RRLSGGQQQRVAIARA 158
Cdd:PRK10790 420 VQQDPVVLAD-TFLANVTLGRDI--------SEEQVWQALETVQLAELARSLPdglytplgeqgNNLSVGQKQLLALARV 490
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1879798416 159 LAMRPDVILFDEPTSALDP---ELVGEVLNTIRqlaqEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGEAKALFAS 234
Cdd:PRK10790 491 LVQTPQILILDEATANIDSgteQAIQQALAAVR----EHTTLVVIAHRLSTIVE-ADTILVLHRGQAVEQGTHQQLLAA 564
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
15-233 |
2.97e-15 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 74.78 E-value: 2.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 15 GQTV-LHGIDLEVQKGEVVAIIGPSGSGKTTLL------RSInlleqpESGTIRV--GDVTIDAGR-SLGPQ-----KGL 79
Cdd:NF033858 12 GKTVaLDDVSLDIPAGCMVGLIGPDGVGKSSLLsliagaRKI------QQGRVEVlgGDMADARHRrAVCPRiaympQGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 80 IRqlrqhvgfvfqnfNLFPHRTVLENIiegpvivkGEDKQESMARARELLAKVGLSgkenSYPRR----LSGGQQQRVAI 155
Cdd:NF033858 86 GK-------------NLYPTLSVFENLdffg-rlfGQDAAERRRRIDELLRATGLA----PFADRpagkLSGGMKQKLGL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 156 ARALAMRPDVILFDEPTSALDP-------ELVgevlNTIRqlaQEKRTM-VIV-THEMSFARDVaDRAIFMDQGRIVEQG 226
Cdd:NF033858 148 CCALIHDPDLLILDEPTTGVDPlsrrqfwELI----DRIR---AERPGMsVLVaTAYMEEAERF-DWLVAMDAGRVLATG 219
|
....*..
gi 1879798416 227 EAKALFA 233
Cdd:NF033858 220 TPAELLA 226
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
3-234 |
4.53e-15 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 74.39 E-value: 4.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 3 AIEVKSLVKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDAGRslgpqkgliRQ 82
Cdd:NF033858 266 AIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGD---------IA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 83 LRQHVGFVFQNFNLFPHRTVLENI--------IEgpvivkgedKQESMARARELLAKVGLSGKENSYPRRLSGGQQQRVA 154
Cdd:NF033858 337 TRRRVGYMSQAFSLYGELTVRQNLelharlfhLP---------AAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLS 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 155 IARALAMRPDVILFDEPTSALDP-------ELVGEvlntirqLAQEKR-TMVIVTHEMSFA-RdvADRAIFMDQGRIVEQ 225
Cdd:NF033858 408 LAVAVIHKPELLILDEPTSGVDPvardmfwRLLIE-------LSREDGvTIFISTHFMNEAeR--CDRISLMHAGRVLAS 478
|
....*....
gi 1879798416 226 GEAKALFAS 234
Cdd:NF033858 479 DTPAALVAA 487
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
22-241 |
9.07e-15 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 72.53 E-value: 9.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 22 IDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPE----SGTIRVGDvtIDAGRsLGPqkgliRQLRQHVG----FVFQN 93
Cdd:PRK15093 26 VSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNwrvtADRMRFDD--IDLLR-LSP-----RERRKLVGhnvsMIFQE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 94 FN--LFPHRTVLENIIEG--PVIVKGEDKQE---SMARARELLAKVGLSGKEN---SYPRRLSGGQQQRVAIARALAMRP 163
Cdd:PRK15093 98 PQscLDPSERVGRQLMQNipGWTYKGRWWQRfgwRKRRAIELLHRVGIKDHKDamrSFPYELTEGECQKVMIAIALANQP 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1879798416 164 DVILFDEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADRAIFMDQGRIVEQGEAKALFASPQQPRTR 241
Cdd:PRK15093 178 RLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNtTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVTTPHHPYTQ 256
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
18-236 |
2.10e-14 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 72.50 E-value: 2.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 18 VLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGdvtidaGRSLGPQkGLiRQLRQHVGFVFQNFNLF 97
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVN------GREIGAY-GL-RELRRQFSMIPQDPVLF 1396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 98 pHRTVLENIieGPVIvkgEDKQESMARARELlakVGLSGK-----ENSYPRRLSG------GQQQRVAIARALAMR-PDV 165
Cdd:PTZ00243 1397 -DGTVRQNV--DPFL---EASSAEVWAALEL---VGLRERvasesEGIDSRVLEGgsnysvGQRQLMCMARALLKKgSGF 1467
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1879798416 166 ILFDEPTSALDPELVGEVLNTIRQlAQEKRTMVIVTHEMsfaRDVA--DRAIFMDQGRIVEQGEAKALFASPQ 236
Cdd:PTZ00243 1468 ILMDEATANIDPALDRQIQATVMS-AFSAYTVITIAHRL---HTVAqyDKIIVMDHGAVAEMGSPRELVMNRQ 1536
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
18-220 |
3.01e-14 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 72.06 E-value: 3.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 18 VLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSinLLEQPESGTIRVGDVTIDaGRSLgpQKGLIRQlrqhVGFVFQNFNLF 97
Cdd:TIGR00956 778 ILNNVDGWVKPGTLTALMGASGAGKTTLLNV--LAERVTTGVITGGDRLVN-GRPL--DSSFQRS----IGYVQQQDLHL 848
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 98 PHRTVLENII-----EGPVIVKGEDKQESMARARELL-------AKVGLSGKEnsyprrLSGGQQQRVAIARALAMRPDV 165
Cdd:TIGR00956 849 PTSTVRESLRfsaylRQPKSVSKSEKMEYVEEVIKLLemesyadAVVGVPGEG------LNVEQRKRLTIGVELVAKPKL 922
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1879798416 166 ILF-DEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMS---FARdvADRAIFMDQG 220
Cdd:TIGR00956 923 LLFlDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQPSailFEE--FDRLLLLQKG 979
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
25-229 |
4.92e-14 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 69.19 E-value: 4.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 25 EVQKGEVVAIIGPSGSGKTTLLRSI-NLLeqPESGTIRVgdvtidAGRSLG--PQKGLIRQ---LRQHVG--F---VFQN 93
Cdd:PRK03695 18 EVRAGEILHLVGPNGAGKSTLLARMaGLL--PGSGSIQF------AGQPLEawSAAELARHrayLSQQQTppFampVFQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 94 FNLfpHRTVLENIiegpvivkgedkQESMARARELLAKVGLSGKENSYPRRLSGGQQQRVAIARA-LAMRPDV------I 166
Cdd:PRK03695 90 LTL--HQPDKTRT------------EAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVvLQVWPDInpagqlL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1879798416 167 LFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGEAK 229
Cdd:PRK03695 156 LLDEPMNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRD 218
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
23-223 |
7.83e-14 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 70.36 E-value: 7.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 23 DLEVQKGEVVAIIGPSGSGKTTLLRSINlleqpesgtirvGDVTIDAGRSLGPQKGLIRQLRQ----HV-GFVFQnfnlf 97
Cdd:PRK11147 23 ELHIEDNERVCLVGRNGAGKSTLMKILN------------GEVLLDDGRIIYEQDLIVARLQQdpprNVeGTVYD----- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 98 phrTVLENIIEGPVIVK---------GEDKQESM--------------------ARARELLAKVGLSGkeNSYPRRLSGG 148
Cdd:PRK11147 86 ---FVAEGIEEQAEYLKryhdishlvETDPSEKNlnelaklqeqldhhnlwqleNRINEVLAQLGLDP--DAALSSLSGG 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1879798416 149 QQQRVAIARALAMRPDVILFDEPTSALDPElvgevlnTIRQLAQ----EKRTMVIVTHEMSFARDVADRAIFMDQGRIV 223
Cdd:PRK11147 161 WLRKAALGRALVSNPDVLLLDEPTNHLDIE-------TIEWLEGflktFQGSIIFISHDRSFIRNMATRIVDLDRGKLV 232
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
14-220 |
1.05e-13 |
|
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: 69.12 E-value: 1.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 14 HGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRvgdvtiDAGR-SLGPQKGLIrqlrqhvgfvfq 92
Cdd:cd03291 48 VGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIK------HSGRiSFSSQFSWI------------ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 93 nfnlFPHrTVLENIIEG--------PVIVKGEDKQESMARARE----LLAKVGLSgkensyprrLSGGQQQRVAIARALA 160
Cdd:cd03291 110 ----MPG-TIKENIIFGvsydeyryKSVVKACQLEEDITKFPEkdntVLGEGGIT---------LSGGQRARISLARAVY 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 161 MRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARdVADRAIFMDQG 220
Cdd:cd03291 176 KDADLYLLDSPFGYLDVFTEKEIFESCVCKLMANKTRILVTSKMEHLK-KADKILILHEG 234
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
18-178 |
1.08e-13 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 67.95 E-value: 1.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 18 VLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRV-GDVTIDAGRSlgpqkglirqlrQHVGFVFQNFNL 96
Cdd:PRK13543 26 VFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIdGKTATRGDRS------------RFMAYLGHLPGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 97 FPHRTVLENI--IEGpviVKGEDKQESMARArelLAKVGLSGKENSYPRRLSGGQQQRVAIARALAMRPDVILFDEPTSA 174
Cdd:PRK13543 94 KADLSTLENLhfLCG---LHGRRAKQMPGSA---LAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYAN 167
|
....
gi 1879798416 175 LDPE 178
Cdd:PRK13543 168 LDLE 171
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
18-235 |
1.84e-13 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 69.81 E-value: 1.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 18 VLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSinLLEQPEsgtIRVGDVTidAGRSLG--PQKGLIRqlrqhvgfvfqnfn 95
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQS--LLSQFE---ISEGRVW--AERSIAyvPQQAWIM-------------- 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 96 lfpHRTVLENIIegpviVKGEDKQESMA---RARELLAKVGL--SGKENSYPRR---LSGGQQQRVAIARALAMRPDVIL 167
Cdd:PTZ00243 734 ---NATVRGNIL-----FFDEEDAARLAdavRVSQLEADLAQlgGGLETEIGEKgvnLSGGQKARVSLARAVYANRDVYL 805
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1879798416 168 FDEPTSALDPElVGE-VLNTIRQLAQEKRTMVIVTHEMSFArDVADRAIFMDQGRIVEQGEAKALFASP 235
Cdd:PTZ00243 806 LDDPLSALDAH-VGErVVEECFLGALAGKTRVLATHQVHVV-PRADYVVALGDGRVEFSGSSADFMRTS 872
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
4-204 |
2.43e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 67.45 E-value: 2.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 4 IEVKSLVKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRvgdvtidagrslgpqkgliRQL 83
Cdd:PRK09544 5 VSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK-------------------RNG 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 84 RQHVGFVFQNFNLFPhrtVLENIIEGPVIVKGEDKQESMARArelLAKVGLSGKENSYPRRLSGGQQQRVAIARALAMRP 163
Cdd:PRK09544 66 KLRIGYVPQKLYLDT---TLPLTVNRFLRLRPGTKKEDILPA---LKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRP 139
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1879798416 164 DVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVI-VTHEM 204
Cdd:PRK09544 140 QLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLmVSHDL 181
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
26-220 |
2.93e-13 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 69.27 E-value: 2.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 26 VQKGEVVAIIGPSGSGKTTLLRSINlleqpesgtirvGDVTIDAGRSLGPQKGLIRQLRQhvgfVFQNFNLFPHRTVLEN 105
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLT------------GDTTVTSGDATVAGKSILTNISD----VHQNMGYCPQFDAIDD 2025
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 106 IIEGP------VIVKGEDKQESMARARELLAKVGLSGKENSYPRRLSGGQQQRVAIARALAMRPDVILFDEPTSALDPEL 179
Cdd:TIGR01257 2026 LLTGRehlylyARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQA 2105
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1879798416 180 VGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQG 220
Cdd:TIGR01257 2106 RRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
18-227 |
5.93e-13 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 67.89 E-value: 5.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 18 VLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSI--NLLEQPESGT-------IRVGDVT--IDAG--------RSLGPQkg 78
Cdd:NF040905 275 VVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVfgRSYGRNISGTvfkdgkeVDVSTVSdaIDAGlayvtedrKGYGLN-- 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 79 LIRQLRQHVgfVFQNFNLFPHRTVLENIIEgpvIVKGEDKQESMA-RARELLAKVGlsgkensyprRLSGGQQQRVAIAR 157
Cdd:NF040905 353 LIDDIKRNI--TLANLGKVSRRGVIDENEE---IKVAEEYRKKMNiKTPSVFQKVG----------NLSGGNQQKVVLSK 417
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1879798416 158 ALAMRPDVILFDEPTSALDpelVG---EVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVeqGE 227
Cdd:NF040905 418 WLFTDPDVLILDEPTRGID---VGakyEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMNEGRIT--GE 485
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
18-242 |
6.14e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 68.08 E-value: 6.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 18 VLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIdagrslgpqkglirqlrqhvgfvfQNFNLF 97
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDV------------------------AKFGLT 1306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 98 PHRTVLENIIEGPVIVKG--------------EDKQESMARA--RELLAK--VGLSGKENSYPRRLSGGQQQRVAIARAL 159
Cdd:PLN03232 1307 DLRRVLSIIPQSPVLFSGtvrfnidpfsehndADLWEALERAhiKDVIDRnpFGLDAEVSEGGENFSVGQRQLLSLARAL 1386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 160 AMRPDVILFDEPTSALDPELVGEVLNTIRqlaQEKR--TMVIVTHEMSFARDvADRAIFMDQGRIVEqgeakalFASPQQ 237
Cdd:PLN03232 1387 LRRSKILVLDEATASVDVRTDSLIQRTIR---EEFKscTMLVIAHRLNTIID-CDKILVLSSGQVLE-------YDSPQE 1455
|
....*
gi 1879798416 238 PRTRQ 242
Cdd:PLN03232 1456 LLSRD 1460
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
11-204 |
1.01e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 67.06 E-value: 1.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 11 KKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDAGRSLgpqkgliRQLRQHVGFV 90
Cdd:PRK10982 6 KSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSK-------EALENGISMV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 91 FQNFNLFPHRTVLENIIEGPVIVKG----EDK--QESMARARELLAKVGLSGKENSyprrLSGGQQQRVAIARALAMRPD 164
Cdd:PRK10982 79 HQELNLVLQRSVMDNMWLGRYPTKGmfvdQDKmyRDTKAIFDELDIDIDPRAKVAT----LSVSQMQMIEIAKAFSYNAK 154
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1879798416 165 VILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEM 204
Cdd:PRK10982 155 IVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKM 194
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
10-221 |
1.63e-12 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 66.68 E-value: 1.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 10 VKKFHGQ--TVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRvgdvtidagrslgPQKGLirqlrqHV 87
Cdd:PRK11819 12 VSKVVPPkkQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEAR-------------PAPGI------KV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 88 GFVFQNFNLFPHRTVLENIIEGPVIVKG----------------EDKQESMARARELLAKVGLSGKENSYPR-------- 143
Cdd:PRK11819 73 GYLPQEPQLDPEKTVRENVEEGVAEVKAaldrfneiyaayaepdADFDALAAEQGELQEIIDAADAWDLDSQleiamdal 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 144 ----------RLSGGQQQRVAIARALAMRPDVILFDEPTSALDPELVG--EvlntiRQLAQEKRTMVIVTHEMSFARDVA 211
Cdd:PRK11819 153 rcppwdakvtKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAwlE-----QFLHDYPGTVVAVTHDRYFLDNVA 227
|
250
....*....|
gi 1879798416 212 DRAIFMDQGR 221
Cdd:PRK11819 228 GWILELDRGR 237
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
19-226 |
1.98e-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: 63.50 E-value: 1.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 19 LHGIDLEVQKGEVVAIIGPSGSGKTTLLRSInlleqpesgtirvgdvtIDAGRSLGPQKGLIRQLRQHVGFVFQnfnlfp 98
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEG-----------------LYASGKARLISFLPKFSRNKLIFIDQ------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 99 hrtvLENIIegpvivkgedkqesmararellaKVGLS----GKENSyprRLSGGQQQRVAIARALAMRPD--VILFDEPT 172
Cdd:cd03238 68 ----LQFLI-----------------------DVGLGyltlGQKLS---TLSGGELQRVKLASELFSEPPgtLFILDEPS 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 173 SALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFArDVADRAIFM------DQGRIVEQG 226
Cdd:cd03238 118 TGLHQQDINQLLEVIKGLIDLGNTVILIEHNLDVL-SSADWIIDFgpgsgkSGGKVVFSG 176
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
14-220 |
2.42e-12 |
|
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: 66.47 E-value: 2.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 14 HGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRvgdvtiDAGR-SLGPQKGLIrqlrqhvgfvfq 92
Cdd:TIGR01271 437 YVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIK------HSGRiSFSPQTSWI------------ 498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 93 nfnlFPHrTVLENIIEGpvIVKGEDKQESMARARELLAKVGLSGKENSYPR-----RLSGGQQQRVAIARALAMRPDVIL 167
Cdd:TIGR01271 499 ----MPG-TIKDNIIFG--LSYDEYRYTSVIKACQLEEDIALFPEKDKTVLgeggiTLSGGQRARISLARAVYKDADLYL 571
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1879798416 168 FDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDvADRAIFMDQG 220
Cdd:TIGR01271 572 LDSPFTHLDVVTEKEIFESCLCKLMSNKTRILVTSKLEHLKK-ADKILLLHEG 623
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
4-228 |
2.51e-12 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 64.66 E-value: 2.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 4 IEVKSLVKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSInlLEQPeSGTIRVGDVTIDaGRS---LGPQKgli 80
Cdd:CHL00131 8 LEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVI--AGHP-AYKILEGDILFK-GESildLEPEE--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 81 rqlRQHVGfVFQNFNlFPhrtvleniIEGPViVKGED--------KQESMARAR-------ELLA-KVGLSGKENSYPRR 144
Cdd:CHL00131 81 ---RAHLG-IFLAFQ-YP--------IEIPG-VSNADflrlaynsKRKFQGLPEldpleflEIINeKLKLVGMDPSFLSR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 145 -----LSGGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHemsFAR--D--VADRAI 215
Cdd:CHL00131 147 nvnegFSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITH---YQRllDyiKPDYVH 223
|
250
....*....|...
gi 1879798416 216 FMDQGRIVEQGEA 228
Cdd:CHL00131 224 VMQNGKIIKTGDA 236
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
22-222 |
5.47e-12 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 64.85 E-value: 5.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 22 IDLEVQKGEVVAIIGPSGSGKTTLLRSI----------NLLEQPESGTIRVGDVTIDAGRSLGPQ----KGLIRQLRQHV 87
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQALfgaypgkfegNVFINGKPVDIRNPAQAIRAGIAMVPEdrkrHGIVPILGVGK 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 88 GFVFQNFNLFPHRTVLENIIEGPVIvkGEDKQESMARARELLAKVGlsgkensyprRLSGGQQQRVAIARALAMRPDVIL 167
Cdd:TIGR02633 359 NITLSVLKSFCFKMRIDAAAELQII--GSAIQRLKVKTASPFLPIG----------RLSGGNQQKAVLAKMLLTNPRVLI 426
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1879798416 168 FDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRI 222
Cdd:TIGR02633 427 LDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
4-227 |
6.12e-12 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 63.66 E-value: 6.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 4 IEVKSLVKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSinlLEQPESGTIRVGDVTIDaGRSLgpqKGLIRQL 83
Cdd:PRK09580 2 LSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSAT---LAGREDYEVTGGTVEFK-GKDL---LELSPED 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 84 RQHVGfVFQNF----------NLFPHRTVLENiiegpviVKGEDKQESMAR---ARELLAKVGLSGKENSYPRR-----L 145
Cdd:PRK09580 75 RAGEG-IFMAFqypveipgvsNQFFLQTALNA-------VRSYRGQEPLDRfdfQDLMEEKIALLKMPEDLLTRsvnvgF 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 146 SGGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVA-DRAIFMDQGRIVE 224
Cdd:PRK09580 147 SGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYQRILDYIKpDYVHVLYQGRIVK 226
|
...
gi 1879798416 225 QGE 227
Cdd:PRK09580 227 SGD 229
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
28-216 |
7.11e-12 |
|
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: 61.62 E-value: 7.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 28 KGEVVAIIGPSGSGKTTLLRSI-NLLEQPESGTIRVgdvtidagrslgpqkglirqlrqhvgfvfqnfnlfphrtvleni 106
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALaRELGPPGGGVIYI-------------------------------------------- 36
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 107 iegpvivkgedkqeSMARARELLAKVGLSGKENSYPRRLSGGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVL-- 184
Cdd:smart00382 37 --------------DGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLll 102
|
170 180 190
....*....|....*....|....*....|....*.
gi 1879798416 185 ----NTIRQLAQEKRTMVIVTHEMSFARDVADRAIF 216
Cdd:smart00382 103 eelrLLLLLKSEKNLTVILTTNDEKDLGPALLRRRF 138
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
29-205 |
7.50e-12 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 64.87 E-value: 7.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 29 GEVVAIIGPSGSGKTTLLrsiNLLEQPESGTIRVGDVTIdagrSLGPQKGliRQLRQHVGFVFQNFNLFPHRTVLENIIE 108
Cdd:PLN03140 906 GVLTALMGVSGAGKTTLM---DVLAGRKTGGYIEGDIRI----SGFPKKQ--ETFARISGYCEQNDIHSPQVTVRESLIY 976
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 109 G-----PVIVKGEDKQESMARARELL-------AKVGLSGKENsyprrLSGGQQQRVAIARALAMRPDVILFDEPTSALD 176
Cdd:PLN03140 977 SaflrlPKEVSKEEKMMFVDEVMELVeldnlkdAIVGLPGVTG-----LSTEQRKRLTIAVELVANPSIIFMDEPTSGLD 1051
|
170 180
....*....|....*....|....*....
gi 1879798416 177 PELVGEVLNTIRQLAQEKRTMVIVTHEMS 205
Cdd:PLN03140 1052 ARAAAIVMRTVRNTVDTGRTVVCTIHQPS 1080
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
26-222 |
1.64e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 63.41 E-value: 1.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 26 VQKGEVVAIIGPSGSGKTTLLRSI----------NLLEQPESGTIRVGDVTIDAGRSLGP----QKGLIRQLRqhvgfVF 91
Cdd:PRK13549 285 LRRGEILGIAGLVGAGRTELVQCLfgaypgrwegEIFIDGKPVKIRNPQQAIAQGIAMVPedrkRDGIVPVMG-----VG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 92 QNFNL-----FPHRTVLENIIEGPVIvkgedkQESMARARELLAKVGLSGKensyprRLSGGQQQRVAIARALAMRPDVI 166
Cdd:PRK13549 360 KNITLaaldrFTGGSRIDDAAELKTI------LESIQRLKVKTASPELAIA------RLSGGNQQKAVLAKCLLLNPKIL 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1879798416 167 LFDEPTSALDpelVG---EVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRI 222
Cdd:PRK13549 428 ILDEPTRGID---VGakyEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
19-247 |
1.73e-11 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 63.37 E-value: 1.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 19 LHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRV-GDVTIDAGRSlgpqkGLIRQLrqhvgfvfqnfnlf 97
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIkGSAALIAISS-----GLNGQL-------------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 98 phrTVLENiIEGPVIVKGEDKQEsmarARELLAKV---GLSGKENSYP-RRLSGGQQQRVAIARALAMRPDVILFDEPTS 173
Cdd:PRK13545 101 ---TGIEN-IELKGLMMGLTKEK----IKEIIPEIiefADIGKFIYQPvKTYSSGMKSRLGFAISVHINPDILVIDEALS 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1879798416 174 ALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGEAKALFAspqqpRTRQFLEKF 247
Cdd:PRK13545 173 VGDQTFTKKCLDKMNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVD-----HYDEFLKKY 241
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
22-222 |
2.41e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 63.15 E-value: 2.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 22 IDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIdagRSLGP----QKGLI-----RQ---------L 83
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEI---NALSTaqrlARGLVylpedRQssglyldapL 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 84 RQHVGFVFQNFNLFPHRTVLENIIegpvivkgedkqesMARARELLAkVGLSGKENSYpRRLSGGQQQRVAIARALAMRP 163
Cdd:PRK15439 359 AWNVCALTHNRRGFWIKPARENAV--------------LERYRRALN-IKFNHAEQAA-RTLSGGNQQKVLIAKCLEASP 422
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1879798416 164 DVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRI 222
Cdd:PRK15439 423 QLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
4-208 |
4.24e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 62.74 E-value: 4.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 4 IEVKSLvkKFHGQT-----VLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDvtidagrSLGPQKG 78
Cdd:PTZ00265 383 IQFKNV--RFHYDTrkdveIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIND-------SHNLKDI 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 79 LIRQLRQHVGFVFQNFNLFPHrTVLENI------------IEGPVIVKGEDKQESMARARELLAKVG------------- 133
Cdd:PTZ00265 454 NLKWWRSKIGVVSQDPLLFSN-SIKNNIkyslyslkdleaLSNYYNEDGNDSQENKNKRNSCRAKCAgdlndmsnttdsn 532
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 134 --LSGKEN----------------------------------SYPRRLSGGQQQRVAIARALAMRPDVILFDEPTSALDP 177
Cdd:PTZ00265 533 elIEMRKNyqtikdsevvdvskkvlihdfvsalpdkyetlvgSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDN 612
|
250 260 270
....*....|....*....|....*....|....
gi 1879798416 178 E---LVGEVLNTIRqlAQEKRTMVIVTHEMSFAR 208
Cdd:PTZ00265 613 KseyLVQKTINNLK--GNENRITIIIAHRLSTIR 644
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
25-215 |
4.54e-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: 59.89 E-value: 4.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 25 EVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIdagrSLGPQKglirqlrqhvgfvfqnfnlfphrtvle 104
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITP----VYKPQY--------------------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 105 niiegpvivkgedkqesmararellakvglsgkensypRRLSGGQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVL 184
Cdd:cd03222 70 --------------------------------------IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAA 111
|
170 180 190
....*....|....*....|....*....|..
gi 1879798416 185 NTIRQLAQE-KRTMVIVTHEMSFARDVADRAI 215
Cdd:cd03222 112 RAIRRLSEEgKKTALVVEHDLAVLDYLSDRIH 143
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
4-212 |
1.18e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 59.19 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 4 IEVKSLVKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTIDAGRSlgpqkglirQL 83
Cdd:PRK13540 2 LDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLC---------TY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 84 RQHVGFVFQNFNLFPHRTVLENIIEGPVIVKGEDKQESMARARELlakvglsGKENSYP-RRLSGGQQQRVAIARALAMR 162
Cdd:PRK13540 73 QKQLCFVGHRSGINPYLTLRENCLYDIHFSPGAVGITELCRLFSL-------EHLIDYPcGLLSSGQKRQVALLRLWMSK 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1879798416 163 PDVILFDEPTSALDpELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVAD 212
Cdd:PRK13540 146 AKLWLLDEPLVALD-ELSLLTIITKIQEHRAKGGAVLLTSHQDLPLNKAD 194
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
4-227 |
1.62e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 60.51 E-value: 1.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 4 IEVKSLVKKfhGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTI---DAGRSLGPQKGLI 80
Cdd:PRK10982 251 LEVRNLTSL--RQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKInnhNANEAINHGFALV 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 81 RQLRQHVGfVFQN----FNlfphrTVLENIIE--GPVIVKGEDKQESMARARELLAKVGLSGKENSYPRrLSGGQQQRVA 154
Cdd:PRK10982 329 TEERRSTG-IYAYldigFN-----SLISNIRNykNKVGLLDNSRMKSDTQWVIDSMRVKTPGHRTQIGS-LSGGNQQKVI 401
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1879798416 155 IARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGR---IVEQGE 227
Cdd:PRK10982 402 IGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLvagIVDTKT 477
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
35-222 |
2.84e-10 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 59.91 E-value: 2.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 35 IGPSGSGKTTLLRSINLLEQPESGTirvgdVTIDAGRSLGpqkglirQLRQHvGFVFQNFnlfphrTVLENIIEGPV--- 111
Cdd:PRK15064 33 IGANGCGKSTFMKILGGDLEPSAGN-----VSLDPNERLG-------KLRQD-QFAFEEF------TVLDTVIMGHTelw 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 112 IVKGE----------------------------DKQESMARARELLAKVGLSGKENSYP-RRLSGGQQQRVAIARALAMR 162
Cdd:PRK15064 94 EVKQErdriyalpemseedgmkvadlevkfaemDGYTAEARAGELLLGVGIPEEQHYGLmSEVAPGWKLRVLLAQALFSN 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1879798416 163 PDVILFDEPTSALDpelvgevLNTIRQLAQE----KRTMVIVTHEMSFARDV----ADraifMDQGRI 222
Cdd:PRK15064 174 PDILLLDEPTNNLD-------INTIRWLEDVlnerNSTMIIISHDRHFLNSVcthmAD----LDYGEL 230
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1-233 |
5.15e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 58.87 E-value: 5.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 1 MSAIEVKSLVKKFHGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTiRVGDVTIDAGRSLgpqkgli 80
Cdd:PRK10938 1 MSSLQISQGTFRLSDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGE-RQSQFSHITRLSF------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 81 RQLRQHVGFVFQNFN---LFPH-----RTVLENIIEGpviVKGEdkqesmARARELLAKVGLSGKENSYPRRLSGGQQQR 152
Cdd:PRK10938 73 EQLQKLVSDEWQRNNtdmLSPGeddtgRTTAEIIQDE---VKDP------ARCEQLAQQFGITALLDRRFKYLSTGETRK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 153 VAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGE----- 227
Cdd:PRK10938 144 TLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEreeil 223
|
....*.
gi 1879798416 228 AKALFA 233
Cdd:PRK10938 224 QQALVA 229
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
18-234 |
6.67e-10 |
|
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: 59.19 E-value: 6.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 18 VLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIRVGDVTI-DAGrslgpqkglIRQLRQHVGFVFQNFNL 96
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIaKIG---------LHDLRFKITIIPQDPVL 1371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 97 FPHrTVLENIieGPVivkGEDKQESMARARELlakVGLSGKENSYPRRL-----------SGGQQQRVAIARALAMRPDV 165
Cdd:TIGR00957 1372 FSG-SLRMNL--DPF---SQYSDEEVWWALEL---AHLKTFVSALPDKLdhecaeggenlSVGQRQLVCLARALLRKTKI 1442
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1879798416 166 ILFDEPTSALDPELVGEVLNTIRQlAQEKRTMVIVTHEMSFARDVAdRAIFMDQGRIVEQGEAKALFAS 234
Cdd:TIGR00957 1443 LVLDEATAAVDLETDNLIQSTIRT-QFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNLLQQ 1509
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
80-205 |
1.05e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 58.50 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 80 IRQLRQHVGFVFQNFNLFpHRTVLENIIEGpvivKGEDKQESMARARELLAK----VGLSGKENS----YPRRLSGGQQQ 151
Cdd:PTZ00265 1291 LKDLRNLFSIVSQEPMLF-NMSIYENIKFG----KEDATREDVKRACKFAAIdefiESLPNKYDTnvgpYGKSLSGGQKQ 1365
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1879798416 152 RVAIARALAMRPDVILFDEPTSALDP---ELVGEVLNTIRQLAQekRTMVIVTHEMS 205
Cdd:PTZ00265 1366 RIAIARALLREPKILLLDEATSSLDSnseKLIEKTIVDIKDKAD--KTIITIAHRIA 1420
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
31-212 |
6.07e-09 |
|
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: 54.54 E-value: 6.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 31 VVAIIGPSGSGKTTLLRSINLL---EQPESGTIRVGDVT-IDAGRSLGpqkglirqlrqHVGFVFQNFN---LFPHRTVl 103
Cdd:cd03240 24 LTLIVGQNGAGKTTIIEALKYAltgELPPNSKGGAHDPKlIREGEVRA-----------QVKLAFENANgkkYTITRSL- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 104 eNIIEGPVIVKGEDKQESMARAREllakvglsgkensyprRLSGGQQQ------RVAIARALAMRPDVILFDEPTSALDP 177
Cdd:cd03240 92 -AILENVIFCHQGESNWPLLDMRG----------------RCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDE 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 1879798416 178 ELVGEVLNTI--RQLAQEKRTMVIVTHEMSFaRDVAD 212
Cdd:cd03240 155 ENIEESLAEIieERKSQKNFQLIVITHDEEL-VDAAD 190
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
19-247 |
1.97e-08 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 53.67 E-value: 1.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 19 LHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTI-RVGDVTIDAGRSlgpqkGLIRQLrqhvgfvfqnfnlf 97
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVdRNGEVSVIAISA-----GLSGQL-------------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 98 phrTVLENIiEGPVIVKGEDKQESMARARELLAKVGLSGKENSYPRRLSGGQQQRVAIARALAMRPDVILFDEPTSALDP 177
Cdd:PRK13546 101 ---TGIENI-EFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQ 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 178 ELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGEAKALFaspqqPRTRQFLEKF 247
Cdd:PRK13546 177 TFAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVL-----PKYEAFLNDF 241
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
4-189 |
2.24e-08 |
|
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: 53.32 E-value: 2.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 4 IEVKSLVKKF--HGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPEsgtirvGDVTIDAgrsLGPQKGLIR 81
Cdd:cd03289 3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE------GDIQIDG---VSWNSVPLQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 82 QLRQHVGFVFQNFNLF--PHRTVLENiiegpvivKGEDKQESMARAREllaKVGLSGKENSYPRRL-----------SGG 148
Cdd:cd03289 74 KWRKAFGVIPQKVFIFsgTFRKNLDP--------YGKWSDEEIWKVAE---EVGLKSVIEQFPGQLdfvlvdggcvlSHG 142
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1879798416 149 QQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQ 189
Cdd:cd03289 143 HKQLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQ 183
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
15-205 |
2.96e-08 |
|
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: 53.98 E-value: 2.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 15 GQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINlleqpESGTIRVGDVTIDAGRSLG--PQKGLI--RQLRQHVGF- 89
Cdd:TIGR00954 464 GDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILG-----ELWPVYGGRLTKPAKGKLFyvPQRPYMtlGTLRDQIIYp 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 90 --VFQNFNLFPHRTVLENIIEgpvIVKGEDKQEsmaraREllakVGLSGKENsYPRRLSGGQQQRVAIARALAMRPDVIL 167
Cdd:TIGR00954 539 dsSEDMKRRGLSDKDLEQILD---NVQLTHILE-----RE----GGWSAVQD-WMDVLSGGEKQRIAMARLFYHKPQFAI 605
|
170 180 190
....*....|....*....|....*....|....*....
gi 1879798416 168 FDEPTSALDPELVGEvlntIRQLAQEKR-TMVIVTHEMS 205
Cdd:TIGR00954 606 LDECTSAVSVDVEGY----MYRLCREFGiTLFSVSHRKS 640
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
28-202 |
5.10e-08 |
|
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: 51.21 E-value: 5.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 28 KGEVVAIIGPSGSGKTTLLRSINLLEqpesgtirvgdvtidAGRSLGPQKGLIRQLRQHVGFVFQNFNLFPHRtvlenii 107
Cdd:cd03227 20 EGSLTIITGPNGSGKSTILDAIGLAL---------------GGAQSATRRRSGVKAGCIVAAVSAELIFTRLQ------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 108 egpvivkgedkqesmararellakvglsgkensyprrLSGGQQQRVAIARALA----MRPDVILFDEPTSALDPELVGEV 183
Cdd:cd03227 78 -------------------------------------LSGGEKELSALALILAlaslKPRPLYILDEIDRGLDPRDGQAL 120
|
170
....*....|....*....
gi 1879798416 184 LNTIRQLAQEKRTMVIVTH 202
Cdd:cd03227 121 AEAILEHLVKGAQVIVITH 139
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
21-222 |
8.43e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 52.55 E-value: 8.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 21 GIDLEVQkgevVAIIGPSGSGKTTLLRSINLLEQPESGTIRvgdvtidagRSLGPQKGLIRQlrQHV-GFVFQNFNLFPH 99
Cdd:PLN03073 531 GIDLDSR----IAMVGPNGIGKSTILKLISGELQPSSGTVF---------RSAKVRMAVFSQ--HHVdGLDLSSNPLLYM 595
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 100 RTVLENIIEgpvivkgedkqesmARARELLAKVGLSGKENSYPR-RLSGGQQQRVAIARALAMRPDVILFDEPTSALDPE 178
Cdd:PLN03073 596 MRCFPGVPE--------------QKLRAHLGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLD 661
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1879798416 179 LVgEVLntIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRI 222
Cdd:PLN03073 662 AV-EAL--IQGLVLFQGGVLMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
117-210 |
1.27e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 52.17 E-value: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 117 DKQESMARARELLAKVGLSGK-ENSYPRRLSGGQQQRVAIARALAMRPDVILFDEPTSALDpelVGEVLNTIRQLAQEKR 195
Cdd:PLN03073 316 DAYTAEARAASILAGLSFTPEmQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD---LHAVLWLETYLLKWPK 392
|
90
....*....|....*
gi 1879798416 196 TMVIVTHEMSFARDV 210
Cdd:PLN03073 393 TFIVVSHAREFLNTV 407
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
123-224 |
1.66e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 51.71 E-value: 1.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 123 ARARELLAKVGLSGKENSYP-RRLSGGQQQRVAIARALAMRPDVILFDEPTSALDpelVGEVLNTIRQLAQEKRTMVIVT 201
Cdd:PRK10636 127 SRAASLLHGLGFSNEQLERPvSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLD---LDAVIWLEKWLKSYQGTLILIS 203
|
90 100
....*....|....*....|...
gi 1879798416 202 HEMSFARDVADRAIFMDQGRIVE 224
Cdd:PRK10636 204 HDRDFLDPIVDKIIHIEQQSLFE 226
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
18-233 |
1.95e-07 |
|
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: 50.68 E-value: 1.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 18 VLHGIDLEVQKGEVVAIIGPSGSGKTTL----LRSINLLEqpesgtirvGDVTIDAgrsLGPQKGLIRQLRQHVGFVFQN 93
Cdd:cd03288 36 VLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIFD---------GKIVIDG---IDISKLPLHTLRSRLSIILQD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 94 ---------FNLFPHRTVLENII-EGPVIVKGEDKQESMARArelLAKVGLSGKENsyprrLSGGQQQRVAIARALAMRP 163
Cdd:cd03288 104 pilfsgsirFNLDPECKCTDDRLwEALEIAQLKNMVKSLPGG---LDAVVTEGGEN-----FSVGQRQLFCLARAFVRKS 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 164 DVILFDEPTSALDPElVGEVLNTIRQLAQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGEAKALFA 233
Cdd:cd03288 176 SILIMDEATASIDMA-TENILQKVVMTAFADRTVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLLA 243
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
4-189 |
1.99e-07 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 51.45 E-value: 1.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 4 IEVKSLVKKF--HGQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPEsGTIRVGDVTIDAgRSLGPQKGLIR 81
Cdd:TIGR01271 1218 MDVQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWNS-VTLQTWRKAFG 1295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 82 QLRQHVgFVFQN---FNLFPHrtvleniiegpvivkgedKQESMARARELLAKVGLSGKENSYPRR-----------LSG 147
Cdd:TIGR01271 1296 VIPQKV-FIFSGtfrKNLDPY------------------EQWSDEEIWKVAEEVGLKSVIEQFPDKldfvlvdggyvLSN 1356
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1879798416 148 GQQQRVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQ 189
Cdd:TIGR01271 1357 GHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQ 1398
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
19-226 |
3.39e-07 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 49.56 E-value: 3.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 19 LHGIDLEVQKGEVVAIIGPSGSGKTTL-------------LRSINLLEQPESGTIRVGDVTIDAGrsLGP-----QKGLI 80
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLafdtiyaegqrryVESLSAYARQFLGQMDKPDVDSIEG--LSPaiaidQKTTS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 81 RQLRQHVGFVFQNFNLFphrtvleniiegpvivkgedkqesmaraRELLAKVGLS---------GKENSYPRR----LSG 147
Cdd:cd03270 89 RNPRSTVGTVTEIYDYL----------------------------RLLFARVGIRerlgflvdvGLGYLTLSRsaptLSG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 148 GQQQRVAIARALAMRPDVIL--FDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARdVADRAIFM------DQ 219
Cdd:cd03270 141 GEAQRIRLATQIGSGLTGVLyvLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIR-AADHVIDIgpgagvHG 219
|
....*..
gi 1879798416 220 GRIVEQG 226
Cdd:cd03270 220 GEIVAQG 226
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
20-202 |
2.27e-06 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 46.93 E-value: 2.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 20 HGIDLEvqkGEVVAIIGPSGSGKTTLLRSINLL--------EQPESGTIRVG------DVTIDAG----RSLGPQKGLIR 81
Cdd:COG0419 17 ETIDFD---DGLNLIVGPNGAGKSTILEAIRYAlygkarsrSKLRSDLINVGseeasvELEFEHGgkryRIERRQGEFAE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 82 QLR----QHVGFVFQNFNLFPHRTVLENI--IEGPVIVKGEDKQESMARARELLAKvgLSGKENsyPRRLSGGQQQRVAI 155
Cdd:COG0419 94 FLEakpsERKEALKRLLGLEIYEELKERLkeLEEALESALEELAELQKLKQEILAQ--LSGLDP--IETLSGGERLRLAL 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1879798416 156 ARALAMrpdviLFDepTSALDPELVGEVLNTIRQLAqekrtmvIVTH 202
Cdd:COG0419 170 ADLLSL-----ILD--FGSLDEERLERLLDALEELA-------IITH 202
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
16-222 |
3.60e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 47.47 E-value: 3.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 16 QTVLHGIDLEVQKGEVVAIIGPSGSGKTTLLRSINLLEQPESGTIrvgdvtidaGRSLGPQKGLIRQlrQHVGFVFQNFN 95
Cdd:PRK10636 325 RIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI---------GLAKGIKLGYFAQ--HQLEFLRADES 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 96 LFPHRTVLEniiegpvivkgedKQESMARARELLAKVGLSGKENSYP-RRLSGGQQQRVAIARALAMRPDVILFDEPTSA 174
Cdd:PRK10636 394 PLQHLARLA-------------PQELEQKLRDYLGGFGFQGDKVTEEtRRFSGGEKARLVLALIVWQRPNLLLLDEPTNH 460
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1879798416 175 LDPELvgevlntiRQLAQE-----KRTMVIVTHEMSFARDVADRAIFMDQGRI 222
Cdd:PRK10636 461 LDLDM--------RQALTEalidfEGALVVVSHDRHLLRSTTDDLYLVHDGKV 505
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
19-248 |
5.60e-06 |
|
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: 46.53 E-value: 5.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 19 LHGIDLEVQKGeVVAIIGPSGSGKTTLLRSINLL-----------------EQPESGTIRVgDVTIDA-----------G 70
Cdd:COG3593 14 IKDLSIELSDD-LTVLVGENNSGKSSILEALRLLlgpsssrkfdeedfylgDDPDLPEIEI-ELTFGSllsrllrlllkE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 71 RSLGPQKGLIRQLRQHVGFVFQNFNlfphrTVLENIIEGpvIVKGEDKQ-ESMARARELLAK---VGLSGKENSYPRRLS 146
Cdd:COG3593 92 EDKEELEEALEELNEELKEALKALN-----ELLSEYLKE--LLDGLDLElELSLDELEDLLKslsLRIEDGKELPLDRLG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 147 GGQQQRVAIARALAM-------RPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIfmdq 219
Cdd:COG3593 165 SGFQRLILLALLSALaelkrapANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTHSPHLLSEVPLENI---- 240
|
250 260 270
....*....|....*....|....*....|.
gi 1879798416 220 gRIVEQGEAKALFAS--PQQPRTRQFLEKFL 248
Cdd:COG3593 241 -RRLRRDSGGTTSTKliDLDDEDLRKLLRYL 270
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
121-204 |
1.20e-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: 46.16 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 121 SMARARELLAKVGLSgkensYPR------RLSGGQQQRVAIARALAMR---PDVILFDEPTSALDPELVGEVLNTIRQLA 191
Cdd:TIGR00630 805 SISRKLQTLCDVGLG-----YIRlgqpatTLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEVLQRLV 879
|
90
....*....|...
gi 1879798416 192 QEKRTMVIVTHEM 204
Cdd:TIGR00630 880 DKGNTVVVIEHNL 892
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
145-212 |
1.99e-05 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 44.53 E-value: 1.99e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1879798416 145 LSGGQQQRVAIARALAMR---PDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARdVAD 212
Cdd:cd03271 170 LSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIK-CAD 239
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
145-212 |
2.98e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.82 E-value: 2.98e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1879798416 145 LSGGQQQRVAIARALAMRPDVILF--DEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHE---MSFARDVAD 212
Cdd:PRK00635 477 LSGGEQERTALAKHLGAELIGITYilDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDeqmISLADRIID 549
|
|
| ABC_ATPase |
pfam09818 |
ATPase of the ABC class; This is the C-terminal ATPase domain from bacterial ABC class ATPases. ... |
146-234 |
1.12e-04 |
|
ATPase of the ABC class; This is the C-terminal ATPase domain from bacterial ABC class ATPases. This entry also includes MRB1590 from Trypanosoma brucei brucei has a central ATPase domain homologous to this domain.
Pssm-ID: 462914 Cd Length: 282 Bit Score: 42.58 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 146 SGGQQQRVAIARALAMRPDVILFDEPTSA--------LDPELVG---EVLNTIRQLAQEKR-----TMVIVTHEMSFARD 209
Cdd:pfam09818 159 SGSTSQAANIMEALEAGASLLLIDEDTSAtnfmirdeRMQALVSkdkEPITPFVDRVRSLYddlgvSTILVVGGSGDYLD 238
|
90 100
....*....|....*....|....*.
gi 1879798416 210 VADRAIFMDQGRIVE-QGEAKALFAS 234
Cdd:pfam09818 239 VADTVILMDEYRPSDvTEEAKEIAEE 264
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
142-202 |
2.03e-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: 2.03e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1879798416 142 PRRLSGGQQQ---RVAIARALAMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTH 202
Cdd:pfam13304 234 AFELSDGTKRllaLLAALLSALPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTH 297
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
13-52 |
4.90e-04 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 37.19 E-value: 4.90e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1879798416 13 FHGQTVlhgidlEVQKGEVVAIIGPSGSGKTTLLRSINLL 52
Cdd:pfam13555 12 FDGHTI------PIDPRGNTLLTGPSGSGKSTLLDAIQTL 45
|
|
| COG4938 |
COG4938 |
Predicted ATPase [General function prediction only]; |
34-202 |
6.98e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443965 [Multi-domain] Cd Length: 277 Bit Score: 39.95 E-value: 6.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 34 IIGPSGSGKTTLLRSINLLEQPE--------SGTIRVGDVTIDAGRSLGP----------QKGLIRQLRQHVGFVFQNFN 95
Cdd:COG4938 25 LIGPNGSGKSTLIQALLLLLQSNfiylpaerSGPARLYPSLVRELSDLGSrgeytadflaELENLEILDDKSKELLEQVE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 96 LFphrtvLENIIEGPVIVKGEDKQEsmararELLAKVGLSGKENSyPRRLSGGQQQRVAIARALAMRP---DVILFDEPT 172
Cdd:COG4938 105 EW-----LEKIFPGKVEVDASSDLV------RLVFRPSGNGKRIP-LSNVGSGVSELLPILLALLSAAkpgSLLIIEEPE 172
|
170 180 190
....*....|....*....|....*....|
gi 1879798416 173 SALDPELVGEVLNTIRQLAQEKRTMVIVTH 202
Cdd:COG4938 173 AHLHPKAQSALAELLAELANSGVQVIIETH 202
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
145-215 |
7.75e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.58 E-value: 7.75e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1879798416 145 LSGGQQQRVAIARAL---AMRPDVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARdVADRAI 215
Cdd:PRK00635 810 LSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNMHVVK-VADYVL 882
|
|
| MobB |
COG1763 |
Molybdopterin-guanine dinucleotide biosynthesis protein [Coenzyme transport and metabolism]; ... |
31-46 |
1.81e-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: 1.81e-03
|
| Udk |
COG0572 |
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ... |
31-49 |
2.24e-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: 38.28 E-value: 2.24e-03
|
| PEPCK_HprK |
cd00820 |
Phosphoenolpyruvate carboxykinase (PEPCK), a critical gluconeogenic enzyme, catalyzes the ... |
15-64 |
3.53e-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: 36.12 E-value: 3.53e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1879798416 15 GQTVLHGIDLEVQKGEVVAIIGPSGSGKTTLlrsinLLEQPESGTIRVGD 64
Cdd:cd00820 1 GTTSLHGVLVDVYGKVGVLITGDSGIGKTEL-----ALELIKRKHRLVGD 45
|
|
| NACHT |
COG5635 |
Predicted NTPase, NACHT family domain [Signal transduction mechanisms]; |
8-62 |
5.02e-03 |
|
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
Pssm-ID: 444362 [Multi-domain] Cd Length: 935 Bit Score: 37.86 E-value: 5.02e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1879798416 8 SLVKKFHGQTVLHGIDLevqKGEVVAIIGPSGSGKTTLLRSI--NLLEQPESGTIRV 62
Cdd:COG5635 162 NLLERIESLKRLELLEA---KKKRLLILGEPGSGKTTLLRYLalELAERYLDAEDPI 215
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
145-201 |
5.17e-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: 5.17e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1879798416 145 LSGGQQQRVAIARALAM-RPD---VILFDEPTSALDPELVGEVLNTIRQLAqeKRTMVIVT 201
Cdd:cd03272 159 LSGGQKSLVALALIFAIqKCDpapFYLFDEIDAALDAQYRTAVANMIKELS--DGAQFITT 217
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|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
145-212 |
5.33e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 37.70 E-value: 5.33e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1879798416 145 LSGGQQQRVAIARALAMRPD---VILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMsfarDV---AD 212
Cdd:COG0178 827 LSGGEAQRVKLASELSKRSTgktLYILDEPTTGLHFHDIRKLLEVLHRLVDKGNTVVVIEHNL----DViktAD 896
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
28-71 |
5.58e-03 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 36.75 E-value: 5.58e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1879798416 28 KGEVVAIIGPSGSGKTTLlrsINLLeQPESgTIRVGDVTIDAGR 71
Cdd:pfam03193 105 KGKTTVLAGQSGVGKSTL---LNAL-LPEL-DLRTGEISEKLGR 143
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
31-62 |
5.62e-03 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 36.17 E-value: 5.62e-03
10 20 30
....*....|....*....|....*....|...
gi 1879798416 31 VVAIIGPSGSGKTTLLRSI-NLLEQPESGTIRV 62
Cdd:pfam13401 7 ILVLTGESGTGKTTLLRRLlEQLPEVRDSVVFV 39
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
31-52 |
7.11e-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: 7.11e-03
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
145-189 |
7.81e-03 |
|
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.
Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 34.90 E-value: 7.81e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1879798416 145 LSGGQQQR---VAIARALAM----------RPDVILFDEPTSALDPELVGEVLNTIRQ 189
Cdd:pfam13558 33 LSGGEKQLlayLPLAAALAAqygsaegrppAPRLVFLDEAFAKLDEENIRTALELLRA 90
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
19-45 |
8.11e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 37.31 E-value: 8.11e-03
10 20
....*....|....*....|....*..
gi 1879798416 19 LHGIDLEVQKGEVVAIIGPSGSGKTTL 45
Cdd:COG0178 16 LKNIDVDIPRNKLVVITGLSGSGKSSL 42
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|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
32-65 |
8.89e-03 |
|
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). The structure of EF-G closely resembles that of the complex between EF-Tu and tRNA. This is an example of molecular mimicry; a protein domain evolved so that it mimics the shape of a tRNA molecule. EF-G in the GTP form binds to the ribosome, primarily through the interaction of its EF-Tu-like domain with the 50S subunit. The binding of EF-G to the ribosome in this manner stimulates the GTPase activity of EF-G. On GTP hydrolysis, EF-G undergoes a conformational change that forces its arm deeper into the A site on the 30S subunit. To accommodate this domain, the peptidyl-tRNA in the A site moves to the P site, carrying the mRNA and the deacylated tRNA with it. The ribosome may be prepared for these rearrangements by the initial binding of EF-G as well. The dissociation of EF-G leaves the ribosome ready to accept the next aminoacyl-tRNA into the A site. This group contains only bacterial members.
Pssm-ID: 206733 [Multi-domain] Cd Length: 268 Bit Score: 36.80 E-value: 8.89e-03
10 20 30
....*....|....*....|....*....|....*
gi 1879798416 32 VAIIGPSGSGKTTLLRSInLLeqpESGTI-RVGDV 65
Cdd:cd04170 2 IALVGHSGSGKTTLAEAL-LY---ATGAIdRLGRV 32
|
|
| RepA_RSF1010_like |
cd01125 |
Hexameric Replicative Helicase RepA of plasmid RSF1010 and related proteins; This family ... |
29-141 |
9.01e-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: 9.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 29 GEVVAIIGPSGSGKTTLLRSINL---LEQPESGTIRV--GDVTIDAGRslGPQKGLIRQLRQHVGFVFQNFNLFPHRTVL 103
Cdd:cd01125 1 GTLGMLVGPPGSGKSFLALDLAVavaTGRDWLGERRVkqGRVVYLAAE--DPRDGLRRRLKAIGAHLGDEDAALAENLVI 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1879798416 104 ENIIEGPVIVKGEDKQESMARAREL---------LAKVGLSGKENSY 141
Cdd:cd01125 79 ENLRGKPVSIDAEAPELERIIEELEgvrliiidtLARVLHGGDENDA 125
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
145-236 |
9.67e-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: 36.91 E-value: 9.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879798416 145 LSGGQQQRVAIARALAMRPDVILF--DEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARdVADRAIFMDQ--- 219
Cdd:TIGR00630 489 LSGGEAQRIRLATQIGSGLTGVLYvlDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEDTIR-AADYVIDIGPgag 567
|
90 100
....*....|....*....|
gi 1879798416 220 ---GRIVEQGEAKALFASPQ 236
Cdd:TIGR00630 568 ehgGEVVASGTPEEILANPD 587
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