|
Name |
Accession |
Description |
Interval |
E-value |
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
270-505 |
2.32e-153 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 436.73 E-value: 2.32e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPE--SLRRRVGM 347
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDinKLRRKVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 348 VFQHFNLFPDHTALENVMLSLTKIKKMPRSEARGIAEARLTEVGLAERKDHRPAGLSGGQQQRVAIARALAMDPEVILFD 427
Cdd:COG1126 82 VFQQFNLFPHLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLFD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2017776620 428 EVTSALDPELVKGVLDLMANLGRQGMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQIFDNPQSERLKRFLAEV 505
Cdd:COG1126 162 EPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHERTRAFLSKV 239
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
270-480 |
6.50e-120 |
|
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: 350.68 E-value: 6.50e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPE--SLRRRVGM 347
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNinELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 348 VFQHFNLFPDHTALENVMLSLTKIKKMPRSEARGIAEARLTEVGLAERKDHRPAGLSGGQQQRVAIARALAMDPEVILFD 427
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2017776620 428 EVTSALDPELVKGVLDLMANLGRQGMTMAVVTHEMGFARRVADQVVFMDEGRI 480
Cdd:cd03262 161 EPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
269-503 |
2.51e-116 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 343.32 E-value: 2.51e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 269 ALRVRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESIlAMKP---------- 338
Cdd:COG4598 8 ALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEI-RLKPdrdgelvpad 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 339 ----ESLRRRVGMVFQHFNLFPDHTALENVMLSLTKIKKMPRSEARGIAEARLTEVGLAERKDHRPAGLSGGQQQRVAIA 414
Cdd:COG4598 87 rrqlQRIRTRLGMVFQSFNLWSHMTVLENVIEAPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 415 RALAMDPEVILFDEVTSALDPELVKGVLDLMANLGRQGMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQIFDNPQ 494
Cdd:COG4598 167 RALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVFGNPK 246
|
....*....
gi 2017776620 495 SERLKRFLA 503
Cdd:COG4598 247 SERLRQFLS 255
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
273-505 |
4.03e-105 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 313.95 E-value: 4.03e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 273 RDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESIL--AMKPESLRRRVGMVFQ 350
Cdd:PRK09493 5 KNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIRQEAGMVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 351 HFNLFPDHTALENVMLSLTKIKKMPRSEARGIAEARLTEVGLAERKDHRPAGLSGGQQQRVAIARALAMDPEVILFDEVT 430
Cdd:PRK09493 85 QFYLFPHLTALENVMFGPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPT 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2017776620 431 SALDPELVKGVLDLMANLGRQGMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQIFDNPQSERLKRFLAEV 505
Cdd:PRK09493 165 SALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEFLQHV 239
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
270-506 |
8.44e-90 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 278.11 E-value: 8.44e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAY----GDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPESL---R 342
Cdd:COG1135 2 IELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELraaR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 343 RRVGMVFQHFNLFPDHTALENVMLSLtKIKKMPRSEARgiaeARLTE----VGLAERKDHRPAGLSGGQQQRVAIARALA 418
Cdd:COG1135 82 RKIGMIFQHFNLLSSRTVAENVALPL-EIAGVPKAEIR----KRVAEllelVGLSDKADAYPSQLSGGQKQRVGIARALA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 419 MDPEVILFDEVTSALDPELVKGVLDLMANLGRQ-GMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQIFDNPQSER 497
Cdd:COG1135 157 NNPKVLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQSEL 236
|
....*....
gi 2017776620 498 LKRFLAEVL 506
Cdd:COG1135 237 TRRFLPTVL 245
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
269-506 |
2.08e-88 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 271.62 E-value: 2.08e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 269 ALRVRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPES-------- 340
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLSqqkglirq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 341 LRRRVGMVFQHFNLFPDHTALENVMLSLTKIKKMPRSEARGIAEARLTEVGLAERKDHRPAGLSGGQQQRVAIARALAMD 420
Cdd:PRK11264 83 LRQHVGFVFQNFNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 421 PEVILFDEVTSALDPELVKGVLDLMANLGRQGMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQIFDNPQSERLKR 500
Cdd:PRK11264 163 PEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPRTRQ 242
|
....*.
gi 2017776620 501 FLAEVL 506
Cdd:PRK11264 243 FLEKFL 248
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
269-497 |
2.29e-87 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 268.83 E-value: 2.29e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 269 ALRVRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRL--------VEpkrGDILLDGESILA--MKP 338
Cdd:COG1117 11 KIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndlipgarVE---GEILLDGEDIYDpdVDV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 339 ESLRRRVGMVFQHFNLFPdHTALENVMLSLTKIKKMPRSEARGIAEARLTEVGL-AERKD--HRPA-GLSGGQQQRVAIA 414
Cdd:COG1117 88 VELRRRVGMVFQKPNPFP-KSIYDNVAYGLRLHGIKSKSELDEIVEESLRKAALwDEVKDrlKKSAlGLSGGQQQRLCIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 415 RALAMDPEVILFDEVTSALDPELVKGVLDLMANLgRQGMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQIFDNPQ 494
Cdd:COG1117 167 RALAVEPEVLLMDEPTSALDPISTAKIEELILEL-KKDYTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIFTNPK 245
|
...
gi 2017776620 495 SER 497
Cdd:COG1117 246 DKR 248
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
269-502 |
5.61e-85 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 262.22 E-value: 5.61e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 269 ALRVRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPE---SLRRRV 345
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKelyELRRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 346 GMVFQHFNLFPDHTALENVMLSLTKIKKMPRSEARGIAEARLTEVGLAERKDHRPAGLSGGQQQRVAIARALAMDPEVIL 425
Cdd:COG1127 85 GMLFQGGALFDSLTVFENVAFPLREHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2017776620 426 FDEVTSALDPELVKGVLDLMANLGRQ-GMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQIFDNPqSERLKRFL 502
Cdd:COG1127 165 YDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASD-DPWVRQFL 241
|
|
| ectoine_ehuA |
TIGR03005 |
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ... |
270-506 |
2.25e-83 |
|
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: 258.61 E-value: 2.25e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPES--------- 340
Cdd:TIGR03005 1 VRFSDVTKRFGILTVLDGLNFSVAAGEKVALIGPSGSGKSTILRILMTLEPIDEGQIQVEGEQLYHMPGRNgplvpadek 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 341 ----LRRRVGMVFQHFNLFPDHTALENVMLSLTKIKKMPRSEARGIAEARLTEVGLAERKDHRPAGLSGGQQQRVAIARA 416
Cdd:TIGR03005 81 hlrqMRNKIGMVFQSFNLFPHKTVLDNVTEAPVLVLGMARAEAEKRAMELLDMVGLADKADHMPAQLSGGQQQRVAIARA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 417 LAMDPEVILFDEVTSALDPELVKGVLDLMANLGRQ-GMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQIFDNPQS 495
Cdd:TIGR03005 161 LAMRPKVMLFDEVTSALDPELVGEVLNVIRRLASEhDLTMLLVTHEMGFAREFADRVCFFDKGRIVEQGKPDEIFRQPKE 240
|
250
....*....|.
gi 2017776620 496 ERLKRFLAEVL 506
Cdd:TIGR03005 241 ERTREFLSKVI 251
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
270-494 |
5.27e-81 |
|
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: 251.73 E-value: 5.27e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAYGD----LDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPESL---R 342
Cdd:cd03258 2 IELKNVSKVFGDtggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELrkaR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 343 RRVGMVFQHFNLFPDHTALENVMLSLtKIKKMPRSEARGIAEARLTEVGLAERKDHRPAGLSGGQQQRVAIARALAMDPE 422
Cdd:cd03258 82 RRIGMIFQHFNLLSSRTVFENVALPL-EIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2017776620 423 VILFDEVTSALDPELVKGVLDLMANLGRQ-GMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQIFDNPQ 494
Cdd:cd03258 161 VLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
269-482 |
8.58e-81 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 250.73 E-value: 8.58e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 269 ALRVRDLSMAYGD----LDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPESL--- 341
Cdd:COG1136 4 LLELRNLTKSYGTgegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELarl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 342 -RRRVGMVFQHFNLFPDHTALENVMLSLTkIKKMPRSEARGIAEARLTEVGLAERKDHRPAGLSGGQQQRVAIARALAMD 420
Cdd:COG1136 84 rRRHIGFVFQFFNLLPELTALENVALPLL-LAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2017776620 421 PEVILFDEVTSALDPELVKGVLDLMANLGRQ-GMTMAVVTHEMGFARRvADQVVFMDEGRIIE 482
Cdd:COG1136 163 PKLILADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHDPELAAR-ADRVIRLRDGRIVS 224
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
270-506 |
1.02e-80 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 251.81 E-value: 1.02e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKP----------- 338
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDkdgqlkvadkn 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 339 --ESLRRRVGMVFQHFNLFPDHTALENVMLSLTKIKKMPRSEARGIAEARLTEVGLAER-KDHRPAGLSGGQQQRVAIAR 415
Cdd:PRK10619 86 qlRLLRTRLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERaQGKYPVHLSGGQQQRVSIAR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 416 ALAMDPEVILFDEVTSALDPELVKGVLDLMANLGRQGMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQIFDNPQS 495
Cdd:PRK10619 166 ALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQS 245
|
250
....*....|.
gi 2017776620 496 ERLKRFLAEVL 506
Cdd:PRK10619 246 PRLQQFLKGSL 256
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
269-504 |
1.04e-79 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 252.71 E-value: 1.04e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 269 ALRVRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPEslRRRVGMV 348
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPE--KRNVGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 349 FQHFNLFPDHTALENVMLSLtKIKKMPRSEARGIAEARLTEVGLAERKDHRPAGLSGGQQQRVAIARALAMDPEVILFDE 428
Cdd:COG3842 83 FQDYALFPHLTVAENVAFGL-RMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2017776620 429 VTSALDPELVKGVLDLMANLGRQ-GMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQIFDNPQSerlkRFLAE 504
Cdd:COG3842 162 PLSALDAKLREEMREELRRLQRElGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPAT----RFVAD 234
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
270-489 |
3.16e-79 |
|
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: 246.71 E-value: 3.16e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVE-----PKRGDILLDGESILA--MKPESLR 342
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDldVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 343 RRVGMVFQHFNLFPdHTALENVMLSLTKIKKMPRSEARGIAEARLTEVGLAER-KDH-RPAGLSGGQQQRVAIARALAMD 420
Cdd:cd03260 81 RRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALWDEvKDRlHALGLSGGQQQRLCLARALANE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2017776620 421 PEVILFDEVTSALDPELVKGVLDLMANLGRQgMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQI 489
Cdd:cd03260 160 PEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
270-500 |
1.64e-78 |
|
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: 244.93 E-value: 1.64e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAY-GDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPESLRRRVGMV 348
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 349 FQhfnlFPDH-----TALENVMLSLtKIKKMPRSEARGIAEARLTEVGLAERKDHRPAGLSGGQQQRVAIARALAMDPEV 423
Cdd:COG1122 81 FQ----NPDDqlfapTVEEDVAFGP-ENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2017776620 424 ILFDEVTSALDPELVKGVLDLMANLGRQGMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQIFDNPqsERLKR 500
Cdd:COG1122 156 LVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDY--ELLEE 230
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
270-494 |
1.59e-77 |
|
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: 242.79 E-value: 1.59e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPE---SLRRRVG 346
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAelyRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 347 MVFQHFNLFPDHTALENVMLSLTKIKKMPRSEARGIAEARLTEVGLAERKDHRPAGLSGGQQQRVAIARALAMDPEVILF 426
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFPLREHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLY 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2017776620 427 DEVTSALDPELVKGVLDLMANLGRQ-GMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQIF--DNPQ 494
Cdd:cd03261 161 DEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRasDDPL 231
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
285-506 |
8.91e-77 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 244.71 E-value: 8.91e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 285 LKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPESL---RRRVGMVFQHFNLFPDHTAL 361
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELrkaRRQIGMIFQHFNLLSSRTVF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 362 ENVMLSLtKIKKMPRSEArgiaEARLTE----VGLAERKDHRPAGLSGGQQQRVAIARALAMDPEVILFDEVTSALDPEL 437
Cdd:PRK11153 101 DNVALPL-ELAGTPKAEI----KARVTEllelVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLLCDEATSALDPAT 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 438 VKGVLDLMANLGRQ-GMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQIFDNPQSERLKRFLAEVL 506
Cdd:PRK11153 176 TRSILELLKDINRElGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTREFIQSTL 245
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
270-480 |
1.46e-76 |
|
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: 239.70 E-value: 1.46e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAYGDLD----VLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPESL---- 341
Cdd:cd03255 1 IELKNLSKTYGGGGekvqALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 342 RRRVGMVFQHFNLFPDHTALENVMLSLtKIKKMPRSEARGIAEARLTEVGLAERKDHRPAGLSGGQQQRVAIARALAMDP 421
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPL-LLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 422 EVILFDEVTSALDPELVKGVLDLMANLGRQ-GMTMAVVTHEMGFARRvADQVVFMDEGRI 480
Cdd:cd03255 160 KIILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHDPELAEY-ADRIIELRDGKI 218
|
|
| HisM |
COG0765 |
ABC-type amino acid transport system, permease component [Amino acid transport and metabolism]; ... |
10-234 |
2.02e-76 |
|
ABC-type amino acid transport system, permease component [Amino acid transport and metabolism];
Pssm-ID: 440528 [Multi-domain] Cd Length: 218 Bit Score: 239.21 E-value: 2.02e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 10 SFLDWDAMAEVLPSMITvGLKNTLILAAASTVLGVIIGMVLAVMGISQSRWLRLPARIYTDIFRGLPAIVTILIIGQGFA 89
Cdd:COG0765 1 MFFDFSVLLDYLPLLLE-GLLVTLLLTVLAIVLGLVLGLLLALARLSPNPVLRWLATAYVEFFRGTPLLVQLFFIYFGLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 90 RIGRELfgpSPFPLGIIALSLIAGAYIGEIFRSGIQSVERGQMEACRALSMSYGQGMRLIVIPQGVRRVLPALVNQFIGN 169
Cdd:COG0765 80 LLGIDL---SPFVAAVIALTLNSAAYLAEIVRAGIQSVPKGQWEAARALGLSRWQTMRRIILPQALRIILPPLGNEFISL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2017776620 170 VKDSSLVYFLGLLaserEIFRVGQDQAVVTGN-LSPLLLAGVFYLLITVPLTHFVNYIDARLRLGR 234
Cdd:COG0765 157 LKDTSLVSVIGVP----ELTRAAQQIASRTFRpFEVYLVAALIYLVLTLPLSLLARRLERRLARGR 218
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
270-505 |
1.89e-75 |
|
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: 246.74 E-value: 1.89e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAY-----GDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPES---L 341
Cdd:COG1123 261 LEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSlreL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 342 RRRVGMVFQHFN--LFPDHTALENVMLSLTKIKKMPRSEARGIAEARLTEVGL-AERKDHRPAGLSGGQQQRVAIARALA 418
Cdd:COG1123 341 RRRVQMVFQDPYssLNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIARALA 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 419 MDPEVILFDEVTSALDPELVKGVLDLMANLGRQ-GMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQIFDNPQSER 497
Cdd:COG1123 421 LEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPQHPY 500
|
....*...
gi 2017776620 498 LKRFLAEV 505
Cdd:COG1123 501 TRALLAAV 508
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
269-503 |
6.21e-75 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 236.45 E-value: 6.21e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 269 ALRVRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESI-LAMKPE-----SLR 342
Cdd:COG4161 2 SIQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdFSQKPSekairLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 343 RRVGMVFQHFNLFPDHTALENVMLSLTKIKKMPRSEARGIAEARLTEVGLAERKDHRPAGLSGGQQQRVAIARALAMDPE 422
Cdd:COG4161 82 QKVGMVFQQYNLWPHLTVMENLIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 423 VILFDEVTSALDPELVKGVLDLMANLGRQGMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSpQQIFDNPQSERLKRFL 502
Cdd:COG4161 162 VLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGD-ASHFTQPQTEAFAHYL 240
|
.
gi 2017776620 503 A 503
Cdd:COG4161 241 S 241
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
270-484 |
7.65e-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: 229.71 E-value: 7.65e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPEslRRRVGMVF 349
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 350 QHFNLFPDHTALENVMLSLtKIKKMPRSEARGIAEARLTEVGLAERKDHRPAGLSGGQQQRVAIARALAMDPEVILFDEV 429
Cdd:cd03259 79 QDYALFPHLTVAENIAFGL-KLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2017776620 430 TSALDPELVKGVLDLMANLGRQ-GMTMAVVTHEMGFARRVADQVVFMDEGRIIEAG 484
Cdd:cd03259 158 LSALDAKLREELREELKELQRElGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
269-489 |
2.76e-71 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 227.25 E-value: 2.76e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 269 ALRVRDLSMAY-GDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPESL---RRR 344
Cdd:COG3638 2 MLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALrrlRRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 345 VGMVFQHFNLFPDHTALENVML----------SLTKIkkMPRSEARGIAEArLTEVGLAERKDHRPAGLSGGQQQRVAIA 414
Cdd:COG3638 82 IGMIFQQFNLVPRLSVLTNVLAgrlgrtstwrSLLGL--FPPEDRERALEA-LERVGLADKAYQRADQLSGGQQQRVAIA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2017776620 415 RALAMDPEVILFDEVTSALDPELVKGVLDLMANLGR-QGMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQI 489
Cdd:COG3638 159 RALVQEPKLILADEPVASLDPKTARQVMDLLRRIAReDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAEL 234
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
285-505 |
4.01e-70 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 228.83 E-value: 4.01e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 285 LKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPESL----RRRVGMVFQHFNLFPDHTA 360
Cdd:COG4175 43 VNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGEVLIDGEDITKLSKKELrelrRKKMSMVFQHFALLPHRTV 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 361 LENVMLSLtKIKKMPRSEARGIAEARLTEVGLAERKDHRPAGLSGGQQQRVAIARALAMDPEVILFDEVTSALDP----- 435
Cdd:COG4175 123 LENVAFGL-EIQGVPKAERRERAREALELVGLAGWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDPlirre 201
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2017776620 436 ---ELvkgvLDLMANLGRqgmTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQIFDNPQSERLKRFLAEV 505
Cdd:COG4175 202 mqdEL----LELQAKLKK---TIVFITHDLDEALRLGDRIAIMKDGRIVQIGTPEEILTNPANDYVADFVEDV 267
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
271-479 |
2.29e-69 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 220.80 E-value: 2.29e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 271 RVRDLSMAYGDLD--VLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPESLRRRVGMV 348
Cdd:cd03225 1 ELKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 349 FQHfnlfPDH-----TALENVMLSLtKIKKMPRSEARGIAEARLTEVGLAERKDHRPAGLSGGQQQRVAIARALAMDPEV 423
Cdd:cd03225 81 FQN----PDDqffgpTVEEEVAFGL-ENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2017776620 424 ILFDEVTSALDPELVKGVLDLMANLGRQGMTMAVVTHEMGFARRVADQVVFMDEGR 479
Cdd:cd03225 156 LLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
270-505 |
2.31e-69 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 221.86 E-value: 2.31e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAmKPESLRRRVGMVF 349
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 350 QHFNLFPDHTALENVMLsLTKIKKMPRSEARGIAEARLTEVGLAERKDHRPAGLSGGQQQRVAIARALAMDPEVILFDEV 429
Cdd:COG1131 80 QEPALYPDLTVRENLRF-FARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2017776620 430 TSALDPELVKGVLDLMANLGRQGMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQIfdnpqserLKRFLAEV 505
Cdd:COG1131 159 TSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL--------KARLLEDV 226
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
269-503 |
4.99e-69 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 221.04 E-value: 4.99e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 269 ALRVRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESI-LAMKPE-----SLR 342
Cdd:PRK11124 2 SIQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdFSKTPSdkairELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 343 RRVGMVFQHFNLFPDHTALENVMLSLTKIKKMPRSEARGIAEARLTEVGLAERKDHRPAGLSGGQQQRVAIARALAMDPE 422
Cdd:PRK11124 82 RNVGMVFQQYNLWPHLTVQQNLIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 423 VILFDEVTSALDPELVKGVLDLMANLGRQGMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQiFDNPQSERLKRFL 502
Cdd:PRK11124 162 VLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASC-FTQPQTEAFKNYL 240
|
.
gi 2017776620 503 A 503
Cdd:PRK11124 241 S 241
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
267-482 |
2.85e-68 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 219.58 E-value: 2.85e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 267 AGALRVRDLSMAY----GDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESIlamkpESLR 342
Cdd:COG1116 5 APALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPV-----TGPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 343 RRVGMVFQHFNLFPDHTALENVMLSLtKIKKMPRSEARGIAEARLTEVGLAERKDHRPAGLSGGQQQRVAIARALAMDPE 422
Cdd:COG1116 80 PDRGVVFQEPALLPWLTVLDNVALGL-ELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2017776620 423 VILFDEVTSALDpELVKGVL--DLMANLGRQGMTMAVVTHEMGFARRVADQVVFMDE--GRIIE 482
Cdd:COG1116 159 VLLMDEPFGALD-ALTRERLqdELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSArpGRIVE 221
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
288-505 |
1.46e-67 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 218.28 E-value: 1.46e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 288 VDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPESL----RRRVGMVFQHFNLFPDHTALEN 363
Cdd:cd03294 43 VSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQSFALLPHRTVLEN 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 364 VMLSLtKIKKMPRSEARGIAEARLTEVGLAERKDHRPAGLSGGQQQRVAIARALAMDPEVILFDEVTSALDP----ELVK 439
Cdd:cd03294 123 VAFGL-EVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPlirrEMQD 201
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2017776620 440 GVLDLMANLGRqgmTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQIFDNPQSERLKRFLAEV 505
Cdd:cd03294 202 ELLRLQAELQK---TIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFFRGV 264
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
269-500 |
1.95e-67 |
|
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: 217.22 E-value: 1.95e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 269 ALRVRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPESLRRRVGMV 348
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 349 FQHFNLFPDHTALENVMLSLT---KIKKMPRSEARGIAEARLTEVGLAERKDHRPAGLSGGQQQRVAIARALAMDPEVIL 425
Cdd:COG1120 81 PQEPPAPFGLTVRELVALGRYphlGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2017776620 426 FDEVTSALDPELVKGVLDLMANLGR-QGMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQIFDnpqSERLKR 500
Cdd:COG1120 161 LDEPTSHLDLAHQLEVLELLRRLAReRGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLT---PELLEE 233
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
270-506 |
3.31e-67 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 220.02 E-value: 3.31e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPeSLRRRVGMVF 349
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNLP-PRERRVGFVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 350 QHFNLFPDHTALENVMLSLtKIKKMPRSEARGIAEARLTEVGLAERKDHRPAGLSGGQQQRVAIARALAMDPEVILFDEV 429
Cdd:COG1118 82 QHYALFPHMTVAENIAFGL-RVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 430 TSALDPELVKgvlDLMANLGR----QGMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQIFDNPQSERLKRFLAEV 505
Cdd:COG1118 161 FGALDAKVRK---ELRRWLRRlhdeLGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFLGCV 237
|
.
gi 2017776620 506 L 506
Cdd:COG1118 238 N 238
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
270-494 |
1.10e-66 |
|
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: 214.61 E-value: 1.10e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKP-ESLRRRVGMV 348
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPhEIARLGIGRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 349 FQHFNLFPDHTALENVMLSLTKIKK---------MPRSEARGIAEARLTEVGLAERKDHRPAGLSGGQQQRVAIARALAM 419
Cdd:cd03219 81 FQIPRLFPELTVLENVMVAAQARTGsglllararREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALAT 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2017776620 420 DPEVILFDEVTSALDPELVKGVLDLMANLGRQGMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQIFDNPQ 494
Cdd:cd03219 161 DPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPR 235
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
270-479 |
1.24e-66 |
|
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: 212.43 E-value: 1.24e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESI--LAMKPESLRRRVGM 347
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLtdLEDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 348 VFQHFNLFPDHTALENVMLsltkikkmprseargiaearltevglaerkdhrpaGLSGGQQQRVAIARALAMDPEVILFD 427
Cdd:cd03229 81 VFQDFALFPHLTVLENIAL-----------------------------------GLSGGQQQRVALARALAMDPDVLLLD 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2017776620 428 EVTSALDPELVKGVLDLMANLGRQ-GMTMAVVTHEMGFARRVADQVVFMDEGR 479
Cdd:cd03229 126 EPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
270-484 |
2.03e-66 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 213.76 E-value: 2.03e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAY-GDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPES---LRRRV 345
Cdd:COG2884 2 IRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipyLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 346 GMVFQHFNLFPDHTALENVMLSLtKIKKMPRSEARGIAEARLTEVGLAERKDHRPAGLSGGQQQRVAIARALAMDPEVIL 425
Cdd:COG2884 82 GVVFQDFRLLPDRTVYENVALPL-RVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2017776620 426 FDEVTSALDPELVKGVLDLMANLGRQGMTMAVVTHEMGFARRVADQVVFMDEGRIIEAG 484
Cdd:COG2884 161 ADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLVRDE 219
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
269-503 |
3.34e-66 |
|
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: 213.90 E-value: 3.34e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 269 ALRVRDLSMAYG----DLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPESLRRR 344
Cdd:COG1124 1 MLEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 345 VGMVFQH----FNlfPDHTALENVMLSLtKIKKMPRSEARgIAEArLTEVGLAER-KDHRPAGLSGGQQQRVAIARALAM 419
Cdd:COG1124 81 VQMVFQDpyasLH--PRHTVDRILAEPL-RIHGLPDREER-IAEL-LEQVGLPPSfLDRYPHQLSGGQRQRVAIARALIL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 420 DPEVILFDEVTSALDPELVKGVLDLMANLGRQ-GMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQIFDNPQSERL 498
Cdd:COG1124 156 EPELLLLDEPTSALDVSVQAEILNLLKDLREErGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKHPYT 235
|
....*
gi 2017776620 499 KRFLA 503
Cdd:COG1124 236 RELLA 240
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
269-495 |
9.12e-66 |
|
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: 220.93 E-value: 9.12e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 269 ALRVRDLSMAY--GDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPK---RGDILLDGESILAMKPESLRR 343
Cdd:COG1123 4 LLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 344 RVGMVFQHF--NLFPdHTALENVMLSLtKIKKMPRSEARGIAEARLTEVGLAERKDHRPAGLSGGQQQRVAIARALAMDP 421
Cdd:COG1123 84 RIGMVFQDPmtQLNP-VTVGDQIAEAL-ENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2017776620 422 EVILFDEVTSALDPELVKGVLDLMANLGRQ-GMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQIFDNPQS 495
Cdd:COG1123 162 DLLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQA 236
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
270-489 |
3.29e-65 |
|
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: 211.27 E-value: 3.29e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAYGDLD-VLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPESL---RRRV 345
Cdd:cd03256 1 IEVENLSKTYPNGKkALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALrqlRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 346 GMVFQHFNLFPDHTALENVML----SLTKIKKMPR---SEARGIAEARLTEVGLAERKDHRPAGLSGGQQQRVAIARALA 418
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSgrlgRRSTWRSLFGlfpKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2017776620 419 MDPEVILFDEVTSALDPELVKGVLDLMANLGRQ-GMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQI 489
Cdd:cd03256 161 QQPKLILADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
269-494 |
4.35e-65 |
|
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: 211.44 E-value: 4.35e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 269 ALRVRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPESLRRRvGMV 348
Cdd:COG0411 4 LLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARL-GIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 349 --FQHFNLFPDHTALENVML------------SLTKIKKMPRSEARGIAEAR--LTEVGLAERKDHRPAGLSGGQQQRVA 412
Cdd:COG0411 83 rtFQNPRLFPELTVLENVLVaaharlgrgllaALLRLPRARREEREARERAEelLERVGLADRADEPAGNLSYGQQRRLE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 413 IARALAMDPEVILFDEVTSALDPELVKGVLDLMANL-GRQGMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQIFD 491
Cdd:COG0411 163 IARALATEPKLLLLDEPAAGLNPEETEELAELIRRLrDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAEVRA 242
|
...
gi 2017776620 492 NPQ 494
Cdd:COG0411 243 DPR 245
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
268-495 |
1.97e-64 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 212.63 E-value: 1.97e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 268 GALRVRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPEslRRRVGM 347
Cdd:COG3839 2 ASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPK--DRNIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 348 VFQHFNLFPDHTALENVMLSLtKIKKMPRSEARgiaeARLTEV----GLAERKDHRPAGLSGGQQQRVAIARALAMDPEV 423
Cdd:COG3839 80 VFQSYALYPHMTVYENIAFPL-KLRKVPKAEID----RRVREAaellGLEDLLDRKPKQLSGGQRQRVALGRALVREPKV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2017776620 424 ILFDEVTSALDPEL-VKGVLDLMANLGRQGMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQIFDNPQS 495
Cdd:COG3839 155 FLLDEPLSNLDAKLrVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPAN 227
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
270-491 |
4.26e-64 |
|
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: 208.31 E-value: 4.26e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAYGDLD-VLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPESL---RRRV 345
Cdd:TIGR02315 2 LEVENLSKVYPNGKqALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLrklRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 346 GMVFQHFNLFPDHTALENVML----SLTKIKKM----PRSEARgIAEARLTEVGLAERKDHRPAGLSGGQQQRVAIARAL 417
Cdd:TIGR02315 82 GMIFQHYNLIERLTVLENVLHgrlgYKPTWRSLlgrfSEEDKE-RALSALERVGLADKAYQRADQLSGGQQQRVAIARAL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2017776620 418 AMDPEVILFDEVTSALDPELVKGVLDLMANLGRQ-GMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQIFD 491
Cdd:TIGR02315 161 AQQPDLILADEPIASLDPKTSKQVMDYLKRINKEdGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELDD 235
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
270-482 |
1.09e-62 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 203.86 E-value: 1.09e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAYGDLD----VLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESIlamkpESLRRRV 345
Cdd:cd03293 1 LEVRNVSKTYGGGGgavtALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPV-----TGPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 346 GMVFQHFNLFPDHTALENVMLSLtKIKKMPRSEARGIAEARLTEVGLAERKDHRPAGLSGGQQQRVAIARALAMDPEVIL 425
Cdd:cd03293 76 GYVFQQDALLPWLTVLDNVALGL-ELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2017776620 426 FDEVTSALDpELVKGVL--DLMANLGRQGMTMAVVTHEMGFARRVADQVVFMDE--GRIIE 482
Cdd:cd03293 155 LDEPFSALD-ALTREQLqeELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRIVA 214
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
270-502 |
5.95e-62 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 203.22 E-value: 5.95e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVE--PK---RGDILLDGESILAMKPESLRRR 344
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEarvSGEVYLDGQDIFKMDVIELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 345 VGMVFQHFNLFPDHTALENVMLSLtKIKKMPRSEARGIAEAR--LTEVGLAERKDHR---PAG-LSGGQQQRVAIARALA 418
Cdd:PRK14247 84 VQMVFQIPNPIPNLSIFENVALGL-KLNRLVKSKKELQERVRwaLEKAQLWDEVKDRldaPAGkLSGGQQQRLCIARALA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 419 MDPEVILFDEVTSALDPELVKGVLDLMANLgRQGMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQIFDNPQSERL 498
Cdd:PRK14247 163 FQPEVLLADEPTANLDPENTAKIESLFLEL-KKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRHELT 241
|
....
gi 2017776620 499 KRFL 502
Cdd:PRK14247 242 EKYV 245
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
270-504 |
6.18e-62 |
|
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: 202.53 E-value: 6.18e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAYGDLD-VLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPESLRRRVGMV 348
Cdd:cd03295 1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 349 FQHFNLFPDHTALENVMLsLTKIKKMPRSEARGIAEARLTEVGL--AERKDHRPAGLSGGQQQRVAIARALAMDPEVILF 426
Cdd:cd03295 81 IQQIGLFPHMTVEENIAL-VPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLLM 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2017776620 427 DEVTSALDPELVKGVLDLMANLGRQ-GMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQIFDNPQSERLKRFLAE 504
Cdd:cd03295 160 DEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVGA 238
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
270-499 |
1.04e-61 |
|
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: 203.05 E-value: 1.04e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAY--GDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGesILAMKPESL---RRR 344
Cdd:TIGR04520 1 IEVENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDG--LDTLDEENLweiRKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 345 VGMVFQHfnlfPDHT------------ALENVMLSLTKIKKmprseaRgIAEArLTEVGLAERKDHRPAGLSGGQQQRVA 412
Cdd:TIGR04520 79 VGMVFQN----PDNQfvgatveddvafGLENLGVPREEMRK------R-VDEA-LKLVGMEDFRDREPHLLSGGQKQRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 413 IARALAMDPEVILFDEVTSALDPELVKGVLDLMANLGR-QGMTMAVVTHEMGFARRvADQVVFMDEGRIIEAGSPQQIFd 491
Cdd:TIGR04520 147 IAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKeEGITVISITHDMEEAVL-ADRVIVMNKGKIVAEGTPREIF- 224
|
....*...
gi 2017776620 492 nPQSERLK 499
Cdd:TIGR04520 225 -SQVELLK 231
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
269-483 |
3.65e-61 |
|
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: 200.35 E-value: 3.65e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 269 ALRVRDLSMAYGD----LDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPESL--- 341
Cdd:COG4181 8 IIELRGLTKTVGTgageLTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARarl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 342 -RRRVGMVFQHFNLFPDHTALENVMLSLtkiKKMPRSEARGIAEARLTEVGLAERKDHRPAGLSGGQQQRVAIARALAMD 420
Cdd:COG4181 88 rARHVGFVFQSFQLLPTLTALENVMLPL---ELAGRRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2017776620 421 PEVILFDEVTSALDPELVKGVLDLMANLGR-QGMTMAVVTHEMGFARRvADQVVFMDEGRIIEA 483
Cdd:COG4181 165 PAILFADEPTGNLDAATGEQIIDLLFELNReRGTTLVLVTHDPALAAR-CDRVLRLRAGRLVED 227
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
270-504 |
2.06e-60 |
|
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: 198.23 E-value: 2.06e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPEslRRRVGMVF 349
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH--KRPVNTVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 350 QHFNLFPDHTALENVMLSLtKIKKMPRSEARGIAEARLTEVGLAERKDHRPAGLSGGQQQRVAIARALAMDPEVILFDEV 429
Cdd:cd03300 79 QNYALFPHLTVFENIAFGL-RLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2017776620 430 TSALDPELVKGVLDLMANLGRQ-GMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQIFDNPQSerlkRFLAE 504
Cdd:cd03300 158 LGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPAN----RFVAD 229
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
270-484 |
8.70e-60 |
|
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: 196.57 E-value: 8.70e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAY----GDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPESL---R 342
Cdd:cd03257 2 LEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 343 RRVGMVFQH--FNLFPDHTALENVMLSLTKIKKMPRSEARGIAEAR-LTEVGLAERKDHR-PAGLSGGQQQRVAIARALA 418
Cdd:cd03257 82 KEIQMVFQDpmSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLlLVGVGLPEEVLNRyPHELSGGQRQRVAIARALA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2017776620 419 MDPEVILFDEVTSALDPELVKGVLDLMANLGRQ-GMTMAVVTHEMGFARRVADQVVFMDEGRIIEAG 484
Cdd:cd03257 162 LNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
270-494 |
9.88e-60 |
|
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: 199.51 E-value: 9.88e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAY----GDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKR---GDILLDGESILAMKPESLR 342
Cdd:COG0444 2 LEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGitsGEILFDGEDLLKLSEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 343 ----RRVGMVFQH----FNlfPDHTALENVMLSLTKIKKMPRSEARGIAEARLTEVGL---AERKDHRPAGLSGGQQQRV 411
Cdd:COG0444 82 kirgREIQMIFQDpmtsLN--PVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLpdpERRLDRYPHELSGGMRQRV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 412 AIARALAMDPEVILFDEVTSALDPELVKGVLDLMANLGRQ-GMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQIF 490
Cdd:COG0444 160 MIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEELF 239
|
....
gi 2017776620 491 DNPQ 494
Cdd:COG0444 240 ENPR 243
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
269-500 |
2.30e-59 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 196.08 E-value: 2.30e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 269 ALRVRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESilamkPESLRRRVGMV 348
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKP-----PRRARRRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 349 FQHFNL---FPdHTALENVMLSLTK---IKKMPRSEARGIAEARLTEVGLAERKDHRPAGLSGGQQQRVAIARALAMDPE 422
Cdd:COG1121 81 PQRAEVdwdFP-ITVRDVVLMGRYGrrgLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPD 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2017776620 423 VILFDEVTSALDPELVKGVLDLMANLGRQGMTMAVVTHEMGFARRVADQVVFMDeGRIIEAGSPQQIFDnpqSERLKR 500
Cdd:COG1121 160 LLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLN-RGLVAHGPPEEVLT---PENLSR 233
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
285-505 |
2.77e-59 |
|
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: 199.69 E-value: 2.77e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 285 LKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPESL----RRRVGMVFQHFNLFPDHTA 360
Cdd:TIGR01186 9 VNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPVELrevrRKKIGMVFQQFALFPHMTI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 361 LENVMLSLtKIKKMPRSEARGIAEARLTEVGLAERKDHRPAGLSGGQQQRVAIARALAMDPEVILFDEVTSALDP----E 436
Cdd:TIGR01186 89 LQNTSLGP-ELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSALDPlirdS 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2017776620 437 LVKGVLDLMANLGRqgmTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQIFDNPQSERLKRFLAEV 505
Cdd:TIGR01186 168 MQDELKKLQATLQK---TIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIGKV 233
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
270-480 |
4.55e-59 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 193.88 E-value: 4.55e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPESLRRRVGMVF 349
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 350 QHFNLFPDhTALENVMLSLTKIKKMPRSEArgiAEARLTEVGLAER-KDHRPAGLSGGQQQRVAIARALAMDPEVILFDE 428
Cdd:COG4619 81 QEPALWGG-TVRDNLPFPFQLRERKFDRER---ALELLERLGLPPDiLDKPVERLSGGERQRLALIRALLLQPDVLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2017776620 429 VTSALDPELVKGVLDLMANL-GRQGMTMAVVTHEMGFARRVADQVVFMDEGRI 480
Cdd:COG4619 157 PTSALDPENTRRVEELLREYlAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
270-502 |
2.36e-57 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 190.35 E-value: 2.36e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAYGDLdvLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPEslRRRVGMVF 349
Cdd:COG3840 2 LRLDDLTYRYGDF--PLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPA--ERPVSMLF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 350 QHFNLFPDHTALENVMLSLTKIKKMPRSEARGIAEArLTEVGLAERKDHRPAGLSGGQQQRVAIARALAMDPEVILFDEV 429
Cdd:COG3840 78 QENNLFPHLTVAQNIGLGLRPGLKLTAEQRAQVEQA-LERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2017776620 430 TSALDPELVKGVLDLMANLGR-QGMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQIFDNPQSERLKRFL 502
Cdd:COG3840 157 FSALDPALRQEMLDLVDELCReRGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYL 230
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
270-504 |
5.28e-56 |
|
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: 188.43 E-value: 5.28e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAYG-----DLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPES---L 341
Cdd:TIGR04521 1 IKLKNVSYIYQpgtpfEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKlkdL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 342 RRRVGMVFQhfnlFPDH-----TALENVM---LSLtkikKMPRSEARGIAEARLTEVGLAER-KDHRPAGLSGGQQQRVA 412
Cdd:TIGR04521 81 RKKVGLVFQ----FPEHqlfeeTVYKDIAfgpKNL----GLSEEEAEERVKEALELVGLDEEyLERSPFELSGGQMRRVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 413 IARALAMDPEVILFDEVTSALDPELVKGVLDLMANLGRQ-GMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQIFD 491
Cdd:TIGR04521 153 IAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEkGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFS 232
|
250 260
....*....|....*....|....
gi 2017776620 492 N-----------PQSERLKRFLAE 504
Cdd:TIGR04521 233 DvdelekigldvPEITELARKLKE 256
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
270-502 |
5.40e-56 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 186.99 E-value: 5.40e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESIlAMKPESLRRRVGMVF 349
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDV-RKEPREARRQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 350 QHFNLFPDHTALENVMLsLTKIKKMPRSEARGIAEARLTEVGLAERKDHRPAGLSGGQQQRVAIARALAMDPEVILFDEV 429
Cdd:COG4555 81 DERGLYDRLTVRENIRY-FAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2017776620 430 TSALDPELVKGVLDLMANLGRQGMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQIFDNPQSERLKRFL 502
Cdd:COG4555 160 TNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGEENLEDAF 232
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
270-503 |
1.86e-55 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 185.57 E-value: 1.86e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPESLRRR-VGMV 348
Cdd:COG0410 4 LEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLgIGYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 349 FQHFNLFPDHTALENVMLSLtkikkMPRSEARGIAEaRLTEVG-----LAERKdHRPAG-LSGGQQQRVAIARALAMDPE 422
Cdd:COG0410 84 PEGRRIFPSLTVEENLLLGA-----YARRDRAEVRA-DLERVYelfprLKERR-RQRAGtLSGGEQQMLAIGRALMSRPK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 423 VILFDEVTSALDPELVKGVLDLMANLGRQGMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQIFDNPqsERLKRFL 502
Cdd:COG0410 157 LLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADP--EVREAYL 234
|
.
gi 2017776620 503 A 503
Cdd:COG0410 235 G 235
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
270-492 |
2.05e-55 |
|
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: 184.95 E-value: 2.05e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPESLRRR-VGMV 348
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAgIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 349 FQHFNLFPDHTALENVMLSLTKIKKMPRSEARGIAEARLTEvgLAERKdHRPAG-LSGGQQQRVAIARALAMDPEVILFD 427
Cdd:cd03224 81 PEGRRIFPELTVEENLLLGAYARRRAKRKARLERVYELFPR--LKERR-KQLAGtLSGGEQQMLAIARALMSRPKLLLLD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2017776620 428 EVTSALDPELVKGVLDLMANLGRQGMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQIFDN 492
Cdd:cd03224 158 EPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
271-484 |
9.68e-55 |
|
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: 181.48 E-value: 9.68e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 271 RVRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPESLRRRVGMVFQ 350
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 351 hfnlfpdhtALENVmlsltkikkmprsearGIAEarltevgLAERKDHRpagLSGGQQQRVAIARALAMDPEVILFDEVT 430
Cdd:cd03214 81 ---------ALELL----------------GLAH-------LADRPFNE---LSGGERQRVLLARALAQEPPILLLDEPT 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2017776620 431 SALDPELVKGVLDLMANLGRQ-GMTMAVVTHEMGFARRVADQVVFMDEGRIIEAG 484
Cdd:cd03214 126 SHLDIAHQIELLELLRRLARErGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
270-502 |
1.72e-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: 182.92 E-value: 1.72e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAYGDLdVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPEslRRRVGMVF 349
Cdd:cd03299 1 LKVENLSKDWKEF-KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 350 QHFNLFPDHTALENVMLSLtKIKKMPRSE----ARGIAEArlteVGLAERKDHRPAGLSGGQQQRVAIARALAMDPEVIL 425
Cdd:cd03299 78 QNYALFPHMTVYKNIAYGL-KKRKVDKKEierkVLEIAEM----LGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2017776620 426 FDEVTSALDPELVKGVLDLMANLGRQ-GMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQIFDNPQSERLKRFL 502
Cdd:cd03299 153 LDEPFSALDVRTKEKLREELKKIRKEfGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFL 230
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
269-504 |
1.88e-54 |
|
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: 182.92 E-value: 1.88e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 269 ALRVRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPEslRRRVGMV 348
Cdd:cd03296 2 SIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 349 FQHFNLFPDHTALENVMLSLtKIKKM----PRSEARGIAEARLTEVGLAERKDHRPAGLSGGQQQRVAIARALAMDPEVI 424
Cdd:cd03296 80 FQHYALFRHMTVFDNVAFGL-RVKPRserpPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 425 LFDEVTSALDPELVKGVLDLMANL-GRQGMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQIFDNPQSERLKRFLA 503
Cdd:cd03296 159 LLDEPFGALDAKVRKELRRWLRRLhDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSFLG 238
|
.
gi 2017776620 504 E 504
Cdd:cd03296 239 E 239
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
270-494 |
8.23e-54 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 181.90 E-value: 8.23e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRL--VEPK---RGDILLDGESILAMKPES--LR 342
Cdd:PRK14239 6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndLNPEvtiTGSIVYNGHNIYSPRTDTvdLR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 343 RRVGMVFQHFNLFPdHTALENVM--LSLTKIKKMPRSEArgIAEARLTEVGL-AERKD--HRPA-GLSGGQQQRVAIARA 416
Cdd:PRK14239 86 KEIGMVFQQPNPFP-MSIYENVVygLRLKGIKDKQVLDE--AVEKSLKGASIwDEVKDrlHDSAlGLSGGQQQRVCIARV 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2017776620 417 LAMDPEVILFDEVTSALDPELVKGVLDLMANLgRQGMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQIFDNPQ 494
Cdd:PRK14239 163 LATSPKIILLDEPTSALDPISAGKIEETLLGL-KDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPK 239
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
270-479 |
6.81e-53 |
|
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: 176.42 E-value: 6.81e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAYGDLD--VLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPESLRRRVGM 347
Cdd:cd03228 1 IEFKNVSFSYPGRPkpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 348 VFQHFNLFPDhTALENVmlsltkikkmprseargiaearltevglaerkdhrpagLSGGQQQRVAIARALAMDPEVILFD 427
Cdd:cd03228 81 VPQDPFLFSG-TIRENI--------------------------------------LSGGQRQRIAIARALLRDPPILILD 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2017776620 428 EVTSALDPELVKGVLDLMANLgRQGMTMAVVTHEMGFARRvADQVVFMDEGR 479
Cdd:cd03228 122 EATSALDPETEALILEALRAL-AKGKTVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
268-489 |
4.24e-52 |
|
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: 188.12 E-value: 4.24e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 268 GALRVRDLSMAYGDLD--VLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPESLRRRV 345
Cdd:COG2274 472 GDIELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQI 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 346 GMVFQHFNLFPDhTALENVMLSLTKIkkmprSEARGIAEARLteVGLAERKDHRPAG-----------LSGGQQQRVAIA 414
Cdd:COG2274 552 GVVLQDVFLFSG-TIRENITLGDPDA-----TDEEIIEAARL--AGLHDFIEALPMGydtvvgeggsnLSGGQRQRLAIA 623
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2017776620 415 RALAMDPEVILFDEVTSALDPELVKGVLDLMANLgRQGMTMAVVTHEMGFARRvADQVVFMDEGRIIEAGSPQQI 489
Cdd:COG2274 624 RALLRNPRILILDEATSALDAETEAIILENLRRL-LKGRTVIIIAHRLSTIRL-ADRIIVLDKGRIVEDGTHEEL 696
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
269-506 |
6.72e-52 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 176.96 E-value: 6.72e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 269 ALRVRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPK-----RGDILLDGESILA--MKPESL 341
Cdd:PRK14267 4 AIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIYSpdVDPIEV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 342 RRRVGMVFQHFNLFPDHTALENVMLSLtKIKKM--PRSEARGIAEARLTEVGLAE----RKDHRPAGLSGGQQQRVAIAR 415
Cdd:PRK14267 84 RREVGMVFQYPNPFPHLTIYDNVAIGV-KLNGLvkSKKELDERVEWALKKAALWDevkdRLNDYPSNLSGGQRQRLVIAR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 416 ALAMDPEVILFDEVTSALDPELVKGVLDLMANLgRQGMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQIFDNPQS 495
Cdd:PRK14267 163 ALAMKPKILLMDEPTANIDPVGTAKIEELLFEL-KKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEH 241
|
250
....*....|.
gi 2017776620 496 ERLKRFLAEVL 506
Cdd:PRK14267 242 ELTEKYVTGAL 252
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
270-505 |
7.65e-52 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 180.53 E-value: 7.65e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPEslRRRVGMVF 349
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--NRHVNTVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 350 QHFNLFPDHTALENVMLSLtKIKKMPRSE-ARGIAEArLTEVGLAERKDHRPAGLSGGQQQRVAIARALAMDPEVILFDE 428
Cdd:PRK09452 93 QSYALFPHMTVFENVAFGL-RMQKTPAAEiTPRVMEA-LRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2017776620 429 VTSALDPELVKGVLDLMANLGRQ-GMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQIFDNPQSERLKRFLAEV 505
Cdd:PRK09452 171 SLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFIGEI 248
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
270-480 |
1.76e-51 |
|
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: 172.97 E-value: 1.76e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAmKPESLRRRVGMVF 349
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 350 QHFNLFPDHTALENVMlsltkikkmprseargiaearltevglaerkdhrpagLSGGQQQRVAIARALAMDPEVILFDEV 429
Cdd:cd03230 80 EEPSLYENLTVRENLK-------------------------------------LSGGMKQRLALAQALLHDPELLILDEP 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2017776620 430 TSALDPELVKGVLDLMANLGRQGMTMAVVTHEMGFARRVADQVVFMDEGRI 480
Cdd:cd03230 123 TSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
270-503 |
1.25e-50 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 181.04 E-value: 1.25e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAYGDLD----VLKGVDLDIAPGTVTCIIGPSGSGKS----TLLRCLNRLVEPKRGDILLDGESILAMKPESL 341
Cdd:COG4172 7 LSVEDLSVAFGQGGgtveAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSEREL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 342 RR----RVGMVFQH----FNlfPDHTALENVMLSLTKIKKMPRSEARGIAEARLTEVGLAE---RKDHRPAGLSGGQQQR 410
Cdd:COG4172 87 RRirgnRIAMIFQEpmtsLN--PLHTIGKQIAEVLRLHRGLSGAAARARALELLERVGIPDperRLDAYPHQLSGGQRQR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 411 VAIARALAMDPEVILFDEVTSALDPELVKGVLDLMANLGRQ-GMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQI 489
Cdd:COG4172 165 VMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRElGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAEL 244
|
250
....*....|....
gi 2017776620 490 FDNPQSERLKRFLA 503
Cdd:COG4172 245 FAAPQHPYTRKLLA 258
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
267-503 |
2.12e-50 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 173.74 E-value: 2.12e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 267 AGALRVRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEP-----KRGDILLDGESILAMKPE-S 340
Cdd:PRK14271 19 APAMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIFNYRDVlE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 341 LRRRVGMVFQHFNLFPdHTALENVMLSLTKIKKMPRSEARGIAEARLTEVGL----AERKDHRPAGLSGGQQQRVAIARA 416
Cdd:PRK14271 99 FRRRVGMLFQRPNPFP-MSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLwdavKDRLSDSPFRLSGGQQQLLCLART 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 417 LAMDPEVILFDEVTSALDPELVKGVLDLMANLGRQgMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQIFDNPQSE 496
Cdd:PRK14271 178 LAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHA 256
|
....*..
gi 2017776620 497 RLKRFLA 503
Cdd:PRK14271 257 ETARYVA 263
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
285-494 |
2.77e-50 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 173.67 E-value: 2.77e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 285 LKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPE----SLRRRVGMVFQhfnlFPDHTA 360
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNkklkPLRKKVGIVFQ----FPEHQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 361 LENvmlslTKIKK---------MPRSEARGIAEARLTEVGLAER-KDHRPAGLSGGQQQRVAIARALAMDPEVILFDEVT 430
Cdd:PRK13634 99 FEE-----TVEKDicfgpmnfgVSEEDAKQKAREMIELVGLPEElLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPT 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2017776620 431 SALDPELVKGVLDLMANLGR-QGMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQIFDNPQ 494
Cdd:PRK13634 174 AGLDPKGRKEMMEMFYKLHKeKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
269-494 |
2.96e-50 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 172.87 E-value: 2.96e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 269 ALRVRDLSMAYGDLD--VLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPESLRRRVG 346
Cdd:PRK13632 7 MIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 347 MVFQH-FNLFPDHTALENVMLSLTKiKKMPRSEARGIAEARLTEVGLAERKDHRPAGLSGGQQQRVAIARALAMDPEVIL 425
Cdd:PRK13632 87 IIFQNpDNQFIGATVEDDIAFGLEN-KKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIII 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 426 FDEVTSALDPELVKGVLDLMANLGRQGM-TMAVVTHEMGFARRvADQVVFMDEGRIIEAGSPQQIFDNPQ 494
Cdd:PRK13632 166 FDESTSMLDPKGKREIKKIMVDLRKTRKkTLISITHDMDEAIL-ADKVIVFSEGKLIAQGKPKEILNNKE 234
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
271-484 |
3.93e-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: 170.79 E-value: 3.93e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 271 RVRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGEsilamKPESLRRRVGMVFQ 350
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGK-----PLEKERKRIGYVPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 351 HFNL---FPdHTALENVMLSLTK----IKKMPRSEARGIAEArLTEVGLAERKDHRPAGLSGGQQQRVAIARALAMDPEV 423
Cdd:cd03235 76 RRSIdrdFP-ISVRDVVLMGLYGhkglFRRLSKADKAKVDEA-LERVGLSELADRQIGELSGGQQQRVLLARALVQDPDL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2017776620 424 ILFDEVTSALDPELVKGVLDLMANLGRQGMTMAVVTHEMGFARRVADQVVFMDeGRIIEAG 484
Cdd:cd03235 154 LLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLN-RTVVASG 213
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
197-488 |
4.98e-50 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 180.36 E-value: 4.98e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 197 VVTGNLSP-LLLAGVFYLL-ITVPLTHFVNYIDArLRlgrqgRGSGAASGLVEVgeLRAASSTAVGNEPR---FKAGALR 271
Cdd:COG1132 270 VLSGSLTVgDLVAFILYLLrLFGPLRQLANVLNQ-LQ-----RALASAERIFEL--LDEPPEIPDPPGAVplpPVRGEIE 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 272 VRDLSMAY-GDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPESLRRRVGMVFQ 350
Cdd:COG1132 342 FENVSFSYpGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQ 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 351 HFNLFPDhTALENVMLSltkikKMPRSEARGIAEARL---------------TEVGlaerkdHRPAGLSGGQQQRVAIAR 415
Cdd:COG1132 422 DTFLFSG-TIRENIRYG-----RPDATDEEVEEAAKAaqahefiealpdgydTVVG------ERGVNLSGGQRQRIAIAR 489
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2017776620 416 ALAMDPEVILFDEVTSALDPELVKGVLDLMANLgRQGMTMAVVTHEMGFARRvADQVVFMDEGRIIEAGSPQQ 488
Cdd:COG1132 490 ALLKDPPILILDEATSALDTETEALIQEALERL-MKGRTTIVIAHRLSTIRN-ADRILVLDDGRIVEQGTHEE 560
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
271-479 |
7.70e-50 |
|
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: 167.81 E-value: 7.70e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 271 RVRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPESLRRRVGMVFQ 350
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 351 hfnlfpdhtalenvmlsltkikkmprseargiaearltevglaerkdhrpagLSGGQQQRVAIARALAMDPEVILFDEVT 430
Cdd:cd00267 81 ----------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPT 108
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2017776620 431 SALDPELVKGVLDLMANLGRQGMTMAVVTHEMGFARRVADQVVFMDEGR 479
Cdd:cd00267 109 SGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
300-505 |
1.04e-48 |
|
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: 170.75 E-value: 1.04e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 300 IIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPEslRRRVGMVFQHFNLFPDHTALENVMLSLtKIKKMPRSEA 379
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPH--LRHINMVFQSYALFPHMTVEENVAFGL-KMRKVPRAEI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 380 RGIAEARLTEVGLAERKDHRPAGLSGGQQQRVAIARALAMDPEVILFDEVTSALDPELVKGV-LDLMANLGRQGMTMAVV 458
Cdd:TIGR01187 78 KPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMqLELKTIQEQLGITFVFV 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2017776620 459 THEMGFARRVADQVVFMDEGRIIEAGSPQQIFDNPQSERLKRFLAEV 505
Cdd:TIGR01187 158 THDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEI 204
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
195-488 |
1.86e-48 |
|
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: 175.72 E-value: 1.86e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 195 QAVVTGNLSPLLLAGVFylLITVPLT-HFVNYIDARLRLGRQGRgsgAASGLVEVGELRAASSTAVGNEPRFKAGALRVR 273
Cdd:COG4987 263 PLVAAGALSGPLLALLV--LAALALFeALAPLPAAAQHLGRVRA---AARRLNELLDAPPAVTEPAEPAPAPGGPSLELE 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 274 DLSMAY--GDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPESLRRRVGMVFQH 351
Cdd:COG4987 338 DVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQR 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 352 FNLFpDHTALENVMLsltkikkmprseARGIA-EARLTE----VGLAERKDHRPAGL-----------SGGQQQRVAIAR 415
Cdd:COG4987 418 PHLF-DTTLRENLRL------------ARPDAtDEELWAalerVGLGDWLAALPDGLdtwlgeggrrlSGGERRRLALAR 484
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2017776620 416 ALAMDPEVILFDEVTSALDPELVKGVLDLMANLGrQGMTMAVVTHEMGFARRvADQVVFMDEGRIIEAGSPQQ 488
Cdd:COG4987 485 ALLRDAPILLLDEPTEGLDAATEQALLADLLEAL-AGRTVLLITHRLAGLER-MDRILVLEDGRIVEQGTHEE 555
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
270-500 |
2.50e-48 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 167.21 E-value: 2.50e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPESLRRRVGMVF 349
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 350 QHFNL-FPdHTALENVMLSLTkIKKMPRSEARGIAEARLTEVGLAERKDHRPAGLSGGQQQRVAIARALA-------MDP 421
Cdd:COG4559 82 QHSSLaFP-FTVEEVVALGRA-PHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepvdGGP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2017776620 422 EVILFDEVTSALDPELVKGVLDLMANLGRQGMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQIFdnpQSERLKR 500
Cdd:COG4559 160 RWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVL---TDELLER 235
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
270-496 |
6.03e-48 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 166.50 E-value: 6.03e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNR---LVEPKR--GDILLDGESILA--MKPESLR 342
Cdd:PRK14243 11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRlndLIPGFRveGKVTFHGKNLYApdVDPVEVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 343 RRVGMVFQHFNLFPDhTALENVMLSlTKIKKMpRSEARGIAEARLTEVGL-AERKDH-RPAG--LSGGQQQRVAIARALA 418
Cdd:PRK14243 91 RRIGMVFQKPNPFPK-SIYDNIAYG-ARINGY-KGDMDELVERSLRQAALwDEVKDKlKQSGlsLSGGQQQRLCIARAIA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 419 MDPEVILFDEVTSALDPELVKGVLDLMANLGRQgMTMAVVTHEMGFARRVADQVVFMD---------EGRIIEAGSPQQI 489
Cdd:PRK14243 168 VQPEVILMDEPCSALDPISTLRIEELMHELKEQ-YTIIIVTHNMQQAARVSDMTAFFNveltegggrYGYLVEFDRTEKI 246
|
....*..
gi 2017776620 490 FDNPQSE 496
Cdd:PRK14243 247 FNSPQQQ 253
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
205-488 |
1.72e-47 |
|
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: 173.02 E-value: 1.72e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 205 LLLAGVFYLlitvPLTHFVNYIDARLRlgrqgrGSGAASGLVEVGELRA-ASSTAVGNEPRFKAGALRVRDLSMAYGD-L 282
Cdd:COG4988 281 LLLAPEFFL----PLRDLGSFYHARAN------GIAAAEKIFALLDAPEpAAPAGTAPLPAAGPPSIELEDVSFSYPGgR 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 283 DVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPESLRRRVGMVFQHFNLFPDhTALE 362
Cdd:COG4988 351 PALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAG-TIRE 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 363 NVMLSLTKIkkmprSEA---RGIAEARLTEV------GLAERKDHRPAGLSGGQQQRVAIARALAMDPEVILFDEVTSAL 433
Cdd:COG4988 430 NLRLGRPDA-----SDEeleAALEAAGLDEFvaalpdGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHL 504
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2017776620 434 DPELVKGVLDLMANLgRQGMTMAVVTHEMGFARRvADQVVFMDEGRIIEAGSPQQ 488
Cdd:COG4988 505 DAETEAEILQALRRL-AKGRTVILITHRLALLAQ-ADRILVLDDGRIVEQGTHEE 557
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
270-503 |
3.09e-47 |
|
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: 171.79 E-value: 3.09e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAY-----------GDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVePKRGDILLDGESILAMKP 338
Cdd:COG4172 276 LEARDLKVWFpikrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 339 E---SLRRRVGMVFQ----HFNlfPDHTALENVM--LSLTKIKkMPRSEARGIAEARLTEVGLAERKDHR-PAGLSGGQQ 408
Cdd:COG4172 355 RalrPLRRRMQVVFQdpfgSLS--PRMTVGQIIAegLRVHGPG-LSAAERRARVAEALEEVGLDPAARHRyPHEFSGGQR 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 409 QRVAIARALAMDPEVILFDEVTSALDPELVKGVLDLMANL-GRQGMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQ 487
Cdd:COG4172 432 QRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLqREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTE 511
|
250
....*....|....*.
gi 2017776620 488 QIFDNPQSERLKRFLA 503
Cdd:COG4172 512 QVFDAPQHPYTRALLA 527
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
270-504 |
1.14e-46 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 163.65 E-value: 1.14e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAYGDLD--VLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGesiLAMKPES---LRRR 344
Cdd:PRK13635 6 IRVEHISFRYPDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGG---MVLSEETvwdVRRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 345 VGMVFQH-FNLFPDHTALENVMLSLTKIKkMPRSEARGIAEARLTEVGLAERKDHRPAGLSGGQQQRVAIARALAMDPEV 423
Cdd:PRK13635 83 VGMVFQNpDNQFVGATVQDDVAFGLENIG-VPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 424 ILFDEVTSALDPELVKGVLDLMANLGRQGM-TMAVVTHEMGFARRvADQVVFMDEGRIIEAGSPQQIF-----------D 491
Cdd:PRK13635 162 IILDEATSMLDPRGRREVLETVRQLKEQKGiTVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFksghmlqeiglD 240
|
250
....*....|...
gi 2017776620 492 NPQSERLKRFLAE 504
Cdd:PRK13635 241 VPFSVKLKELLKR 253
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
270-484 |
1.59e-45 |
|
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: 158.57 E-value: 1.59e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPEslRRRVGMVF 349
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK--DRDIAMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 350 QHFNLFPDHTALENVMLSLtKIKKMPRSEargiAEARLTEV----GLAERKDHRPAGLSGGQQQRVAIARALAMDPEVIL 425
Cdd:cd03301 79 QNYALYPHMTVYDNIAFGL-KLRKVPKDE----IDERVREVaellQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 426 FDEVTSALDPEL-VKGVLDLMANLGRQGMTMAVVTHEMGFARRVADQVVFMDEGRIIEAG 484
Cdd:cd03301 154 MDEPLSNLDAKLrVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
270-494 |
2.06e-45 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 161.82 E-value: 2.06e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAY-----------GDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKP 338
Cdd:COG4608 8 LEVRDLKKHFpvrgglfgrtvGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 339 ESL---RRRVGMVFQ--HFNLFPDHTALENVMLSLTKIKKMPRSEARGIAEARLTEVGL-AERKDHRPAGLSGGQQQRVA 412
Cdd:COG4608 88 RELrplRRRMQMVFQdpYASLNPRMTVGDIIAEPLRIHGLASKAERRERVAELLELVGLrPEHADRYPHEFSGGQRQRIG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 413 IARALAMDPEVILFDEVTSALDPELVKGVLDLMANLGRQ-GMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQIFD 491
Cdd:COG4608 168 IARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDElGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPRDELYA 247
|
...
gi 2017776620 492 NPQ 494
Cdd:COG4608 248 RPL 250
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
269-502 |
2.67e-45 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 159.43 E-value: 2.67e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 269 ALRVRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPK-----RGDILLDGESILAMKP--ESL 341
Cdd:PRK14258 7 AIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELEsevrvEGRVEFFNQNIYERRVnlNRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 342 RRRVGMVFQHFNLFPdHTALENVMLSLTKIKKMPRSEARGIAEARLTEVGL---AERKDHRPA-GLSGGQQQRVAIARAL 417
Cdd:PRK14258 87 RRQVSMVHPKPNLFP-MSVYDNVAYGVKIVGWRPKLEIDDIVESALKDADLwdeIKHKIHKSAlDLSGGQQQRLCIARAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 418 AMDPEVILFDEVTSALDPELVKGVLDLMANLG-RQGMTMAVVTHEMGFARRVADQVVFM--DEGRI---IEAGSPQQIFD 491
Cdd:PRK14258 166 AVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlRSELTMVIVSHNLHQVSRLSDFTAFFkgNENRIgqlVEFGLTKKIFN 245
|
250
....*....|.
gi 2017776620 492 NPQSERLKRFL 502
Cdd:PRK14258 246 SPHDSRTREYV 256
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
271-481 |
3.20e-45 |
|
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: 157.42 E-value: 3.20e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 271 RVRDLSMAYGDL-DVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESIlamKPESLRRRVGMVF 349
Cdd:cd03226 1 RIENISFSYKKGtEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI---KAKERRKSIGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 350 QH--FNLFPDhTALENVMLSLtkikkMPRSEARGIAEARLTEVGLAERKDHRPAGLSGGQQQRVAIARALAMDPEVILFD 427
Cdd:cd03226 78 QDvdYQLFTD-SVREELLLGL-----KELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2017776620 428 EVTSALDPELVKGVLDLMANLGRQGMTMAVVTHEMGFARRVADQVVFMDEGRII 481
Cdd:cd03226 152 EPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
285-431 |
4.07e-45 |
|
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: 155.11 E-value: 4.07e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 285 LKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPESLRRRVGMVFQHFNLFPDHTALENV 364
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2017776620 365 MLSLTkIKKMPRSEARGIAEARLTEVGLAERKDHR----PAGLSGGQQQRVAIARALAMDPEVILFDEVTS 431
Cdd:pfam00005 81 RLGLL-LKGLSKREKDARAEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
270-493 |
4.54e-45 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 160.79 E-value: 4.54e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAYGD-----LDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDI----LLDGESILAMKP-- 338
Cdd:PRK13631 22 LRVKNLYCVFDEkqeneLVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdIYIGDKKNNHELit 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 339 ----------ESLRRRVGMVFQ--HFNLFPDhTALENVMLSLTKIKkMPRSEARGIAEARLTEVGLAER-KDHRPAGLSG 405
Cdd:PRK13631 102 npyskkiknfKELRRRVSMVFQfpEYQLFKD-TIEKDIMFGPVALG-VKKSEAKKLAKFYLNKMGLDDSyLERSPFGLSG 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 406 GQQQRVAIARALAMDPEVILFDEVTSALDPELVKGVLDLMANLGRQGMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGS 485
Cdd:PRK13631 180 GQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGT 259
|
....*...
gi 2017776620 486 PQQIFDNP 493
Cdd:PRK13631 260 PYEIFTDQ 267
|
|
| ArtM |
COG4160 |
ABC-type arginine/histidine transport system, permease component [Amino acid transport and ... |
12-230 |
7.00e-45 |
|
ABC-type arginine/histidine transport system, permease component [Amino acid transport and metabolism];
Pssm-ID: 443325 [Multi-domain] Cd Length: 229 Bit Score: 157.18 E-value: 7.00e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 12 LDWDAMAEVLPSMITvGLKNTLILAAASTVLGVIIGMVLAVMGISQSRWLRLPARIYTDIFRGLPAIVTILIIGQGFARI 91
Cdd:COG4160 1 MDLDLLFEYLPLLLS-GLPLTLQLLALSLLLGFLLAVPLALARASGNRLLRWPARGYIYVFRGTPLLVQLFLIYYGLGQF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 92 G--RE-----LFGpSPFPLGIIALSLIAGAYIGEIFRSGIQSVERGQMEACRALSMSYGQGMRLIVIPQGVRRVLPALVN 164
Cdd:COG4160 80 EwvREswlwpLLR-DPWFCALLALTLNTAAYTAEIFRGAIRAVPKGEIEAARALGMSRWQTFRRIILPSALRRALPAYSN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2017776620 165 QFIGNVKDSSLVYFLGLLaserEIFRVGQDQAVVTGN-LSPLLLAGVFYLLITVPLTHFVNYIDARL 230
Cdd:COG4160 159 EVILMLKATALASTITVM----DLTGVARRIYSRTYDpFEPFLIAALIYLVITFLLTRLFRLLERRL 221
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
270-503 |
1.32e-44 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 156.53 E-value: 1.32e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPESLRRR-VGMV 348
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAgIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 349 FQHFNLFPDHTALENVMLSLTKIkkmPRSEARGIAEA-RLTEVgLAERKdHRPAG-LSGGQQQRVAIARALAMDPEVILF 426
Cdd:TIGR03410 81 PQGREIFPRLTVEENLLTGLAAL---PRRSRKIPDEIyELFPV-LKEML-GRRGGdLSGGQQQQLAIARALVTRPKLLLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 427 DEVTSALDPELVK---GVLDLMANLGrqGMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPqqifDNPQSERLKRFLA 503
Cdd:TIGR03410 156 DEPTEGIQPSIIKdigRVIRRLRAEG--GMAILLVEQYLDFARELADRYYVMERGRVVASGAG----DELDEDKVRRYLA 229
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
274-498 |
1.34e-44 |
|
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: 160.27 E-value: 1.34e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 274 DLSMAYGDLDVlkGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDI------LLDGESILAMKPEslRRRVGM 347
Cdd:COG4148 6 DFRLRRGGFTL--DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIrlggevLQDSARGIFLPPH--RRRIGY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 348 VFQHFNLFPDHTALENVMLSLtkiKKMPRSEaRGIAEARLTEV-GLAERKDHRPAGLSGGQQQRVAIARALAMDPEVILF 426
Cdd:COG4148 82 VFQEARLFPHLSVRGNLLYGR---KRAPRAE-RRISFDEVVELlGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLM 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2017776620 427 DEVTSALDPELVKGVLDLMANLGRQ-GMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQIFDNPQSERL 498
Cdd:COG4148 158 DEPLAALDLARKAEILPYLERLRDElDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDLLPL 230
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
270-489 |
1.53e-44 |
|
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: 156.13 E-value: 1.53e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAYGDLD--VLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILaMKPESLRRRVGM 347
Cdd:cd03263 1 LQIRNLTKTYKKGTkpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIR-TDRKAARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 348 VFQHFNLFPDHTALENVMLSlTKIKKMPRSEARGIAEARLTEVGLAERKDHRPAGLSGGQQQRVAIARALAMDPEVILFD 427
Cdd:cd03263 80 CPQFDALFDELTVREHLRFY-ARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2017776620 428 EVTSALDPELVKGVLDLMANLgRQGMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQI 489
Cdd:cd03263 159 EPTSGLDPASRRAIWDLILEV-RKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
270-484 |
2.16e-44 |
|
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: 155.34 E-value: 2.16e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAYGDLDVlkGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPEslRRRVGMVF 349
Cdd:cd03298 1 VRLDKIRFSYGEQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVSMLF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 350 QHFNLFPDHTALENVMLSLTKIKKMpRSEARGIAEARLTEVGLAERKDHRPAGLSGGQQQRVAIARALAMDPEVILFDEV 429
Cdd:cd03298 77 QENNLFAHLTVEQNVGLGLSPGLKL-TAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2017776620 430 TSALDPELVKGVLDLMANLGRQ-GMTMAVVTHEMGFARRVADQVVFMDEGRIIEAG 484
Cdd:cd03298 156 FAALDPALRAEMLDLVLDLHAEtKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
269-500 |
2.72e-44 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 156.47 E-value: 2.72e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 269 ALRVRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPESLRRRVGMV 348
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 349 FQHFNL-FPdHTALENVMLSLtkikkMPRS----EARGIAEARLTEVGLAERKDHRPAGLSGGQQQRVAIARALA----- 418
Cdd:PRK13548 82 PQHSSLsFP-FTVEEVVAMGR-----APHGlsraEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwep 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 419 -MDPEVILFDEVTSALDPELVKGVLDLMANL-GRQGMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQIFdnpQSE 496
Cdd:PRK13548 156 dGPPRWLLLDEPTSALDLAHQHHVLRLARQLaHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVL---TPE 232
|
....
gi 2017776620 497 RLKR 500
Cdd:PRK13548 233 TLRR 236
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
283-476 |
5.23e-44 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 155.36 E-value: 5.23e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 283 DVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAM----KPESLRRRVGMVFQHFNLFPDH 358
Cdd:PRK11629 23 DVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLssaaKAELRNQKLGFIYQFHHLLPDF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 359 TALENVMLSLTkIKKMPRSEARGIAEARLTEVGLAERKDHRPAGLSGGQQQRVAIARALAMDPEVILFDEVTSALDPELV 438
Cdd:PRK11629 103 TALENVAMPLL-IGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNA 181
|
170 180 190
....*....|....*....|....*....|....*....
gi 2017776620 439 KGVLDLMANLG-RQGMTMAVVTHEMGFARRVADQVVFMD 476
Cdd:PRK11629 182 DSIFQLLGELNrLQGTAFLVVTHDLQLAKRMSRQLEMRD 220
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
269-482 |
2.96e-43 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 153.86 E-value: 2.96e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 269 ALRVRDLSMAYGDLD----VLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESIlaMKPESLRrr 344
Cdd:COG4525 3 MLTVRHVSVRYPGGGqpqpALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPV--TGPGADR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 345 vGMVFQHFNLFPDHTALENVMLSLtKIKKMPRSEARGIAEARLTEVGLAERKDHRPAGLSGGQQQRVAIARALAMDPEVI 424
Cdd:COG4525 79 -GVVFQKDALLPWLNVLDNVAFGL-RLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2017776620 425 LFDEVTSALDP-------ELvkgVLDLMAnlgRQGMTMAVVTHEMGFARRVADQVVFMD--EGRIIE 482
Cdd:COG4525 157 LMDEPFGALDAltreqmqEL---LLDVWQ---RTGKGVFLITHSVEEALFLATRLVVMSpgPGRIVE 217
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
269-482 |
4.15e-43 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 159.80 E-value: 4.15e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 269 ALRVRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKP-ESLRRRVGM 347
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPrDAQAAGIAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 348 VFQHFNLFPDHTALENVMLS--LTKIKKMPRSEARGIAEARLTEVGLAERKDHRPAGLSGGQQQRVAIARALAMDPEVIL 425
Cdd:COG1129 84 IHQELNLVPNLSVAENIFLGrePRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLI 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2017776620 426 FDEVTSALDPELVKGVLDLMANLGRQGMTMAVVTHEMGFARRVADQVVFMDEGRIIE 482
Cdd:COG1129 164 LDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVG 220
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
268-491 |
4.53e-43 |
|
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: 152.38 E-value: 4.53e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 268 GALRVRDLSMAY-GDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPESLRRRVG 346
Cdd:cd03254 1 GEIEFENVNFSYdEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 347 MVFQHFNLFPDhTALENVMLSltkikkMPRSEARGIAEArLTEVGLAERKDHRPAG-----------LSGGQQQRVAIAR 415
Cdd:cd03254 81 VVLQDTFLFSG-TIMENIRLG------RPNATDEEVIEA-AKEAGAHDFIMKLPNGydtvlgenggnLSQGERQLLAIAR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2017776620 416 ALAMDPEVILFDEVTSALDPELVKGVLDLMANLgRQGMTMAVVTHEMGFARRvADQVVFMDEGRIIEAGSPQQIFD 491
Cdd:cd03254 153 AMLRDPKILILDEATSNIDTETEKLIQEALEKL-MKGRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEGTHDELLA 226
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
270-497 |
6.79e-43 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 153.69 E-value: 6.79e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAYGD-LDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPESL--RRRVG 346
Cdd:PRK13639 2 LETRDLKYSYPDgTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLevRKTVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 347 MVFQHfnlfPDH-----TALENVMLSLTKIKkMPRSEARGIAEARLTEVGLAERKDHRPAGLSGGQQQRVAIARALAMDP 421
Cdd:PRK13639 82 IVFQN----PDDqlfapTVEEDVAFGPLNLG-LSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2017776620 422 EVILFDEVTSALDPELVKGVLDLMANLGRQGMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQIFDNPQSER 497
Cdd:PRK13639 157 EIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIETIR 232
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
285-480 |
9.69e-43 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 151.02 E-value: 9.69e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 285 LKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPES---LRRRVGMVFQHFNLFPDHTAL 361
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipyLRRKIGVVFQDFRLLPDRNVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 362 ENVMLSLTKIKKMPRSEARGIAEArLTEVGLAERKDHRPAGLSGGQQQRVAIARALAMDPEVILFDEVTSALDPELVKGV 441
Cdd:cd03292 97 ENVAFALEVTGVPPREIRKRVPAA-LELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEI 175
|
170 180 190
....*....|....*....|....*....|....*....
gi 2017776620 442 LDLMANLGRQGMTMAVVTHEMGFARRVADQVVFMDEGRI 480
Cdd:cd03292 176 MNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
270-504 |
9.81e-43 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 155.26 E-value: 9.81e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESIlaMKPESLRRRVGMVF 349
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDV--THRSIQQRDICMVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 350 QHFNLFPdHTAL-ENVMLSLtKIKKMPRSEARG-IAEArLTEVGLAERKDHRPAGLSGGQQQRVAIARALAMDPEVILFD 427
Cdd:PRK11432 85 QSYALFP-HMSLgENVGYGL-KMLGVPKEERKQrVKEA-LELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2017776620 428 EVTSALDPELVKGVLDLMANLGRQ-GMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQIFDNPQSERLKRFLAE 504
Cdd:PRK11432 162 EPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASFMGD 239
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
275-505 |
2.51e-42 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 154.09 E-value: 2.51e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 275 LSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPESlrRRVGMVFQHFNL 354
Cdd:PRK10851 8 IKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD--RKVGFVFQHYAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 355 FPDHTALENVMLSLTKIKKMPRSEARGIAE--ARLTE-VGLAERKDHRPAGLSGGQQQRVAIARALAMDPEVILFDEVTS 431
Cdd:PRK10851 86 FRHMTVFDNIAFGLTVLPRRERPNAAAIKAkvTQLLEmVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFG 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2017776620 432 ALDPELVKGVLDLMANLGRQ-GMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQIFDNPQSERLKRFLAEV 505
Cdd:PRK10851 166 ALDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFMGEV 240
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
266-500 |
3.99e-42 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 151.49 E-value: 3.99e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 266 KAGALRVRDLSMAYGDLD--VLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGD---ILLDGESILAMKPES 340
Cdd:PRK13640 2 KDNIVEFKHVSFTYPDSKkpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLTAKTVWD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 341 LRRRVGMVFQH-FNLFPDHTALENVMLSLTKiKKMPRSEARGIAEARLTEVGLAERKDHRPAGLSGGQQQRVAIARALAM 419
Cdd:PRK13640 82 IREKVGIVFQNpDNQFVGATVGDDVAFGLEN-RAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 420 DPEVILFDEVTSALDPELVKGVLDLMANLGRQ-GMTMAVVTHEMGFArRVADQVVFMDEGRIIEAGSPQQIFDNPqsERL 498
Cdd:PRK13640 161 EPKIIILDESTSMLDPAGKEQILKLIRKLKKKnNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKV--EML 237
|
..
gi 2017776620 499 KR 500
Cdd:PRK13640 238 KE 239
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
270-504 |
1.39e-41 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 152.68 E-value: 1.39e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPesLRRRVGMVF 349
Cdd:PRK11607 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPP--YQRPINMMF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 350 QHFNLFPDHTALENVMLSLtKIKKMPRSEARGIAEARLTEVGLAERKDHRPAGLSGGQQQRVAIARALAMDPEVILFDEV 429
Cdd:PRK11607 98 QSYALFPHMTVEQNIAFGL-KQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEP 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2017776620 430 TSALDPELV-KGVLDLMANLGRQGMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQIFDNPQSerlkRFLAE 504
Cdd:PRK11607 177 MGALDKKLRdRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTT----RYSAE 248
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
285-490 |
3.03e-41 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 149.12 E-value: 3.03e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 285 LKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKP----ESLRRRVGMVFQhfnlFP---- 356
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKnkdiKQIRKKVGLVFQ----FPesql 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 357 -DHTALENVMLSLTKIKkMPRSEARGIAEARLTEVGLAER-KDHRPAGLSGGQQQRVAIARALAMDPEVILFDEVTSALD 434
Cdd:PRK13649 99 fEETVLKDVAFGPQNFG-VSQEEAEALAREKLALVGISESlFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2017776620 435 PELVKGVLDLMANLGRQGMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQIF 490
Cdd:PRK13649 178 PKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIF 233
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
270-490 |
5.33e-41 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 147.85 E-value: 5.33e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPESLRRRVGMVF 349
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 350 QHfnlfpdHTALENVmlSLTKIKKMPRS-----------EARGIAEARLTEVGLAERKDHRPAGLSGGQQQRVAIARALA 418
Cdd:PRK11231 83 QH------HLTPEGI--TVRELVAYGRSpwlslwgrlsaEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2017776620 419 MDPEVILFDEVTSALDPELVKGVLDLMANLGRQGMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQIF 490
Cdd:PRK11231 155 QDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVM 226
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
270-488 |
6.21e-41 |
|
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: 146.99 E-value: 6.21e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAYGD-LDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPESLRRRVGMV 348
Cdd:cd03253 1 IEFENVTFAYDPgRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 349 FQHFNLFPDhTALENVM---LSLT---------------KIKKMPrseargiaEARLTEVGlaERkdhrpaG--LSGGQQ 408
Cdd:cd03253 81 PQDTVLFND-TIGYNIRygrPDATdeevieaakaaqihdKIMRFP--------DGYDTIVG--ER------GlkLSGGEK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 409 QRVAIARALAMDPEVILFDEVTSALDPELVKGVLDLMANLGRqGMTMAVVTHemgfarRV-----ADQVVFMDEGRIIEA 483
Cdd:cd03253 144 QRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSK-GRTTIVIAH------RLstivnADKIIVLKDGRIVER 216
|
....*
gi 2017776620 484 GSPQQ 488
Cdd:cd03253 217 GTHEE 221
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
269-488 |
6.75e-41 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 153.64 E-value: 6.75e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 269 ALRVRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKP-ESLRRRVGM 347
Cdd:COG3845 5 ALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPrDAIALGIGM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 348 VFQHFNLFPDHTALENVMLSL--TKIKKMPRSEARGIAEARLTEVGLAERKDHRPAGLSGGQQQRVAIARALAMDPEVIL 425
Cdd:COG3845 85 VHQHFMLVPNLTVAENIVLGLepTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGARILI 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2017776620 426 FDEVTSALDPELVKGVLDLMANLGRQGMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQ 488
Cdd:COG3845 165 LDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAE 227
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
270-468 |
1.41e-40 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 144.93 E-value: 1.41e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESIlAMKPESLRRRVGMVF 349
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPI-RDAREDYRRRLAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 350 QHFNLFPDHTALENVMLsLTKIKKMPRSEARgIAEArLTEVGLAERKDHRPAGLSGGQQQRVAIARALAMDPEVILFDEV 429
Cdd:COG4133 82 HADGLKPELTVRENLRF-WAALYGLRADREA-IDEA-LEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEP 158
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2017776620 430 TSALDPELVKGVLDLMANLGRQGMTMAVVTH---EMGFARRV 468
Cdd:COG4133 159 FTALDAAGVALLAELIAAHLARGGAVLLTTHqplELAAARVL 200
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
270-500 |
1.57e-40 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 147.16 E-value: 1.57e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAYGDLD------VLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPE-SLR 342
Cdd:PRK13633 5 IKCKNVSYKYESNEesteklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLwDIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 343 RRVGMVFQHfnlfPDHTAL-----ENVMLSLTKIKkMPRSEARGIAEARLTEVGLAERKDHRPAGLSGGQQQRVAIARAL 417
Cdd:PRK13633 85 NKAGMVFQN----PDNQIVativeEDVAFGPENLG-IPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGIL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 418 AMDPEVILFDEVTSALDPELVKGVLDLMANLGRQ-GMTMAVVTHEMGFARRvADQVVFMDEGRIIEAGSPQQIFdnPQSE 496
Cdd:PRK13633 160 AMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKyGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIF--KEVE 236
|
....
gi 2017776620 497 RLKR 500
Cdd:PRK13633 237 MMKK 240
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
272-502 |
2.07e-40 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 146.83 E-value: 2.07e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 272 VRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPESL---RRRVGMV 348
Cdd:PRK11831 10 MRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRKRMSML 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 349 FQHFNLFPDHTALENVMLSLTKIKKMPRSEARGIAEARLTEVGLAERKDHRPAGLSGGQQQRVAIARALAMDPEVILFDE 428
Cdd:PRK11831 90 FQSGALFTDMNVFDNVAYPLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDE 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2017776620 429 VTSALDP----ELVKGVLDLMANLgrqGMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQIFDNPQSeRLKRFL 502
Cdd:PRK11831 170 PFVGQDPitmgVLVKLISELNSAL---GVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPDP-RVRQFL 243
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
272-502 |
2.66e-40 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 145.96 E-value: 2.66e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 272 VRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVE------PKRGDILLDGESILAMKPESLRRRV 345
Cdd:PRK14246 13 ISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQIDAIKLRKEV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 346 GMVFQHFNLFPDHTALENVMLSLTKIKKMPRSEARGIAEARLTEVGL----AERKDHRPAGLSGGQQQRVAIARALAMDP 421
Cdd:PRK14246 93 GMVFQQPNPFPHLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLwkevYDRLNSPASQLSGGQQQRLTIARALALKP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 422 EVILFDEVTSALDPELVKGVLDLMANLGRQgMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQIFDNPQSERLKRF 501
Cdd:PRK14246 173 KVLLMDEPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKY 251
|
.
gi 2017776620 502 L 502
Cdd:PRK14246 252 V 252
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
270-484 |
3.69e-40 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 144.26 E-value: 3.69e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAYGDLDVLKGVDLDIAPGtVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMkPESLRRRVGMVF 349
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQ-PQKLRRRIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 350 QHFNLFPDHTALENVMLsLTKIKKMPRSEARGIAEARLTEVGLAERKDHRPAGLSGGQQQRVAIARALAMDPEVILFDEV 429
Cdd:cd03264 79 QEFGVYPNFTVREFLDY-IAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2017776620 430 TSALDPELVKGVLDLMANLGrQGMTMAVVTHEMGFARRVADQVVFMDEGRIIEAG 484
Cdd:cd03264 158 TAGLDPEERIRFRNLLSELG-EDRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
270-484 |
4.14e-40 |
|
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: 143.90 E-value: 4.14e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILamKPESLRRRVGMVF 349
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQ--KNIEALRRIGALI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 350 QHFNLFPDHTALENVMLSLtKIKKMPRSEARGIaearLTEVGLAERKDHRPAGLSGGQQQRVAIARALAMDPEVILFDEV 429
Cdd:cd03268 79 EAPGFYPNLTARENLRLLA-RLLGIRKKRIDEV----LDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2017776620 430 TSALDPELVKGVLDLMANLGRQGMTMAVVTHEMGFARRVADQVVFMDEGRIIEAG 484
Cdd:cd03268 154 TNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
268-491 |
5.23e-40 |
|
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: 152.18 E-value: 5.23e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 268 GALRVRDLSMAYG--DLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPESLRRRV 345
Cdd:TIGR02203 329 GDVEFRNVTFRYPgrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQV 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 346 GMVFQHFNLFPDhTALENVMLSLTKIKKMPRSEaRGIAEARLTEV------GLaerkdHRPAG-----LSGGQQQRVAIA 414
Cdd:TIGR02203 409 ALVSQDVVLFND-TIANNIAYGRTEQADRAEIE-RALAAAYAQDFvdklplGL-----DTPIGengvlLSGGQRQRLAIA 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 415 RALAMDPEVILFDEVTSALDPE---LVKGVLD-LManlgrQGMTMAVVTHEMGFARRvADQVVFMDEGRIIEAGSPQQIF 490
Cdd:TIGR02203 482 RALLKDAPILILDEATSALDNEserLVQAALErLM-----QGRTTLVIAHRLSTIEK-ADRIVVMDDGRIVERGTHNELL 555
|
.
gi 2017776620 491 D 491
Cdd:TIGR02203 556 A 556
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
285-505 |
1.25e-39 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 148.26 E-value: 1.25e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 285 LKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPESL----RRRVGMVFQHFNLFPDHTA 360
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELrevrRKKIAMVFQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 361 LENVMLSLtKIKKMPRSEARGIAEARLTEVGLAERKDHRPAGLSGGQQQRVAIARALAMDPEVILFDEVTSALDPELVKG 440
Cdd:PRK10070 124 LDNTAFGM-ELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2017776620 441 VLDLMANL-GRQGMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQIFDNPQSERLKRFLAEV 505
Cdd:PRK10070 203 MQDELVKLqAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGV 268
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
285-478 |
2.32e-39 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 142.60 E-value: 2.32e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 285 LKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPESLrrrvgMVFQHFNLFPDHTALENV 364
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNYSLLPWLTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 365 MLSLTKI-KKMPRSEARGIAEARLTEVGLAERKDHRPAGLSGGQQQRVAIARALAMDPEVILFDEVTSALDPeLVKGVL- 442
Cdd:TIGR01184 76 ALAVDRVlPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDA-LTRGNLq 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 2017776620 443 -DLMANLGRQGMTMAVVTHEMGFARRVADQVVFMDEG 478
Cdd:TIGR01184 155 eELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
270-481 |
2.39e-39 |
|
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: 2.39e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKP-ESLRRRVGMV 348
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPrDARRAGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 349 FQhfnlfpdhtalenvmlsltkikkmprseargiaearltevglaerkdhrpagLSGGQQQRVAIARALAMDPEVILFDE 428
Cdd:cd03216 81 YQ----------------------------------------------------LSVGERQMVEIARALARNARLLILDE 108
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2017776620 429 VTSALDPELVKGVLDLMANLGRQGMTMAVVTHEMGFARRVADQVVFMDEGRII 481
Cdd:cd03216 109 PTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
285-484 |
2.91e-39 |
|
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: 141.66 E-value: 2.91e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 285 LKGVDLDIA---PGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDI------LLDGESILAMKPEslRRRVGMVFQHFNLF 355
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIvlngtvLFDSRKKINLPPQ--QRKIGLVFQQYALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 356 PDHTALENVMLSLtkiKKMPRSEARGIAEARLTEVGLAERKDHRPAGLSGGQQQRVAIARALAMDPEVILFDEVTSALDP 435
Cdd:cd03297 88 PHLNVRENLAFGL---KRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDR 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2017776620 436 ----ELVKGVLDLMANLgrqGMTMAVVTHEMGFARRVADQVVFMDEGRIIEAG 484
Cdd:cd03297 165 alrlQLLPELKQIKKNL---NIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
270-504 |
3.25e-39 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 142.82 E-value: 3.25e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESIlAMKPESLRRRVGMV- 348
Cdd:PRK11300 6 LSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHI-EGLPGHQIARMGVVr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 349 -FQHFNLFPDHTALENVMLS------------LTKIKKMPRSEARGIAEAR--LTEVGLAERKDhRPAG-LSGGQQQRVA 412
Cdd:PRK11300 85 tFQHVRLFREMTVIENLLVAqhqqlktglfsgLLKTPAFRRAESEALDRAAtwLERVGLLEHAN-RQAGnLAYGQQRRLE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 413 IARALAMDPEVILFDEVTSALDPELVKGVLDLMANLGRQ-GMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQIFD 491
Cdd:PRK11300 164 IARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRN 243
|
250
....*....|...
gi 2017776620 492 NPqsERLKRFLAE 504
Cdd:PRK11300 244 NP--DVIKAYLGE 254
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
273-503 |
3.44e-39 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 145.94 E-value: 3.44e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 273 RDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPEslRRRVGMVFQHF 352
Cdd:PRK11000 7 RNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPA--ERGVGMVFQSY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 353 NLFPDHTALENVM--LSLTKIKKMPRseargiaEARLTEVG----LAERKDHRPAGLSGGQQQRVAIARALAMDPEVILF 426
Cdd:PRK11000 85 ALYPHLSVAENMSfgLKLAGAKKEEI-------NQRVNQVAevlqLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2017776620 427 DEVTSALDPELVKGVLDLMANLGRQ-GMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQIFDNPQSerlkRFLA 503
Cdd:PRK11000 158 DEPLSNLDAALRVQMRIEISRLHKRlGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPAN----RFVA 231
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
270-498 |
6.21e-39 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 142.82 E-value: 6.21e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAYGD-LDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDG-ESILAMKPESLRRRVGM 347
Cdd:PRK13644 2 IRLENVSYSYPDgTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGiDTGDFSKLQGIRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 348 VFQHFNL-FPDHTALENVMLSLTKIKkMPRSEARGIAEARLTEVGLAERKDHRPAGLSGGQQQRVAIARALAMDPEVILF 426
Cdd:PRK13644 82 VFQNPETqFVGRTVEEDLAFGPENLC-LPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2017776620 427 DEVTSALDPELVKGVLDLMANLGRQGMTMAVVTHEMGfARRVADQVVFMDEGRIIEAGSPQQIFDNPQSERL 498
Cdd:PRK13644 161 DEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLE-ELHDADRIIVMDRGKIVLEGEPENVLSDVSLQTL 231
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
270-505 |
6.82e-39 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 142.46 E-value: 6.82e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEpkrGD------ILLDGESI-----LAMKP 338
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLIT---GDksagshIELLGRTVqregrLARDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 339 ESLRRRVGMVFQHFNLFPDHTALENVMLSLTKIKKMPRSEARGIAEAR-------LTEVGLAERKDHRPAGLSGGQQQRV 411
Cdd:PRK09984 82 RKSRANTGYIFQQFNLVNRLSVLENVLIGALGSTPFWRTCFSWFTREQkqralqaLTRVGMVHFAHQRVSTLSGGQQQRV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 412 AIARALAMDPEVILFDEVTSALDPELVKGVLDLMANLGRQ-GMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQiF 490
Cdd:PRK09984 162 AIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQ-F 240
|
250
....*....|....*
gi 2017776620 491 DNPQSERLKRFLAEV 505
Cdd:PRK09984 241 DNERFDHLYRSINRV 255
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
270-504 |
7.22e-39 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 142.28 E-value: 7.22e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAY---------GDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESiLAMKPES 340
Cdd:COG4167 5 LEVRNLSKTFkyrtglfrrQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHK-LEYGDYK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 341 LR-RRVGMVFQHFNlfpdhTALeNVMLSLTKIKKMPRSEARGI-AEAR-------LTEVGL-AERKDHRPAGLSGGQQQR 410
Cdd:COG4167 84 YRcKHIRMIFQDPN-----TSL-NPRLNIGQILEEPLRLNTDLtAEEReerifatLRLVGLlPEHANFYPHMLSSGQKQR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 411 VAIARALAMDPEVILFDEVTSALDPELVKGVLDLMANL-GRQGMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQI 489
Cdd:COG4167 158 VALARALILQPKIIIADEALAALDMSVRSQIINLMLELqEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAEV 237
|
250
....*....|....*
gi 2017776620 490 FDNPQSERLKRFLAE 504
Cdd:COG4167 238 FANPQHEVTKRLIES 252
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
283-491 |
9.69e-39 |
|
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: 141.08 E-value: 9.69e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 283 DVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPESLRRRVGMVFQHFNLFpDHTALE 362
Cdd:cd03252 16 VILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGVVLQENVLF-NRSIRD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 363 NVMLSLTKIKKMPRSEARGIAEARLTEVGLAERKD----HRPAGLSGGQQQRVAIARALAMDPEVILFDEVTSALDPELV 438
Cdd:cd03252 95 NIALADPGMSMERVIEAAKLAGAHDFISELPEGYDtivgEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYESE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2017776620 439 KGVLDLMANLGrQGMTMAVVTHEMGFARRvADQVVFMDEGRIIEAGSPQQIFD 491
Cdd:cd03252 175 HAIMRNMHDIC-AGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLA 225
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
285-504 |
1.04e-38 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 142.66 E-value: 1.04e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 285 LKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKP----ESLRRRVGMVFQhfnlFPDHTA 360
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGnknlKKLRKKVSLVFQ----FPEAQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 361 LENVMLSltKIKKMPRS------EARGIAEARLTEVGLAER-KDHRPAGLSGGQQQRVAIARALAMDPEVILFDEVTSAL 433
Cdd:PRK13641 99 FENTVLK--DVEFGPKNfgfsedEAKEKALKWLKKVGLSEDlISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2017776620 434 DPELVKGVLDLMANLGRQGMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQIFDNPQSERlKRFLAE 504
Cdd:PRK13641 177 DPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKEWLK-KHYLDE 246
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
271-500 |
1.33e-38 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 140.99 E-value: 1.33e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 271 RVRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPESLRRRVGMVFQ 350
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAILRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 351 --HFNL------------FP---------DHTALENVM--LSLTkikkmprsearGIAEARLTEvglaerkdhrpagLSG 405
Cdd:COG4604 83 enHINSrltvrelvafgrFPyskgrltaeDREIIDEAIayLDLE-----------DLADRYLDE-------------LSG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 406 GQQQRVAIARALAMDPEVILFDEVTSALDPelvKGVLDLMANLGR----QGMTMAVVTHEMGFARRVADQVVFMDEGRII 481
Cdd:COG4604 139 GQRQRAFIAMVLAQDTDYVLLDEPLNNLDM---KHSVQMMKLLRRladeLGKTVVIVLHDINFASCYADHIVAMKDGRVV 215
|
250
....*....|....*....
gi 2017776620 482 EAGSPQQIFdnpQSERLKR 500
Cdd:COG4604 216 AQGTPEEII---TPEVLSD 231
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
271-488 |
1.46e-38 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 140.75 E-value: 1.46e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 271 RVRDLSMAY---GDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPESLRRRVGM 347
Cdd:cd03249 2 EFKNVSFRYpsrPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 348 VFQHFNLFpDHTALENVMLSLTKIKKMPRSEARGIAEARLTEVGLAERKDHR--PAG--LSGGQQQRVAIARALAMDPEV 423
Cdd:cd03249 82 VSQEPVLF-DGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLvgERGsqLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2017776620 424 ILFDEVTSALDPE---LVKGVLDLManlgRQGMTMAVVTHEMGFARRvADQVVFMDEGRIIEAGSPQQ 488
Cdd:cd03249 161 LLLDEATSALDAEsekLVQEALDRA----MKGRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGTHDE 223
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
272-489 |
1.48e-38 |
|
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: 140.20 E-value: 1.48e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 272 VRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAmKPESLRRRVGMVFQH 351
Cdd:cd03265 3 VENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 352 FNLFPDHTALENVMLsLTKIKKMPRSEARGIAEARLTEVGLAERKDHRPAGLSGGQQQRVAIARALAMDPEVILFDEVTS 431
Cdd:cd03265 82 LSVDDELTGWENLYI-HARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2017776620 432 ALDPELVKGVLDLMANLGR-QGMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQI 489
Cdd:cd03265 161 GLDPQTRAHVWEYIEKLKEeFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
270-491 |
2.17e-38 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 140.06 E-value: 2.17e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAYGDLD--VLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPESLRRRVGM 347
Cdd:cd03251 1 VEFKNVTFRYPGDGppVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 348 VFQHFNLFPDhTALENVMLSLTKIkkmprSEARGIAEARL---------TEVGLAERKDHRPAGLSGGQQQRVAIARALA 418
Cdd:cd03251 81 VSQDVFLFND-TVAENIAYGRPGA-----TREEVEEAARAanahefimeLPEGYDTVIGERGVKLSGGQRQRIAIARALL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2017776620 419 MDPEVILFDEVTSALDPE---LVKGVLD-LMANlgrqgMTMAVVTHEMGFARRvADQVVFMDEGRIIEAGSPQQIFD 491
Cdd:cd03251 155 KDPPILILDEATSALDTEserLVQAALErLMKN-----RTTFVIAHRLSTIEN-ADRIVVLEDGKIVERGTHEELLA 225
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
270-488 |
4.10e-38 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 138.38 E-value: 4.10e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPK---RGDILLDGESILAMKPEslRRRVG 346
Cdd:COG4136 2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPAE--QRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 347 MVFQHFNLFPDHTALENVMLSLTKikKMPRSEARGIAEARLTEVGLAERKDHRPAGLSGGQQQRVAIARALAMDPEVILF 426
Cdd:COG4136 80 ILFQDDLLFPHLSVGENLAFALPP--TIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2017776620 427 DEVTSALDPELVKGVLDLM-ANLGRQGMTMAVVTHEMGFARrvadqvvfmDEGRIIEAGSPQQ 488
Cdd:COG4136 158 DEPFSKLDAALRAQFREFVfEQIRQRGIPALLVTHDEEDAP---------AAGRVLDLGNWQH 211
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
269-494 |
4.38e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 140.64 E-value: 4.38e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 269 ALRVRDLSMAYGD-LDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPESLRRRVGM 347
Cdd:PRK13647 4 IIEVEDLHFRYKDgTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 348 VFQHfnlfPDH-----TALENVMLSLTKIKkMPRSEARGIAEARLTEVGLAERKDHRPAGLSGGQQQRVAIARALAMDPE 422
Cdd:PRK13647 84 VFQD----PDDqvfssTVWDDVAFGPVNMG-LDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2017776620 423 VILFDEVTSALDPELVKGVLDLMANLGRQGMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPqQIFDNPQ 494
Cdd:PRK13647 159 VIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDK-SLLTDED 229
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
270-484 |
4.50e-38 |
|
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: 138.57 E-value: 4.50e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKpeslRRRVGMVF 349
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----RNRIGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 350 QHFNLFPDHTALEnVMLSLTKIKKMPRSEARGIAEARLTEVGLAERKDHRPAGLSGGQQQRVAIARALAMDPEVILFDEV 429
Cdd:cd03269 77 EERGLYPKMKVID-QLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2017776620 430 TSALDPELVKGVLDLMANLGRQGMTMAVVTHEMGFARRVADQVVFMDEGRIIEAG 484
Cdd:cd03269 156 FSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
270-492 |
4.78e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 141.38 E-value: 4.78e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAYG-----DLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDIL----------------L 328
Cdd:PRK13651 3 IKVKNIVKIFNkklptELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEwifkdeknkkktkekeK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 329 DGESILAMKPES--------LRRRVGMVFQ--HFNLFpDHTALENVM---LSLtkikKMPRSEARGIAEARLTEVGLAER 395
Cdd:PRK13651 83 VLEKLVIQKTRFkkikkikeIRRRVGVVFQfaEYQLF-EQTIEKDIIfgpVSM----GVSKEEAKKRAAKYIELVGLDES 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 396 KDHR-PAGLSGGQQQRVAIARALAMDPEVILFDEVTSALDPELVKGVLDLMANLGRQGMTMAVVTHEMGFARRVADQVVF 474
Cdd:PRK13651 158 YLQRsPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIF 237
|
250
....*....|....*...
gi 2017776620 475 MDEGRIIEAGSPQQIFDN 492
Cdd:PRK13651 238 FKDGKIIKDGDTYDILSD 255
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
270-484 |
1.17e-37 |
|
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: 137.50 E-value: 1.17e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAYGDLD----VLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAmKPESLRRRV 345
Cdd:cd03266 2 ITADALTKRFRDVKktvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 346 GMVFQHFNLFPDHTALENVmLSLTKIKKMPRSEARGIAEARLTEVGLAERKDHRPAGLSGGQQQRVAIARALAMDPEVIL 425
Cdd:cd03266 81 GFVSDSTGLYDRLTARENL-EYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2017776620 426 FDEVTSALDPELVKGVLDLMANLGRQGMTMAVVTHEMGFARRVADQVVFMDEGRIIEAG 484
Cdd:cd03266 160 LDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
261-480 |
1.26e-37 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 138.66 E-value: 1.26e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 261 NEPRFKAGA-LRVRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDiLLDGESILAMKPE 339
Cdd:PRK11247 3 NTARLNQGTpLLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGE-LLAGTAPLAEARE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 340 SLRrrvgMVFQHFNLFPDHTALENVMLSLtkikkmpRSEARGIAEARLTEVGLAERKDHRPAGLSGGQQQRVAIARALAM 419
Cdd:PRK11247 82 DTR----LMFQDARLLPWKKVIDNVGLGL-------KGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIH 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2017776620 420 DPEVILFDEVTSALDPELVKGVLDLMANLGRQ-GMTMAVVTHEMGFARRVADQVVFMDEGRI 480
Cdd:PRK11247 151 RPGLLLLDEPLGALDALTRIEMQDLIESLWQQhGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
270-493 |
2.06e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 138.78 E-value: 2.06e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAY-GDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPESLRRRVGMV 348
Cdd:PRK13652 4 IETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 349 FQHfnlfPDH-----TALENVMLSLTKIKKMPRSEARGIAEArLTEVGLAERKDHRPAGLSGGQQQRVAIARALAMDPEV 423
Cdd:PRK13652 84 FQN----PDDqifspTVEQDIAFGPINLGLDEETVAHRVSSA-LHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQV 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2017776620 424 ILFDEVTSALDPELVKGVLDLMANLG-RQGMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQIFDNP 493
Cdd:PRK13652 159 LVLDEPTAGLDPQGVKELIDFLNDLPeTYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
270-494 |
2.28e-37 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 138.14 E-value: 2.28e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGES----ILAMKPESLRRRV 345
Cdd:PRK11701 7 LSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDgqlrDLYALSEAERRRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 346 -----GMVFQHF--NLFPDHTALENVMLSLTKIKKMPRSEARGIAEARLTEVGL-AERKDHRPAGLSGGQQQRVAIARAL 417
Cdd:PRK11701 87 lrtewGFVHQHPrdGLRMQVSAGGNIGERLMAVGARHYGDIRATAGDWLERVEIdAARIDDLPTTFSGGMQQRLQIARNL 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2017776620 418 AMDPEVILFDEVTSALDPELVKGVLDLMANLGRQ-GMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQIFDNPQ 494
Cdd:PRK11701 167 VTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRElGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGLTDQVLDDPQ 244
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
285-504 |
3.68e-37 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 138.33 E-value: 3.68e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 285 LKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPESLRRRVGMVFQH-FNLFPDHTALEN 363
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIGMVFQNpDNQFVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 364 VMLSLTKiKKMPRSEARGIAEARLTEVGLAERKDHRPAGLSGGQQQRVAIARALAMDPEVILFDEVTSALDPElvkGVLD 443
Cdd:PRK13650 103 VAFGLEN-KGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPE---GRLE 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2017776620 444 LMANL----GRQGMTMAVVTHEMGfarRVA--DQVVFMDEGRIIEAGSPQQIF-----------DNPQSERLKRFLAE 504
Cdd:PRK13650 179 LIKTIkgirDDYQMTVISITHDLD---EVAlsDRVLVMKNGQVESTSTPRELFsrgndllqlglDIPFTTSLVQSLRQ 253
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
285-492 |
4.59e-37 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 138.26 E-value: 4.59e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 285 LKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESIL--AMKPESLRRRVGMVFQhfnlFPDHTALE 362
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkKVKLSDIRKKVGLVFQ----YPEYQLFE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 363 ------------NVMLSLTKIKKMPRsEARGIaearlteVGLA--ERKDHRPAGLSGGQQQRVAIARALAMDPEVILFDE 428
Cdd:PRK13637 99 etiekdiafgpiNLGLSEEEIENRVK-RAMNI-------VGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2017776620 429 VTSALDPELVKGVLDLMANLGRQ-GMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQIFDN 492
Cdd:PRK13637 171 PTAGLDPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKE 235
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
269-503 |
5.45e-37 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 139.59 E-value: 5.45e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 269 ALRVRDLSMAY-GDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPESlrRRVGM 347
Cdd:PRK11650 3 GLKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD--RDIAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 348 VFQHFNLFPDHTALENVMLSLtKIKKMPRSE-ARGIAE-ARLTEVG-LAERKdhrPAGLSGGQQQRVAIARALAMDPEVI 424
Cdd:PRK11650 81 VFQNYALYPHMSVRENMAYGL-KIRGMPKAEiEERVAEaARILELEpLLDRK---PRELSGGQRQRVAMGRAIVREPAVF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 425 LFDEVTSALDPEL-VKGVLDLMANLGRQGMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQIFDNPQSerlkRFLA 503
Cdd:PRK11650 157 LFDEPLSNLDAKLrVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPAS----TFVA 232
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
238-475 |
5.74e-37 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 143.20 E-value: 5.74e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 238 GSGAASGLVEVGELRAASSTAVGNEPRFKAGALRVRDLSMAYGDLD-VLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLN 316
Cdd:TIGR02857 290 GVAAAEALFAVLDAAPRPLAGKAPVTAAPASSLEFSGVSVAYPGRRpALRPVSFTVPPGERVALVGPSGAGKSTLLNLLL 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 317 RLVEPKRGDILLDGESILAMKPESLRRRVGMVFQHFNLFPDhTALENVMLSLtkikkmPRSEARGIAEArLTEVGLAE-- 394
Cdd:TIGR02857 370 GFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAG-TIAENIRLAR------PDASDAEIREA-LERAGLDEfv 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 395 ---------RKDHRPAGLSGGQQQRVAIARALAMDPEVILFDEVTSALDPELVKGVLDLMANLgRQGMTMAVVTHEMGFA 465
Cdd:TIGR02857 442 aalpqgldtPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRAL-AQGRTVLLVTHRLALA 520
|
250
....*....|
gi 2017776620 466 RRvADQVVFM 475
Cdd:TIGR02857 521 AL-ADRIVVL 529
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
268-480 |
5.91e-37 |
|
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: 136.06 E-value: 5.91e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 268 GALRVRDLSMAY---GDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPESLRRR 344
Cdd:cd03248 10 GIVKFQNVTFAYptrPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 345 VGMVFQHFNLFPdHTALENVMLSLTKIKKMPRSEARGIAEA----RLTEVGLAERKDHRPAGLSGGQQQRVAIARALAMD 420
Cdd:cd03248 90 VSLVGQEPVLFA-RSLQDNIAYGLQSCSFECVKEAAQKAHAhsfiSELASGYDTEVGEKGSQLSGGQKQRVAIARALIRN 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 421 PEVILFDEVTSALDPELVKGVLDLMANlGRQGMTMAVVTHEMGFARRvADQVVFMDEGRI 480
Cdd:cd03248 169 PQVLILDEATSALDAESEQQVQQALYD-WPERRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
285-495 |
1.01e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 136.80 E-value: 1.01e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 285 LKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPESLRRRVGMVFQH-FNLFPDHT---- 359
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGIVFQNpDNQFVGSIvkyd 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 360 ---ALENVMLSLTKIKkmprseaRGIAEArLTEVGLAERKDHRPAGLSGGQQQRVAIARALAMDPEVILFDEVTSALDPE 436
Cdd:PRK13648 105 vafGLENHAVPYDEMH-------RRVSEA-LKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPD 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 437 LVKGVLDLMANLGR-QGMTMAVVTHEMGFARRvADQVVFMDEGRIIEAGSPQQIFDNPQS 495
Cdd:PRK13648 177 ARQNLLDLVRKVKSeHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDHAEE 235
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
269-489 |
2.61e-36 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 136.39 E-value: 2.61e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 269 ALRVRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESIlamkPESLRRRVGMV 348
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPL----DPEDRRRIGYL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 349 FQHFNLFPDHTALEnVMLSLTKIKKMPRSEARGIAEARLTEVGLAERKDHRPAGLSGGQQQRVAIARALAMDPEVILFDE 428
Cdd:COG4152 77 PEERGLYPKMKVGE-QLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDE 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2017776620 429 VTSALDPELVKGVLDLMANLGRQGMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQI 489
Cdd:COG4152 156 PFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI 216
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
288-493 |
3.42e-36 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 137.55 E-value: 3.42e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 288 VDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESI------LAMKPEslRRRVGMVFQHFNLFPDHTAL 361
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLfdsrkgIFLPPE--KRRIGYVFQEARLFPHLSVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 362 ENVMLSLTKIkkmpRSEARGIAEARLTEV-GLAERKDHRPAGLSGGQQQRVAIARALAMDPEVILFDEVTSALDPELVKG 440
Cdd:TIGR02142 94 GNLRYGMKRA----RPSERRISFERVIELlGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2017776620 441 VLDLMANLGRQ-GMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQIFDNP 493
Cdd:TIGR02142 170 ILPYLERLHAEfGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
195-493 |
5.51e-36 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 142.17 E-value: 5.51e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 195 QAVVTGNLSPLLLagVFYLLITVPLTHFVNYIDARLrlGRQGRGSGAASGLVEVGELRAASSTAVGNEPRFKAGALRVRD 274
Cdd:TIGR00958 408 QLVLTGKVSSGNL--VSFLLYQEQLGEAVRVLSYVY--SGMMQAVGASEKVFEYLDRKPNIPLTGTLAPLNLEGLIEFQD 483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 275 LSMAY---GDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPESLRRRVGMVFQH 351
Cdd:TIGR00958 484 VSFSYpnrPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQE 563
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 352 FNLFpDHTALENVMLSLTkikKMPRSEARGIAEARL-------------TEVGlaerkdhrPAG--LSGGQQQRVAIARA 416
Cdd:TIGR00958 564 PVLF-SGSVRENIAYGLT---DTPDEEIMAAAKAANahdfimefpngydTEVG--------EKGsqLSGGQKQRIAIARA 631
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2017776620 417 LAMDPEVILFDEVTSALDPELVKGVLDLMAnlgRQGMTMAVVTHEMGFARRvADQVVFMDEGRIIEAGSPQQIFDNP 493
Cdd:TIGR00958 632 LVRKPRVLILDEATSALDAECEQLLQESRS---RASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
285-494 |
6.12e-36 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 136.25 E-value: 6.12e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 285 LKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPE---SLRRRVGMVFQ--HFNLFPDHT 359
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEaqkLLRQKIQIVFQnpYGSLNPRKK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 360 A---LENVMLSLTKikkMPRSEARGIAEARLTEVGL-AERKDHRPAGLSGGQQQRVAIARALAMDPEVILFDEVTSALDP 435
Cdd:PRK11308 111 VgqiLEEPLLINTS---LSAAERREKALAMMAKVGLrPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDV 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 436 ELVKGVLDLMANLGRQ-GMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQIFDNPQ 494
Cdd:PRK11308 188 SVQAQVLNLMMDLQQElGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPR 247
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
282-467 |
6.73e-36 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 133.37 E-value: 6.73e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 282 LDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPE---SLR-RRVGMVFQHFNLFPD 357
Cdd:PRK10584 23 LSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEaraKLRaKHVGFVFQSFMLIPT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 358 HTALENVMLSlTKIKKMPRSEARGIAEARLTEVGLAERKDHRPAGLSGGQQQRVAIARALAMDPEVILFDEVTSALDPEL 437
Cdd:PRK10584 103 LNALENVELP-ALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQT 181
|
170 180 190
....*....|....*....|....*....|.
gi 2017776620 438 VKGVLDLMANLGR-QGMTMAVVTHEMGFARR 467
Cdd:PRK10584 182 GDKIADLLFSLNReHGTTLILVTHDLQLAAR 212
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
270-480 |
1.14e-35 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 132.31 E-value: 1.14e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAY-GDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPES---LRRRV 345
Cdd:PRK10908 2 IRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 346 GMVFQHFNLFPDHTALENVMLSLTkIKKMPRSEARGIAEARLTEVGLAERKDHRPAGLSGGQQQRVAIARALAMDPEVIL 425
Cdd:PRK10908 82 GMIFQDHHLLMDRTVYDNVAIPLI-IAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2017776620 426 FDEVTSALDPELVKGVLDLMANLGRQGMTMAVVTHEMGFARRVADQVVFMDEGRI 480
Cdd:PRK10908 161 ADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
266-485 |
1.44e-35 |
|
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: 139.96 E-value: 1.44e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 266 KAGALRVRDLSMAY-GDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPESLRRR 344
Cdd:COG5265 354 GGGEVRFENVSFGYdPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAA 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 345 VGMVFQHFNLFPDhTALENVmlsltkikkmpR------SEARGIAEARL---------------TEVGlaER--Kdhrpa 401
Cdd:COG5265 434 IGIVPQDTVLFND-TIAYNI-----------AygrpdaSEEEVEAAARAaqihdfieslpdgydTRVG--ERglK----- 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 402 gLSGGQQQRVAIARALAMDPEVILFDEVTSALDPELVKGVLDLMANLGRqGMTMAVVTHemgfarRV-----ADQVVFMD 476
Cdd:COG5265 495 -LSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVAR-GRTTLVIAH------RLstivdADEILVLE 566
|
....*....
gi 2017776620 477 EGRIIEAGS 485
Cdd:COG5265 567 AGRIVERGT 575
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
282-479 |
1.58e-35 |
|
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: 132.17 E-value: 1.58e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 282 LDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILL--DGESI-LAMKPES----LRRR-VGMVFQHFN 353
Cdd:COG4778 24 LPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWVdLAQASPReilaLRRRtIGYVSQFLR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 354 LFPDHTALENVMLSLTKiKKMPRSEARGIAEARLTEVGLAERK-DHRPAGLSGGQQQRVAIARALAMDPEVILFDEVTSA 432
Cdd:COG4778 104 VIPRVSALDVVAEPLLE-RGVDREEARARARELLARLNLPERLwDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTAS 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2017776620 433 LDPELVKGVLDLMANLGRQGMTMAVVTHEMGFARRVADQVVFMDEGR 479
Cdd:COG4778 183 LDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
270-487 |
2.74e-35 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 139.47 E-value: 2.74e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAY----GDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPESL---- 341
Cdd:PRK10535 5 LELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 342 RRRVGMVFQHFNLFPDHTALENVMLSLTkIKKMPRSEARGIAEARLTEVGLAERKDHRPAGLSGGQQQRVAIARALAMDP 421
Cdd:PRK10535 85 REHFGFIFQRYHLLSHLTAAQNVEVPAV-YAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGG 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2017776620 422 EVILFDEVTSALDPELVKGVLDLMANLGRQGMTMAVVTHEMGFARRvADQVVFMDEGRIIEAGSPQ 487
Cdd:PRK10535 164 QVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQ-AERVIEIRDGEIVRNPPAQ 228
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
270-490 |
3.22e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 133.05 E-value: 3.22e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAYGD-LDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESI--LAMKPESLRRRVG 346
Cdd:PRK13636 6 LKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdySRKGLMKLRESVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 347 MVFQHfnlfPDH-----TALENVMLSLTKIKkMPRSEARGIAEARLTEVGLAERKDHRPAGLSGGQQQRVAIARALAMDP 421
Cdd:PRK13636 86 MVFQD----PDNqlfsaSVYQDVSFGAVNLK-LPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 422 EVILFDEVTSALDPELVKGVLDLMANLGRQ-GMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQIF 490
Cdd:PRK13636 161 KVLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF 230
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
275-500 |
3.76e-35 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 132.50 E-value: 3.76e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 275 LSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPE---SLRRRVGMVFQH 351
Cdd:PRK10419 18 LSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAqrkAFRRDIQMVFQD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 352 ----FNlfPDHTALENVMLSLTKIKKMPRSEARGIAEARLTEVGLA-ERKDHRPAGLSGGQQQRVAIARALAMDPEVILF 426
Cdd:PRK10419 98 sisaVN--PRKTVREIIREPLRHLLSLDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQLQRVCLARALAVEPKLLIL 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2017776620 427 DEVTSALDPELVKGVLDLMANLGRQ-GMTMAVVTHEMGFARRVADQVVFMDEGRIIE--AGSPQQIFDNPQSERLKR 500
Cdd:PRK10419 176 DEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIVEtqPVGDKLTFSSPAGRVLQN 252
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
288-490 |
4.28e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 132.94 E-value: 4.28e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 288 VDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRG-----DILLDGESILA-MKPesLRRRVGMVFQhfnlFPDHTAL 361
Cdd:PRK13643 25 IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGkvtvgDIVVSSTSKQKeIKP--VRKKVGVVFQ----FPESQLF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 362 ENVMLSLTKIKK----MPRSEARGIAEARLTEVGLA-ERKDHRPAGLSGGQQQRVAIARALAMDPEVILFDEVTSALDPE 436
Cdd:PRK13643 99 EETVLKDVAFGPqnfgIPKEKAEKIAAEKLEMVGLAdEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPK 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2017776620 437 LVKGVLDLMANLGRQGMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQIF 490
Cdd:PRK13643 179 ARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
285-490 |
4.35e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 132.60 E-value: 4.35e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 285 LKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILA------MKPesLRRRVGMVFQ--HFNLFP 356
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHktkdkyIRP--VRKRIGMVFQfpESQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 357 DhtALENVMLSLTKIKKMPRSEARGIAEARLTEVGLAER-KDHRPAGLSGGQQQRVAIARALAMDPEVILFDEVTSALDP 435
Cdd:PRK13646 101 D--TVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFSRDvMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDP 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2017776620 436 ELVKGVLDLMANLG-RQGMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQIF 490
Cdd:PRK13646 179 QSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELF 234
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
270-498 |
8.23e-35 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 131.26 E-value: 8.23e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPESLRRRVGMVF 349
Cdd:PRK10253 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 350 QHFNLFPDHTALEnvMLSLTKIKKMP-----RSEARGIAEARLTEVGLAERKDHRPAGLSGGQQQRVAIARALAMDPEVI 424
Cdd:PRK10253 88 QNATTPGDITVQE--LVARGRYPHQPlftrwRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIM 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2017776620 425 LFDEVTSALDPELVKGVLDLMANLGR-QGMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQIFDNPQSERL 498
Cdd:PRK10253 166 LLDEPTTWLDISHQIDLLELLSELNReKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERI 240
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
267-485 |
1.93e-34 |
|
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: 137.57 E-value: 1.93e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 267 AGALRVRDLSMAYGD--LDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPESLRRR 344
Cdd:TIGR01846 453 RGAITFENIRFRYAPdsPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQ 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 345 VGMVFQHFNLFpDHTALENVMLSLTKIkkmprSEARGIAEARLTEV---------GLAERKDHRPAGLSGGQQQRVAIAR 415
Cdd:TIGR01846 533 MGVVLQENVLF-SRSIRDNIALCNPGA-----PFEHVIHAAKLAGAhdfiselpqGYNTEVGEKGANLSGGQRQRIAIAR 606
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 416 ALAMDPEVILFDEVTSALDPELVKGVLDLMANLGRqGMTMAVVTHEMGfARRVADQVVFMDEGRIIEAGS 485
Cdd:TIGR01846 607 ALVGNPRILIFDEATSALDYESEALIMRNMREICR-GRTVIIIAHRLS-TVRACDRIIVLEKGQIAESGR 674
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
289-496 |
2.79e-34 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 128.93 E-value: 2.79e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 289 DLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPEslRRRVGMVFQHFNLFPDHTALENVMLSL 368
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RRPVSMLFQENNLFSHLTVAQNIGLGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 369 T---KIKKMPRSEARGIAEarltEVGLAERKDHRPAGLSGGQQQRVAIARALAMDPEVILFDEVTSALDPELVKGVLDLM 445
Cdd:PRK10771 97 NpglKLNAAQREKLHAIAR----QMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLV 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2017776620 446 ANLGRQ-GMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQIFDNPQSE 496
Cdd:PRK10771 173 SQVCQErQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLSGKASA 224
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
270-480 |
3.66e-34 |
|
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: 126.56 E-value: 3.66e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAYGDLD--VLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPESLRRRVGM 347
Cdd:cd03246 1 LEVENVSFRYPGAEppVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 348 VFQHFNLFPDhTALENVmlsltkikkmprseargiaearltevglaerkdhrpagLSGGQQQRVAIARALAMDPEVILFD 427
Cdd:cd03246 81 LPQDDELFSG-SIAENI--------------------------------------LSGGQRQRLGLARALYGNPRILVLD 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2017776620 428 EVTSALDPELVKGVLDLMANLGRQGMTMAVVTHEMGFARRvADQVVFMDEGRI 480
Cdd:cd03246 122 EPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
268-484 |
5.32e-34 |
|
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: 127.71 E-value: 5.32e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 268 GALRVRDLSMAYGD--LDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPESLRRRV 345
Cdd:cd03245 1 GRIEFRNVSFSYPNqeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 346 GMVFQHFNLFPDhTALENVMLSLTKIKK---MPRSEARGIAE-ARLTEVGLAERKDHRPAGLSGGQQQRVAIARALAMDP 421
Cdd:cd03245 81 GYVPQDVTLFYG-TLRDNITLGAPLADDeriLRAAELAGVTDfVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2017776620 422 EVILFDEVTSALDPELVKGVLDLMANLGRqGMTMAVVTHEMGFArRVADQVVFMDEGRIIEAG 484
Cdd:cd03245 160 PILLLDEPTSAMDMNSEERLKERLRQLLG-DKTLIIITHRPSLL-DLVDRIIVMDSGRIVADG 220
|
|
| PRK15100 |
PRK15100 |
cystine ABC transporter permease; |
32-235 |
1.26e-33 |
|
cystine ABC transporter permease;
Pssm-ID: 185055 [Multi-domain] Cd Length: 220 Bit Score: 126.79 E-value: 1.26e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 32 TLILAAASTVLGVIIGMVLAVMGISQSRWLRLPARIYTDIFRGLPAIVTILIIGQGFARIGRELfgpSPFPLGIIALSLI 111
Cdd:PRK15100 22 TLQLSIGGMFFGLLLGFILALMRLSPIWPVRWLARFYVSIFRGTPLIAQLFMIYYGLPQFGIEL---DPIPAAMIGLSLN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 112 AGAYIGEIFRSGIQSVERGQMEACRALSMSYGQGMRLIVIPQGVRRVLPALVNQFIGNVKDSSLVYFLGLlaseREIFRV 191
Cdd:PRK15100 99 TAAYAAETLRAAISSIDKGQWEAAASIGMTRWQTLRRAILPQAARTALPPLSNSFISLVKDTSLAATIQV----PELFRQ 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2017776620 192 GQDQAVVTGNLSPLLLAG--VFYLLITVpLTHFVNYIDARLRLGRQ 235
Cdd:PRK15100 175 AQLITSRTLEVFTMYLAAslIYWIMATV-LSALQNRFENQLNRQER 219
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
280-484 |
1.86e-33 |
|
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: 125.36 E-value: 1.86e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 280 GDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLN--RLVEPKRGDILLDGESIlamKPESLRRRVGMVFQHFNLFPD 357
Cdd:cd03213 20 SGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGRPL---DKRSFRKIIGYVPQDDILHPT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 358 HTALENVMLSltkikkmprseargiAEARltevglaerkdhrpaGLSGGQQQRVAIARALAMDPEVILFDEVTSALDPEL 437
Cdd:cd03213 97 LTVRETLMFA---------------AKLR---------------GLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSS 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2017776620 438 VKGVLDLMANLGRQGMTMAVVTH----EMgFarRVADQVVFMDEGRIIEAG 484
Cdd:cd03213 147 ALQVMSLLRRLADTGRTIICSIHqpssEI-F--ELFDKLLLLSQGRVIYFG 194
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
196-460 |
2.03e-33 |
|
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: 132.87 E-value: 2.03e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 196 AVVTGNLSPLLLAgvfyLLITVPLTHFVNYIDARLRLGRQGRGSGAASGLVEVgeLRAASSTAVGNEPRFKAGA-----L 270
Cdd:TIGR02868 262 AVADGRLAPVTLA----VLVLLPLAAFEAFAALPAAAQQLTRVRAAAERIVEV--LDAAGPVAEGSAPAAGAVGlgkptL 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 271 RVRDLSMAY-GDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPESLRRRVGMVF 349
Cdd:TIGR02868 336 ELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCA 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 350 QHFNLFpDHTALENVMLSltkikkmpRSEARGI-AEARLTEVGLAERKDHRPAGL-----------SGGQQQRVAIARAL 417
Cdd:TIGR02868 416 QDAHLF-DTTVRENLRLA--------RPDATDEeLWAALERVGLADWLRALPDGLdtvlgeggarlSGGERQRLALARAL 486
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2017776620 418 AMDPEVILFDEVTSALDPELVKGVLDLMANlGRQGMTMAVVTH 460
Cdd:TIGR02868 487 LADAPILLLDEPTEHLDAETADELLEDLLA-ALSGRTVVLITH 528
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
268-488 |
5.45e-33 |
|
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: 133.16 E-value: 5.45e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 268 GALRVRDLSMAYGDlD---VLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPESLRRR 344
Cdd:TIGR03797 450 GAIEVDRVTFRYRP-DgplILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAVRRQ 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 345 VGMVFQHFNLFPDhTALENVMLSltkiKKMPRSEARGIAEarltEVGLAERKDHRPAG-----------LSGGQQQRVAI 413
Cdd:TIGR03797 529 LGVVLQNGRLMSG-SIFENIAGG----APLTLDEAWEAAR----MAGLAEDIRAMPMGmhtvisegggtLSGGQRQRLLI 599
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2017776620 414 ARALAMDPEVILFDEVTSALDPELVKGVldlMANLGRQGMTMAVVTHEMGFARRvADQVVFMDEGRIIEAGSPQQ 488
Cdd:TIGR03797 600 ARALVRKPRILLFDEATSALDNRTQAIV---SESLERLKVTRIVIAHRLSTIRN-ADRIYVLDAGRVVQQGTYDE 670
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
269-491 |
6.24e-33 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 127.23 E-value: 6.24e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 269 ALRVRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPESlRRRVGMV 348
Cdd:PRK13537 7 PIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA-RQRVGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 349 FQHFNLFPDHTALENvMLSLTKIKKMPRSEARGIAEARLTEVGLAERKDHRPAGLSGGQQQRVAIARALAMDPEVILFDE 428
Cdd:PRK13537 86 PQFDNLDPDFTVREN-LLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2017776620 429 VTSALDPELVKGVLDLMANLGRQGMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQIFD 491
Cdd:PRK13537 165 PTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIE 227
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
269-501 |
9.48e-33 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 125.20 E-value: 9.48e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 269 ALRVRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRG---DIL---LDGESILAmkpesLR 342
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGndvRLFgerRGGEDVWE-----LR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 343 RRVGMV---FQHFnlFPDHTALENVMLS-LTK---IKKMPRSEARGIAEARLTEVGLAERKDHRPAGLSGGQQQRVAIAR 415
Cdd:COG1119 78 KRIGLVspaLQLR--FPRDETVLDVVLSgFFDsigLYREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIAR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 416 ALAMDPEVILFDEVTSALDP---ELVKGVLDLMANLGrqGMTMAVVTH---EM--GFarrvaDQVVFMDEGRIIEAGSPQ 487
Cdd:COG1119 156 ALVKDPELLILDEPTAGLDLgarELLLALLDKLAAEG--APTLVLVTHhveEIppGI-----THVLLLKDGRVVAAGPKE 228
|
250
....*....|....
gi 2017776620 488 QIFdnpQSERLKRF 501
Cdd:COG1119 229 EVL---TSENLSEA 239
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
267-490 |
3.88e-32 |
|
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: 129.48 E-value: 3.88e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 267 AGALRVRDLSMAY--GDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPESLRRR 344
Cdd:COG4618 328 KGRLSVENLTVVPpgSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRH 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 345 VGMVFQHFNLFPDhTALENvmlsltkIKKMPRSEARGIAEA-----------RL-----TEVGlaerkdHRPAGLSGGQQ 408
Cdd:COG4618 408 IGYLPQDVELFDG-TIAEN-------IARFGDADPEKVVAAaklagvhemilRLpdgydTRIG------EGGARLSGGQR 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 409 QRVAIARALAMDPEVILFDEVTSALDPELVKGVLDLMANLGRQGMTMAVVTHEMGfARRVADQVVFMDEGRIIEAGSPQQ 488
Cdd:COG4618 474 QRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPS-LLAAVDKLLVLRDGRVQAFGPRDE 552
|
..
gi 2017776620 489 IF 490
Cdd:COG4618 553 VL 554
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
281-492 |
8.31e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 123.96 E-value: 8.31e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 281 DLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILA-----MKPESLRRRVGMVFQ--HFN 353
Cdd:PRK13645 23 EFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPAnlkkiKEVKRLRKEIGLVFQfpEYQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 354 LFPDhTALENVMLSLTKIKKMPRSEARGIAEArLTEVGLAERKDHR-PAGLSGGQQQRVAIARALAMDPEVILFDEVTSA 432
Cdd:PRK13645 103 LFQE-TIEKDIAFGPVNLGENKQEAYKKVPEL-LKLVQLPEDYVKRsPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGG 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2017776620 433 LDPELVKGVLDLMANLGR-QGMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQIFDN 492
Cdd:PRK13645 181 LDPKGEEDFINLFERLNKeYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN 241
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
270-494 |
1.08e-31 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 122.06 E-value: 1.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMkPESLRRRVGMVF 349
Cdd:COG1137 4 LEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHL-PMHKRARLGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 350 --QHFNLFPDHTALENVMLSLtKIKKMPRSEARGIAEARLTEVGLAERKDHRPAGLSGGQQQRVAIARALAMDPEVILFD 427
Cdd:COG1137 83 lpQEASIFRKLTVEDNILAVL-ELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2017776620 428 EVTSALDPELVKGVLDLMANLGRQGM-----------TMAVVthemgfarrvaDQVVFMDEGRIIEAGSPQQIFDNPQ 494
Cdd:COG1137 162 EPFAGVDPIAVADIQKIIRHLKERGIgvlitdhnvreTLGIC-----------DRAYIISEGKVLAEGTPEEILNNPL 228
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
250-505 |
1.26e-31 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 128.82 E-value: 1.26e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 250 ELRAASSTAVGNEPrfkagALRVRDLSMAYG-----------DLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRL 318
Cdd:PRK10261 299 EPPIEQDTVVDGEP-----ILQVRNLVTRFPlrsgllnrvtrEVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRL 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 319 VEPKRGDILLDGESI---LAMKPESLRRRVGMVFQ--HFNLFPDHTALENVMLSLTKIKKMPRSEARGIAEARLTEVGLA 393
Cdd:PRK10261 374 VESQGGEIIFNGQRIdtlSPGKLQALRRDIQFIFQdpYASLDPRQTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGLL 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 394 ERKDHR-PAGLSGGQQQRVAIARALAMDPEVILFDEVTSALDPELVKGVLDLMANLGRQ-GMTMAVVTHEMGFARRVADQ 471
Cdd:PRK10261 454 PEHAWRyPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHR 533
|
250 260 270
....*....|....*....|....*....|....
gi 2017776620 472 VVFMDEGRIIEAGSPQQIFDNPQSERLKRFLAEV 505
Cdd:PRK10261 534 VAVMYLGQIVEIGPRRAVFENPQHPYTRKLMAAV 567
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
267-485 |
1.47e-31 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 128.15 E-value: 1.47e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 267 AGALRVRDLSMAY-GDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPESLRRRV 345
Cdd:PRK13657 332 KGAVEFDDVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 346 GMVFQHFNLF------------PDHTaLENVMLSLTkikkmpRSEARGIAEARltEVGLAERKDHRPAGLSGGQQQRVAI 413
Cdd:PRK13657 412 AVVFQDAGLFnrsiednirvgrPDAT-DEEMRAAAE------RAQAHDFIERK--PDGYDTVVGERGRQLSGGERQRLAI 482
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2017776620 414 ARALAMDPEVILFDEVTSALDPEL---VKGVLDLManlgRQGMTMAVVTHEMGFARRvADQVVFMDEGRIIEAGS 485
Cdd:PRK13657 483 ARALLKDPPILILDEATSALDVETeakVKAALDEL----MKGRTTFIIAHRLSTVRN-ADRILVFDNGRVVESGS 552
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
270-490 |
1.71e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 122.51 E-value: 1.71e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAY---GDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPESLRRRVG 346
Cdd:PRK13642 5 LEVENLVFKYekeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 347 MVFQH-FNLFPDHTALENVMLSLTKiKKMPRSEARGIAEARLTEVGLAERKDHRPAGLSGGQQQRVAIARALAMDPEVIL 425
Cdd:PRK13642 85 MVFQNpDNQFVGATVEDDVAFGMEN-QGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIII 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2017776620 426 FDEVTSALDPELVKGVLDLMANL-GRQGMTMAVVTHEMGFARRvADQVVFMDEGRIIEAGSPQQIF 490
Cdd:PRK13642 164 LDESTSMLDPTGRQEIMRVIHEIkEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELF 228
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
270-493 |
4.52e-31 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 124.18 E-value: 4.52e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPESLRRRVGMVF 349
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 350 QHFNLFPDHTALENVMLS----LTKIKKMPRSEARGIAEArLTEVGLAERKDHRPAGLSGGQQQRVAIARALAMDPEVIL 425
Cdd:PRK09536 84 QDTSLSFEFDVRQVVEMGrtphRSRFDTWTETDRAAVERA-MERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2017776620 426 FDEVTSALDPELVKGVLDLMANLGRQGMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQIFDNP 493
Cdd:PRK09536 163 LDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTAD 230
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
270-493 |
8.28e-31 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 119.18 E-value: 8.28e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMkPESLRRRVGMVF 349
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKL-PMHKRARLGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 350 --QHFNLFPDHTALENVMLSLtKIKKMPRSEARGIAEARLTEVGLAERKDHRPAGLSGGQQQRVAIARALAMDPEVILFD 427
Cdd:cd03218 80 lpQEASIFRKLTVEENILAVL-EIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2017776620 428 EVTSALDPELVKGVLDLMANLGRQGMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQIFDNP 493
Cdd:cd03218 159 EPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANE 224
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
269-482 |
1.28e-30 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 119.42 E-value: 1.28e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 269 ALRVRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAmkPESLRrrvGMV 348
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEG--PGAER---GVV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 349 FQHFNLFPDHTALENVMLSLtKIKKMPRSEARGIAEARLTEVGLAERKDHRPAGLSGGQQQRVAIARALAMDPEVILFDE 428
Cdd:PRK11248 76 FQNEGLLPWRNVQDNVAFGL-QLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2017776620 429 VTSALDPELVKGVLDLMANL-GRQGMTMAVVTHEMGFARRVADQVVFM--DEGRIIE 482
Cdd:PRK11248 155 PFGALDAFTREQMQTLLLKLwQETGKQVLLITHDIEEAVFMATELVLLspGPGRVVE 211
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
284-491 |
2.13e-30 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 118.65 E-value: 2.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 284 VLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGE--SILAmkpeslrrrVGMVFQhfnlfPDHTAL 361
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRvsALLE---------LGAGFH-----PELTGR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 362 ENVMLSLTkIKKMPRSEARgiaeARLTEV----GLAERKDhRPAG-LSGGQQQRVAIARALAMDPEVILFDEVTSALDPE 436
Cdd:COG1134 107 ENIYLNGR-LLGLSRKEID----EKFDEIvefaELGDFID-QPVKtYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAA 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2017776620 437 LVKGVLDLMANLGRQGMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQIFD 491
Cdd:COG1134 181 FQKKCLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEVIA 235
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
270-503 |
3.44e-30 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 123.66 E-value: 3.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAYGDLD----VLKGVDLDIAPGTVTCIIGPSGSGKS-TLLRCLNRLVEPK----RGDILLDGESILAMKPES 340
Cdd:PRK15134 6 LAIENLSVAFRQQQtvrtVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLHASEQT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 341 LRR----RVGMVFQH--FNLFPDHTALENVMLSLTKIKKMPRSEARGIAEARLTEVGL---AERKDHRPAGLSGGQQQRV 411
Cdd:PRK15134 86 LRGvrgnKIAMIFQEpmVSLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIrqaAKRLTDYPHQLSGGERQRV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 412 AIARALAMDPEVILFDEVTSALDPELVKGVLDLMANLGRQ-GMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQIF 490
Cdd:PRK15134 166 MIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLF 245
|
250
....*....|...
gi 2017776620 491 DNPQSERLKRFLA 503
Cdd:PRK15134 246 SAPTHPYTQKLLN 258
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
268-486 |
4.20e-30 |
|
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: 117.21 E-value: 4.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 268 GALRVRDLSMAYG-DLD-VLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPESLRRRV 345
Cdd:cd03244 1 GDIEFKNVSLRYRpNLPpVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 346 GMVFQ---------HFNLFPDHT--------ALENVMLsLTKIKKMPrsearGIAEARLTEVGLaerkdhrpaGLSGGQQ 408
Cdd:cd03244 81 SIIPQdpvlfsgtiRSNLDPFGEysdeelwqALERVGL-KEFVESLP-----GGLDTVVEEGGE---------NLSVGQR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 409 QRVAIARALAMDPEVILFDEVTSALDPELVKgvldLMANLGRQGM---TMAVVTHemgfarRV-----ADQVVFMDEGRI 480
Cdd:cd03244 146 QLLCLARALLRKSKILVLDEATASVDPETDA----LIQKTIREAFkdcTVLTIAH------RLdtiidSDRILVLDKGRV 215
|
....*.
gi 2017776620 481 IEAGSP 486
Cdd:cd03244 216 VEFDSP 221
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
270-484 |
6.00e-30 |
|
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: 115.10 E-value: 6.00e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAYGDLD--VLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKpESLRRRVGM 347
Cdd:cd03247 1 LSINNVSFSYPEQEqqVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 348 VFQHFNLFpDHTALENvmlsltkikkmprseargiaearltevgLAERkdhrpagLSGGQQQRVAIARALAMDPEVILFD 427
Cdd:cd03247 80 LNQRPYLF-DTTLRNN----------------------------LGRR-------FSGGERQRLALARILLQDAPIVLLD 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2017776620 428 EVTSALDPELVKGVLDLMANLGRqGMTMAVVTHEM-GFARrvADQVVFMDEGRIIEAG 484
Cdd:cd03247 124 EPTVGLDPITERQLLSLIFEVLK-DKTLIWITHHLtGIEH--MDKILFLENGKIIMQG 178
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
269-491 |
8.93e-30 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 119.17 E-value: 8.93e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 269 ALRVRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAmKPESLRRRVGMV 348
Cdd:PRK13536 41 AIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIGVV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 349 FQHFNLFPDHTALENvMLSLTKIKKMPRSEARGIAEARLTEVGLAERKDHRPAGLSGGQQQRVAIARALAMDPEVILFDE 428
Cdd:PRK13536 120 PQFDNLDLEFTVREN-LLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDE 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2017776620 429 VTSALDPELVKGVLDLMANLGRQGMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQIFD 491
Cdd:PRK13536 199 PTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALID 261
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
281-484 |
1.19e-29 |
|
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: 115.83 E-value: 1.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 281 DLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEP---KRGDILLDGEsilAMKPESLRRRVGMVFQHFNLFPD 357
Cdd:cd03234 19 YARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQ---PRKPDQFQKCVAYVRQDDILLPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 358 HTALEN----VMLSLTKIKKMPRSEARgIAEARLTEVGLAERKDHRPAGLSGGQQQRVAIARALAMDPEVILFDEVTSAL 433
Cdd:cd03234 96 LTVRETltytAILRLPRKSSDAIRKKR-VEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2017776620 434 DPELVKGVLDLMANLGRQGMTMAVVTHEMG---FarRVADQVVFMDEGRIIEAG 484
Cdd:cd03234 175 DSFTALNLVSTLSQLARRNRIVILTIHQPRsdlF--RLFDRILLLSSGEIVYSG 226
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
270-461 |
1.24e-29 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 115.97 E-value: 1.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPESLRRRVGMVF 349
Cdd:PRK10247 8 LQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 350 QHFNLFPDhTALENVML--SLTKIKKMPRSEARGIAEARLTEVGLaerkDHRPAGLSGGQQQRVAIARALAMDPEVILFD 427
Cdd:PRK10247 88 QTPTLFGD-TVYDNLIFpwQIRNQQPDPAIFLDDLERFALPDTIL----TKNIAELSGGEKQRISLIRNLQFMPKVLLLD 162
|
170 180 190
....*....|....*....|....*....|....*
gi 2017776620 428 EVTSALDPELVKGVLDLMANLGR-QGMTMAVVTHE 461
Cdd:PRK10247 163 EITSALDESNKHNVNEIIHRYVReQNIAVLWVTHD 197
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
278-473 |
2.72e-29 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 113.87 E-value: 2.72e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 278 AYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGesilamkpeslRRRVGMVFQHFNL--- 354
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-----------GARVAYVPQRSEVpds 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 355 FPdHTALENVMLSL---TKIKKMPRSEARGIAEARLTEVGLAERKDHRPAGLSGGQQQRVAIARALAMDPEVILFDEVTS 431
Cdd:NF040873 70 LP-LTVRDLVAMGRwarRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTT 148
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2017776620 432 ALDPELVKGVLDLMANLGRQGMTMAVVTHEMGFARRvADQVV 473
Cdd:NF040873 149 GLDAESRERIIALLAEEHARGATVVVVTHDLELVRR-ADPCV 189
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
270-489 |
4.03e-29 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 120.29 E-value: 4.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRL--VEPKRGDIL----------------LDGE 331
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIyhvalcekcgyverpsKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 332 SIL----AMKPE-------------SLRRRVGMVFQH-FNLFPDHTALENVMLSLTKIKkMPRSEARGIAEARLTEVGLA 393
Cdd:TIGR03269 81 PCPvcggTLEPEevdfwnlsdklrrRIRKRIAIMLQRtFALYGDDTVLDNVLEALEEIG-YEGKEAVGRAVDLIEMVQLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 394 ERKDHRPAGLSGGQQQRVAIARALAMDPEVILFDEVTSALDPELVKGVLD-LMANLGRQGMTMAVVTHEMGFARRVADQV 472
Cdd:TIGR03269 160 HRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNaLEEAVKASGISMVLTSHWPEVIEDLSDKA 239
|
250
....*....|....*..
gi 2017776620 473 VFMDEGRIIEAGSPQQI 489
Cdd:TIGR03269 240 IWLENGEIKEEGTPDEV 256
|
|
| ectoine_ehuD |
TIGR03003 |
ectoine/hydroxyectoine ABC transporter, permease protein EhuD; Members of this family are ... |
13-230 |
4.19e-29 |
|
ectoine/hydroxyectoine ABC transporter, permease protein EhuD; Members of this family are presumed to act as permease subunits of ectoine ABC transporters. Operons containing this gene also contain the other genes of the ABC transporter and typically are found next to either ectoine utilization or ectoine biosynthesis operons.
Pssm-ID: 132048 [Multi-domain] Cd Length: 212 Bit Score: 114.18 E-value: 4.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 13 DWDAMAEVLPSMItVGLKNTLILAAASTVLGVIIGMVLAVMGISQSRWLRLPARIYTDIFRGLPAIVTILIIGQGFARIG 92
Cdd:TIGR03003 2 DWEFVRQILPTLI-EGLKITILATALGFAIAAVLGLVFAILRRSAPTPISWPTSFVVEFIRGTPLLVQLYFLYYVLPDIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 93 RELfgpSPFPLGIIALSLIAGAYIGEIFRSGIQSVERGQMEACRALSMSYGQGMRLIVIPQGVRRVLPALVNQFIGNVKD 172
Cdd:TIGR03003 81 IRL---PALVAGVLGLGLHYATYAAEVYRAGIEAVPRGQWEAATALNLTARQTYRHIILPQAIPPIIPALGNYLVAMFKE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2017776620 173 SSLVYFLGLLaserEIFrvgqDQAVVTGN-----LSPLLLAGVFYLLITVPLTHFVNYIDARL 230
Cdd:TIGR03003 158 TPVLSAITVL----ELM----NQAKSIGNstfryLEPMTLVGVFFLILSIISVFFLRRLEARL 212
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
261-488 |
4.72e-29 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 120.70 E-value: 4.72e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 261 NEPRFKAGALRVRDLSMAYGD--LDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKP 338
Cdd:PRK11160 330 STAAADQVSLTLNNVSFTYPDqpQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSE 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 339 ESLRRRVGMVFQHFNLFpDHTALENVMLSLTKIkkmprSEARGIAEarLTEVGLAERKDH------------RPagLSGG 406
Cdd:PRK11160 410 AALRQAISVVSQRVHLF-SATLRDNLLLAAPNA-----SDEALIEV--LQQVGLEKLLEDdkglnawlgeggRQ--LSGG 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 407 QQQRVAIARALAMDPEVILFDEVTSALDPELVKGVLDLMANLGrQGMTMAVVTHemgfaRRVA----DQVVFMDEGRIIE 482
Cdd:PRK11160 480 EQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHA-QNKTVLMITH-----RLTGleqfDRICVMDNGQIIE 553
|
....*.
gi 2017776620 483 AGSPQQ 488
Cdd:PRK11160 554 QGTHQE 559
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
282-494 |
6.69e-29 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 116.73 E-value: 6.69e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 282 LDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPESL---RRRVGMVFQH--FNLFP 356
Cdd:PRK15079 34 LKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWravRSDIQMIFQDplASLNP 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 357 DHTALENVMLSL-TKIKKMPRSEARGIAEARLTEVGLAERKDHR-PAGLSGGQQQRVAIARALAMDPEVILFDEVTSALD 434
Cdd:PRK15079 114 RMTIGEIIAEPLrTYHPKLSRQEVKDRVKAMMLKVGLLPNLINRyPHEFSGGQCQRIGIARALILEPKLIICDEPVSALD 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2017776620 435 PELVKGVLDLMANLGRQ-GMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQIFDNPQ 494
Cdd:PRK15079 194 VSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPL 254
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
268-491 |
7.78e-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: 120.61 E-value: 7.78e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 268 GALRVRDLSMAYG-DLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPESLRRRVG 346
Cdd:TIGR01193 472 GDIVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFIN 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 347 MVFQHFNLFpDHTALENVML-SLTKIKKMPRSEARGIAEARlTEV-----GLAERKDHRPAGLSGGQQQRVAIARALAMD 420
Cdd:TIGR01193 552 YLPQEPYIF-SGSILENLLLgAKENVSQDEIWAACEIAEIK-DDIenmplGYQTELSEEGSSISGGQKQRIALARALLTD 629
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2017776620 421 PEVILFDEVTSALDPELVKGVLDLMANLgrQGMTMAVVTHEMGFARRVaDQVVFMDEGRIIEAGSPQQIFD 491
Cdd:TIGR01193 630 SKVLILDESTSNLDTITEKKIVNNLLNL--QDKTIIFVAHRLSVAKQS-DKIIVLDHGKIIEQGSHDELLD 697
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
270-490 |
1.14e-28 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 114.72 E-value: 1.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPE--SLRRRVGM 347
Cdd:PRK13638 2 LATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGllALRQQVAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 348 VFQHfnlfPDHTAL-----ENVMLSLTKIKKMPRSEARGIAEArLTEVGlAERKDHRPAG-LSGGQQQRVAIARALAMDP 421
Cdd:PRK13638 82 VFQD----PEQQIFytdidSDIAFSLRNLGVPEAEITRRVDEA-LTLVD-AQHFRHQPIQcLSHGQKKRVAIAGALVLQA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2017776620 422 EVILFDEVTSALDPELVKGVLDLMANLGRQGMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQIF 490
Cdd:PRK13638 156 RYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
272-481 |
1.22e-28 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 119.01 E-value: 1.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 272 VRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGesilamkpeslRRRVGMVFQH 351
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-----------GLRIGYLPQE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 352 FNLFPDHTALENVMLSLTKIK-----------KMPRSEARGI----------------AEAR----LTEVGLAERKDHRP 400
Cdd:COG0488 70 PPLDDDLTVLDTVLDGDAELRaleaeleeleaKLAEPDEDLErlaelqeefealggweAEARaeeiLSGLGFPEEDLDRP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 401 AG-LSGGQQQRVAIARALAMDPEVILFDEVTSALDpelVKGVL---DLMANlgRQGmTMAVVTHEMGFARRVADQVVFMD 476
Cdd:COG0488 150 VSeLSGGWRRRVALARALLSEPDLLLLDEPTNHLD---LESIEwleEFLKN--YPG-TVLVVSHDRYFLDRVATRILELD 223
|
....*
gi 2017776620 477 EGRII 481
Cdd:COG0488 224 RGKLT 228
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
270-503 |
1.28e-28 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 119.04 E-value: 1.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAY-----------GDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVePKRGDILLDGESILAMKP 338
Cdd:PRK15134 276 LDVEQLQVAFpirkgilkrtvDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 339 ESL---RRRVGMVFQHFN--LFPDHTALENVMLSLTKIKKMPRSEARgiaEAR----LTEVGLAERKDHR-PAGLSGGQQ 408
Cdd:PRK15134 355 RQLlpvRHRIQVVFQDPNssLNPRLNVLQIIEEGLRVHQPTLSAAQR---EQQviavMEEVGLDPETRHRyPAEFSGGQR 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 409 QRVAIARALAMDPEVILFDEVTSALDPELVKGVLDLMANL-GRQGMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQ 487
Cdd:PRK15134 432 QRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLqQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCE 511
|
250
....*....|....*.
gi 2017776620 488 QIFDNPQSERLKRFLA 503
Cdd:PRK15134 512 RVFAAPQQEYTRQLLA 527
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
270-503 |
1.64e-28 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 114.12 E-value: 1.64e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAY---------GDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESiLAMKPES 340
Cdd:PRK15112 5 LEVRNLSKTFryrtgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHP-LHFGDYS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 341 LR-RRVGMVFQhfnlfpDHTALENVMLSLTKIKKMP-RSEARGIAEAR-------LTEVGLaeRKDHR---PAGLSGGQQ 408
Cdd:PRK15112 84 YRsQRIRMIFQ------DPSTSLNPRQRISQILDFPlRLNTDLEPEQRekqiietLRQVGL--LPDHAsyyPHMLAPGQK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 409 QRVAIARALAMDPEVILFDEVTSALDPELVKGVLDLMANLG-RQGMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQ 487
Cdd:PRK15112 156 QRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQeKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTA 235
|
250
....*....|....*.
gi 2017776620 488 QIFDNPQSERLKRFLA 503
Cdd:PRK15112 236 DVLASPLHELTKRLIA 251
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
270-503 |
2.31e-28 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 113.26 E-value: 2.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMaYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKStlLRCLNRL------VEPKRGDILLDGESILamkPESLR- 342
Cdd:PRK10418 5 IELRNIAL-QAAQPLVHGVSLTLQRGRVLALVGGSGSGKS--LTCAAALgilpagVRQTAGRVLLDGKPVA---PCALRg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 343 RRVGMVFQH----FNlfPDHTALENVMLSLTKIKKmPRSEARGIAEarLTEVGLAERK---DHRPAGLSGGQQQRVAIAR 415
Cdd:PRK10418 79 RKIATIMQNprsaFN--PLHTMHTHARETCLALGK-PADDATLTAA--LEAVGLENAArvlKLYPFEMSGGMLQRMMIAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 416 ALAMDPEVILFDEVTSALDPELVKGVLDLMANLGR-QGMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQIFDNPQ 494
Cdd:PRK10418 154 ALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQkRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPK 233
|
....*....
gi 2017776620 495 SERLKRFLA 503
Cdd:PRK10418 234 HAVTRSLVS 242
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
284-481 |
4.61e-28 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 112.49 E-value: 4.61e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 284 VLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPESLRRRVGMVFQHFNL--FPDHTAL 361
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAKYIGRVFQDPMMgtAPSMTIE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 362 ENVMLSLTKIKKmpRSEARGIAEARLTEV---------GLAERKDHRPAGLSGGQQQrvaiARALAM----DPEVILFDE 428
Cdd:COG1101 101 ENLALAYRRGKR--RGLRRGLTKKRRELFrellatlglGLENRLDTKVGLLSGGQRQ----ALSLLMatltKPKLLLLDE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2017776620 429 VTSALDPELVKGVLDLMANL-GRQGMTMAVVTHEMGFARRVADQVVFMDEGRII 481
Cdd:COG1101 175 HTAALDPKTAALVLELTEKIvEENNLTTLMVTHNMEQALDYGNRLIMMHEGRII 228
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
270-486 |
5.41e-28 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 110.69 E-value: 5.41e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCL--NRLVEPKRGDILLDGESILAMKP-ESLRRRVG 346
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTImgHPKYEVTEGEILFKGEDITDLPPeERARLGIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 347 MVFQHfnlfPdhTALENVmlsltKIKKMPRSeargiaearlteVGlaerkdhrpAGLSGGQQQRVAIARALAMDPEVILF 426
Cdd:cd03217 81 LAFQY----P--PEIPGV-----KNADFLRY------------VN---------EGFSGGEKKRNEILQLLLLEPDLAIL 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2017776620 427 DEVTSALDPELVKGVLDLMANLGRQGMTMAVVTH-EMGFARRVADQVVFMDEGRIIEAGSP 486
Cdd:cd03217 129 DEPDSGLDIDALRLVAEVINKLREEGKSVLIITHyQRLLDYIKPDRVHVLYDGRIVKSGDK 189
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
248-489 |
9.84e-28 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 116.44 E-value: 9.84e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 248 VGELRAASSTAVGNEprfkagALRVRDLSMAYGDLD--VLKGVD---LDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPK 322
Cdd:TIGR03269 264 VSEVEKECEVEVGEP------IIKVRNVSKRYISVDrgVVKAVDnvsLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPT 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 323 RGDI-LLDGESILAM-KPESL-----RRRVGMVFQHFNLFPDHTALENVMLSLTKikKMPRSEARGIAEARLTEVGLAER 395
Cdd:TIGR03269 338 SGEVnVRVGDEWVDMtKPGPDgrgraKRYIGILHQEYDLYPHRTVLDNLTEAIGL--ELPDELARMKAVITLKMVGFDEE 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 396 K-----DHRPAGLSGGQQQRVAIARALAMDPEVILFDEVTSALDPELVKGVLDLMANlGRQGM--TMAVVTHEMGFARRV 468
Cdd:TIGR03269 416 KaeeilDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILK-AREEMeqTFIIVSHDMDFVLDV 494
|
250 260
....*....|....*....|.
gi 2017776620 469 ADQVVFMDEGRIIEAGSPQQI 489
Cdd:TIGR03269 495 CDRAALMRDGKIVKIGDPEEI 515
|
|
| TM_PBP2 |
cd06261 |
Transmembrane subunit (TM) found in Periplasmic Binding Protein (PBP)-dependent ATP-Binding ... |
29-215 |
1.73e-27 |
|
Transmembrane subunit (TM) found in Periplasmic Binding Protein (PBP)-dependent ATP-Binding Cassette (ABC) transporters which generally bind type 2 PBPs. These types of transporters consist of a PBP, two TMs, and two cytoplasmic ABC ATPase subunits, and are mainly involved in importing solutes from the environment. The solute is captured by the PBP which delivers it to a gated translocation pathway formed by the two TMs. The two ABCs bind and hydrolyze ATP and drive the transport reaction. For these transporters the ABCs and TMs are on independent polypeptide chains. These systems transport a diverse range of substrates. Most are specific for a single substrate or a group of related substrates; however some transporters are more promiscuous, transporting structurally diverse substrates such as the histidine/lysine and arginine transporter in Enterobacteriaceae. In the latter case, this is achieved through binding different PBPs with different specificities to the TMs. For other promiscuous transporters such as the multiple-sugar transporter Msm of Streptococcus mutans, the PBP has a wide substrate specificity. These transporters include the maltose-maltodextrin, phosphate and sulfate transporters, among others.
Pssm-ID: 119394 [Multi-domain] Cd Length: 190 Bit Score: 108.91 E-value: 1.73e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 29 LKNTLILAAASTVLGVIIGMVLAVMGISQSRWLRLPARIYTDIFRGLPAIVTILIIGQGFARIGRELFGPSPFPLGIIAL 108
Cdd:cd06261 1 LLNTLLLALIATLLALVLGLLLGIILARKRGKLDRLLRRIIDLLLSLPSLVLGLLLVLLFGVLLGWGILPGLGLPALILA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 109 SLIAGAYIGEIFRSGIQSVERGQMEACRALSMSYGQGMRLIVIPQGVRRVLPALVNQFIGNVKDSSLVYFLGLLASEREI 188
Cdd:cd06261 81 LLLIAPFARLIRRAALESIPKDLVEAARALGASPWQIFRRIILPLALPPILTGLVLAFARALGEFALVSFLGGGEAPGPG 160
|
170 180
....*....|....*....|....*..
gi 2017776620 189 FRVGQDQAVVTGNLSPLLLAGVFYLLI 215
Cdd:cd06261 161 TGLLLIFAILFPGDLGVAAAVALILLL 187
|
|
| PRK15107 |
PRK15107 |
glutamate/aspartate ABC transporter permease GltK; |
13-229 |
3.23e-27 |
|
glutamate/aspartate ABC transporter permease GltK;
Pssm-ID: 185062 [Multi-domain] Cd Length: 224 Bit Score: 109.15 E-value: 3.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 13 DWDAMAEVLPSMITvGLKNTLILAAASTVLGVIIGMVLAVMGISQSRWLRLPARIYTDIFRGLPAIVTILIIGQGFARIG 92
Cdd:PRK15107 5 DWSSIVPSLPYLLD-GLVITLKITVTAVVIGILWGTILAVMRLSSFKPVAWFAKAYVNVFRSIPLVMVLLWFYLIVPGFL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 93 RELFGPSP-----FPLGIIALSLIAGAYIGEIFRSGIQSVERGQMEACRALSMSYGQGMRLIVIPQGVRRVLPALVNQFI 167
Cdd:PRK15107 84 QNVLGLSPktdirLISAMVAFSMFEAAYYSEIIRAGIQSISRGQSSAALALGMTHWQSMKLIILPQAFRAMVPLLLTQGI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2017776620 168 GNVKDSSLVYFLGLLASEREIFRVGQDQAVvtgNLSPLLLAGVFYLLITVPLTHFVNYIDAR 229
Cdd:PRK15107 164 VLFQDTSLVYVLSLADFFRTASTIGERDGT---QVEMILFAGFVYFVISLSASLLVSYLKKR 222
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
269-480 |
5.55e-26 |
|
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: 104.44 E-value: 5.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 269 ALRVRDLSMAygdlDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPESLRRRvGMV 348
Cdd:cd03215 4 VLEVRGLSVK----GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRA-GIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 349 F-----QHFNLFPDHTALENVMLsltkikkmprseargiaearltevglaerkdhrPAGLSGGQQQRVAIARALAMDPEV 423
Cdd:cd03215 79 YvpedrKREGLVLDLSVAENIAL---------------------------------SSLLSGGNQQKVVLARWLARDPRV 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2017776620 424 ILFDEVTSALDPELVKGVLDLMANLGRQGMTMAVVTHEMGFARRVADQVVFMDEGRI 480
Cdd:cd03215 126 LILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
268-485 |
6.07e-26 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 111.26 E-value: 6.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 268 GALRVRDLSMAY--GDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPESLRRRV 345
Cdd:PRK11176 340 GDIEFRNVTFTYpgKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQV 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 346 GMVFQHFNLFPDhTALENVMLSLTKikKMPRSEArgIAEARLT---------EVGLAERKDHRPAGLSGGQQQRVAIARA 416
Cdd:PRK11176 420 ALVSQNVHLFND-TIANNIAYARTE--QYSREQI--EEAARMAyamdfinkmDNGLDTVIGENGVLLSGGQRQRIAIARA 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2017776620 417 LAMDPEVILFDEVTSALDPELVKGVLDLMANLgRQGMTMAVVTHEMGFARRvADQVVFMDEGRIIEAGS 485
Cdd:PRK11176 495 LLRDSPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLSTIEK-ADEILVVEDGEIVERGT 561
|
|
| PRK11123 |
PRK11123 |
arginine ABC transporter permease ArtQ; |
17-240 |
8.57e-26 |
|
arginine ABC transporter permease ArtQ;
Pssm-ID: 182979 [Multi-domain] Cd Length: 238 Bit Score: 105.53 E-value: 8.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 17 MAEVLPSMITVGLknTLILAAASTVLGVIIGMVLAVMGISQSRWLRLPARIYTDIFRGLPAIVTILII------------ 84
Cdd:PRK11123 1 MNEFFPLASAAGM--TVGLAVCALIVGLALAMLFAVWESAKWRPVAWPGTALVTLLRGLPEILVVLFIyfgssqllltls 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 85 ---------GQGFARIGRELFGPSPFPLGIIALSLIAGAYIGEIFRSGIQSVERGQMEACRALSMSYGQGMRLIVIPQGV 155
Cdd:PRK11123 79 dgftlnlgfVQIPVQMDIENFEVSPFLCGVIALSLLYAAYASQTLRGALKAVPVGQWESGQALGLSKSAIFFRLVMPQMW 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 156 RRVLPALVNQFIGNVKDSSLVYFLGLlaseREIFRvgQDQAVVTGNLSPL---LLAGVFYLLITVPLTHFVNYIDarLRL 232
Cdd:PRK11123 159 RHALPGLGNQWLVLLKDTALVSLISV----NDLML--QTKSIATRTQEPFtwyIIAAAIYLVITLISQYILKRIE--LRA 230
|
....*...
gi 2017776620 233 GRQGRGSG 240
Cdd:PRK11123 231 TRFERRPS 238
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
271-489 |
1.10e-24 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 102.94 E-value: 1.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 271 RVRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPESLRRRVGMVFQ 350
Cdd:PRK10575 13 ALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 351 HFNLFPDHTALEnvmlsLTKIKKMP--------RSEARGIAEARLTEVGLAERKDHRPAGLSGGQQQRVAIARALAMDPE 422
Cdd:PRK10575 93 QLPAAEGMTVRE-----LVAIGRYPwhgalgrfGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSR 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2017776620 423 VILFDEVTSALDPELVKGVLDLMANLGRQ-GMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQI 489
Cdd:PRK10575 168 CLLLDEPTSALDIAHQVDVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
263-484 |
1.36e-24 |
|
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: 101.84 E-value: 1.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 263 PRFKAGALRVRDLSMA-----YGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGE--SILA 335
Cdd:cd03220 11 PTYKGGSSSLKKLGILgrkgeVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRvsSLLG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 336 MkpeslrrrvGMVFQhfnlfPDHTALENVMLSLTkIKKMPRSEARgiaeARLTEV-GLAERKD--HRPAG-LSGGQQQRV 411
Cdd:cd03220 91 L---------GGGFN-----PELTGRENIYLNGR-LLGLSRKEID----EKIDEIiEFSELGDfiDLPVKtYSSGMKARL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2017776620 412 AIARALAMDPEVILFDEVTSALDPELVKGVLDLMANLGRQGMTMAVVTHEMGFARRVADQVVFMDEGRIIEAG 484
Cdd:cd03220 152 AFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
247-481 |
3.16e-24 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 105.49 E-value: 3.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 247 EVGELRAASSTAVGNEprfkagALRVRDLSMAygdlDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDI 326
Cdd:COG1129 240 ELEDLFPKRAAAPGEV------VLEVEGLSVG----GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEI 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 327 LLDGESI------------LAMKPESlRRRVGmvfqhfnLFPDHTALENVML-SLTKIKK---MPRSEARGIAEARLTEV 390
Cdd:COG1129 310 RLDGKPVrirsprdairagIAYVPED-RKGEG-------LVLDLSIRENITLaSLDRLSRgglLDRRRERALAEEYIKRL 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 391 GLAERKDHRPAG-LSGGQQQRVAIARALAMDPEVILFDEVTsaldpelvKGV--------LDLMANLGRQGMTMAVVTHE 461
Cdd:COG1129 382 RIKTPSPEQPVGnLSGGNQQKVVLAKWLATDPKVLILDEPT--------RGIdvgakaeiYRLIRELAAEGKAVIVISSE 453
|
250 260
....*....|....*....|
gi 2017776620 462 MGFARRVADQVVFMDEGRII 481
Cdd:COG1129 454 LPELLGLSDRILVMREGRIV 473
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
270-463 |
3.42e-24 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 99.74 E-value: 3.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPEslRRRVGMVF 349
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDE--PHENILYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 350 QHFN-LFPDHTALENvmlsLTKIKKMPRSEARGIAEArLTEVGLAERkDHRPAG-LSGGQQQRVAIARALAMDPEVILFD 427
Cdd:TIGR01189 79 GHLPgLKPELSALEN----LHFWAAIHGGAQRTIEDA-LAAVGLTGF-EDLPAAqLSAGQQRRLALARLWLSRRPLWILD 152
|
170 180 190
....*....|....*....|....*....|....*..
gi 2017776620 428 EVTSALDPELVKGVLDLM-ANLGRQGMTMAVVTHEMG 463
Cdd:TIGR01189 153 EPTTALDKAGVALLAGLLrAHLARGGIVLLTTHQDLG 189
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
270-479 |
7.30e-24 |
|
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: 99.08 E-value: 7.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAYGD-----LDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLnrLvepkrGDI-LLDGESilamkpeSLRR 343
Cdd:cd03250 1 ISVEDASFTWDSgeqetSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSAL--L-----GELeKLSGSV-------SVPG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 344 RVGMVFQ---HFN-------LF--P-DHTALENVM--LSLTK-IKKMPRSEargiaearLTEVGlaERkdhrpaG--LSG 405
Cdd:cd03250 67 SIAYVSQepwIQNgtireniLFgkPfDEERYEKVIkaCALEPdLEILPDGD--------LTEIG--EK------GinLSG 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2017776620 406 GQQQRVAIARALAMDPEVILFDEVTSALDPELVKGVLD-LMANLGRQGMTMAVVTHEMGFARRvADQVVFMDEGR 479
Cdd:cd03250 131 GQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFEnCILGLLLNNKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
270-498 |
8.85e-24 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 99.97 E-value: 8.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESIlAMKP--ESLRRRVGM 347
Cdd:PRK10895 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDI-SLLPlhARARRGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 348 VFQHFNLFPDHTALENVMLSLTKIKKMPRSEARGIAEARLTEVGLAERKDHRPAGLSGGQQQRVAIARALAMDPEVILFD 427
Cdd:PRK10895 83 LPQEASIFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLD 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2017776620 428 EVTSALDPELVKGVLDLMANLGRQGMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQIFDNPQSERL 498
Cdd:PRK10895 163 EPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRV 233
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
297-486 |
1.11e-23 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 105.48 E-value: 1.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 297 VTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESIlAMKPESLRRRVGMVFQHFNLFPDHTALENvMLSLTKIKKMPR 376
Cdd:TIGR01257 958 ITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHHLTVAEH-ILFYAQLKGRSW 1035
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 377 SEARGIAEARLTEVGLAERKDHRPAGLSGGQQQRVAIARALAMDPEVILFDEVTSALDPELVKGVLDLMANLgRQGMTMA 456
Cdd:TIGR01257 1036 EEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKY-RSGRTII 1114
|
170 180 190
....*....|....*....|....*....|
gi 2017776620 457 VVTHEMGFARRVADQVVFMDEGRIIEAGSP 486
Cdd:TIGR01257 1115 MSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
270-505 |
1.69e-23 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 104.17 E-value: 1.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAY----GDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDG-------ESILAMKP 338
Cdd:PRK10261 13 LAVENLNIAFmqeqQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsRQVIELSE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 339 ES---LRRRVG----MVFQH--FNLFPDHTALENVMLSLTKIKKMPRSEARGIAEARLTEVGLAERK---DHRPAGLSGG 406
Cdd:PRK10261 93 QSaaqMRHVRGadmaMIFQEpmTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQtilSRYPHQLSGG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 407 QQQRVAIARALAMDPEVILFDEVTSALDPELVKGVLDLMANLgRQGMTMAV--VTHEMGFARRVADQVVFMDEGRIIEAG 484
Cdd:PRK10261 173 MRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVL-QKEMSMGVifITHDMGVVAEIADRVLVMYQGEAVETG 251
|
250 260
....*....|....*....|.
gi 2017776620 485 SPQQIFDNPQSERLKRFLAEV 505
Cdd:PRK10261 252 SVEQIFHAPQHPYTRALLAAV 272
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
285-488 |
1.75e-23 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 103.97 E-value: 1.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 285 LKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEP---KRGDILLDGESILAmkpESLRRRVGMVFQHFNLFPDHTAL 361
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPIDA---KEMRAISAYVQQDDLFIPTLTVR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 362 ENVMLSLTKikKMPR----SEARGIAEARLTEVGLAERKD------HRPAGLSGGQQQRVAIARALAMDPEVILFDEVTS 431
Cdd:TIGR00955 118 EHLMFQAHL--RMPRrvtkKEKRERVDEVLQALGLRKCANtrigvpGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTS 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 432 ALDPELVKGVLDLMANLGRQGMTMAVVTHEMG---FarRVADQVVFMDEGRIIEAGSPQQ 488
Cdd:TIGR00955 196 GLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSselF--ELFDKIILMAEGRVAYLGSPDQ 253
|
|
| glnP |
PRK09494 |
glutamine ABC transporter permease protein; Reviewed |
13-232 |
2.05e-23 |
|
glutamine ABC transporter permease protein; Reviewed
Pssm-ID: 181907 [Multi-domain] Cd Length: 219 Bit Score: 98.20 E-value: 2.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 13 DWDAMAEVLPSMITvGLKNTLILAAASTVLGVIIGMVLAVMGISQSRWLRLPARIYTDIFRGLPAIVTILIIGqgFA--- 89
Cdd:PRK09494 4 DWSAIWPAIPLLLE-GAKMTLWISVLGLAGGLVIGLLAGFARAYGGWIANHIALVFIELIRGTPIVVQVMFIY--FAlpm 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 90 -----RIgrelfgpSPFPLGIIALSLIAGAYIGEIFRSGIQSVERGQMEACRALSMSYGQGMRLIVIPQGVRRVLPALVN 164
Cdd:PRK09494 81 afndlRI-------DPFTAAVVTIMINSGAYIAEITRGAVLSIHKGFREAGLALGLSRRETLRYVIGPLALRRMLPPLGN 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2017776620 165 QFIGNVKDSSLVYFLGLlaseREIFRVGQDqaVVTGNLSPLLL---AGVFYLLITVPLTHFVNYIDARLRL 232
Cdd:PRK09494 154 QWIISIKDTSLFIVIGV----AELTRQGQE--IIAGNFRALEIwsaVAVIYLIITLVLSFILRRLERRMKI 218
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
268-486 |
2.35e-23 |
|
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: 97.87 E-value: 2.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 268 GALRVRDLSMAYG-DL-DVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPESLRRRV 345
Cdd:cd03369 5 GEIEVENLSVRYApDLpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 346 GMVFQHFNLFPDhtaleNVMLSLTKIKKMprSEARGIAEARLTEVGLaerkdhrpaGLSGGQQQRVAIARALAMDPEVIL 425
Cdd:cd03369 85 TIIPQDPTLFSG-----TIRSNLDPFDEY--SDEEIYGALRVSEGGL---------NLSQGQRQLLCLARALLKRPRVLV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2017776620 426 FDEVTSAL----DPELVKGVLDLMANlgrqgMTMAVVTHEMgfaRRVA--DQVVFMDEGRIIEAGSP 486
Cdd:cd03369 149 LDEATASIdyatDALIQKTIREEFTN-----STILTIAHRL---RTIIdyDKILVMDAGEVKEYDHP 207
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
280-494 |
3.35e-23 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 100.72 E-value: 3.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 280 GDLDvLKgVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDI------LLDGESILAMKPEslRRRVGMVFQHFN 353
Cdd:PRK11144 11 GDLC-LT-VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIvlngrvLFDAEKGICLPPE--KRRIGYVFQDAR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 354 LFPDHTALENVMLSLTKikKMPrseargiAE-ARLTE-VGLAERKDHRPAGLSGGQQQRVAIARALAMDPEVILFDEVTS 431
Cdd:PRK11144 87 LFPHYKVRGNLRYGMAK--SMV-------AQfDKIVAlLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2017776620 432 ALDPELVKGVLDLMANLGRQ-GMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQIFDNPQ 494
Cdd:PRK11144 158 SLDLPRKRELLPYLERLAREiNIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSA 221
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
270-489 |
3.49e-23 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 102.56 E-value: 3.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPE-SLRRRVGMV 348
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKlAAQLGIGII 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 349 FQHFNLFPDHTALENVMLSLTKIKK------MPRSEARGIAEARLTEVGLAERKDHRPAGLSGGQQQRVAIARALAMDPE 422
Cdd:PRK09700 86 YQELSVIDELTVLENLYIGRHLTKKvcgvniIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAK 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2017776620 423 VILFDEVTSALDPELVKGVLDLMANLGRQGMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQI 489
Cdd:PRK09700 166 VIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDV 232
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
270-460 |
5.90e-23 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 96.48 E-value: 5.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPESLRRRVGmvf 349
Cdd:PRK13539 3 LEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLG--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 350 qHFNLFPDH-TALENvmlsLTKIKKMPRSEARGIAEArLTEVGLAeRKDHRPAG-LSGGQQQRVAIARALAMDPEVILFD 427
Cdd:PRK13539 80 -HRNAMKPAlTVAEN----LEFWAAFLGGEELDIAAA-LEAVGLA-PLAHLPFGyLSAGQKRRVALARLLVSNRPIWILD 152
|
170 180 190
....*....|....*....|....*....|....
gi 2017776620 428 EVTSALDPELVKGVLDLM-ANLGRQGMTMAvVTH 460
Cdd:PRK13539 153 EPTAALDAAAVALFAELIrAHLAQGGIVIA-ATH 185
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
270-504 |
7.57e-23 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 99.05 E-value: 7.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAYGDLDV-LKGVD---LDIAPGTVTCIIGPSGSGKSTLLRCLNRLVE-PKR---GDILLDGESILAMKPESL 341
Cdd:PRK11022 4 LNVDKLSVHFGDESApFRAVDrisYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDyPGRvmaEKLEFNGQDLQRISEKER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 342 RRRVG----MVFQH--FNLFPDHTALENVMLSLTKIKKMPRSEARGIAEARLTEVGL---AERKDHRPAGLSGGQQQRVA 412
Cdd:PRK11022 84 RNLVGaevaMIFQDpmTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIpdpASRLDVYPHQLSGGMSQRVM 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 413 IARALAMDPEVILFDEVTSALDPELVKGVLDLMANLGRQ-GMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQIFD 491
Cdd:PRK11022 164 IAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKeNMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFR 243
|
250
....*....|....*.
gi 2017776620 492 NPQ---SERLKRFLAE 504
Cdd:PRK11022 244 APRhpyTQALLRALPE 259
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
270-482 |
1.03e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 101.29 E-value: 1.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLdGESIlamkpeslrrRVGMVF 349
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV----------KIGYFD 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 350 QHF-NLFPDHTALENVMLSLtkiKKMPRSEARGIAEArlteVGLAERKDHRPAG-LSGGQQQRVAIARALAMDPEVILFD 427
Cdd:COG0488 385 QHQeELDPDKTVLDELRDGA---PGGTEQEVRGYLGR----FLFSGDDAFKPVGvLSGGEKARLALAKLLLSPPNVLLLD 457
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2017776620 428 EVTSALDPELVKGVLDLMANLgrQGmTMAVVTHEMGFARRVADQVVFMDEGRIIE 482
Cdd:COG0488 458 EPTNHLDIETLEALEEALDDF--PG-TVLLVSHDRYFLDRVATRILEFEDGGVRE 509
|
|
| PRK15069 |
PRK15069 |
histidine ABC transporter permease HisM; |
28-219 |
9.75e-22 |
|
histidine ABC transporter permease HisM;
Pssm-ID: 185029 [Multi-domain] Cd Length: 234 Bit Score: 93.96 E-value: 9.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 28 GLKNTLILAAASTVLGVIIGMVLAVMGISQSRWLRLPARIYTDIFRGLPAIVTILIIGQGFARI----GREL---FGPSP 100
Cdd:PRK15069 22 GLAITLWLLVASVVIGFVLAVPLAIARVSSNKWIRFPVWLYTYVFRGTPLYVQLLVFYTGMYSLeivrGTDLldaFFRSG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 101 FPLGIIALSLIAGAYIGEIFRSGIQSVERGQMEACRALSMSYGQGMRLIVIPQGVRRVLPALVNQFIGNVKDSSLVYflg 180
Cdd:PRK15069 102 LNCTILAFTLNTCAYTTEIFAGAIRSVPHGEIEAARAYGMSTFKLYRRIILPSALRRALPAYSNEVILMLHATTLAF--- 178
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2017776620 181 lLASEREIFRVGQDQAVVT-GNLSPLLLAGVFYLLITVPL 219
Cdd:PRK15069 179 -TATVPDILKIARDINSATyQPFQAFGIAAVLYLIISFVL 217
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
270-485 |
2.60e-21 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 93.17 E-value: 2.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRlvEPK----RGDILLDGESILAMKPEsLRRRV 345
Cdd:CHL00131 8 LEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPAykilEGDILFKGESILDLEPE-ERAHL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 346 G--MVFQHFNLFPDHTALENVMLSL-TKIKKMPRSEARGIA-----EARLTEVGLAERKDHRPA--GLSGGQQQRVAIAR 415
Cdd:CHL00131 85 GifLAFQYPIEIPGVSNADFLRLAYnSKRKFQGLPELDPLEfleiiNEKLKLVGMDPSFLSRNVneGFSGGEKKRNEILQ 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2017776620 416 ALAMDPEVILFDEVTSALDPELVKGVLDLMANLGRQGMTMAVVTHemgFARR----VADQVVFMDEGRIIEAGS 485
Cdd:CHL00131 165 MALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITH---YQRLldyiKPDYVHVMQNGKIIKTGD 235
|
|
| HEQRo_perm_3TM |
TIGR01726 |
amine acid ABC transporter, permease protein, 3-TM region, His/Glu/Gln/Arg/opine family; This ... |
24-122 |
3.07e-21 |
|
amine acid ABC transporter, permease protein, 3-TM region, His/Glu/Gln/Arg/opine family; This model represents one of several classes of multiple membrane spanning regions found immediately N-terminal to the domain described by pfam00528, binding-protein-dependent transport systems inner membrane component. The region covered by this model generally is predicted to contain three transmembrane helices. Substrate specificities attributed to members of this family include histidine, arginine, glutamine, glutamate, and (in Agrobacterium) the opines octopine and nopaline. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130787 [Multi-domain] Cd Length: 99 Bit Score: 88.36 E-value: 3.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 24 MITVGLKNTLILAAASTVLGVIIGMVLAVMGISQSRWLRLPARIYTDIFRGLPAIVTILIIGQGFARIGRELfgpSPFPL 103
Cdd:TIGR01726 4 FLLKGLLLTLLLSVLSILLGLVLGLLLALLRLSGNRPLRWIATVYVELFRGTPLLVQLFFIYFGLPLIGIRL---SPLTA 80
|
90
....*....|....*....
gi 2017776620 104 GIIALSLIAGAYIGEIFRS 122
Cdd:TIGR01726 81 AVIALTLFYGAYLAEIFRG 99
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
281-493 |
1.39e-20 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 94.78 E-value: 1.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 281 DLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPESLRRRVGMVFQHFNLFPDHTA 360
Cdd:PRK10789 327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVA 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 361 lENVMLSLTKIKKMPRSEARGIAEA-----RL-----TEVGlaerkdHRPAGLSGGQQQRVAIARALAMDPEVILFDEVT 430
Cdd:PRK10789 407 -NNIALGRPDATQQEIEHVARLASVhddilRLpqgydTEVG------ERGVMLSGGQKQRISIARALLLNAEILILDDAL 479
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2017776620 431 SALDPELVKGVLDLMANLGrQGMTMAVVTHEMGfARRVADQVVFMDEGRIIEAGSPQQIFDNP 493
Cdd:PRK10789 480 SAVDGRTEHQILHNLRQWG-EGRTVIISAHRLS-ALTEASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
270-493 |
1.51e-20 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 92.48 E-value: 1.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAY----GDLDVLKGVDLDIAPGTVTCIIGPSGSGKS-TLLRCLNRLVEPKR--GDILLDGESILAMKPESLR 342
Cdd:PRK09473 13 LDVKDLRVTFstpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAANGRigGSATFNGREILNLPEKELN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 343 R----RVGMVFQH--FNLFPDHTALENVMLSLTKIKKMPRSEARGIAEARLTEVGLAE-RKDHR--PAGLSGGQQQRVAI 413
Cdd:PRK09473 93 KlraeQISMIFQDpmTSLNPYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMPEaRKRMKmyPHEFSGGMRQRVMI 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 414 ARALAMDPEVILFDEVTSALDPELVKGVLDLMANLGRQ-GMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQIFDN 492
Cdd:PRK09473 173 AMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQ 252
|
.
gi 2017776620 493 P 493
Cdd:PRK09473 253 P 253
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
253-495 |
1.73e-20 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 95.62 E-value: 1.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 253 AASSTAVGNEPrFKAGALRVRDLSMAY--GDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDG 330
Cdd:PTZ00243 1293 PASPTSAAPHP-VQAGSLVFEGVQMRYreGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNG 1371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 331 ESILAMKPESLRRRVGMVFQHFNLFpDHTALENV-------------MLSLTKIKKMPRSEARGIaEARLTEVGLaerkd 397
Cdd:PTZ00243 1372 REIGAYGLRELRRQFSMIPQDPVLF-DGTVRQNVdpfleassaevwaALELVGLRERVASESEGI-DSRVLEGGS----- 1444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 398 hrpaGLSGGQQQRVAIARA-LAMDPEVILFDEVTSALDPELVKGVldlmanlgrQGMTMA------VVThemgFARR--- 467
Cdd:PTZ00243 1445 ----NYSVGQRQLMCMARAlLKKGSGFILMDEATANIDPALDRQI---------QATVMSafsaytVIT----IAHRlht 1507
|
250 260 270
....*....|....*....|....*....|
gi 2017776620 468 VA--DQVVFMDEGRIIEAGSPQQIFDNPQS 495
Cdd:PTZ00243 1508 VAqyDKIIVMDHGAVAEMGSPRELVMNRQS 1537
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
270-481 |
3.59e-20 |
|
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: 93.35 E-value: 3.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRlVEPK---RGDILLDGESILAMK-PESLRRRV 345
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSG-VYPHgtwDGEIYWSGSPLKASNiRDTERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 346 GMVFQHFNLFPDHTALENVML--SLT-KIKKMPRSEARGIAEARLTEVGLAERKDHRPAG-LSGGQQQRVAIARALAMDP 421
Cdd:TIGR02633 81 VIIHQELTLVPELSVAENIFLgnEITlPGGRMAYNAMYLRAKNLLRELQLDADNVTRPVGdYGGGQQQLVEIAKALNKQA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 422 EVILFDEVTSALDPELVKGVLDLMANLGRQGMTMAVVTHEMGFARRVADQVVFMDEGRII 481
Cdd:TIGR02633 161 RLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHV 220
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
270-491 |
5.39e-20 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 89.13 E-value: 5.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAygdlDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVePKRGDILLDGESILAMKPESLRRRVGM-- 347
Cdd:COG4138 1 LQLNDVAVA----GRLGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAELARHRAYls 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 348 ----------VFQHFNLF----PDHTALENVMLSLTkikkmprsEARGIAEarltevglaerKDHRPAG-LSGGQQQRVA 412
Cdd:COG4138 76 qqqsppfampVFQYLALHqpagASSEAVEQLLAQLA--------EALGLED-----------KLSRPLTqLSGGEWQRVR 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 413 IARAL-----AMDPE--VILFDEVTSALDPELVKGVLDLMANLGRQGMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGS 485
Cdd:COG4138 137 LAAVLlqvwpTINPEgqLLLLDEPMNSLDVAQQAALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGE 216
|
....*.
gi 2017776620 486 PQQIFD 491
Cdd:COG4138 217 TAEVMT 222
|
|
| BatB |
COG4597 |
ABC-type amino acid transport system, permease component [Amino acid transport and metabolism]; ... |
24-175 |
1.07e-19 |
|
ABC-type amino acid transport system, permease component [Amino acid transport and metabolism];
Pssm-ID: 443651 [Multi-domain] Cd Length: 397 Bit Score: 90.98 E-value: 1.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 24 MITVGLKNTLILAAASTVLGVIIGMVLAVMGISQSRWLRLPARIYTDIFRGLPAIVTILI-----------------IGQ 86
Cdd:COG4597 87 AFLVGLLNTLLVAVLGIVLATILGFLVGIARLSSNWLVSKLATVYVEIFRNIPLLLQIFFwyfavlealpsprqslsLFD 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 87 GFARIGRELFGPSP-------------------------------------FPLGIIALSLIAG---------------- 113
Cdd:COG4597 167 GVFLNNRGLYLPAPvfepgfgwvlaallaaivaafvlrrwarrrqeatgqrFPVWWISLALLVGlpllaflllgaplsld 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 114 -------------------------------AYIGEIFRSGIQSVERGQMEACRALSMSYGQGMRLIVIPQGVRRVLPAL 162
Cdd:COG4597 247 ypelkgfnfrggltlspefvalllalslytaAFIAEIVRAGIQAVSKGQTEAARALGLRPGQTLRLVVLPQALRVIIPPL 326
|
250
....*....|...
gi 2017776620 163 VNQFIGNVKDSSL 175
Cdd:COG4597 327 TSQYLNLTKNSSL 339
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
270-481 |
1.13e-19 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 88.01 E-value: 1.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPES-LRRRVGMV 348
Cdd:PRK11614 6 LSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKiMREAVAIV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 349 FQHFNLFPDHTALENVMLSLTKIKKMPRSEArgIAEARLTEVGLAERKDHRPAGLSGGQQQRVAIARALAMDPEVILFDE 428
Cdd:PRK11614 86 PEGRRVFSRMTVEENLAMGGFFAERDQFQER--IKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2017776620 429 VTSALDPELVKGVLDLMANLGRQGMTMAVVTHEMGFARRVADQVVFMDEGRII 481
Cdd:PRK11614 164 PSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVV 216
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
270-492 |
1.51e-19 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 91.65 E-value: 1.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPeSLRRRVG--M 347
Cdd:PRK15439 12 LCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTP-AKAHQLGiyL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 348 VFQHFNLFPDHTALENVMLSLTkikKMPRSEARgiAEARLTEVGLAERKDHRPAGLSGGQQQRVAIARALAMDPEVILFD 427
Cdd:PRK15439 91 VPQEPLLFPNLSVKENILFGLP---KRQASMQK--MKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2017776620 428 EVTSALDPELVKGVLDLMANLGRQGMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQIFDN 492
Cdd:PRK15439 166 EPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTD 230
|
|
| ectoine_ehuC |
TIGR03004 |
ectoine/hydroxyectoine ABC transporter, permease protein EhuC; Members of this family are ... |
24-236 |
2.47e-19 |
|
ectoine/hydroxyectoine ABC transporter, permease protein EhuC; Members of this family are presumed to act as permease subunits of ectoine ABC transporters. Operons containing this gene also contain the other genes of the ABC transporter and typically are found next to either ectoine utilization or ectoine biosynthesis operons. Permease subunits EhuC and EhuD are homologous.
Pssm-ID: 132049 [Multi-domain] Cd Length: 214 Bit Score: 86.44 E-value: 2.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 24 MITVGLKNTLILAAASTVLGVIIGMVLAVMGISQSRWLRLPARIYTDIFRGLPAIVTILIIGQGFARIGRELfgpSPFPL 103
Cdd:TIGR03004 6 LLLQGAWVTMQITLAGSVLATVLAFFAGLGRVSGGPILRTVALCYIEVFRGTSLLVQLFWFYFVLPLIGLSL---DPVTT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 104 GIIALSLIAGAYIGEIFRSGIQSVERGQMEACRALSMSYGQGMRLIVIPQGVRRVLPALVNQFIGNVKDSSLVyflGLLA 183
Cdd:TIGR03004 83 GVMVLGLHAGAYGAEIVRGALSSVSVQQLEACRALNFTRFQTLRRISLPQALVEMMPAFGNLAIELLKLTSLV---SLIS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2017776620 184 SEREIFRVGQDQAVVTGNLSPLLLAGVFYLLITVPLTHFVNYIDARLRLGRQG 236
Cdd:TIGR03004 160 LADLTFAAQSIRNLTLDTLSIFAITLLCYFVMALIIMLIMRVLERVVRRGNVF 212
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
270-465 |
2.55e-19 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 86.01 E-value: 2.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPESLRrrvgmvf 349
Cdd:PRK13538 2 LEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQ------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 350 qhfNLF---------PDHTALENvMLSLTKIKKMPRSEArgIAEArLTEVGLAERKDhRPAG-LSGGQQQRVAIARALAM 419
Cdd:PRK13538 75 ---DLLylghqpgikTELTALEN-LRFYQRLHGPGDDEA--LWEA-LAQVGLAGFED-VPVRqLSAGQQRRVALARLWLT 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2017776620 420 DPEVILFDEVTSALDpelVKGVLDL----MANLGRQGmtMAVVT--HEMGFA 465
Cdd:PRK13538 147 RAPLWILDEPFTAID---KQGVARLeallAQHAEQGG--MVILTthQDLPVA 193
|
|
| BPD_transp_1 |
pfam00528 |
Binding-protein-dependent transport system inner membrane component; The alignments cover the ... |
43-231 |
4.16e-19 |
|
Binding-protein-dependent transport system inner membrane component; The alignments cover the most conserved region of the proteins, which is thought to be located in a cytoplasmic loop between two transmembrane domains. The members of this family have a variable number of transmembrane helices.
Pssm-ID: 334128 [Multi-domain] Cd Length: 183 Bit Score: 85.04 E-value: 4.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 43 GVIIGMVLAVMgisQSRWLRLPARIYTDIFRGLPAIVTILIIgqgFARIGRELFGPSPFPlGIIALSLIAGAYIGEIFRS 122
Cdd:pfam00528 1 GIPLGIIAALR---RGRRLDRLLRPLIDLLQALPSFVLAILL---VVIAILSILGHGILP-AIILALLGWAGYARLIRRA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 123 GIQSVERGQMEACRALSMSYGQGMRLIVIPQGVRRVLPALVNQFIGNVKDSSLVYFLGLLASEREIFRVGQDQAVVTGNL 202
Cdd:pfam00528 74 ALRSLPSDLVEAARALGASRWQIFRKIILPNALPPILTGLALAFGGALGGAVLLEFLGSWPGLGLLLIEAILGYDYPEIQ 153
|
170 180
....*....|....*....|....*....
gi 2017776620 203 SPLLLAGVFYLLITVPLTHFVNYIDARLR 231
Cdd:pfam00528 154 GPVLAAALILLLLNLLVDILQRLLDPRVR 182
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
267-460 |
4.65e-19 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 90.25 E-value: 4.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 267 AGALRVRDLSMAYGDLDVL-KGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILL-DGESILAM--KP---- 338
Cdd:COG4178 360 DGALALEDLTLRTPDGRPLlEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARVLFLpqRPylpl 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 339 ESLRRRVgmvfqhfnLFPDHTAlenvmlsltkikKMPRSEargIAEArLTEVGLA------ERKDHRPAGLSGGQQQRVA 412
Cdd:COG4178 440 GTLREAL--------LYPATAE------------AFSDAE---LREA-LEAVGLGhlaerlDEEADWDQVLSLGEQQRLA 495
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2017776620 413 IARALAMDPEVILFDEVTSALDPELVKGVLDLMANLgRQGMTMAVVTH 460
Cdd:COG4178 496 FARLLLHKPDWLFLDEATSALDEENEAALYQLLREE-LPGTTVISVGH 542
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
250-490 |
5.78e-19 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 90.16 E-value: 5.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 250 ELRAASSTAVGNEPR-FKAGALRVRDLSMAY-GDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDIL 327
Cdd:PRK10790 320 ELMDGPRQQYGNDDRpLQSGRIDIDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIR 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 328 LDGESILAMKPESLRRRVGMVFQHFNLFPDhTALENVMLsltkikkmprseARGIAEAR----LTEVGLAERKDHRPAG- 402
Cdd:PRK10790 400 LDGRPLSSLSHSVLRQGVAMVQQDPVVLAD-TFLANVTL------------GRDISEEQvwqaLETVQLAELARSLPDGl 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 403 ----------LSGGQQQRVAIARALAMDPEVILFDEVTSALDPELVKGVLDLMANLgRQGMTMAVVTHEMGFARRvADQV 472
Cdd:PRK10790 467 ytplgeqgnnLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAV-REHTTLVVIAHRLSTIVE-ADTI 544
|
250
....*....|....*...
gi 2017776620 473 VFMDEGRIIEAGSPQQIF 490
Cdd:PRK10790 545 LVLHRGQAVEQGTHQQLL 562
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
267-482 |
7.80e-19 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 89.20 E-value: 7.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 267 AGALRVRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESI-LAMKPESLRRRV 345
Cdd:PRK11288 2 SPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrFASTTAALAAGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 346 GMVFQHFNLFPDHTALENVMLSL--TKIKKMPRSEARGIAEARLTEVGLAERKDHRPAGLSGGQQQRVAIARALAMDPEV 423
Cdd:PRK11288 82 AIIYQELHLVPEMTVAENLYLGQlpHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 424 ILFDEVTSALDPELVKGVLDLMANLGRQGMTMAVVTHEMGFARRVADQV-VFMDeGRIIE 482
Cdd:PRK11288 162 IAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAItVFKD-GRYVA 220
|
|
| PRK15135 |
PRK15135 |
histidine ABC transporter permease HisQ; |
24-181 |
7.97e-19 |
|
histidine ABC transporter permease HisQ;
Pssm-ID: 185089 [Multi-domain] Cd Length: 228 Bit Score: 85.23 E-value: 7.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 24 MITVGLKNTLILAAASTVLGVIIGMVLAVMGISQSRWLRLPARIYTDIFRGLPAIVTILIIGQGFA--------RIGREL 95
Cdd:PRK15135 8 VILQGALVTLELALSSVVLAVIIGLIGAGGKLSQNRLLGLIFEGYTTLIRGVPDLVLMLLIFYGLQialnsvteALGVGQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 96 FGPSPFPLGIIALSLIAGAYIGEIFRSGIQSVERGQMEACRALSMSYGQGMRLIVIPQGVRRVLPALVNQFIGNVKDSSL 175
Cdd:PRK15135 88 IDIDPMVAGIITLGFIYGAYFTETFRGAFMAVPKGHIEAATAFGFTRGQVFRRIMFPAMMRYALPGIGNNWQVILKATAL 167
|
....*.
gi 2017776620 176 VYFLGL 181
Cdd:PRK15135 168 VSLLGL 173
|
|
| PhnE |
TIGR01097 |
phosphonate ABC transporter, permease protein PhnE; Phosphonates are a class of compound ... |
13-180 |
1.61e-18 |
|
phosphonate ABC transporter, permease protein PhnE; Phosphonates are a class of compound analogous to organic phosphates, but in which the C-O-P linkage is replaced by a direct, stable C-P bond. Some bacteria can utilize phosphonates as a source of phosphorus. This family consists of permease proteins of known or predicted phosphonate ABC transporters. Often this protein is found as a duplicated pair, occasionally as a fused pair. Certain "second" copies score in between the trusted and noise cutoff and should be considered true hits (by context). [Transport and binding proteins, Anions]
Pssm-ID: 273441 [Multi-domain] Cd Length: 250 Bit Score: 84.90 E-value: 1.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 13 DWDAMAEVLPSMItvglkNTLILAAASTVLGVIIGMVLAVMG---ISQSRWLRLPARIYTDIFRGLPAIVTILIigqgFA 89
Cdd:TIGR01097 49 DWSYLPRILKALL-----ETLAMAILGTVLAAVLAVPLALLAarnITPSPWLYGLARLLLNFLRAIPELVWALI----FV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 90 RIgrelFGPSPFPlGIIALSLIAGAYIGEIFRSGIQSVERGQMEACRALSMSYGQGMRLIVIPQgvrrVLPALVN----Q 165
Cdd:TIGR01097 120 AA----VGLGPFA-GVLALAFHTVGFLGKLFAEAIEEVDPGPVEALRATGASKLQVIRYGVLPQ----VLPQFLSytlyR 190
|
170
....*....|....*
gi 2017776620 166 FIGNVKDSSLVYFLG 180
Cdd:TIGR01097 191 FEINVRAAAVLGLVG 205
|
|
| artM |
PRK11122 |
arginine ABC transporter permease ArtM; |
17-229 |
2.63e-18 |
|
arginine ABC transporter permease ArtM;
Pssm-ID: 182978 [Multi-domain] Cd Length: 222 Bit Score: 83.85 E-value: 2.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 17 MAEVLPSMITvGLKNTLILAAASTVLGVIIGMVLAVMGISQSRWLRLPARIYTDIFRGLPAIVTILIIgqgfarigreLF 96
Cdd:PRK11122 1 MLEYLPELLK-GLHTSLTLTVASLLVALVLALIFTIILTLKTPVLVWLVRGYITLFTGTPLLVQIFLI----------YY 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 97 GPSPFP-----------------LGIIALSLIAGAYIGEIFRSGIQSVERGQMEACRALSMSYGQGMRlIVIPQGVRRVL 159
Cdd:PRK11122 70 GPGQFPwlqeypwlwhllsqpwlCAMLALALNSAAYSTQLFYGAVRAIPEGQWQSCAALGMSKKQTLR-ILLPYAFKRAL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 160 PALVNQFIGNVKDSSLVYFLGLLaserEIFRVGQDQAVVTGNLSPLLLAGVFYLLITVPLTHFVNYIDAR 229
Cdd:PRK11122 149 SSYSNEVVLVFKSTSLAYTITLM----DVMGYSQLLYGRTYDVMVFGAAGIIYLVVNGLLTLLMRLIERK 214
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
240-489 |
3.72e-18 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 87.59 E-value: 3.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 240 GAASGLVEVGELRAASSTAVGNEPRFKAG-ALRVRDLSMAYGDLDVLKG-VDLDIAPGTVTCIIGPSGSGKSTLLrclNR 317
Cdd:PRK11174 319 GAAESLVTFLETPLAHPQQGEKELASNDPvTIEAEDLEILSPDGKTLAGpLNFTLPAGQRIALVGPSGAGKTSLL---NA 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 318 LVE--PKRGDILLDGESILAMKPESLRRRVGMVFQHFNLFPDhTALENVML---SLTKIKKMPRSEARGIAE--ARLTEv 390
Cdd:PRK11174 396 LLGflPYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHG-TLRDNVLLgnpDASDEQLQQALENAWVSEflPLLPQ- 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 391 GLAERKDHRPAGLSGGQQQRVAIARALAMDPEVILFDEVTSALDPELVKGVLDLMANLGRQGMTMaVVTHEMGFARRVaD 470
Cdd:PRK11174 474 GLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTL-MVTHQLEDLAQW-D 551
|
250
....*....|....*....
gi 2017776620 471 QVVFMDEGRIIEAGSPQQI 489
Cdd:PRK11174 552 QIWVMQDGQIVQQGDYAEL 570
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
271-460 |
4.37e-18 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 83.08 E-value: 4.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 271 RVRDLSMAYG------DLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRlvepkrgdilldgesilAMKPESLRRR 344
Cdd:COG2401 26 RVAIVLEAFGvelrvvERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAG-----------------ALKGTPVAGC 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 345 VGMVFQHFNlfPDHTALENVmlsltkikkmPRSEARGIAEARLTEVGLAE----RKdhRPAGLSGGQQQRVAIARALAMD 420
Cdd:COG2401 89 VDVPDNQFG--REASLIDAI----------GRKGDFKDAVELLNAVGLSDavlwLR--RFKELSTGQKFRFRLALLLAER 154
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2017776620 421 PEVILFDEVTSALDPELVKGVLDLMANLGRQ-GMTMAVVTH 460
Cdd:COG2401 155 PKLLVIDEFCSHLDRQTAKRVARNLQKLARRaGITLVVATH 195
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
267-495 |
4.44e-18 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 87.87 E-value: 4.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 267 AGALRVRDLSMAY-GDLD-VLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPESLRRR 344
Cdd:PLN03130 1235 SGSIKFEDVVLRYrPELPpVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKV 1314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 345 VGMVFQ---------HFNL--FPDHT------ALENVMLsltkiKKMPRSEARGIaEARLTEVGlaerkdhrpAGLSGGQ 407
Cdd:PLN03130 1315 LGIIPQapvlfsgtvRFNLdpFNEHNdadlweSLERAHL-----KDVIRRNSLGL-DAEVSEAG---------ENFSVGQ 1379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 408 QQRVAIARALAMDPEVILFDEVTSALDpelvKGVLDLMANLGRQ---GMTMAVVTHEMGFARRvADQVVFMDEGRIIEAG 484
Cdd:PLN03130 1380 RQLLSLARALLRRSKILVLDEATAAVD----VRTDALIQKTIREefkSCTMLIIAHRLNTIID-CDRILVLDAGRVVEFD 1454
|
250
....*....|.
gi 2017776620 485 SPQQIFDNPQS 495
Cdd:PLN03130 1455 TPENLLSNEGS 1465
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
248-481 |
5.73e-18 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 86.62 E-value: 5.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 248 VGELRAASSTA-------VGNEPRF-------KAGA--LRVRDLSMA-YGDLDVLKGVDLDIAPGTVTCIIGPSGSGKST 310
Cdd:COG3845 220 VGTVDTAETSEeelaelmVGREVLLrvekapaEPGEvvLEVENLSVRdDRGVPALKDVSLEVRAGEILGIAGVAGNGQSE 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 311 LLRCLNRLVEPKRGDILLDGESILAMKPESLRRRvGMVF-----QHFNLFPDHTALENVMlsLTKIKKMP--------RS 377
Cdd:COG3845 300 LAEALAGLRPPASGSIRLDGEDITGLSPRERRRL-GVAYipedrLGRGLVPDMSVAENLI--LGRYRRPPfsrggfldRK 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 378 EARGIAEArltevgLAERKDHRPAG-------LSGGQQQRVAIARALAMDPEVILFDEVTSALDPELVKGVLDLMANLGR 450
Cdd:COG3845 377 AIRAFAEE------LIEEFDVRTPGpdtparsLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRD 450
|
250 260 270
....*....|....*....|....*....|.
gi 2017776620 451 QGMTMAVVTHEMGFARRVADQVVFMDEGRII 481
Cdd:COG3845 451 AGAAVLLISEDLDEILALSDRIAVMYEGRIV 481
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
273-489 |
7.68e-18 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 87.10 E-value: 7.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 273 RDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAmKPESLRRRVGMVFQHF 352
Cdd:NF033858 270 RGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDA-GDIATRRRVGYMSQAF 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 353 NLFPDHTALENVMLSlTKIKKMPRSEARG-IAEArLTEVGLAERKDHRPAGLSGGQQQRVAIARALAMDPEVILFDEVTS 431
Cdd:NF033858 349 SLYGELTVRQNLELH-ARLFHLPAAEIAArVAEM-LERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTS 426
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2017776620 432 ALDPELVKGVLDLMANLGRQ-GMTMAVVTHEMGFARRvADQVVFMDEGRIIEAGSPQQI 489
Cdd:NF033858 427 GVDPVARDMFWRLLIELSREdGVTIFISTHFMNEAER-CDRISLMHAGRVLASDTPAAL 484
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
270-481 |
9.85e-18 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 85.75 E-value: 9.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRlVEPK---RGDILLDGESILAMK-PESLRRRV 345
Cdd:PRK13549 6 LEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG-VYPHgtyEGEIIFEGEELQASNiRDTERAGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 346 GMVFQHFNLFPDHTALENVML--SLTKIKKMPRSEARGIAEARLTEVGLAERKDHRPAGLSGGQQQRVAIARALAMDPEV 423
Cdd:PRK13549 85 AIIHQELALVKELSVLENIFLgnEITPGGIMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2017776620 424 ILFDEVTSALDPELVKGVLDLMANLGRQGMTMAVVTHEMGFARRVADQVVFMDEGRII 481
Cdd:PRK13549 165 LILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHI 222
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
270-479 |
1.06e-17 |
|
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: 79.80 E-value: 1.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGesilamkpeslRRRVGMVF 349
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS-----------TVKIGYFE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 350 QhfnlfpdhtalenvmlsltkikkmprseargiaearltevglaerkdhrpagLSGGQQQRVAIARALAMDPEVILFDEV 429
Cdd:cd03221 70 Q----------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEP 97
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2017776620 430 TSALDPELVKGVLDLMANLgrQGmTMAVVTHEMGFARRVADQVVFMDEGR 479
Cdd:cd03221 98 TNHLDLESIEALEEALKEY--PG-TVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
270-489 |
1.91e-17 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 82.18 E-value: 1.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCL-NRLVEPK-------RGDILLDGESILAMKPESL 341
Cdd:PRK13547 2 LTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALaGDLTGGGaprgarvTGDVTLNGEPLAAIDAPRL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 342 RRRVGMVFQHFNLFPDHTALENVMLSltKIKKMPRSEA-----RGIAEARLTEVGLAERKDHRPAGLSGGQQQRVAIARA 416
Cdd:PRK13547 82 ARLRAVLPQAAQPAFAFSAREIVLLG--RYPHARRAGAlthrdGEIAWQALALAGATALVGRDVTTLSGGELARVQFARV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 417 LAM---------DPEVILFDEVTSALDPELVKGVLDLMANLGRQ-GMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSP 486
Cdd:PRK13547 160 LAQlwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDwNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAP 239
|
...
gi 2017776620 487 QQI 489
Cdd:PRK13547 240 ADV 242
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
260-484 |
2.55e-17 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 84.93 E-value: 2.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 260 GNEPRFKAGALRVRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPK--RGDILLDGESIlamk 337
Cdd:PLN03211 59 SNIKRILGHKPKISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKP---- 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 338 PESLRRRVGMVFQHFNLFPDHTALEN-VMLSLTKI-KKMPRSEARGIAEARLTEVGLAERKDHRPA-----GLSGGQQQR 410
Cdd:PLN03211 135 TKQILKRTGFVTQDDILYPHLTVRETlVFCSLLRLpKSLTKQEKILVAESVISELGLTKCENTIIGnsfirGISGGERKR 214
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2017776620 411 VAIARALAMDPEVILFDEVTSALDPELVKGVLDLMANLGRQGMTMAVVTHEMgfARRVA---DQVVFMDEGRIIEAG 484
Cdd:PLN03211 215 VSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQP--SSRVYqmfDSVLVLSEGRCLFFG 289
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
270-482 |
2.99e-17 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 84.64 E-value: 2.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAYGDLDV-LKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPESLRRRVGMV 348
Cdd:PRK10522 323 LELRNVTFAYQDNGFsVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAV 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 349 FQHFNLFpDHTalenvmlsLTKIKKMPRSEArgiAEARLTEVGLAER---KDHRPAG--LSGGQQQRVAIARALAMDPEV 423
Cdd:PRK10522 403 FTDFHLF-DQL--------LGPEGKPANPAL---VEKWLERLKMAHKlelEDGRISNlkLSKGQKKRLALLLALAEERDI 470
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 424 ILFDEVTSALDPELVKGV-LDLMANLGRQGMTMAVVTHEMGFARRvADQVVFMDEGRIIE 482
Cdd:PRK10522 471 LLLDEWAADQDPHFRREFyQVLLPLLQEMGKTIFAISHDDHYFIH-ADRLLEMRNGQLSE 529
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
285-506 |
3.03e-17 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 81.85 E-value: 3.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 285 LKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPESLrrrVGMVFQHFNL---FPdhTAL 361
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL---VAYVPQSEEVdwsFP--VLV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 362 ENVMLsLTKIKKM-----PRSEARGIAEARLTEVGLAERKdHRPAG-LSGGQQQRVAIARALAMDPEVILFDEVTSALDP 435
Cdd:PRK15056 98 EDVVM-MGRYGHMgwlrrAKKRDRQIVTAALARVDMVEFR-HRQIGeLSGGQKKRVFLARAIAQQGQVILLDEPFTGVDV 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2017776620 436 ELVKGVLDLMANLGRQGMTMAVVTHEMGFARRVADQVVfMDEGRIIEAGSPQQIFdnpQSERLKRFLAEVL 506
Cdd:PRK15056 176 KTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTV-MVKGTVLASGPTETTF---TAENLELAFSGVL 242
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
273-481 |
3.11e-17 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 84.40 E-value: 3.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 273 RDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESI-LAMKPESLRRRVGMVFQH 351
Cdd:PRK10982 2 SNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdFKSSKEALENGISMVHQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 352 FNLFPDHTALENVMLSLTKIK-------KMPRSeargiAEARLTEVGLAERKDHRPAGLSGGQQQRVAIARALAMDPEVI 424
Cdd:PRK10982 82 LNLVLQRSVMDNMWLGRYPTKgmfvdqdKMYRD-----TKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIV 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2017776620 425 LFDEVTSALDPELVKGVLDLMANLGRQGMTMAVVTHEMGFARRVADQVVFMDEGRII 481
Cdd:PRK10982 157 IMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWI 213
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
285-482 |
3.34e-17 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 84.07 E-value: 3.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 285 LKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRlVEPK---RGDILLDGEsILAMKPESLRRRVGMVF--QHFNLFPDHT 359
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSG-VYPHgsyEGEILFDGE-VCRFKDIRDSEALGIVIihQELALIPYLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 360 ALENVMLSLTKIKK--MPRSEARGIAEARLTEVGLAERKDHRPAGLSGGQQQRVAIARALAMDPEVILFDEVTSALDPEL 437
Cdd:NF040905 95 IAENIFLGNERAKRgvIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTAALNEED 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2017776620 438 VKGVLDLMANLGRQGMTMAVVTHEMGFARRVADQVVFMDEGRIIE 482
Cdd:NF040905 175 SAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGRTIE 219
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
270-469 |
5.98e-17 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 79.46 E-value: 5.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPESLRrrvGMVF 349
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIAR---GLLY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 350 -QHFNlfpdhtALENVMLSLTKIKKMPRSEARGIAEARLTEVGLAERKDHRPAGLSGGQQQRVAIARALAMDPEVILFDE 428
Cdd:cd03231 78 lGHAP------GIKTTLSVLENLRFWHADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDE 151
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2017776620 429 VTSALDPELVKGVLDLMA-NLGRQGMTMAVVTHEMGFARRVA 469
Cdd:cd03231 152 PTTALDKAGVARFAEAMAgHCARGGMVVLTTHQDLGLSEAGA 193
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
279-481 |
6.46e-17 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 80.07 E-value: 6.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 279 YGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPEsLRRRVGMVF-QHFNLFPD 357
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKK-FLRRIGVVFgQKTQLWWD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 358 HTALENVMLsLTKIKKMPRSEARGIAEaRLTEVGLAERKDHRPA-GLSGGQQQRVAIARALAMDPEVILFDEVTSALDPE 436
Cdd:cd03267 110 LPVIDSFYL-LAAIYDLPPARFKKRLD-ELSELLDLEELLDTPVrQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVV 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2017776620 437 LVKGVLDLMANLGRQ-GMTMAVVTHEMGFARRVADQVVFMDEGRII 481
Cdd:cd03267 188 AQENIRNFLKEYNRErGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
268-490 |
4.22e-16 |
|
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: 78.03 E-value: 4.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 268 GALRVRDLSMAYGDL--DVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPESLRRRV 345
Cdd:cd03288 18 GEIKIHDLCVRYENNlkPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 346 GMVFQ---------HFNLFPDHTALENVM---LSLTKIKKMPRSEARGIaEARLTEVGlaerkdhrpAGLSGGQQQRVAI 413
Cdd:cd03288 98 SIILQdpilfsgsiRFNLDPECKCTDDRLweaLEIAQLKNMVKSLPGGL-DAVVTEGG---------ENFSVGQRQLFCL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 414 ARALAMDPEVILFDEVTSALDPE----LVKGVLDLMANlgRQGMTMAVVTHEMgfarRVADQVVFMDEGRIIEAGSPQQI 489
Cdd:cd03288 168 ARAFVRKSSILIMDEATASIDMAteniLQKVVMTAFAD--RTVVTIAHRVSTI----LDADLVLVLSRGILVECDTPENL 241
|
.
gi 2017776620 490 F 490
Cdd:cd03288 242 L 242
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
269-489 |
5.43e-16 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 80.94 E-value: 5.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 269 ALRVRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDI-LLDGEsilaMKPESLRRRVG- 346
Cdd:NF033858 1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVeVLGGD----MADARHRRAVCp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 347 ----MVfQHF--NLFPDHTALENV-----MLSLTKIKKmprsEARgIAEArLTEVGLAERKDhRPAG-LSGGQQQRVAIA 414
Cdd:NF033858 77 riayMP-QGLgkNLYPTLSVFENLdffgrLFGQDAAER----RRR-IDEL-LRATGLAPFAD-RPAGkLSGGMKQKLGLC 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 415 RALAMDPEVILFDEVTSALDPelvkgvL------DLMANL--GRQGMTMAVVTHEMGFARRVaDQVVFMDEGRIIEAGSP 486
Cdd:NF033858 149 CALIHDPDLLILDEPTTGVDP------LsrrqfwELIDRIraERPGMSVLVATAYMEEAERF-DWLVAMDAGRVLATGTP 221
|
...
gi 2017776620 487 QQI 489
Cdd:NF033858 222 AEL 224
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
278-491 |
5.50e-16 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 81.53 E-value: 5.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 278 AYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGEsiLAMKPE-------SLRRRVgmVFQ 350
Cdd:TIGR00957 647 ARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS--VAYVPQqawiqndSLRENI--LFG 722
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 351 HFNLFPDHTALENVMLSLTKIKKMPRSEArgiaearlTEVGlaerkdHRPAGLSGGQQQRVAIARALAMDPEVILFDEVT 430
Cdd:TIGR00957 723 KALNEKYYQQVLEACALLPDLEILPSGDR--------TEIG------EKGVNLSGGQKQRVSLARAVYSNADIYLFDDPL 788
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2017776620 431 SALDPELVKGVLDLManLGRQGM----TMAVVTHEMGFARRVaDQVVFMDEGRIIEAGSPQQIFD 491
Cdd:TIGR00957 789 SAVDAHVGKHIFEHV--IGPEGVlknkTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLQ 850
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
280-478 |
7.41e-16 |
|
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: 75.74 E-value: 7.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 280 GDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCL-NR----LVEpkrGDILLDGESilamKPESLRRRVGMVFQHFNL 354
Cdd:cd03232 18 GKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLaGRktagVIT---GEILINGRP----LDKNFQRSTGYVEQQDVH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 355 FPDHTALENVMLSltkikkmprseargiaeARLTEVGLAERKdhrpaglsggqqqRVAIARALAMDPEVILFDEVTSALD 434
Cdd:cd03232 91 SPNLTVREALRFS-----------------ALLRGLSVEQRK-------------RLTIGVELAAKPSILFLDEPTSGLD 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2017776620 435 PELVKGVLDLMANLGRQGMTMAVVTHEMG---FARrvADQVVFMDEG 478
Cdd:cd03232 141 SQAAYNIVRFLKKLADSGQAILCTIHQPSasiFEK--FDRLLLLKRG 185
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
270-484 |
1.30e-15 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 76.37 E-value: 1.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCL--NRLVEPKRGDILLDGESILAMKPESlrrRVG- 346
Cdd:PRK09580 2 LSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDLLELSPED---RAGe 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 347 ---MVFQH-------FNLFPDHTALeNVMLSLTKIKKMPRSEARGIAEARLTEVGLAERKDHRPA--GLSGGQQQRVAIA 414
Cdd:PRK09580 79 gifMAFQYpveipgvSNQFFLQTAL-NAVRSYRGQEPLDRFDFQDLMEEKIALLKMPEDLLTRSVnvGFSGGEKKRNDIL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2017776620 415 RALAMDPEVILFDEVTSALDPELVKGVLDLMANLGRQGMTMAVVTHEMGFARRVA-DQVVFMDEGRIIEAG 484
Cdd:PRK09580 158 QMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYQRILDYIKpDYVHVLYQGRIVKSG 228
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
269-489 |
1.58e-15 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 77.85 E-value: 1.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 269 ALRVRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSG--KSTLLRclnRLVEPKRGDILLDGESILAMKpESLRRRVG 346
Cdd:NF000106 13 AVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPA---HV*GPDAGRRPWRF*TWCANR-RALRRTIG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 347 MVFQ-HFNLFPDHTALENVMLsLTKIKKMPRSEARGIAEARLTEVGLAERKDHRPAGLSGGQQQRVAIARALAMDPEVIL 425
Cdd:NF000106 89 *HRPvR*GRRESFSGRENLYM-IGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLY 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2017776620 426 FDEVTSALDPELVKGVLDLMANLGRQGMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQI 489
Cdd:NF000106 168 LDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
272-505 |
1.63e-15 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 76.29 E-value: 1.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 272 VRDLSMAYGD----LDVLKGvdlDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESIlAMKPESLRrrvgm 347
Cdd:cd03237 1 YTYPTMKKTLgeftLEVEGG---SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV-SYKPQYIK----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 348 vfqhfnlfPDHTALENVMLSlTKIKKMprsearGIAEARLTEV----GLAERKDHRPAGLSGGQQQRVAIARALAMDPEV 423
Cdd:cd03237 72 --------ADYEGTVRDLLS-SITKDF------YTHPYFKTEIakplQIEQILDREVPELSGGELQRVAIAACLSKDADI 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 424 ILFDEVTSALDPE---LVKGVLDLMANLGRQgmTMAVVTHEMGFARRVADQV-VFMDE-GRIIEAGSPQqifdnPQSERL 498
Cdd:cd03237 137 YLLDEPSAYLDVEqrlMASKVIRRFAENNEK--TAFVVEHDIIMIDYLADRLiVFEGEpSVNGVANPPQ-----SLRSGM 209
|
....*..
gi 2017776620 499 KRFLAEV 505
Cdd:cd03237 210 NRFLKNL 216
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
270-493 |
2.74e-15 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 76.87 E-value: 2.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSM----AYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPK---RGDIL-LDGESILAMKPESL 341
Cdd:COG4170 4 LDIRNLTIeidtPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNwhvTADRFrWNGIDLLKLSPRER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 342 RRRVG----MVFQHFN--LFPDHTALENVMLSltkikkMPRSEARG-----------IAEARLTEVGLaerKDHR----- 399
Cdd:COG4170 84 RKIIGreiaMIFQEPSscLDPSAKIGDQLIEA------IPSWTFKGkwwqrfkwrkkRAIELLHRVGI---KDHKdimns 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 400 -PAGLSGGQQQRVAIARALAMDPEVILFDEVTSALDPELVKGVLDLMANLGR-QGMTMAVVTHEMGFARRVADQVVFMDE 477
Cdd:COG4170 155 yPHELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQlQGTSILLISHDLESISQWADTITVLYC 234
|
250
....*....|....*.
gi 2017776620 478 GRIIEAGSPQQIFDNP 493
Cdd:COG4170 235 GQTVESGPTEQILKSP 250
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
270-482 |
4.71e-15 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 77.53 E-value: 4.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAYGDLD-----VLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPESLRRR 344
Cdd:COG4615 328 LELRGVTYRYPGEDgdegfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQL 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 345 VGMVFQHFNLFPDHTALENvmlsltkikkmPRSEARgiAEARLTEVGLAER---KDHR--PAGLSGGQQQRVAIARALAM 419
Cdd:COG4615 408 FSAVFSDFHLFDRLLGLDG-----------EADPAR--ARELLERLELDHKvsvEDGRfsTTDLSQGQRKRLALLVALLE 474
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2017776620 420 DPEVILFDEVTSALDPELvKGV--LDLMANLGRQGMTMAVVTH-EMGFArrVADQVVFMDEGRIIE 482
Cdd:COG4615 475 DRPILVFDEWAADQDPEF-RRVfyTELLPELKARGKTVIAISHdDRYFD--LADRVLKMDYGKLVE 537
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
285-485 |
7.86e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 75.51 E-value: 7.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 285 LKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPEsLRRRVGMVF-QHFNLFPDHTALEN 363
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKE-FARRIGVVFgQRSQLWWDLPAIDS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 364 VMLsLTKIKKMPRSEARgiaeARLTEvgLAERKD-----HRPA-GLSGGQQQRVAIARALAMDPEVILFDEVTSALDPEL 437
Cdd:COG4586 117 FRL-LKAIYRIPDAEYK----KRLDE--LVELLDlgellDTPVrQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVS 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2017776620 438 VKGVLDLMANLGRQ-GMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGS 485
Cdd:COG4586 190 KEAIREFLKEYNRErGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGS 238
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
268-495 |
5.04e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 75.01 E-value: 5.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 268 GALRVRDLSMAY--GDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPESLRRRV 345
Cdd:PLN03232 1233 GSIKFEDVHLRYrpGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVL 1312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 346 GMVFQ---------HFNL--FPDHT------ALENvmlslTKIKKMPRSEARGIaEARLTEVGlaerkdhrpAGLSGGQQ 408
Cdd:PLN03232 1313 SIIPQspvlfsgtvRFNIdpFSEHNdadlweALER-----AHIKDVIDRNPFGL-DAEVSEGG---------ENFSVGQR 1377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 409 QRVAIARALAMDPEVILFDEVTSALDPElVKGVLDLMANLGRQGMTMAVVTHEMGFARRvADQVVFMDEGRIIEAGSPQQ 488
Cdd:PLN03232 1378 QLLSLARALLRRSKILVLDEATASVDVR-TDSLIQRTIREEFKSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQE 1455
|
....*..
gi 2017776620 489 IFDNPQS 495
Cdd:PLN03232 1456 LLSRDTS 1462
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
292-489 |
5.69e-14 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 71.50 E-value: 5.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 292 IAPGTVTCIIGPSGSGKSTLLRCLNRLVePKRGDILLDGESILAMKPESLRRRVG-----------M-VFQHFNLF-PDH 358
Cdd:PRK03695 19 VRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELARHRAylsqqqtppfaMpVFQYLTLHqPDK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 359 TALENVMLSLTKikkmprseargIAEArlteVGLAErKDHRPAG-LSGGQQQRVAIARA-LAMDPEV------ILFDEVT 430
Cdd:PRK03695 98 TRTEAVASALNE-----------VAEA----LGLDD-KLGRSVNqLSGGEWQRVRLAAVvLQVWPDInpagqlLLLDEPM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2017776620 431 SALDpelV--KGVLD-LMANLGRQGMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQI 489
Cdd:PRK03695 162 NSLD---VaqQAALDrLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEV 220
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
270-494 |
7.50e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 71.30 E-value: 7.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILldgesilamKPESLrrRVGMVF 349
Cdd:PRK09544 5 VSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK---------RNGKL--RIGYVP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 350 QHFNLFPdhtalenvMLSLTKIKKM---PRSEARGIAEArLTEVGLAERKDHRPAGLSGGQQQRVAIARALAMDPEVILF 426
Cdd:PRK09544 74 QKLYLDT--------TLPLTVNRFLrlrPGTKKEDILPA-LKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVL 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2017776620 427 DEVTSALDPELVKGVLDLMANLGRQ-GMTMAVVTHEMGFARRVADQVVFMDEgRIIEAGSPQQIFDNPQ 494
Cdd:PRK09544 145 DEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGTPEVVSLHPE 212
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
276-481 |
7.99e-14 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 73.83 E-value: 7.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 276 SMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNrlvepkrGDILLD-GESILA-------MKPESLRRRVGM 347
Cdd:PRK11147 10 WLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILN-------GEVLLDdGRIIYEqdlivarLQQDPPRNVEGT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 348 VF-----------QHFNLFpdHTALENVML--SLTKIKKMPRSEA----RGI--AEARLTEV----GLAerKDHRPAGLS 404
Cdd:PRK11147 83 VYdfvaegieeqaEYLKRY--HDISHLVETdpSEKNLNELAKLQEqldhHNLwqLENRINEVlaqlGLD--PDAALSSLS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2017776620 405 GGQQQRVAIARALAMDPEVILFDEVTSALDPELVKGVLDLMANLgrQGmTMAVVTHEMGFARRVADQVVFMDEGRII 481
Cdd:PRK11147 159 GGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTF--QG-SIIFISHDRSFIRNMATRIVDLDRGKLV 232
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
268-489 |
1.28e-13 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 73.83 E-value: 1.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 268 GALRVRDLSMAY-GDLD-VLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPESLRRRV 345
Cdd:TIGR00957 1283 GRVEFRNYCLRYrEDLDlVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKI 1362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 346 GMVFQHFNLFPDhtaleNVMLSLTKIKKMPRSE---ARGIAEARLTEVGLAERKDHRPA----GLSGGQQQRVAIARALA 418
Cdd:TIGR00957 1363 TIIPQDPVLFSG-----SLRMNLDPFSQYSDEEvwwALELAHLKTFVSALPDKLDHECAeggeNLSVGQRQLVCLARALL 1437
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2017776620 419 MDPEVILFDEVTSALDPElvkgVLDLMANLGR---QGMTMAVVTHE----MGFARrvadqVVFMDEGRIIEAGSPQQI 489
Cdd:TIGR00957 1438 RKTKILVLDEATAAVDLE----TDNLIQSTIRtqfEDCTVLTIAHRlntiMDYTR-----VIVLDKGEVAEFGAPSNL 1506
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
280-461 |
2.75e-13 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 72.83 E-value: 2.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 280 GDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNrlvEPKRGDILLDGESILAMKP--ESLRRRVGMVFQHFNLFPD 357
Cdd:TIGR00956 774 EKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLA---ERVTTGVITGGDRLVNGRPldSSFQRSIGYVQQQDLHLPT 850
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 358 HTALENVMLS--LTKIKKMPRSEARGIAEARLTEVGLAERKDhrpA-------GLSGGQQQRVAIARALAMDPEVILF-D 427
Cdd:TIGR00956 851 STVRESLRFSayLRQPKSVSKSEKMEYVEEVIKLLEMESYAD---AvvgvpgeGLNVEQRKRLTIGVELVAKPKLLLFlD 927
|
170 180 190
....*....|....*....|....*....|....
gi 2017776620 428 EVTSALDPELVKGVLDLMANLGRQGMTMAVVTHE 461
Cdd:TIGR00956 928 EPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQ 961
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
284-481 |
3.17e-13 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 71.89 E-value: 3.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 284 VLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLvepkrgDILLDGESILamkpeSLRRRVGMVFQHFNLFPDHTALEN 363
Cdd:TIGR03719 20 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV------DKDFNGEARP-----QPGIKVGYLPQEPQLDPTKTVREN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 364 VMLSLTKIKKM-------------PRSEARGIAE--ARLTEVGLA------ERK-------------DHRPAGLSGGQQQ 409
Cdd:TIGR03719 89 VEEGVAEIKDAldrfneisakyaePDADFDKLAAeqAELQEIIDAadawdlDSQleiamdalrcppwDADVTKLSGGERR 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2017776620 410 RVAIARALAMDPEVILFDEVTSALDPElvkGVLDLMANLGRQGMTMAVVTHEMGFARRVADQVVFMDEGRII 481
Cdd:TIGR03719 169 RVALCRLLLSKPDMLLLDEPTNHLDAE---SVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELDRGRGI 237
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
285-492 |
5.54e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 71.93 E-value: 5.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 285 LKGVDLDIAPGTVTCIIGPSGSGKSTLLRC-LNRLVEPKRGDILLDGEsiLAMKPEslrrrVGMVFqhfnlfpDHTALEN 363
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAmLGELSHAETSSVVIRGS--VAYVPQ-----VSWIF-------NATVREN 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 364 VMLSltkIKKMPRSEARGI------------AEARLTEVGlaerkdHRPAGLSGGQQQRVAIARALAMDPEVILFDEVTS 431
Cdd:PLN03232 699 ILFG---SDFESERYWRAIdvtalqhdldllPGRDLTEIG------ERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLS 769
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2017776620 432 ALDPELVKGVLDLMANLGRQGMTMAVVTHEMGFARRVaDQVVFMDEGRIIEAGSPQQIFDN 492
Cdd:PLN03232 770 ALDAHVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLM-DRIILVSEGMIKEEGTFAELSKS 829
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
281-492 |
6.20e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 70.97 E-value: 6.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 281 DLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKP-ESLRRRVGMVFQH---FNLFP 356
Cdd:PRK09700 275 DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPlDAVKKGMAYITESrrdNGFFP 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 357 DHTALENVMLSlTKIKKMPRSEARGIAEARlTEVGLAERK-----------DHRPAGLSGGQQQRVAIARALAMDPEVIL 425
Cdd:PRK09700 355 NFSIAQNMAIS-RSLKDGGYKGAMGLFHEV-DEQRTAENQrellalkchsvNQNITELSGGNQQKVLISKWLCCCPEVII 432
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2017776620 426 FDEVTSALDPELVKGVLDLMANLGRQGMTMAVVTHEMGFARRVADQVVFMDEGRIieagspQQIFDN 492
Cdd:PRK09700 433 FDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRL------TQILTN 493
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
285-433 |
6.24e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 70.80 E-value: 6.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 285 LKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKP-ESLRRRVGMVFQHFNLFPDHTALEN 363
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPkSSQEAGIGIIHQELNLIPQLTIAEN 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2017776620 364 VMLSLTKIKKMPR---SEARGIAEARLTEVGLaERKDHRPAG-LSGGQQQRVAIARALAMDPEVILFDEVTSAL 433
Cdd:PRK10762 100 IFLGREFVNRFGRidwKKMYAEADKLLARLNL-RFSSDKLVGeLSIGEQQMVEIAKVLSFESKVIIMDEPTDAL 172
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
270-460 |
7.99e-13 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 67.57 E-value: 7.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKpeslRRRVGMVF 349
Cdd:PRK13543 12 LAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGD----RSRFMAYL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 350 QHF-NLFPDHTALENVM----LSLTKIKKMPRSEargiaearLTEVGLAERKDHRPAGLSGGQQQRVAIARALAMDPEVI 424
Cdd:PRK13543 88 GHLpGLKADLSTLENLHflcgLHGRRAKQMPGSA--------LAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLW 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 2017776620 425 LFDEVTSALDPELVKGVLDLMANLGRQGMTMAVVTH 460
Cdd:PRK13543 160 LLDEPYANLDLEGITLVNRMISAHLRGGGAALVTTH 195
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
270-480 |
1.49e-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: 69.47 E-value: 1.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAYGDLDVLKGVD---LDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPK-RGDILLDGESI------------ 333
Cdd:TIGR02633 258 LEARNLTCWDVINPHRKRVDdvsFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVdirnpaqairag 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 334 LAMKPESlRRRVGMVfqhfnlfPDHTALENVMLS-LTKIKKMPRSEARGIAEARLTEVGLAERKDHRP----AGLSGGQQ 408
Cdd:TIGR02633 338 IAMVPED-RKRHGIV-------PILGVGKNITLSvLKSFCFKMRIDAAAELQIIGSAIQRLKVKTASPflpiGRLSGGNQ 409
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2017776620 409 QRVAIARALAMDPEVILFDEVTSALDPELVKGVLDLMANLGRQGMTMAVVTHEMGFARRVADQVVFMDEGRI 480
Cdd:TIGR02633 410 QKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
282-481 |
3.62e-12 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 65.36 E-value: 3.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 282 LDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPK---RGDILLDGESILAMKpESLRRRVGMVFQHFNLFPDH 358
Cdd:cd03233 20 IPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFA-EKYPGEIIYVSEEDVHFPTL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 359 TALENVMLSLtkikkmprsEARGIAEARltevglaerkdhrpaGLSGGQQQRVAIARALAMDPEVILFDEVTSALDP--- 435
Cdd:cd03233 99 TVRETLDFAL---------RCKGNEFVR---------------GISGGERKRVSIAEALVSRASVLCWDNSTRGLDSsta 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2017776620 436 -ELVKgVLDLMANLgrQGMT-MAVVTHEMGFARRVADQVVFMDEGRII 481
Cdd:cd03233 155 lEILK-CIRTMADV--LKTTtFVSLYQASDEIYDLFDKVLVLYEGRQI 199
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
281-466 |
3.77e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 69.29 E-value: 3.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 281 DLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILL-DGESILAMKPESLRRRVGMVFQHFNLFPDHT 359
Cdd:PTZ00265 397 DVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSI 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 360 AlENVMLSLTKIKKM-------------------PRSEARGIAEARLTEV-------GLAE-RKDHR------------- 399
Cdd:PTZ00265 477 K-NNIKYSLYSLKDLealsnyynedgndsqenknKRNSCRAKCAGDLNDMsnttdsnELIEmRKNYQtikdsevvdvskk 555
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 400 ---------------------PAGLSGGQQQRVAIARALAMDPEVILFDEVTSALDPELVKGVLDLMANL-GRQGMTMAV 457
Cdd:PTZ00265 556 vlihdfvsalpdkyetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLkGNENRITII 635
|
....*....
gi 2017776620 458 VTHEMGFAR 466
Cdd:PTZ00265 636 IAHRLSTIR 644
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
260-489 |
2.34e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 65.84 E-value: 2.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 260 GNEPRFKAGA--LRVRDLSMaygdlDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMK 337
Cdd:PRK15439 257 GNRRQQAAGApvLTVEDLTG-----EGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALS 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 338 PESlRRRVGMVF-----QHFNLFPDHTALENVMlSLTkIKKMP----RSEARGIAEARLTEVGLAERKDHRPA-GLSGGQ 407
Cdd:PRK15439 332 TAQ-RLARGLVYlpedrQSSGLYLDAPLAWNVC-ALT-HNRRGfwikPARENAVLERYRRALNIKFNHAEQAArTLSGGN 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 408 QQRVAIARALAMDPEVILFDEVTSALDPELVKGVLDLMANLGRQGMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQ 487
Cdd:PRK15439 409 QQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEISGALTGA 488
|
..
gi 2017776620 488 QI 489
Cdd:PRK15439 489 AI 490
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
266-489 |
2.67e-11 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 66.58 E-value: 2.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 266 KAGALRVRDLSMAYGDLDVlKGVD---LDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAmkpeslr 342
Cdd:TIGR01257 1934 KTDILRLNELTKVYSGTSS-PAVDrlcVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT------- 2005
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 343 rRVGMVFQHFNLFPDHTALENVMLS------LTKIKKMPRSEARGIAEARLTEVGLAERKDHRPAGLSGGQQQRVAIARA 416
Cdd:TIGR01257 2006 -NISDVHQNMGYCPQFDAIDDLLTGrehlylYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIA 2084
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2017776620 417 LAMDPEVILFDEVTSALDPELVKGVLDLMANLGRQGMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQI 489
Cdd:TIGR01257 2085 LIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHL 2157
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
269-492 |
2.80e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 66.30 E-value: 2.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 269 ALRVRDLSMAY---GDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPkrgdiLLDGESILamkpeslRRRV 345
Cdd:PLN03130 614 AISIKNGYFSWdskAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPP-----RSDASVVI-------RGTV 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 346 GMVFQHFNLFpDHTALENVMLSL----TKIKKMPRSEARG-----IAEARLTEVGlaerkdHRPAGLSGGQQQRVAIARA 416
Cdd:PLN03130 682 AYVPQVSWIF-NATVRDNILFGSpfdpERYERAIDVTALQhdldlLPGGDLTEIG------ERGVNISGGQKQRVSMARA 754
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2017776620 417 LAMDPEVILFDEVTSALDPELVKGVLDLMANLGRQGMTMAVVTHEMGFARRVaDQVVFMDEGRIIEAGSPQQIFDN 492
Cdd:PLN03130 755 VYSNSDVYIFDDPLSALDAHVGRQVFDKCIKDELRGKTRVLVTNQLHFLSQV-DRIILVHEGMIKEEGTYEELSNN 829
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
268-435 |
2.83e-11 |
|
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: 64.11 E-value: 2.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 268 GALRVRDLSMAY--GDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKrGDILLDGESILAMKPESLRRRV 345
Cdd:cd03289 1 GQMTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 346 GMVFQHFNLFPDhtaleNVMLSLTKIKKMPRSEARGIAEarltEVGLAERKDHRPAG-----------LSGGQQQRVAIA 414
Cdd:cd03289 80 GVIPQKVFIFSG-----TFRKNLDPYGKWSDEEIWKVAE----EVGLKSVIEQFPGQldfvlvdggcvLSHGHKQLMCLA 150
|
170 180
....*....|....*....|.
gi 2017776620 415 RALAMDPEVILFDEVTSALDP 435
Cdd:cd03289 151 RSVLSKAKILLLDEPSAHLDP 171
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
263-469 |
3.18e-11 |
|
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: 65.73 E-value: 3.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 263 PRFKAGALRVRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLdGESIlamkpeslr 342
Cdd:TIGR03719 316 PRLGDKVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV--------- 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 343 rRVGMVFQ-HFNLFPDHTALENV-----MLSLTKIKKMPRSEArgiaeARLTEVGLAERKdhRPAGLSGGQQQRVAIARA 416
Cdd:TIGR03719 386 -KLAYVDQsRDALDPNKTVWEEIsggldIIKLGKREIPSRAYV-----GRFNFKGSDQQK--KVGQLSGGERNRVHLAKT 457
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2017776620 417 LAMDPEVILFDEVTSALDPELVKGVLDLMANLGrqGMTMaVVTHEMGFARRVA 469
Cdd:TIGR03719 458 LKSGGNVLLLDEPTNDLDVETLRALEEALLNFA--GCAV-VISHDRWFLDRIA 507
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
270-460 |
4.27e-11 |
|
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: 61.40 E-value: 4.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAYGDLDVL-KGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDIlldgesilaMKPEslRRRVGMV 348
Cdd:cd03223 1 IELENLSLATPDGRVLlKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI---------GMPE--GEDLLFL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 349 FQHfNLFPDHTALENVMLSLTKIkkmprseargiaearltevglaerkdhrpagLSGGQQQRVAIARALAMDPEVILFDE 428
Cdd:cd03223 70 PQR-PYLPLGTLREQLIYPWDDV-------------------------------LSGGEQQRLAFARLLLHKPKFVFLDE 117
|
170 180 190
....*....|....*....|....*....|...
gi 2017776620 429 VTSALDPElvkgVLDLMANLGRQ-GMTMAVVTH 460
Cdd:cd03223 118 ATSALDEE----SEDRLYQLLKElGITVISVGH 146
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
294-475 |
6.04e-11 |
|
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: 64.81 E-value: 6.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 294 PGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDI------------------------LLDGESILAMKPeslrrrvgmvf 349
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELKPNLGDYdeepswdevlkrfrgtelqdyfkkLANGEIKVAHKP----------- 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 350 QHFNLFPDH------TALENVmlsltkikkmprsEARGIAEARLTEVGLAERKDHRPAGLSGGQQQRVAIARALAMDPEV 423
Cdd:COG1245 167 QYVDLIPKVfkgtvrELLEKV-------------DERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADF 233
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2017776620 424 ILFDEVTSALDpelVK---GVLDLMANLGRQGMTMAVVTHEMGFARRVADQVVFM 475
Cdd:COG1245 234 YFFDEPSSYLD---IYqrlNVARLIRELAEEGKYVLVVEHDLAILDYLADYVHIL 285
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
270-493 |
1.33e-10 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 62.51 E-value: 1.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAY----GDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCL------NRLVEPKRgdILLDGESILAMKPE 339
Cdd:PRK15093 4 LDIRNLTIEFktsdGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAIcgvtkdNWRVTADR--MRFDDIDLLRLSPR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 340 SLRRRVG----MVFQHFNLFPDHTalENVMLSLtkIKKMPRSEARGIAEAR-----------LTEVGLaerKDHR----- 399
Cdd:PRK15093 82 ERRKLVGhnvsMIFQEPQSCLDPS--ERVGRQL--MQNIPGWTYKGRWWQRfgwrkrraielLHRVGI---KDHKdamrs 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 400 -PAGLSGGQQQRVAIARALAMDPEVILFDEVTSALDPELVKGVLDLMANLGR-QGMTMAVVTHEMGFARRVADQVVFMDE 477
Cdd:PRK15093 155 fPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnNNTTILLISHDLQMLSQWADKINVLYC 234
|
250
....*....|....*.
gi 2017776620 478 GRIIEAGSPQQIFDNP 493
Cdd:PRK15093 235 GQTVETAPSKELVTTP 250
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
261-445 |
1.39e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 63.50 E-value: 1.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 261 NEPRFkagalRVRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCL---------NRLV--EPKRGDilld 329
Cdd:PRK10938 257 NEPRI-----VLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLItgdhpqgysNDLTlfGRRRGS---- 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 330 GESILAMKpeslrRRVGMVFQHFNLfpDH---TALENVMLS----LTKIKKMPRSEARGIAEARLTEVGLAERKDHRP-A 401
Cdd:PRK10938 328 GETIWDIK-----KHIGYVSSSLHL--DYrvsTSVRNVILSgffdSIGIYQAVSDRQQKLAQQWLDILGIDKRTADAPfH 400
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2017776620 402 GLSGGQQQRVAIARALAMDPEVILFDEVTSALDP---ELVKGVLDLM 445
Cdd:PRK10938 401 SLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPlnrQLVRRFVDVL 447
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
283-505 |
1.75e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 63.59 E-value: 1.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 283 DVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCL-NRLVEPKRGD---ILLDGESILAMKPEsLRRRVGMVFQHFNLFPDH 358
Cdd:TIGR00956 75 DILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIaSNTDGFHIGVegvITYDGITPEEIKKH-YRGDVVYNAETDVHFPHL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 359 TALENVMLSL------TKIKKMPRSE-ARGIAEARLTEVGLAERKDHRPA-----GLSGGQQQRVAIARALAMDPEVILF 426
Cdd:TIGR00956 154 TVGETLDFAArcktpqNRPDGVSREEyAKHIADVYMATYGLSHTRNTKVGndfvrGVSGGERKRVSIAEASLGGAKIQCW 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 427 DEVTSALDP----ELVKgVLDLMANLGRQGMTMAVV-----THEMgFarrvaDQVVFMDEGRIIEAGSPQQI-------- 489
Cdd:TIGR00956 234 DNATRGLDSatalEFIR-ALKTSANILDTTPLVAIYqcsqdAYEL-F-----DKVIVLYEGYQIYFGPADKAkqyfekmg 306
|
250
....*....|....*.
gi 2017776620 490 FDNPQSERLKRFLAEV 505
Cdd:TIGR00956 307 FKCPDRQTTADFLTSL 322
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
268-479 |
2.74e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 63.12 E-value: 2.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 268 GALRVRDLSMAY---GDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKR--------------------- 323
Cdd:PTZ00265 1164 GKIEIMDVNFRYisrPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKNdhhivfknehtndmtneqdyq 1243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 324 ---------------------------------GDILLDGESILAMKPESLRRRVGMVFQHFNLFpDHTALENVML---- 366
Cdd:PTZ00265 1244 gdeeqnvgmknvnefsltkeggsgedstvfknsGKILLDGVDICDYNLKDLRNLFSIVSQEPMLF-NMSIYENIKFgked 1322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 367 -SLTKIKKMPRSEA-----RGIAEARLTEVGlaerkdhrPAG--LSGGQQQRVAIARALAMDPEVILFDEVTSALDPE-- 436
Cdd:PTZ00265 1323 aTREDVKRACKFAAidefiESLPNKYDTNVG--------PYGksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNse 1394
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2017776620 437 --LVKGVLDLMANLGRQGMTMAvvtHEMGFARRVADQVVFMDEGR 479
Cdd:PTZ00265 1395 klIEKTIVDIKDKADKTIITIA---HRIASIKRSDKIVVFNNPDR 1436
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
274-505 |
6.89e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 61.36 E-value: 6.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 274 DLSMAYGD--LDVLKGvdlDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDIllDGESILAMKPESLRRRVGMvfqh 351
Cdd:PRK13409 345 DLTKKLGDfsLEVEGG---EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV--DPELKISYKPQYIKPDYDG---- 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 352 fnlfpdhtaleNVMLSLTKIKKMPRS-----EargIAEaRLtevGLAERKDHRPAGLSGGQQQRVAIARALAMDPEVILF 426
Cdd:PRK13409 416 -----------TVEDLLRSITDDLGSsyyksE---IIK-PL---QLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLL 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 427 DEVTSALDPE---LVKGVLDLMANlgRQGMTMAVVTHEMGFARRVADQV-VFMDE-GRIIEAGSPQqifdnPQSERLKRF 501
Cdd:PRK13409 478 DEPSAHLDVEqrlAVAKAIRRIAE--EREATALVVDHDIYMIDYISDRLmVFEGEpGKHGHASGPM-----DMREGMNRF 550
|
....
gi 2017776620 502 LAEV 505
Cdd:PRK13409 551 LKEL 554
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
288-480 |
9.40e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 60.70 E-value: 9.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 288 VDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKP-ESLRRrvGMVF-----QHFNLFPDHTAL 361
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPrDAIRA--GIMLcpedrKAEGIIPVHSVA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 362 ENVMLSLTKIKKMPRSEARGIAEARLTEVGLAERKDHRPAG------LSGGQQQRVAIARALAMDPEVILFDEVTSALDP 435
Cdd:PRK11288 350 DNINISARRHHLRAGCLINNRWEAENADRFIRSLNIKTPSReqlimnLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDV 429
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2017776620 436 ELVKGVLDLMANLGRQGMTMAVVTHEMGFARRVADQVVFMDEGRI 480
Cdd:PRK11288 430 GAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
281-478 |
1.00e-09 |
|
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: 58.50 E-value: 1.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 281 DLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDI-----LLDGESILAMKPESlRRRVGMVFQHFNLF 355
Cdd:cd03290 13 GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnkNESEPSFEATRSRN-RYSVAYAAQKPWLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 356 pDHTALENVMLSLTKIKKmpRSEARGIAEARLTEVGLAERKDHRPAG-----LSGGQQQRVAIARALAMDPEVILFDEVT 430
Cdd:cd03290 92 -NATVEENITFGSPFNKQ--RYKAVTDACSLQPDIDLLPFGDQTEIGerginLSGGQRQRICVARALYQNTNIVFLDDPF 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2017776620 431 SALDPELV-----KGVLDLMANLGRqgmTMAVVTHEMGFARRvADQVVFMDEG 478
Cdd:cd03290 169 SALDIHLSdhlmqEGILKFLQDDKR---TLVLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
300-480 |
1.08e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 60.71 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 300 IIGPSGSGKSTLLRCLNRlVEPKR--GDILLDGESI------------LAMKPESlRRRVGMVfqhfnlfPDHTALENVM 365
Cdd:PRK13549 293 IAGLVGAGRTELVQCLFG-AYPGRweGEIFIDGKPVkirnpqqaiaqgIAMVPED-RKRDGIV-------PVMGVGKNIT 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 366 LS-LTKIKKMPRSEARgiAEARLTEVGLAERK------DHRPAGLSGGQQQRVAIARALAMDPEVILFDEVTSALDP--- 435
Cdd:PRK13549 364 LAaLDRFTGGSRIDDA--AELKTILESIQRLKvktaspELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVgak 441
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2017776620 436 -ELVKgvldLMANLGRQGMTMAVVTHEMGFARRVADQVVFMDEGRI 480
Cdd:PRK13549 442 yEIYK----LINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
300-480 |
1.31e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 60.40 E-value: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 300 IIGPSG---SGKSTLLRCLNRLVEPKRGDILLDGESILAMKP-ESL----------RRRVGMVFqhfnlfpDHTALENvm 365
Cdd:PRK10762 280 ILGVSGlmgAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPqDGLangivyisedRKRDGLVL-------GMSVKEN-- 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 366 LSLTKIKKMPRSEARGIAEARLTEVGLAER--------KDHRPAGLSGGQQQRVAIARALAMDPEVILFDEVTSALDPEL 437
Cdd:PRK10762 351 MSLTALRYFSRAGGSLKHADEQQAVSDFIRlfniktpsMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGA 430
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2017776620 438 VKGVLDLMANLGRQGMTMAVVTHEMGFARRVADQVVFMDEGRI 480
Cdd:PRK10762 431 KKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
284-506 |
1.47e-09 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 60.69 E-value: 1.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 284 VLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGesilamkpeslrrRVGMVFQHFNLFPDhTALEN 363
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------RISFSPQTSWIMPG-TIKDN 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 364 VMLSLTKIKKMPRSEargIAEARLTE-VGLAERKDHRPAG-----LSGGQQQRVAIARALAMDPEVILFDEVTSALDPEL 437
Cdd:TIGR01271 507 IIFGLSYDEYRYTSV---IKACQLEEdIALFPEKDKTVLGeggitLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVT 583
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 438 VKGVLD-----LMANlgrqgMTMAVVTHEMGFARRvADQVVFMDEGRIIEAGSPQQI----------------FDNPQSE 496
Cdd:TIGR01271 584 EKEIFEsclckLMSN-----KTRILVTSKLEHLKK-ADKILLLHEGVCYFYGTFSELqakrpdfsslllgleaFDNFSAE 657
|
250
....*....|
gi 2017776620 497 RLKRFLAEVL 506
Cdd:TIGR01271 658 RRNSILTETL 667
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
285-484 |
1.55e-09 |
|
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: 57.33 E-value: 1.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 285 LKGVDLDIAPGTVTCIIGPSGSGKSTLLRclnrlvepkrgDILldgesilamkPESLRRRVGMVFQHFNlfpdhtalENV 364
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVN-----------EGL----------YASGKARLISFLPKFS--------RNK 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 365 MLSLTKIKkmprseargiaeaRLTEVGLAERKDHRPAG-LSGGQQQRVAIARALAMDPE--VILFDEVTSALDPELVKGV 441
Cdd:cd03238 62 LIFIDQLQ-------------FLIDVGLGYLTLGQKLStLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQL 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2017776620 442 LDLMANLGRQGMTMAVVTHEMGFARRvADQVVFM------DEGRIIEAG 484
Cdd:cd03238 129 LEVIKGLIDLGNTVILIEHNLDVLSS-ADWIIDFgpgsgkSGGKVVFSG 176
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
294-434 |
1.88e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 60.21 E-value: 1.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 294 PGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDI------------------------LLDGESILAMKP---ESLRRRV- 345
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGELIPNLGDYeeepswdevlkrfrgtelqnyfkkLYNGEIKVVHKPqyvDLIPKVFk 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 346 GMVFQhfnlfpdhtALENVmlsltkikkmprsEARGIAEARLTEVGLAERKDHRPAGLSGGQQQRVAIARALAMDPEVIL 425
Cdd:PRK13409 178 GKVRE---------LLKKV-------------DERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYF 235
|
....*....
gi 2017776620 426 FDEVTSALD 434
Cdd:PRK13409 236 FDEPTSYLD 244
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
284-485 |
2.44e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 60.18 E-value: 2.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 284 VLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILldGESILAMKPE-------SLRRRVgmvfqhfnLFP 356
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW--AERSIAYVPQqawimnaTVRGNI--------LFF 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 357 DhtalENVMLSLTKIKKMPRSEA--RGIAEARLTEVGlaerkdHRPAGLSGGQQQRVAIARALAMDPEVILFDEVTSALD 434
Cdd:PTZ00243 745 D----EEDAARLADAVRVSQLEAdlAQLGGGLETEIG------EKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALD 814
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2017776620 435 P---ELVkgVLDLManLGR-QGMTMAVVTHEMGFARRvADQVVFMDEGRIIEAGS 485
Cdd:PTZ00243 815 AhvgERV--VEECF--LGAlAGKTRVLATHQVHVVPR-ADYVVALGDGRVEFSGS 864
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
284-497 |
2.53e-09 |
|
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: 58.33 E-value: 2.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 284 VLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGesilamkpeslrrRVGMVFQHFNLFPDhTALEN 363
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSSQFSWIMPG-TIKEN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 364 VMLSLTKIKKMPRSEargIAEARLTE--VGLAErKDHRPAG-----LSGGQQQRVAIARALAMDPEVILFDEVTSALDPE 436
Cdd:cd03291 118 IIFGVSYDEYRYKSV---VKACQLEEdiTKFPE-KDNTVLGeggitLSGGQRARISLARAVYKDADLYLLDSPFGYLDVF 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2017776620 437 LVKGVLD-----LMANlgrqgMTMAVVTHEMGFARRvADQVVFMDEGRIIEAGSpqqiFDNPQSER 497
Cdd:cd03291 194 TEKEIFEscvckLMAN-----KTRILVTSKMEHLKK-ADKILILHEGSSYFYGT----FSELQSLR 249
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
294-445 |
3.18e-09 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 55.46 E-value: 3.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 294 PGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGD-ILLDGESILAMKPESLRrrvgmvfqhfnlfpdhtalenvmlsltkik 372
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGvIYIDGEDILEEVLDQLL------------------------------ 50
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2017776620 373 kmprseargiaearltevglAERKDHRPAGLSGGQQQRVAIARALAMDPEVILFDEVTSALDPELVKGVLDLM 445
Cdd:smart00382 51 --------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLE 103
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
284-438 |
3.26e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 59.36 E-value: 3.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 284 VLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPkrgdilLDGESILAmkpESLrrRVGMVFQHFNLFPDHTALEN 363
Cdd:PRK11819 22 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKE------FEGEARPA---PGI--KVGYLPQEPQLDPEKTVREN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 364 VMLSLTKIKKmprseargiAEARLTEVG------------LAERK---------------DHR----------PAG---- 402
Cdd:PRK11819 91 VEEGVAEVKA---------ALDRFNEIYaayaepdadfdaLAAEQgelqeiidaadawdlDSQleiamdalrcPPWdakv 161
|
170 180 190
....*....|....*....|....*....|....*...
gi 2017776620 403 --LSGGQQQRVAIARALAMDPEVILFDEVTSALDPELV 438
Cdd:PRK11819 162 tkLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESV 199
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
293-462 |
6.09e-09 |
|
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: 56.99 E-value: 6.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 293 APGTVTCIIGPSGSGKSTLLRCLNRLVEPKRG---------DI---------------LLDGESILAMKPeslrrrvgmv 348
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGkfddppdwdEIldefrgselqnyftkLLEGDVKVIVKP---------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 349 fQHFNLFPDhTALENVMLSLTKIKKmprseaRGIAEARLTEVGLAERKDHRPAGLSGGQQQRVAIARALAMDPEVILFDE 428
Cdd:cd03236 94 -QYVDLIPK-AVKGKVGELLKKKDE------RGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDE 165
|
170 180 190
....*....|....*....|....*....|....
gi 2017776620 429 VTSALDPELVKGVLDLMANLGRQGMTMAVVTHEM 462
Cdd:cd03236 166 PSSYLDIKQRLNAARLIRELAEDDNYVLVVEHDL 199
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
285-467 |
1.48e-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: 53.90 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 285 LKGVDLDIAPGTVTCIIGPSGSGKSTLLRClnrlvepkrgdILLdgesILAMKPESLRRRVGMVFQHFnlfpdhtalenv 364
Cdd:cd03227 11 FVPNDVTFGEGSLTIITGPNGSGKSTILDA-----------IGL----ALGGAQSATRRRSGVKAGCI------------ 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 365 mlsltkikkmprsEARGIAEARLTEVGLaerkdhrpaglSGGQQQRVAIARALA---MDPE-VILFDEVTSALDPELVKG 440
Cdd:cd03227 64 -------------VAAVSAELIFTRLQL-----------SGGEKELSALALILAlasLKPRpLYILDEIDRGLDPRDGQA 119
|
170 180
....*....|....*....|....*..
gi 2017776620 441 VLDLMANLGRQGMTMAVVTHEMGFARR 467
Cdd:cd03227 120 LAEAILEHLVKGAQVIVITHLPELAEL 146
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
268-435 |
1.71e-08 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 57.23 E-value: 1.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 268 GALRVRDLSMAY--GDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKrGDILLDGESILAMKPESLRRRV 345
Cdd:TIGR01271 1216 GQMDVQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWNSVTLQTWRKAF 1294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 346 GMVFQHFNLFPDhtaleNVMLSLTKIKKMPRSEARGIAEarltEVGLAERKDHRPAG-----------LSGGQQQRVAIA 414
Cdd:TIGR01271 1295 GVIPQKVFIFSG-----TFRKNLDPYEQWSDEEIWKVAE----EVGLKSVIEQFPDKldfvlvdggyvLSNGHKQLMCLA 1365
|
170 180
....*....|....*....|.
gi 2017776620 415 RALAMDPEVILFDEVTSALDP 435
Cdd:TIGR01271 1366 RSILSKAKILLLDEPSAHLDP 1386
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
270-461 |
2.39e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 54.19 E-value: 2.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESIlAMKPESLRRRVGMVF 349
Cdd:PRK13540 2 LDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI-KKDLCTYQKQLCFVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 350 QHFNLFPDHTALENVMLSLTKikkmpRSEARGIAEArLTEVGLAERKDHrPAG-LSGGQQQRVAIARALAMDPEVILFDE 428
Cdd:PRK13540 81 HRSGINPYLTLRENCLYDIHF-----SPGAVGITEL-CRLFSLEHLIDY-PCGlLSSGQKRQVALLRLWMSKAKLWLLDE 153
|
170 180 190
....*....|....*....|....*....|...
gi 2017776620 429 VTSALDPELVKGVLDLMANLGRQGMTMAVVTHE 461
Cdd:PRK13540 154 PLVALDELSLLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
269-326 |
4.41e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 55.67 E-value: 4.41e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2017776620 269 ALRVRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDI 326
Cdd:PRK15064 319 ALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV 376
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
274-506 |
5.22e-08 |
|
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: 52.57 E-value: 5.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 274 DLSMAYGDLDVLkgVDL-DIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESIlAMKPEslrrrvgmvfqhf 352
Cdd:cd03222 5 DCVKRYGVFFLL--VELgVVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITP-VYKPQ------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 353 nlfpdhtalenvmlsltKIKkmprseargiaearltevglaerkdhrpagLSGGQQQRVAIARALAMDPEVILFDEVTSA 432
Cdd:cd03222 69 -----------------YID------------------------------LSGGELQRVAIAAALLRNATFYLFDEPSAY 101
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2017776620 433 LDPELVKGVLDLMANLGRQGM-TMAVVTHEMGFARRVADQVvfmdegrIIEAGSPQQ--IFDNPQSER--LKRFLAEVL 506
Cdd:cd03222 102 LDIEQRLNAARAIRRLSEEGKkTALVVEHDLAVLDYLSDRI-------HVFEGEPGVygIASQPKGTRegINRFLRGYL 173
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
285-492 |
6.09e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 55.28 E-value: 6.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 285 LKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPESLRRRVgmvfqhfnlfpdhTALENV 364
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSGLNGQL-------------TGIENI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 365 -----MLSLTKiKKMPRSEARGIAEArltEVGlaeRKDHRPAG-LSGGQQQRVAIARALAMDPEVILFDEVTSALDPELV 438
Cdd:PRK13545 107 elkglMMGLTK-EKIKEIIPEIIEFA---DIG---KFIYQPVKtYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFT 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2017776620 439 KGVLDLMANLGRQGMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQIFDN 492
Cdd:PRK13545 180 KKCLDKMNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDH 233
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
274-436 |
1.12e-07 |
|
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: 54.41 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 274 DLSMAYGD--LDVLKGvdlDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDIllDGESILAMKPESLRRRVGMVFQH 351
Cdd:COG1245 346 DLTKSYGGfsLEVEGG---EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV--DEDLKISYKPQYISPDYDGTVEE 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 352 F------NLFPDHTALENVM--LSLTKIkkmprseargiAEARLTEvglaerkdhrpagLSGGQQQRVAIARALAMDPEV 423
Cdd:COG1245 421 FlrsantDDFGSSYYKTEIIkpLGLEKL-----------LDKNVKD-------------LSGGELQRVAIAACLSRDADL 476
|
170
....*....|...
gi 2017776620 424 ILFDEVTSALDPE 436
Cdd:COG1245 477 YLLDEPSAHLDVE 489
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
285-486 |
1.27e-07 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 53.00 E-value: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 285 LKGVDLDIAPGTVTCIIGPSGSGKSTLL-----RCLNRL-----VEPKRGD-----------ILLDgESILAMKPESLRR 343
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLIndtlyPALARRlhlkkEQPGNHDrieglehidkvIVID-QSPIGRTPRSNPA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 344 RVGMVFQHF-NLFPD--------HTALEnVML---SLTKIKKMPRSEAR-------GIAE--ARLTEVGLAERKDHRPAG 402
Cdd:cd03271 90 TYTGVFDEIrELFCEvckgkrynRETLE-VRYkgkSIADVLDMTVEEALeffenipKIARklQTLCDVGLGYIKLGQPAT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 403 -LSGGQQQRVAIARALAM---DPEVILFDEVTSALDPELVKGVLDLMANLGRQGMTMAVVTHEMGFArRVADQVVFMDE- 477
Cdd:cd03271 169 tLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVI-KCADWIIDLGPe 247
|
250
....*....|....
gi 2017776620 478 -----GRIIEAGSP 486
Cdd:cd03271 248 ggdggGQVVASGTP 261
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
270-480 |
1.38e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 54.02 E-value: 1.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLdGESIlamkpeslrrRVGMVF 349
Cdd:PRK10636 313 LKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL-AKGI----------KLGYFA 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 350 QH---FnLFPDHTALENvmlsLTKI-KKMPRSEAR------GIAEARLTEVglAERkdhrpagLSGGQQQRVAIARALAM 419
Cdd:PRK10636 382 QHqleF-LRADESPLQH----LARLaPQELEQKLRdylggfGFQGDKVTEE--TRR-------FSGGEKARLVLALIVWQ 447
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 420 DPEVILFDEVTSALDpelvkgvLDLmanlgRQGMTMA---------VVTHEMGFARRVADQVVFMDEGRI 480
Cdd:PRK10636 448 RPNLLLLDEPTNHLD-------LDM-----RQALTEAlidfegalvVVSHDRHLLRSTTDDLYLVHDGKV 505
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
285-484 |
5.12e-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: 50.72 E-value: 5.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 285 LKGVDLDIAPGTVTCIIGPSGSGKSTLlrCLNRLVEPKRGDILldgESIlamkPESLRRRVGMVFQhfnlfPDHTALENv 364
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSL--AFDTIYAEGQRRYV---ESL----SAYARQFLGQMDK-----PDVDSIEG- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 365 mLSLT------KIKKMPRSEARGIAE---------AR---------LTEVGLAERKDHRPAG-LSGGQQQRVAIARALAM 419
Cdd:cd03270 76 -LSPAiaidqkTTSRNPRSTVGTVTEiydylrllfARvgirerlgfLVDVGLGYLTLSRSAPtLSGGEAQRIRLATQIGS 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2017776620 420 DPEVIL--FDEVTSALDPELVKGVLDLMANLGRQGMTMAVVTHEMGFARRvADQVVFMDEGRIIEAG 484
Cdd:cd03270 155 GLTGVLyvLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIRA-ADHVIDIGPGAGVHGG 220
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
282-461 |
5.85e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 52.54 E-value: 5.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 282 LDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCL-----NRLVEpkrGDILLDGesiLAMKPESLRRRVGMVFQHFNLFP 356
Cdd:PLN03140 893 LQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLagrktGGYIE---GDIRISG---FPKKQETFARISGYCEQNDIHSP 966
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 357 DHTALENVMLS--LTKIKKMPRSEARGIAEARLTEVGLAERKDH---RPA--GLSGGQQQRVAIARALAMDPEVILFDEV 429
Cdd:PLN03140 967 QVTVRESLIYSafLRLPKEVSKEEKMMFVDEVMELVELDNLKDAivgLPGvtGLSTEQRKRLTIAVELVANPSIIFMDEP 1046
|
170 180 190
....*....|....*....|....*....|..
gi 2017776620 430 TSALDPELVKGVLDLMANLGRQGMTMAVVTHE 461
Cdd:PLN03140 1047 TSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQ 1078
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
289-489 |
7.33e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 51.55 E-value: 7.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 289 DLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPESLRRRVGMVFQHFN---LFPD-----HTA 360
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKLVSDEWQRNNtdmLSPGeddtgRTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 361 LENVMLSltkIKKMPRSEArgIAEarltEVGLAERKDHRPAGLSGGQQQRVAIARALAMDPEVILFDEVTSALDPELVKG 440
Cdd:PRK10938 103 AEIIQDE---VKDPARCEQ--LAQ----QFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQ 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2017776620 441 VLDLMANLGRQGMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQI 489
Cdd:PRK10938 174 LAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEI 222
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
287-480 |
7.68e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 51.78 E-value: 7.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 287 GVDLDiapgTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILldgesilamkpESLRRRVGMVFQHFnlfpdhtaLENVML 366
Cdd:PLN03073 531 GIDLD----SRIAMVGPNGIGKSTILKLISGELQPSSGTVF-----------RSAKVRMAVFSQHH--------VDGLDL 587
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 367 SLTKIKKMPRSEArGIAE----ARLTEVGLAERKDHRPA-GLSGGQQQRVAIARALAMDPEVILFDEVTSALDPELVKGV 441
Cdd:PLN03073 588 SSNPLLYMMRCFP-GVPEqklrAHLGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEAL 666
|
170 180 190
....*....|....*....|....*....|....*....
gi 2017776620 442 LDLMAnLGRQGMTMavVTHEMGFARRVADQVVFMDEGRI 480
Cdd:PLN03073 667 IQGLV-LFQGGVLM--VSHDEHLISGSVDELWVVSEGKV 702
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
285-489 |
8.81e-07 |
|
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: 51.55 E-value: 8.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 285 LKGVDLDIAPGTVTCIIGPSGSGKSTLL-----RCL-NRL----VEPKRGD-----------ILLDGESI---------- 333
Cdd:TIGR00630 624 LKNITVSIPLGLFTCITGVSGSGKSTLIndtlyPALaNRLngakTVPGRYTsieglehldkvIHIDQSPIgrtprsnpat 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 334 -----------LAMKPESLRRrvGMVFQHF----------------------NLFPD--------HTA------LENVML 366
Cdd:TIGR00630 704 ytgvfdeirelFAETPEAKVR--GYTPGRFsfnvkggrceacqgdgvikiemHFLPDvyvpcevcKGKrynretLEVKYK 781
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 367 --SLTKIKKMPRSEARGIAEA---------RLTEVGLAERKDHRPA-GLSGGQQQRVAIARAL---AMDPEVILFDEVTS 431
Cdd:TIGR00630 782 gkNIADVLDMTVEEAYEFFEAvpsisrklqTLCDVGLGYIRLGQPAtTLSGGEAQRIKLAKELskrSTGRTLYILDEPTT 861
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2017776620 432 ALDPELVKGVLDLMANLGRQGMTMAVVTHEMGFArRVADQVVFMDE------GRIIEAGSPQQI 489
Cdd:TIGR00630 862 GLHFDDIKKLLEVLQRLVDKGNTVVVIEHNLDVI-KTADYIIDLGPeggdggGTVVASGTPEEV 924
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
383-499 |
1.64e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 50.63 E-value: 1.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 383 AEARLTEV--GL---AERKDHRPAGLSGGQQQRVAIARALAMDPEVILFDEVTSALDpelVKGVLDLMANLGRQGMTMAV 457
Cdd:PLN03073 320 AEARAASIlaGLsftPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD---LHAVLWLETYLLKWPKTFIV 396
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2017776620 458 VTHEMGFARRVADQVVFMDEGRIIEAGSPQQIFDNPQSERLK 499
Cdd:PLN03073 397 VSHAREFLNTVVTDILHLHGQKLVTYKGDYDTFERTREEQLK 438
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
285-501 |
1.69e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 49.43 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 285 LKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGE-SILAMKPeslrrrvgmvfqhfNLFPDHTALEN 363
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEvSVIAISA--------------GLSGQLTGIEN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 364 V---MLSLTKIKKMPRSEARGIAEarLTEVGlaeRKDHRPA-GLSGGQQQRVAIARALAMDPEVILFDEVTSALDPELVK 439
Cdd:PRK13546 106 IefkMLCMGFKRKEIKAMTPKIIE--FSELG---EFIYQPVkKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQ 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2017776620 440 GVLDLMANLGRQGMTMAVVTHEMGFARRVADQVVFMDEGRIIEAGSPQQIFdnPQSER-LKRF 501
Cdd:PRK13546 181 KCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVL--PKYEAfLNDF 241
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
270-436 |
1.72e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 50.50 E-value: 1.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 270 LRVRDLSMAYGDLDVLKGVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLdGESIlamkpeslrrRVGMVF 349
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETV----------KLAYVD 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 350 Q-HFNLFPDHTALENV-----MLSLTKiKKMPrseARGIAeARLTEVGLAERKdhrPAG-LSGGQQQRVAIARALAMDPE 422
Cdd:PRK11819 394 QsRDALDPNKTVWEEIsggldIIKVGN-REIP---SRAYV-GRFNFKGGDQQK---KVGvLSGGERNRLHLAKTLKQGGN 465
|
170
....*....|....
gi 2017776620 423 VILFDEVTSALDPE 436
Cdd:PRK11819 466 VLLLDEPTNDLDVE 479
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
291-460 |
3.81e-06 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 49.36 E-value: 3.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 291 DIAPGTVTCIIGPSGSGKSTLLRCLN--------RLVEPKRGDILLdgesiLAMKP----ESLRRRVgmvfqhfnLFPDh 358
Cdd:TIGR00954 474 EVPSGNNLLICGPNGCGKSSLFRILGelwpvyggRLTKPAKGKLFY-----VPQRPymtlGTLRDQI--------IYPD- 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 359 talenvmlsltKIKKMPRseaRGIAEARLTEVGLAERKDH---RPAG----------LSGGQQQRVAIARALAMDPEVIL 425
Cdd:TIGR00954 540 -----------SSEDMKR---RGLSDKDLEQILDNVQLTHileREGGwsavqdwmdvLSGGEKQRIAMARLFYHKPQFAI 605
|
170 180 190
....*....|....*....|....*....|....*.
gi 2017776620 426 FDEVTSALDPElvkgVLDLMANLGRQ-GMTMAVVTH 460
Cdd:TIGR00954 606 LDECTSAVSVD----VEGYMYRLCREfGITLFSVSH 637
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
290-460 |
4.31e-06 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 47.70 E-value: 4.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 290 LDIAPGtVTCIIGPSGSGKSTLLRCL-------NRLVEPKRGDILLDGES--------ILAMKPESLRRRVGMVFQHFNL 354
Cdd:COG0419 19 IDFDDG-LNLIVGPNGAGKSTILEAIryalygkARSRSKLRSDLINVGSEeasvelefEHGGKRYRIERRQGEFAEFLEA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 355 FPDH--TALENvMLSLTKIKKMPR--SEARGIAEARLTEVGLAERKDHR----------PAGLSGGQQQRVAIARALAMd 420
Cdd:COG0419 98 KPSErkEALKR-LLGLEIYEELKErlKELEEALESALEELAELQKLKQEilaqlsgldpIETLSGGERLRLALADLLSL- 175
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2017776620 421 peviLFDevTSALDPELVKGVLDLMANLgrqgmtmAVVTH 460
Cdd:COG0419 176 ----ILD--FGSLDEERLERLLDALEEL-------AIITH 202
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
403-480 |
7.78e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 48.19 E-value: 7.78e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2017776620 403 LSGGQQQRVAIARALAMDPEVILFDEVTSALDPELVKGVLDLMANLGRQGMTMAVVTHEMGFARRVADQVVFMDEGRI 480
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| FbpB |
COG1178 |
ABC-type Fe3+ transport system, permease component [Inorganic ion transport and metabolism]; |
29-163 |
1.32e-05 |
|
ABC-type Fe3+ transport system, permease component [Inorganic ion transport and metabolism];
Pssm-ID: 440791 [Multi-domain] Cd Length: 538 Bit Score: 47.85 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 29 LKNTLILAAASTVLGVIIGMVLAvmgisqsrWL----RLPARiytDIFRGL-------PAIVTILIIGQGFARIG----- 92
Cdd:COG1178 56 LGNTLLLALLVTLLSLLLGVPLA--------WLlartDFPGR---RLLRWLlllplalPPYVVALAWIALFGPNGllntl 124
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2017776620 93 -RELFGPSPFPL----GII---ALSLIAGAYIgeIFRSGIQSVERGQMEACRALSMSYGQGMRLIVIPQgvrrVLPALV 163
Cdd:COG1178 125 lRALFGLEPPDIyglgGIIlvlVLFNYPYVYL--LLRAALRSIDASLEEAARSLGASPWRAFRRVTLPL----LRPAIA 197
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
285-502 |
3.02e-05 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 46.15 E-value: 3.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 285 LKGVDLDIAPGtVTCIIGPSGSGKSTLLRCLNRLVEPKRGDILLDGESILAMKPESLRRRVGMVFQH-----FNLFPDHT 359
Cdd:COG3593 14 IKDLSIELSDD-LTVLVGENNSGKSSILEALRLLLGPSSSRKFDEEDFYLGDDPDLPEIEIELTFGSllsrlLRLLLKEE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 360 ALENVMLSLTKIKKMPRSEARGIAE---------------------------ARLTEVGLAERKDHRPAGLSGGQQQRVA 412
Cdd:COG3593 93 DKEELEEALEELNEELKEALKALNEllseylkelldgldlelelsldeledlLKSLSLRIEDGKELPLDRLGSGFQRLIL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 413 IARALAM-------DPEVILFDEVTSALDPELVKGVLDLMANLGRQGMTMAVVTHEMGFARRV-ADQVVFMDEGRIIEAG 484
Cdd:COG3593 173 LALLSALaelkrapANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTHSPHLLSEVpLENIRRLRRDSGGTTS 252
|
250
....*....|....*...
gi 2017776620 485 SPQQIFDNPQSERLKRFL 502
Cdd:COG3593 253 TKLIDLDDEDLRKLLRYL 270
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
285-312 |
3.59e-05 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 46.60 E-value: 3.59e-05
10 20
....*....|....*....|....*...
gi 2017776620 285 LKGVDLDIAPGTVTCIIGPSGSGKSTLL 312
Cdd:PRK00349 625 LKNVDVEIPLGKFTCVTGVSGSGKSTLI 652
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
285-311 |
3.97e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 46.56 E-value: 3.97e-05
10 20
....*....|....*....|....*..
gi 2017776620 285 LKGVDLDIAPGTVTCIIGPSGSGKSTL 311
Cdd:COG0178 621 LKNVDVEIPLGVLTCVTGVSGSGKSTL 647
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
301-434 |
5.10e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 45.65 E-value: 5.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 301 IGPSGSGKSTLLRCLNRLVEPKRGDILLD-GEsilamkpeslrrRVGMVFQHFNLFPDHTALENVML---SLTKIKK--- 373
Cdd:PRK15064 33 IGANGCGKSTFMKILGGDLEPSAGNVSLDpNE------------RLGKLRQDQFAFEEFTVLDTVIMghtELWEVKQerd 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 374 ----MPR-SEARGI----------------AEAR----LTEVGLAERKDHRP-AGLSGGQQQRVAIARALAMDPEVILFD 427
Cdd:PRK15064 101 riyaLPEmSEEDGMkvadlevkfaemdgytAEARagelLLGVGIPEEQHYGLmSEVAPGWKLRVLLAQALFSNPDILLLD 180
|
....*..
gi 2017776620 428 EVTSALD 434
Cdd:PRK15064 181 EPTNNLD 187
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
287-321 |
5.37e-05 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 41.05 E-value: 5.37e-05
10 20 30
....*....|....*....|....*....|....*
gi 2017776620 287 GVDLDIAPGTVTCIIGPSGSGKSTLLRCLNRLVEP 321
Cdd:pfam13555 14 GHTIPIDPRGNTLLTGPSGSGKSTLLDAIQTLLVP 48
|
|
| FbpB |
COG1178 |
ABC-type Fe3+ transport system, permease component [Inorganic ion transport and metabolism]; |
12-152 |
6.61e-05 |
|
ABC-type Fe3+ transport system, permease component [Inorganic ion transport and metabolism];
Pssm-ID: 440791 [Multi-domain] Cd Length: 538 Bit Score: 45.54 E-value: 6.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 12 LDWDAMAEVLPSMITVG-LKNTLILAAASTVLGVIIGMVLAVMgisqSRWLRLPARIYTDIFRGLPAIVTILIIGQGFAR 90
Cdd:COG1178 322 LTLDNYRFVLLDPSLLRaLLNSLLLALLAALLAVLLALLLAYL----VRRRRGRLARLLDRLAMLPYAVPGIVLGLGLLL 397
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2017776620 91 IGRELFGPS---PFPLGIIALSLIAGAYIGEIFRSGIQSVERGQMEACRALSMSYGQGMRLIVIP 152
Cdd:COG1178 398 LFNRPLPLLlygTLAILVLAYVVRFLPFALRSLEAALAQIDPSLEEAARSLGASPLRTLRRVTLP 462
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
285-315 |
5.25e-04 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 41.33 E-value: 5.25e-04
10 20 30
....*....|....*....|....*....|.
gi 2017776620 285 LKGVDLDIAPGtVTCIIGPSGSGKSTLLRCL 315
Cdd:pfam13476 9 FRDQTIDFSKG-LTLITGPNGSGKTTILDAI 38
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
397-502 |
5.38e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.89 E-value: 5.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 397 DHRPAG-----LSGGQQQRVAIARAL---AMDPEVILFDEVTSALDPELVKGVLDLMANLGRQGMTMAVVTHEMGFArRV 468
Cdd:PRK00635 799 DYLPLGrplssLSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNMHVV-KV 877
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2017776620 469 ADQVVFMDE------GRIIEAGSPQQIF--DNPQSERLKRFL 502
Cdd:PRK00635 878 ADYVLELGPeggnlgGYLLASCSPEELIhlHTPTAKALRPYL 919
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
401-495 |
6.83e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.51 E-value: 6.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 401 AGLSGGQQQRVAIARALAMDPEVILF--DEVTSALDPELVKGVLDLMANLGRQGMTMAVVTHE---MGFARRVAD----Q 471
Cdd:PRK00635 475 ATLSGGEQERTALAKHLGAELIGITYilDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDeqmISLADRIIDigpgA 554
|
90 100
....*....|....*....|....
gi 2017776620 472 VVFmdEGRIIEAGSPQQIFDNPQS 495
Cdd:PRK00635 555 GIF--GGEVLFNGSPREFLAKSDS 576
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
285-311 |
7.76e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 42.32 E-value: 7.76e-04
10 20
....*....|....*....|....*..
gi 2017776620 285 LKGVDLDIAPGTVTCIIGPSGSGKSTL 311
Cdd:COG0178 16 LKNIDVDIPRNKLVVITGLSGSGKSSL 42
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
387-495 |
1.78e-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: 41.15 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 387 LTEVGLAERKDHRPAG-LSGGQQQRVAIARALAMDPEVILF--DEVTSALDPELVKGVLDLMANLGRQGMTMAVVTHEMG 463
Cdd:TIGR00630 472 LIDVGLDYLSLSRAAGtLSGGEAQRIRLATQIGSGLTGVLYvlDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDED 551
|
90 100 110
....*....|....*....|....*....|....*...
gi 2017776620 464 fARRVADQVVFMDE------GRIIEAGSPQQIFDNPQS 495
Cdd:TIGR00630 552 -TIRAADYVIDIGPgagehgGEVVASGTPEEILANPDS 588
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
401-502 |
2.64e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.58 E-value: 2.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 401 AGLSGGQQQRVAIARALAMDPE---VILFDEVTSALDPELVKGVLDLMANLGRQGMTMAVVTHEMGFARRvADQVVFMD- 476
Cdd:PRK00635 1698 SSLSLSEKIAIKIAKFLYLPPKhptLFLLDEIATSLDNQQKSALLVQLRTLVSLGHSVIYIDHDPALLKQ-ADYLIEMGp 1776
|
90 100 110
....*....|....*....|....*....|.
gi 2017776620 477 -----EGRIIEAGSPQQIFDNPQSErLKRFL 502
Cdd:PRK00635 1777 gsgktGGKILFSGPPKDISASKDSL-LKTYM 1806
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
285-318 |
3.72e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 39.53 E-value: 3.72e-03
10 20 30
....*....|....*....|....*....|....
gi 2017776620 285 LKGVDLDIAPgtVTCIIGPSGSGKSTLLRCLNRL 318
Cdd:COG4637 13 LRDLELPLGP--LTVLIGANGSGKSNLLDALRFL 44
|
|
| RepA_RSF1010_like |
cd01125 |
Hexameric Replicative Helicase RepA of plasmid RSF1010 and related proteins; This family ... |
295-386 |
3.79e-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: 38.90 E-value: 3.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 295 GTVTCIIGPSGSGKSTLLRCLNRLV----------EPKRGDIL-LDGESilamKPESLRRRVGMVFQHFNLFPDHTA--- 360
Cdd:cd01125 1 GTLGMLVGPPGSGKSFLALDLAVAVatgrdwlgerRVKQGRVVyLAAED----PRDGLRRRLKAIGAHLGDEDAALAenl 76
|
90 100
....*....|....*....|....*..
gi 2017776620 361 -LENVMLSLTKIKKMPRSEARGIAEAR 386
Cdd:cd01125 77 vIENLRGKPVSIDAEAPELERIIEELE 103
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
297-467 |
4.05e-03 |
|
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: 38.74 E-value: 4.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 297 VTCIIGPSGSGKSTLLRCLN----RLVEP--KRGDILLDgesiLAMKPESlRRRVGMVFQHFNlfpDHT--------ALE 362
Cdd:cd03240 24 LTLIVGQNGAGKTTIIEALKyaltGELPPnsKGGAHDPK----LIREGEV-RAQVKLAFENAN---GKKytitrslaILE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 363 NVMLSltkikkmPRSEARGIAEarltevglaerkdhRPAG-LSGGQQQ------RVAIARALAMDPEVILFDEVTSALDP 435
Cdd:cd03240 96 NVIFC-------HQGESNWPLL--------------DMRGrCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDE 154
|
170 180 190
....*....|....*....|....*....|....
gi 2017776620 436 ELVKGVL-DLMANLGRQG-MTMAVVTHEMGFARR 467
Cdd:cd03240 155 ENIEESLaEIIEERKSQKnFQLIVITHDEELVDA 188
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
297-318 |
7.34e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 38.52 E-value: 7.34e-03
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
294-448 |
8.53e-03 |
|
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213239 [Multi-domain] Cd Length: 243 Bit Score: 38.01 E-value: 8.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 294 PGTVTCIIGPSGSGKSTLLRCLnRLV---------EPKRGDILLDGESILAM------------------KPE-SLRRRV 345
Cdd:cd03272 22 SPKHNVVVGRNGSGKSNFFAAI-RFVlsdeythlrEEQRQALLHEGSGPSVMsayveiifdnsdnrfpidKEEvRLRRTI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017776620 346 GmvfqhfnLFPDHTALENVMLSLTKIKKMprSEARGIA---------EARLTEVGLAERKD-HRPAGLSGGQQQRVAIAR 415
Cdd:cd03272 101 G-------LKKDEYFLDKKNVTKNDVMNL--LESAGFSrsnpyyivpQGKINSLTNMKQDEqQEMQQLSGGQKSLVALAL 171
|
170 180 190
....*....|....*....|....*....|....*..
gi 2017776620 416 ALAM---DPE-VILFDEVTSALDPELVKGVLDLMANL 448
Cdd:cd03272 172 IFAIqkcDPApFYLFDEIDAALDAQYRTAVANMIKEL 208
|
|
| |
