|
Name |
Accession |
Description |
Interval |
E-value |
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
11-236 |
1.33e-52 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 170.24 E-value: 1.33e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 11 HLSRHHLGHgaEVVLRDLDVQLEHGERVALLGASGAGKSTLLEAL----------------------RSALHEQGTPAAW 68
Cdd:COG3638 7 NLSKRYPGG--TPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLnglveptsgeilvdgqdvtalrGRALRRLRRRIGM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 69 CPQRQGLVPQLSVYHNIFMGRLDQqsSLTNLLNLLRPRPAHWQAVAAVCEPLGIAGLMERSVEALSGGQRQRVAIARALY 148
Cdd:COG3638 85 IFQQFNLVPRLSVLTNVLAGRLGR--TSTWRSLLGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIARALV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 149 QGHDLFLGDEPVASVDPHQASQ---LIHWIHSRHATSVVA-LHQKELALTHFTRVIGLgKDengnGKVLLDANTDDLKPQ 224
Cdd:COG3638 163 QEPKLILADEPVASLDPKTARQvmdLLRRIAREDGITVVVnLHQVDLARRYADRIIGL-RD----GRVVFDGPPAELTDA 237
|
250
....*....|..
gi 1148626600 225 DLDCLYPAASSE 236
Cdd:COG3638 238 VLREIYGGEAEE 249
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
11-230 |
9.63e-43 |
|
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: 145.02 E-value: 9.63e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 11 HLSRHHlGHGaEVVLRDLDVQLEHGERVALLGASGAGKSTLL--------------------------EALRSALHEQGT 64
Cdd:cd03256 5 NLSKTY-PNG-KKALKDVSLSINPGEFVALIGPSGAGKSTLLrclnglveptsgsvlidgtdinklkgKALRQLRRQIGM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 65 paAWcpQRQGLVPQLSVYHNIFMGRLDQqsSLTNLLNLLRPRPAHWQAVAAVCEPLGIAGLMERSVEALSGGQRQRVAIA 144
Cdd:cd03256 83 --IF--QQFNLIERLSVLENVLSGRLGR--RSTWRSLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 145 RALYQGHDLFLGDEPVASVDPHQASQLIHWI----HSRHATSVVALHQKELALTHFTRVIGLgKDengnGKVLLDANTDD 220
Cdd:cd03256 157 RALMQQPKLILADEPVASLDPASSRQVMDLLkrinREEGITVIVSLHQVDLAREYADRIVGL-KD----GRIVFDGPPAE 231
|
250
....*....|
gi 1148626600 221 LKPQDLDCLY 230
Cdd:cd03256 232 LTDEVLDEIY 241
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
5-230 |
2.44e-35 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 125.97 E-value: 2.44e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 5 TPSPLLHLSRHHLGHGAEVVLRDLDVQLEHGERVALLGASGAGKSTLLEALrsaLHEQ----------GTPAAWCPQRQG 74
Cdd:COG1121 2 MMMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAI---LGLLpptsgtvrlfGKPPRRARRRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 75 LVPQ---------LSVYHNIFMGRLdqqsslTNLLNLLRPRPAHWQAVAAVCEPLGIAGLMERSVEALSGGQRQRVAIAR 145
Cdd:COG1121 79 YVPQraevdwdfpITVRDVVLMGRY------GRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLAR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 146 ALYQGHDLFLGDEPVASVDP-HQAS--QLIHWIHSRHATSVVALHQKELALTHFTRVIGLgkdengNGKVLLDANTDD-L 221
Cdd:COG1121 153 ALAQDPDLLLLDEPFAGVDAaTEEAlyELLRELRREGKTILVVTHDLGAVREYFDRVLLL------NRGLVAHGPPEEvL 226
|
....*....
gi 1148626600 222 KPQDLDCLY 230
Cdd:COG1121 227 TPENLSRAY 235
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
16-206 |
1.26e-34 |
|
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: 124.00 E-value: 1.26e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 16 HLGHGAEVVLRDLDVQLEHGERVALLGASGAGKSTLLEALRSALHEQ-------GTP-AAWCP----QRQGLVPQ----- 78
Cdd:COG1120 8 SVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSsgevlldGRDlASLSRrelaRRIAYVPQeppap 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 79 --LSVYHNIFMGRLDQQSSLTnllnllRPRPAHWQAVAAVCEPLGIAGLMERSVEALSGGQRQRVAIARALYQGHDLFLG 156
Cdd:COG1120 88 fgLTVRELVALGRYPHLGLFG------RPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1148626600 157 DEPVASVDPHQASQLIHWI----HSRHATSVVALHQKELALTHFTRVIGLGKDE 206
Cdd:COG1120 162 DEPTSHLDLAHQLEVLELLrrlaRERGRTVVMVLHDLNLAARYADRLVLLKDGR 215
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
20-230 |
1.72e-34 |
|
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: 123.56 E-value: 1.72e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 20 GAEVVLRDLDVQLEHGERVALLGASGAGKSTLLEAL----------------------RSALHEQGTPAAWCPQRQGLVP 77
Cdd:TIGR02315 13 NGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCInrlvepssgsillegtditklrGKKLRKLRRRIGMIFQHYNLIE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 78 QLSVYHNIFMGRLDQQSSLTNLLnllRPRPAHWQAVAAVC-EPLGIAGLMERSVEALSGGQRQRVAIARALYQGHDLFLG 156
Cdd:TIGR02315 93 RLTVLENVLHGRLGYKPTWRSLL---GRFSEEDKERALSAlERVGLADKAYQRADQLSGGQQQRVAIARALAQQPDLILA 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1148626600 157 DEPVASVDPHQASQLIHW---IHSRHA-TSVVALHQKELALTHFTRVIGLgkdenGNGKVLLDANTDDLKPQDLDCLY 230
Cdd:TIGR02315 170 DEPIASLDPKTSKQVMDYlkrINKEDGiTVIINLHQVDLAKKYADRIVGL-----KAGEIVFDGAPSELDDEVLRHIY 242
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
17-205 |
7.49e-33 |
|
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: 118.40 E-value: 7.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 17 LGHGAEVVLRDLDVQLEHGERVALLGASGAGKSTLLEAL-------RSALHEQGTPAAWCPQRQGLVPQ---------LS 80
Cdd:cd03235 7 VSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAIlgllkptSGSIRVFGKPLEKERKRIGYVPQrrsidrdfpIS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 81 VYHNIFMGRLdqqsslTNLLNLLRPRPAHWQAVAAVCEPLGIAGLMERSVEALSGGQRQRVAIARALYQGHDLFLGDEPV 160
Cdd:cd03235 87 VRDVVLMGLY------GHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPF 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1148626600 161 ASVDPHQASQLIHWI---HSRHATSVVALHQKELALTHFTRVIGLGKD 205
Cdd:cd03235 161 AGVDPKTQEDIYELLrelRREGMTILVVTHDLGLVLEYFDRVLLLNRT 208
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
14-200 |
2.64e-29 |
|
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: 109.09 E-value: 2.64e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 14 RHHLGHGAEVVLRDLDVQLEHGERVALLGASGAGKSTLLEALRSALHEQ-------GTPAAWCPQRQ-----GLVPQ--- 78
Cdd:cd03225 6 SFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTsgevlvdGKDLTKLSLKElrrkvGLVFQnpd 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 79 -----LSVYHNIFMGRLDQQSsltnllnllrPRPAHWQAVAAVCEPLGIAGLMERSVEALSGGQRQRVAIARALYQGHDL 153
Cdd:cd03225 86 dqffgPTVEEEVAFGLENLGL----------PEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1148626600 154 FLGDEPVASVDPHQASQLIHWIHSRHA---TSVVALHQKELALTHFTRVI 200
Cdd:cd03225 156 LLLDEPTAGLDPAGRRELLELLKKLKAegkTIIIVTHDLDLLLELADRVI 205
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
29-221 |
3.08e-28 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 106.76 E-value: 3.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 29 DVQLEHGERVALLGASGAGKSTLLEALRSALHEQ------------GTPAAWCP-----QRQGLVPQLSVYHNIFMGRld 91
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDsgrilwngqdltALPPAERPvsmlfQENNLFPHLTVAQNIGLGL-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 92 qqssltnlLNLLRPRPAHWQAVAAVCEPLGIAGLMERSVEALSGGQRQRVAIARALYQGHDLFLGDEPVASVDPHQASQL 171
Cdd:COG3840 97 --------RPGLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEM 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1148626600 172 IHWI----HSRHATSVVALHQKELALTHFTRVIGLgkdenGNGKVLLDANTDDL 221
Cdd:COG3840 169 LDLVdelcRERGLTVLMVTHDPEDAARIADRVLLV-----ADGRIAADGPTAAL 217
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
16-213 |
5.32e-28 |
|
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: 104.82 E-value: 5.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 16 HLGHGAEVVLRDLDVQLEHGERVALLGASGAGKSTLLEALrsalheqgtpAAWCPQRQGLVpqlsvyhnifmgRLDQQSS 95
Cdd:cd03214 6 SVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTL----------AGLLKPSSGEI------------LLDGKDL 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 96 LTNLLNLLRPRPAHwqaVAAVCEPLGIAGLMERSVEALSGGQRQRVAIARALYQGHDLFLGDEPVASVDPHQASQLIHWI 175
Cdd:cd03214 64 ASLSPKELARKIAY---VPQALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELL 140
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1148626600 176 ----HSRHATSVVALHQKELALTHFTRVIGLgkdenGNGKVL 213
Cdd:cd03214 141 rrlaRERGKTVVMVLHDLNLAARYADRVILL-----KDGRIV 177
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
18-200 |
6.35e-28 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 105.01 E-value: 6.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 18 GHGAEVVLRDLDVQLEHGERVALLGASGAGKSTLLEALRSAL--------HEQGTPAAWCPQRQGLVPQL--SVYHNIFM 87
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLrptsgtvrRAGGARVAYVPQRSEVPDSLplTVRDLVAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 88 GRLdqqsslTNLLNLLRPRPAHWQAVAAVCEPLGIAGLMERSVEALSGGQRQRVAIARALYQGHDLFLGDEPVASVDPHQ 167
Cdd:NF040873 81 GRW------ARRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAES 154
|
170 180 190
....*....|....*....|....*....|....*.
gi 1148626600 168 AS---QLIHWIHSRHATSVVALHQKELALTHFTRVI 200
Cdd:NF040873 155 REriiALLAEEHARGATVVVVTHDLELVRRADPCVL 190
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
19-221 |
4.51e-27 |
|
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: 103.95 E-value: 4.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 19 HGAEVVLRDLDVQLEHGERVALLGASGAGKSTLLEALrSAL--HEQGT-----------PAAWCPQRQGLVPQ------- 78
Cdd:COG1122 11 PGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLL-NGLlkPTSGEvlvdgkditkkNLRELRRKVGLVFQnpddqlf 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 79 -LSVYHNI-F----MGRldqqssltnllnllrPRPAHWQAVAAVCEPLGIAGLMERSVEALSGGQRQRVAIARALYQGHD 152
Cdd:COG1122 90 aPTVEEDVaFgpenLGL---------------PREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1148626600 153 LFLGDEPVASVDPHQASQLIHWI---HSRHATSVVALHQKELALTHFTRVIGLgkdenGNGKVLLDANTDDL 221
Cdd:COG1122 155 VLVLDEPTAGLDPRGRRELLELLkrlNKEGKTVIIVTHDLDLVAELADRVIVL-----DDGRIVADGTPREV 221
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
27-202 |
1.25e-26 |
|
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: 102.19 E-value: 1.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 27 DLDVQLEHGERVALLGASGAGKSTLLEAL---------RSALHEQ---GTPAAWCP-----QRQGLVPQLSVYHNIFMGR 89
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIagfetpqsgRVLINGVdvtAAPPADRPvsmlfQENNLFAHLTVEQNVGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 90 ldqqssltnlLNLLRPRPAHWQAVAAVCEPLGIAGLMERSVEALSGGQRQRVAIARALYQGHDLFLGDEPVASVDP---H 166
Cdd:cd03298 96 ----------SPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPalrA 165
|
170 180 190
....*....|....*....|....*....|....*..
gi 1148626600 167 QASQLIHWIHS-RHATSVVALHQKELALTHFTRVIGL 202
Cdd:cd03298 166 EMLDLVLDLHAeTKMTVLMVTHQPEDAKRLAQRVVFL 202
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
16-202 |
1.91e-26 |
|
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: 101.80 E-value: 1.91e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 16 HLGHGAEVVLRDLDVQLEHGERVALLGASGAGKSTLLEAL-------RSALHEQGTPAAWCP----------------QR 72
Cdd:cd03255 11 GGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILggldrptSGEVRVDGTDISKLSekelaafrrrhigfvfQS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 73 QGLVPQLSVYHNIFMGrldqqssltnLLNLLRPRPAHWQAVAAVCEPLGIAGLMERSVEALSGGQRQRVAIARALYQGHD 152
Cdd:cd03255 91 FNLLPDLTALENVELP----------LLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1148626600 153 LFLGDEPVASVDPHQASQLIHWI----HSRHATSVVALHQKELALtHFTRVIGL 202
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLrelnKEAGTTIVVVTHDPELAE-YADRIIEL 213
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
9-194 |
3.04e-26 |
|
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: 101.06 E-value: 3.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 9 LLHLSRHHlghGAEVVLRDLDVQLEHGERVALLGASGAGKSTLLEAL-------RSALHEQGTPAAWCPQRQ---GLVPQ 78
Cdd:cd03259 3 LKGLSKTY---GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIaglerpdSGEILIDGRDVTGVPPERrniGMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 79 -------LSVYHNIFMGrLDQQSsltnllnllRPRPAHWQAVAAVCEPLGIAGLMERSVEALSGGQRQRVAIARALYQGH 151
Cdd:cd03259 80 dyalfphLTVAENIAFG-LKLRG---------VPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREP 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1148626600 152 DLFLGDEPVASVDPHQASQLIHWI----HSRHATSVVALHQKELALT 194
Cdd:cd03259 150 SLLLLDEPLSALDAKLREELREELkelqRELGITTIYVTHDQEEALA 196
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
7-200 |
4.11e-26 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 101.27 E-value: 4.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 7 SPLLHLS----RHHLGHGAEVVLRDLDVQLEHGERVALLGASGAGKSTLL-------------------------EALRS 57
Cdd:COG1136 2 SPLLELRnltkSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLnilggldrptsgevlidgqdisslsERELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 58 AL--HEQGtpaaWCPQRQGLVPQLSVYHNIFMGRLdqqssltnllNLLRPRPAHWQAVAAVCEPLGIAGLMERSVEALSG 135
Cdd:COG1136 82 RLrrRHIG----FVFQFFNLLPELTALENVALPLL----------LAGVSRKERRERARELLERVGLGDRLDHRPSQLSG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1148626600 136 GQRQRVAIARALYQGHDLFLGDEPVASVDPHQASQLI----HWIHSRHATSVVALHQKELAlTHFTRVI 200
Cdd:COG1136 148 GQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLellrELNRELGTTIVMVTHDPELA-ARADRVI 215
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
25-230 |
1.85e-24 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 97.78 E-value: 1.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 25 LRDLDVQLEHGERVALLGASGAGKSTLLEALRSALHEQGTPAAWCP------QRQG---------------------LVP 77
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAGSHIEllgrtvQREGrlardirksrantgyifqqfnLVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 78 QLSVYHNIFMGRLDQQSSLTNLLNLLRPRPAHwQAVAAVCEpLGIAGLMERSVEALSGGQRQRVAIARALYQGHDLFLGD 157
Cdd:PRK09984 100 RLSVLENVLIGALGSTPFWRTCFSWFTREQKQ-RALQALTR-VGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILAD 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1148626600 158 EPVASVDPHQASQLIHWIHSRHA----TSVVALHQKELALTHFTRVIGLGKdengnGKVLLDANTDDLKPQDLDCLY 230
Cdd:PRK09984 178 EPIASLDPESARIVMDTLRDINQndgiTVVVTLHQVDYALRYCERIVALRQ-----GHVFYDGSSQQFDNERFDHLY 249
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
20-227 |
8.98e-24 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 95.13 E-value: 8.98e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 20 GAEVVLRDLDVQLEHGERVALLGASGAGKSTLLEALRSALH-EQGT-----------PAAWC------PQRQGLVPQLSV 81
Cdd:COG1131 11 GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRpTSGEvrvlgedvardPAEVRrrigyvPQEPALYPDLTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 82 YHNI-FMGRLdqqssltnllnLLRPRPAHWQAVAAVCEPLGIAGLMERSVEALSGGQRQRVAIARALyqGHD---LFLgD 157
Cdd:COG1131 91 RENLrFFARL-----------YGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALAL--LHDpelLIL-D 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1148626600 158 EPVASVDPHQASQ---LIHWIHSRHATSVVALHQKELALTHFTRVIGLGKdengnGKVLLDANTDDLKPQDLD 227
Cdd:COG1131 157 EPTSGLDPEARRElweLLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDK-----GRIVADGTPDELKARLLE 224
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
16-204 |
1.78e-23 |
|
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: 92.31 E-value: 1.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 16 HLGHGAEVVLRDLDVQLEHGERVALLGASGAGKSTLLEALrsalheqgtpaawcpqrQGLVPQLSVyhNIfmgRLDQQSS 95
Cdd:cd00267 6 SFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAI-----------------AGLLKPTSG--EI---LIDGKDI 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 96 LTNLLNLLRPRpahwqavaavceplgIAGLMErsveaLSGGQRQRVAIARALYQGHDLFLGDEPVASVDPHQASQL---I 172
Cdd:cd00267 64 AKLPLEELRRR---------------IGYVPQ-----LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLlelL 123
|
170 180 190
....*....|....*....|....*....|..
gi 1148626600 173 HWIHSRHATSVVALHQKELALTHFTRVIGLGK 204
Cdd:cd00267 124 RELAEEGRTVIIVTHDPELAELAADRVIVLKD 155
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
25-161 |
5.56e-23 |
|
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: 90.78 E-value: 5.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 25 LRDLDVQLEHGERVALLGASGAGKSTLLEALR--------------SALHEQGTPA-----AWCPQRQGLVPQLSVYHNI 85
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAgllsptegtilldgQDLTDDERKSlrkeiGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 86 FMGRLDQqssltnllnlLRPRPAHWQAVAAVCEPLGIAGLMERSVEA----LSGGQRQRVAIARALYQGHDLFLGDEPVA 161
Cdd:pfam00005 81 RLGLLLK----------GLSKREKDARAEEALEKLGLGDLADRPVGErpgtLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
8-203 |
6.89e-23 |
|
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: 92.16 E-value: 6.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 8 PLLHLSRHHLGHGAEVVLRDLDVQLEHGERVALLGASGAGKSTLL------------------EALRSALHEQGTPAAWC 69
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLrilagllppsagevlwngEPIRDAREDYRRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 70 PQRQGLVPQLSVYHNI-FMGRLDQqssltnllnLLRPRPAHWQAVAAVceplGIAGLMERSVEALSGGQRQRVAIARALY 148
Cdd:COG4133 81 GHADGLKPELTVRENLrFWAALYG---------LRADREAIDEALEAV----GLAGLADLPVRQLSAGQKRRVALARLLL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1148626600 149 QGHDLFLGDEPVASVDPHQASQLIHWIhSRHATS----VVALHQkELALThFTRVIGLG 203
Cdd:COG4133 148 SPAPLWLLDEPFTALDAAGVALLAELI-AAHLARggavLLTTHQ-PLELA-AARVLDLG 203
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
16-206 |
1.17e-22 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 91.80 E-value: 1.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 16 HLGHGAEVVLRDLDVQLEHGERVALLGASGAGKSTLLEALRS--ALHE-----------QGTPAAW------CPQRQGLV 76
Cdd:COG4619 7 SFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADldPPTSgeiyldgkplsAMPPPEWrrqvayVPQEPALW 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 77 PQlSVYHNIfmgrldqqssltNLLNLLRPRPAHWQAVAAVCEPLGI-AGLMERSVEALSGGQRQRVAIARALYQGHDLFL 155
Cdd:COG4619 87 GG-TVRDNL------------PFPFQLRERKFDRERALELLERLGLpPDILDKPVERLSGGERQRLALIRALLLQPDVLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1148626600 156 GDEPVASVDPHQASQLIHWIHS---RHATSVVAL-HQKELALTHFTRVIGLGKDE 206
Cdd:COG4619 154 LDEPTSALDPENTRRVEELLREylaEEGRAVLWVsHDPEQIERVADRVLTLEAGR 208
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
20-192 |
1.28e-22 |
|
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: 95.82 E-value: 1.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 20 GAEVVLRDLDVQLEHGERVALLGASGAGKSTLLEAL----------------------RSALHEQgtpAAWCPQRQGLVP 77
Cdd:TIGR02857 333 GRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLlgfvdptegsiavngvpladadADSWRDQ---IAWVPQHPFLFA 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 78 QlSVYHNIFMGRLDQQSSLTNLLNLlrpRPAHWQAVAAVcePLGIAGLMERSVEALSGGQRQRVAIARALYQGHDLFLGD 157
Cdd:TIGR02857 410 G-TIAENIRLARPDASDAEIREALE---RAGLDEFVAAL--PQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLD 483
|
170 180 190
....*....|....*....|....*....|....*..
gi 1148626600 158 EPVASVDPHQASQLIHWIH--SRHATSVVALHQKELA 192
Cdd:TIGR02857 484 EPTAHLDAETEAEVLEALRalAQGRTVLLVTHRLALA 520
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
20-166 |
1.34e-22 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 94.37 E-value: 1.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 20 GAEVVLRDLDVQLEHGERVALLGASGAGKSTLLEALrSALHE-------------QGTPAAwcpQRQ-GLVPQ------- 78
Cdd:COG3839 14 GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMI-AGLEDptsgeiliggrdvTDLPPK---DRNiAMVFQsyalyph 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 79 LSVYHNI-F---MGRLDQQSSLtnllnllrprpahwQAVAAVCEPLGIAGLMERSVEALSGGQRQRVAIARALYQGHDLF 154
Cdd:COG3839 90 MTVYENIaFplkLRKVPKAEID--------------RRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVF 155
|
170
....*....|..
gi 1148626600 155 LGDEPVASVDPH 166
Cdd:COG3839 156 LLDEPLSNLDAK 167
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
20-200 |
2.23e-22 |
|
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: 95.21 E-value: 2.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 20 GAEVVLRDLDVQLEHGERVALLGASGAGKSTLLEAL----------------------RSALHEQgtpAAWCPQRQGLVP 77
Cdd:COG4988 348 GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLlgflppysgsilingvdlsdldPASWRRQ---IAWVPQNPYLFA 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 78 QlSVYHNIFMGRLDqqssltnllnllrprpAHWQAVAAVCEPLGIAGLMERSVE-----------ALSGGQRQRVAIARA 146
Cdd:COG4988 425 G-TIRENLRLGRPD----------------ASDEELEAALEAAGLDEFVAALPDgldtplgeggrGLSGGQAQRLALARA 487
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1148626600 147 LYQGHDLFLGDEPVASVDPHQASQLIHWIH--SRHATSVVALHQKELaLTHFTRVI 200
Cdd:COG4988 488 LLRDAPLLLLDEPTAHLDAETEAEILQALRrlAKGRTVILITHRLAL-LAQADRIL 542
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-165 |
3.64e-22 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 91.69 E-value: 3.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 1 MTQATPspLLHLS----RHHLGHGAEVVLRDLDVQLEHGERVALLGASGAGKSTLLEAL--------------RSALHEQ 62
Cdd:COG1116 1 MSAAAP--ALELRgvskRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIaglekptsgevlvdGKPVTGP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 63 GTPAAWCPQRQGLVPQLSVYHNIFMGrLDQQssltnllnlLRPRPAHWQAVAAVCEPLGIAGLMERSVEALSGGQRQRVA 142
Cdd:COG1116 79 GPDRGVVFQEPALLPWLTVLDNVALG-LELR---------GVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVA 148
|
170 180
....*....|....*....|...
gi 1148626600 143 IARALYQGHDLFLGDEPVASVDP 165
Cdd:COG1116 149 IARALANDPEVLLMDEPFGALDA 171
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
20-199 |
3.88e-22 |
|
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: 90.39 E-value: 3.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 20 GAEVVLRDLDVQLEHGERVALLGASGAGKSTLLEALrsALHEQGT---------------PA----AWCPQRQGLVPQLS 80
Cdd:cd03301 11 GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMI--AGLEEPTsgriyiggrdvtdlpPKdrdiAMVFQNYALYPHMT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 81 VYHNIFMGrldqqssltnLLNLLRPRPAHWQAVAAVCEPLGIAGLMERSVEALSGGQRQRVAIARALYQGHDLFLGDEPV 160
Cdd:cd03301 89 VYDNIAFG----------LKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1148626600 161 ASVDPH---QASQLIHWIHSRH-ATSVVALHQKELALTHFTRV 199
Cdd:cd03301 159 SNLDAKlrvQMRAELKRLQQRLgTTTIYVTHDQVEAMTMADRI 201
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
22-212 |
1.92e-21 |
|
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: 88.93 E-value: 1.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 22 EVVLRDLDVQLEHGERVALLGASGAGKSTLLEALRSALH-EQGT------------PA----AWCPQRQGLVPQLSVYHN 84
Cdd:cd03299 12 EFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKpDSGKillngkditnlpPEkrdiSYVPQNYALFPHMTVYKN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 85 IFMGrldqqssltnLLNLLRPRPAHWQAVAAVCEPLGIAGLMERSVEALSGGQRQRVAIARALYQGHDLFLGDEPVASVD 164
Cdd:cd03299 92 IAYG----------LKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1148626600 165 PHQASQLIHWIHS-RHATSVVALHqkelaLTH-FTRVIGLGkDENG---NGKV 212
Cdd:cd03299 162 VRTKEKLREELKKiRKEFGVTVLH-----VTHdFEEAWALA-DKVAimlNGKL 208
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
16-159 |
1.95e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 92.44 E-value: 1.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 16 HLGHGAEVVLRDLDVQLEHGERVALLGASGAGKSTLLEALR--------SALHEQGTPAAWCPQRQGLVPQLSVYHNIFM 87
Cdd:COG0488 5 SKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAgelepdsgEVSIPKGLRIGYLPQEPPLDDDLTVLDTVLD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 88 G---------RLDQQSSLTNLLNLLRPRPAHWQA-------------VAAVCEPLGIAG-LMERSVEALSGGQRQRVAIA 144
Cdd:COG0488 85 GdaelraleaELEELEAKLAEPDEDLERLAELQEefealggweaearAEEILSGLGFPEeDLDRPVSELSGGWRRRVALA 164
|
170
....*....|....*
gi 1148626600 145 RALYQGHDLFLGDEP 159
Cdd:COG0488 165 RALLSEPDLLLLDEP 179
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
7-229 |
2.26e-21 |
|
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: 92.27 E-value: 2.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 7 SPLLHLS--RHHLGHGAEVVLRDLDVQLEHGERVALLGASGAGKSTLLEALRSALHEQGT---------------PAAWC 69
Cdd:COG1123 2 TPLLEVRdlSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGRisgevlldgrdllelSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 70 PQRQGLVPQlSVYHNIFMGRLDQQSSLTNLLNLLrPRPAHWQAVAAVCEPLGIAGLMERSVEALSGGQRQRVAIARALYQ 149
Cdd:COG1123 82 GRRIGMVFQ-DPMTQLNPVTVGDQIAEALENLGL-SRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 150 GHDLFLGDEPVASVDP---HQASQLIHWIHSRHATSVVAL-HQKELALTHFTRVIGLGKdengnGKVLLDANTDDL--KP 223
Cdd:COG1123 160 DPDLLIADEPTTALDVttqAEILDLLRELQRERGTTVLLItHDLGVVAEIADRVVVMDD-----GRIVEDGPPEEIlaAP 234
|
....*.
gi 1148626600 224 QDLDCL 229
Cdd:COG1123 235 QALAAV 240
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
6-194 |
4.39e-21 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 90.16 E-value: 4.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 6 PSPLLHLSRHHLGHGAEVVLRDLDVQLEHGERVALLGASGAGKSTLLEALrsALHEQ--------------GTPAAwcpQ 71
Cdd:COG3842 2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMI--AGFETpdsgrilldgrdvtGLPPE---K 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 72 RQ-GLVPQ-------LSVYHNI-F---MGRLdqqssltnllnllrPRPAHWQAVAAVCEPLGIAGLMERSVEALSGGQRQ 139
Cdd:COG3842 77 RNvGMVFQdyalfphLTVAENVaFglrMRGV--------------PKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQ 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1148626600 140 RVAIARALYQGHDLFLGDEPVASVDPHQASQLIHWIHSRH----ATSVVALHQKELALT 194
Cdd:COG3842 143 RVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQrelgITFIYVTHDQEEALA 201
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
24-167 |
5.85e-21 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 88.25 E-value: 5.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 24 VLRDLDVQLEHGERVALLGASGAGKSTLLEALRSALHEQ-------GTP-AAWCPQ----RQGLVPQ-------LSVYHN 84
Cdd:COG4559 16 LLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSsgevrlnGRPlAAWSPWelarRRAVLPQhsslafpFTVEEV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 85 IFMGRLdqqssltnllNLLRPRPAHWQAVAAVCEPLGIAGLMERSVEALSGGQRQRVAIARALYQGHD--------LFLg 156
Cdd:COG4559 96 VALGRA----------PHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAQLWEpvdggprwLFL- 164
|
170
....*....|..
gi 1148626600 157 DEPVASVDP-HQ 167
Cdd:COG4559 165 DEPTSALDLaHQ 176
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
23-175 |
8.99e-21 |
|
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: 87.11 E-value: 8.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 23 VVLRDLDVQLEHGERVALLGASGAGKSTLLEAL-------RSALHEQGTP-AAWCPQ---RQGLV---------PQLSVY 82
Cdd:cd03219 14 VALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLIsgflrptSGSVLFDGEDiTGLPPHeiaRLGIGrtfqiprlfPELTVL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 83 HNIFMGRLDQQSSLTNLLNLLRPRPAHWQAVAAVCEPLGIAGLMERSVEALSGGQRQRVAIARALYQGHDLFLGDEPVAS 162
Cdd:cd03219 94 ENVMVAAQARTGSGLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAG 173
|
170
....*....|...
gi 1148626600 163 VDPHQASQLIHWI 175
Cdd:cd03219 174 LNPEETEELAELI 186
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
23-204 |
1.19e-20 |
|
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: 86.69 E-value: 1.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 23 VVLRDLDVQLEHGERVALLGASGAGKSTLLEAL-------RSALHEQGTPAAWCPQRQ--------GLV-------PQLS 80
Cdd:cd03292 15 AALDGINISISAGEFVFLVGPSGAGKSTLLKLIykeelptSGTIRVNGQDVSDLRGRAipylrrkiGVVfqdfrllPDRN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 81 VYHNI-FMGRLDQQSsltnllnllrprPAHWQA-VAAVCEPLGIAGLMERSVEALSGGQRQRVAIARALYQGHDLFLGDE 158
Cdd:cd03292 95 VYENVaFALEVTGVP------------PREIRKrVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADE 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1148626600 159 PVASVDPHQASQ---LIHWIHSRHATSVVALHQKELALTHFTRVIGLGK 204
Cdd:cd03292 163 PTGNLDPDTTWEimnLLKKINKAGTTVVVATHAKELVDTTRHRVIALER 211
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
16-159 |
1.54e-20 |
|
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: 86.33 E-value: 1.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 16 HLGHGAEVVLRDLDVQLEHGERVALLGASGAGKSTLLEALrSALHEQ-------------GTPA--------AWCPQRQG 74
Cdd:cd03224 7 NAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTI-MGLLPPrsgsirfdgrditGLPPheraragiGYVPEGRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 75 LVPQLSVYHNIFMGRldqqssltnllNLLRPRPAHWQaVAAVCE--PLgiagLMERS---VEALSGGQRQRVAIARALYQ 149
Cdd:cd03224 86 IFPELTVEENLLLGA-----------YARRRAKRKAR-LERVYElfPR----LKERRkqlAGTLSGGEQQMLAIARALMS 149
|
170
....*....|
gi 1148626600 150 GHDLFLGDEP 159
Cdd:cd03224 150 RPKLLLLDEP 159
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
21-208 |
4.48e-20 |
|
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: 84.83 E-value: 4.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 21 AEVVLRDLDVQLEHGERVALLGASGAGKSTLLEALRSALH-EQGT-----PAAWCPQrQGLVPQLSVYHNIFMGR-LDQQ 93
Cdd:cd03250 17 TSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEkLSGSvsvpgSIAYVSQ-EPWIQNGTIRENILFGKpFDEE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 94 SsltnllnllrprpaHWQAVAAVC-EP-LGI--AGLM----ERSVeALSGGQRQRVAIARALYQGHDLFLGDEPVASVDP 165
Cdd:cd03250 96 R--------------YEKVIKACAlEPdLEIlpDGDLteigEKGI-NLSGGQKQRISLARAVYSDADIYLLDDPLSAVDA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1148626600 166 HQASQLI------HWIHSRhaTSVVALHQKELaLTHFTRVIGLgkdENG 208
Cdd:cd03250 161 HVGRHIFencilgLLLNNK--TRILVTHQLQL-LPHADQIVVL---DNG 203
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
11-171 |
5.18e-20 |
|
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: 84.83 E-value: 5.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 11 HLSRHHLGHGAEV-VLRDLDVQLEHGERVALLGASGAGKSTLLEALrSALHEQ--------GTPAAWCPQRQGLVPQ--- 78
Cdd:cd03293 5 NVSKTYGGGGGAVtALEDISLSVEEGEFVALVGPSGCGKSTLLRII-AGLERPtsgevlvdGEPVTGPGPDRGYVFQqda 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 79 ----LSVYHNIFMGrLDQQSSLTNLLnllRPRPAHWqaVAAVceplGIAGLMERSVEALSGGQRQRVAIARALYQGHDLF 154
Cdd:cd03293 84 llpwLTVLDNVALG-LELQGVPKAEA---RERAEEL--LELV----GLSGFENAYPHQLSGGMRQRVALARALAVDPDVL 153
|
170
....*....|....*..
gi 1148626600 155 LGDEPVASVDPHQASQL 171
Cdd:cd03293 154 LLDEPFSALDALTREQL 170
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
24-200 |
8.55e-20 |
|
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: 83.20 E-value: 8.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 24 VLRDLDVQLEHGERVALLGASGAGKSTLLEAL-RSALHEQGT-----------PAAWCPQRQGLVPQ------LSVYHNI 85
Cdd:cd03228 17 VLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLlRLYDPTSGEilidgvdlrdlDLESLRKNIAYVPQdpflfsGTIRENI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 86 fmgrldqqssltnllnllrprpahwqavaavceplgiaglmersveaLSGGQRQRVAIARALYQGHDLFLGDEPVASVDP 165
Cdd:cd03228 97 -----------------------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDP 129
|
170 180 190
....*....|....*....|....*....|....*..
gi 1148626600 166 HQASQLIHWIH--SRHATSVVALHQKELALtHFTRVI 200
Cdd:cd03228 130 ETEALILEALRalAKGKTVIVIAHRLSTIR-DADRII 165
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
20-187 |
1.99e-19 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 84.05 E-value: 1.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 20 GAEVVLRDLDVQLEHGERVALLGASGAGKSTLLEAL-------RSALHEQGTP-AAWCP----QRQGLVPQ-------LS 80
Cdd:PRK13548 13 GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALsgelspdSGEVRLNGRPlADWSPaelaRRRAVLPQhsslsfpFT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 81 VYHNIFMGRLDQQSSLTNLLnllrprpahwQAVAAVCEPLGIAGLMERSVEALSGGQRQRVAIARALYQGHD-------L 153
Cdd:PRK13548 93 VEEVVAMGRAPHGLSRAEDD----------ALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAQLWEpdgpprwL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1148626600 154 FLgDEPVASVDP-HQ------ASQLIHwihsRHATSVVA-LH 187
Cdd:PRK13548 163 LL-DEPTSALDLaHQhhvlrlARQLAH----ERGLAVIVvLH 199
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
30-222 |
4.64e-19 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 82.59 E-value: 4.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 30 VQLEHGERVALLGASGAGKSTLLEAL-------RSALHEQGTPAAWCPQRQGLVPQ---------LSVYHNIFMGRldqq 93
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAIlglippaKGTVKVAGASPGKGWRHIGYVPQrhefawdfpISVAHTVMSGR---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 94 ssLTNLLNLLRPRPAHWQAVAAVCEPLGIAGLMERSVEALSGGQRQRVAIARALYQGHDLFLGDEPVASVDPHQASQLIH 173
Cdd:TIGR03771 77 --TGHIGWLRRPCVADFAAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLTE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1148626600 174 WIHSRHA---TSVVALHQKELALTHFTRVIGLgkdengNGKVLLDANTDDLK 222
Cdd:TIGR03771 155 LFIELAGagtAILMTTHDLAQAMATCDRVVLL------NGRVIADGTPQQLQ 200
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
27-164 |
5.41e-19 |
|
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: 84.38 E-value: 5.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 27 DLDVQLEHGERVALLGASGAGKSTLLEAL---------RSALHEQ----GTPAAWCP--QRQ-GLVPQ-------LSVYH 83
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIaglerpdsgRIRLGGEvlqdSARGIFLPphRRRiGYVFQearlfphLSVRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 84 NIFMGRldqqssltnllnLLRPRPAHWQAVAAVCEPLGIAGLMERSVEALSGGQRQRVAIARALYQGHDLFLGDEPVASV 163
Cdd:COG4148 97 NLLYGR------------KRAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAAL 164
|
.
gi 1148626600 164 D 164
Cdd:COG4148 165 D 165
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
27-195 |
1.05e-18 |
|
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: 81.19 E-value: 1.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 27 DLDVQLE-HGERVALLGASGAGKSTLLEAL-------RSALHEQGTPaaWC---------PQRQG---------LVPQLS 80
Cdd:cd03297 14 TLKIDFDlNEEVTGIFGASGAGKSTLLRCIaglekpdGGTIVLNGTV--LFdsrkkinlpPQQRKiglvfqqyaLFPHLN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 81 VYHNIFMGrldqqssltnlLNLLRPRPAHwQAVAAVCEPLGIAGLMERSVEALSGGQRQRVAIARALYQGHDLFLGDEPV 160
Cdd:cd03297 92 VRENLAFG-----------LKRKRNREDR-ISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPF 159
|
170 180 190
....*....|....*....|....*....|....*
gi 1148626600 161 ASVDPHQASQLIHWIHSRHATsvvaLHQKELALTH 195
Cdd:cd03297 160 SALDRALRLQLLPELKQIKKN----LNIPVIFVTH 190
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
24-200 |
1.05e-18 |
|
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: 84.43 E-value: 1.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 24 VLRDLDVQLEHGERVALLGASGAGKSTLLEALRSALHEQ-------GTPA------------AWCPQRqglvPQL---SV 81
Cdd:COG4987 350 VLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQsgsitlgGVDLrdldeddlrrriAVVPQR----PHLfdtTL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 82 YHNIFMGRLDqqssltnllnllrprpAHWQAVAAVCEPLGIAGLMERSVE-----------ALSGGQRQRVAIARALYQG 150
Cdd:COG4987 426 RENLRLARPD----------------ATDEELWAALERVGLGDWLAALPDgldtwlgeggrRLSGGERRRLALARALLRD 489
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1148626600 151 HDLFLGDEPVASVDPHQASQLIHWI--HSRHATSVVALHQkELALTHFTRVI 200
Cdd:COG4987 490 APILLLDEPTEGLDAATEQALLADLleALAGRTVLLITHR-LAGLERMDRIL 540
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
20-221 |
1.08e-18 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 81.68 E-value: 1.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 20 GAEVVLRDLDVQLEHGERVALLGASGAGKSTLL------------EALRSALHEQGTPAAWCPQRQ--GLV-------PQ 78
Cdd:PRK09493 12 GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLrcinkleeitsgDLIVDGLKVNDPKVDERLIRQeaGMVfqqfylfPH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 79 LSVYHNIFMGRLDQQSSLTNLlnllrprpAHWQAVaavcEPLGIAGLMERS---VEALSGGQRQRVAIARALYQGHDLFL 155
Cdd:PRK09493 92 LTALENVMFGPLRVRGASKEE--------AEKQAR----ELLAKVGLAERAhhyPSELSGGQQQRVAIARALAVKPKLML 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1148626600 156 GDEPVASVDP---HQASQLIHWIHSRHATSVVALHQKELALTHFTRVIGLGKdengnGKVLLDANTDDL 221
Cdd:PRK09493 160 FDEPTSALDPelrHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDK-----GRIAEDGDPQVL 223
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
24-203 |
1.15e-18 |
|
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: 81.15 E-value: 1.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 24 VLRDLDVQLEHGERVALLGASGAGKSTLLEALRSALHE-QGT---PAAWCPQRQ-----GLVPQlSVYHNIFMgrldqQS 94
Cdd:cd03226 15 ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKEsSGSillNGKPIKAKErrksiGYVMQ-DVDYQLFT-----DS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 95 SLTNLLNLLRPRPAHWQAVAAVCEPLGIAGLMERSVEALSGGQRQRVAIARALYQGHDLFLGDEPVASVDPH---QASQL 171
Cdd:cd03226 89 VREELLLGLKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKnmeRVGEL 168
|
170 180 190
....*....|....*....|....*....|..
gi 1148626600 172 IHWIHSRHATSVVALHQKELALTHFTRVIGLG 203
Cdd:cd03226 169 IRELAAQGKAVIVITHDYEFLAKVCDRVLLLA 200
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
24-225 |
2.12e-18 |
|
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: 83.73 E-value: 2.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 24 VLRDLDVQLEHGERVALLGASGAGKSTLLEALrSALHE--QGT------------PAAWcpQRQ-GLVPQ---L---SVY 82
Cdd:COG2274 490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLL-LGLYEptSGRilidgidlrqidPASL--RRQiGVVLQdvfLfsgTIR 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 83 HNIFMGRLDqqssltnllnllrprpAHWQAVAAVCE-----------PLGIAGLMERSVEALSGGQRQRVAIARALYQGH 151
Cdd:COG2274 567 ENITLGDPD----------------ATDEEIIEAARlaglhdfiealPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNP 630
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1148626600 152 DLFLGDEPVASVDPHQASQLIHWI--HSRHATSVVALHQKELaLTHFTRVIGLgkdenGNGKVLLDANTDDLKPQD 225
Cdd:COG2274 631 RILILDEATSALDAETEAIILENLrrLLKGRTVIIIAHRLST-IRLADRIIVL-----DKGRIVEDGTHEELLARK 700
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
20-208 |
2.21e-18 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 80.48 E-value: 2.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 20 GAEVVLRDLDVQLEHGERVALLGASGAGKSTLLE----ALR-------------SALHEQGTPAAwcpqRQ--GLVPQ-- 78
Cdd:COG2884 13 GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKllygEERptsgqvlvngqdlSRLKRREIPYL----RRriGVVFQdf 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 79 -----LSVYHNI-----FMGRldqqssltnllnllrPRPAHWQAVAAVCEPLGIAGLMERSVEALSGGQRQRVAIARALY 148
Cdd:COG2884 89 rllpdRTVYENValplrVTGK---------------SRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1148626600 149 QGHDLFLGDEPVASVDPHQAS---QLIHWIHSRHATSVVALHQKELALTHFTRVIGLgkdENG 208
Cdd:COG2884 154 NRPELLLADEPTGNLDPETSWeimELLEEINRRGTTVLIATHDLELVDRMPKRVLEL---EDG 213
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
25-204 |
2.26e-18 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 80.37 E-value: 2.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 25 LRDLDVQLEHGERVALLGASGAGKSTLLEALRSALHEQ-------GTPAAWCPQRQ---------------GLVPQLSVY 82
Cdd:TIGR02673 18 LHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSrgqvriaGEDVNRLRGRQlpllrrrigvvfqdfRLLPDRTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 83 HNIFMgrldqqssltNLLNLLRPRPAHWQAVAAVCEPLGIAGLMERSVEALSGGQRQRVAIARALYQGHDLFLGDEPVAS 162
Cdd:TIGR02673 98 ENVAL----------PLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLADEPTGN 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1148626600 163 VDPHQASQ---LIHWIHSRHATSVVALHQKELALTHFTRVIGLGK 204
Cdd:TIGR02673 168 LDPDLSERildLLKRLNKRGTTVIVATHDLSLVDRVAHRVIILDD 212
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
20-165 |
2.74e-18 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 83.29 E-value: 2.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 20 GAEVVLRDLDVQLEHGERVALLGASGAGKSTL--------------------------LEALRSALheqgtpaawcpqrq 73
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLvnlllrfydptsgrilidgvdirdltLESLRRQI-------------- 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 74 GLVPQ------LSVYHNIFMGRLDqqssltnllnllrprpAHWQAVAAVCEplgIAGLM---------------ERSVEa 132
Cdd:COG1132 417 GVVPQdtflfsGTIRENIRYGRPD----------------ATDEEVEEAAK---AAQAHefiealpdgydtvvgERGVN- 476
|
170 180 190
....*....|....*....|....*....|...
gi 1148626600 133 LSGGQRQRVAIARALYQGHDLFLGDEPVASVDP 165
Cdd:COG1132 477 LSGGQRQRIAIARALLKDPPILILDEATSALDT 509
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
8-173 |
5.98e-18 |
|
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: 82.41 E-value: 5.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 8 PLLHLSRHHLGH-GAEVVLRDLDVQLEHGERVALLGASGAGKSTLLEALRSALHEQ-------GTPAAWCPQ-----RQG 74
Cdd:TIGR02868 333 PTLELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLqgevtldGVPVSSLDQdevrrRVS 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 75 LVPQ------LSVYHNIFMGRLDqqssltnllnllrprpAHWQAVAAVCEPLGIAGLMERSVE-----------ALSGGQ 137
Cdd:TIGR02868 413 VCAQdahlfdTTVRENLRLARPD----------------ATDEELWAALERVGLADWLRALPDgldtvlgeggaRLSGGE 476
|
170 180 190
....*....|....*....|....*....|....*.
gi 1148626600 138 RQRVAIARALYQGHDLFLGDEPVASVDPHQASQLIH 173
Cdd:TIGR02868 477 RQRLALARALLADAPILLLDEPTEHLDAETADELLE 512
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
19-208 |
6.60e-18 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 79.67 E-value: 6.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 19 HGAEVVLRDLDVQLEHGERVALLGASGAGKSTLLEAL------RSA----------LHEQGTPAAWCPQRQ--GLV---- 76
Cdd:PRK11124 12 YGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLnllempRSGtlniagnhfdFSKTPSDKAIRELRRnvGMVfqqy 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 77 ---PQLSVYHNIF------MGRLDQQssltnllnllrprpAHWQAVAaVCEPLGIAGLMERSVEALSGGQRQRVAIARAL 147
Cdd:PRK11124 92 nlwPHLTVQQNLIeapcrvLGLSKDQ--------------ALARAEK-LLERLRLKPYADRFPLHLSGGQQQRVAIARAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1148626600 148 YQGHDLFLGDEPVASVDPHQASQLIHWIH---SRHATSVVALHQKELALTHFTRVIGLgkdENG 208
Cdd:PRK11124 157 MMEPQVLLFDEPTAALDPEITAQIVSIIRelaETGITQVIVTHEVEVARKTASRVVYM---ENG 217
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-172 |
8.01e-18 |
|
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: 81.87 E-value: 8.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 4 ATPSPLL---HLSRHHLGHGAEVV--LRDLDVQLEHGERVALLGASGAGKSTLLEAL-----------------RSALHE 61
Cdd:COG1123 255 AAAEPLLevrNLSKRYPVRGKGGVraVDDVSLTLRRGETLGLVGESGSGKSTLARLLlgllrptsgsilfdgkdLTKLSR 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 62 QGTPAAWcpQRQGLVPQ---------LSVYHNIFMGrLDQQSSLtnllnllrPRPAHWQAVAAVCEPLGI-AGLMERSVE 131
Cdd:COG1123 335 RSLRELR--RRVQMVFQdpysslnprMTVGDIIAEP-LRLHGLL--------SRAERRERVAELLERVGLpPDLADRYPH 403
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1148626600 132 ALSGGQRQRVAIARALYQGHDLFLGDEPVASVDPHQASQLI 172
Cdd:COG1123 404 ELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQIL 444
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
28-188 |
8.73e-18 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 81.81 E-value: 8.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 28 LDVQLEHGERVALLGASGAGKSTLLEALRSALHEQGT------------PAAWcpqRQGLV-----PQL---SVYHNIFM 87
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQGSlkingielreldPESW---RKHLSwvgqnPQLphgTLRDNVLL 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 88 GRL---DQQSsltnllnllrprpahWQAV--AAVCE-----PLGIAGLMERSVEALSGGQRQRVAIARALYQGHDLFLGD 157
Cdd:PRK11174 446 GNPdasDEQL---------------QQALenAWVSEflpllPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLD 510
|
170 180 190
....*....|....*....|....*....|...
gi 1148626600 158 EPVASVDPHQASQLIHWIH--SRHATSVVALHQ 188
Cdd:PRK11174 511 EPTASLDAHSEQLVMQALNaaSRRQTTLMVTHQ 543
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
20-171 |
9.23e-18 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 81.60 E-value: 9.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 20 GAEVVLRDLDVQLEHGERVALLGASGAGKSTLLEALrSALHEQG--------------TPAAwcPQRQG---------LV 76
Cdd:COG1129 15 GGVKALDGVSLELRPGEVHALLGENGAGKSTLMKIL-SGVYQPDsgeilldgepvrfrSPRD--AQAAGiaiihqelnLV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 77 PQLSVYHNIFMGRLdqqssltnllnLLRPRPAHWQAV----AAVCEPLGIAGLMERSVEALSGGQRQRVAIARALYQGHD 152
Cdd:COG1129 92 PNLSVAENIFLGRE-----------PRRGGLIDWRAMrrraRELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDAR 160
|
170
....*....|....*....
gi 1148626600 153 LFLGDEPVASVDPHQASQL 171
Cdd:COG1129 161 VLILDEPTASLTEREVERL 179
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
20-204 |
1.10e-17 |
|
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: 78.92 E-value: 1.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 20 GAEVVLRDLDVQLEHGERVALLGASGAGKSTLLEALR-----------------SALHEQGTPAAWCPQRQGLVPQLSVY 82
Cdd:cd03296 13 GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAglerpdsgtilfggedaTDVPVQERNVGFVFQHYALFRHMTVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 83 HNIFMGRLDQQSSLTNLLNLLRPRpahwqaVAAVCEPLGIAGLMERSVEALSGGQRQRVAIARALYQGHDLFLGDEPVAS 162
Cdd:cd03296 93 DNVAFGLRVKPRSERPPEAEIRAK------VHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1148626600 163 VDPHQASQLIHW---IHSR-HATSVVALHQKELALTHFTRVIGLGK 204
Cdd:cd03296 167 LDAKVRKELRRWlrrLHDElHVTTVFVTHDQEEALEVADRVVVMNK 212
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
20-222 |
1.32e-17 |
|
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: 78.75 E-value: 1.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 20 GAEVVLRDLDVQLEHGERVALLGASGAGKSTLLEALRSALHEQ-------GTPAA-----------WCPQRQGLVPQLSV 81
Cdd:COG4555 12 GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDsgsilidGEDVRkeprearrqigVLPDERGLYDRLTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 82 YHNI-FMGRLdqqssltnllnLLRPRPAHWQAVAAVCEPLGIAGLMERSVEALSGGQRQRVAIARALYQGHDLFLGDEPV 160
Cdd:COG4555 92 RENIrYFAEL-----------YGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1148626600 161 ASVDPHqASQLIHWIHSRHATS----VVALHQKELALTHFTRVIGLgkdenGNGKVLLDANTDDLK 222
Cdd:COG4555 161 NGLDVM-ARRLLREILRALKKEgktvLFSSHIMQEVEALCDRVVIL-----HKGKVVAQGSLDELR 220
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
29-165 |
1.38e-17 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 78.47 E-value: 1.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 29 DVQLEHGERVALLGASGAGKSTLLEALRSALH-EQG-----------TPAAWCP-----QRQGLVPQLSVYHNIFMG--- 88
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTpASGsltlngqdhttTPPSRRPvsmlfQENNLFSHLTVAQNIGLGlnp 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1148626600 89 --RLDQQSSltnllnllrprpahwQAVAAVCEPLGIAGLMERSVEALSGGQRQRVAIARALYQGHDLFLGDEPVASVDP 165
Cdd:PRK10771 99 glKLNAAQR---------------EKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDP 162
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
20-200 |
1.53e-17 |
|
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: 77.23 E-value: 1.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 20 GAEVVLRDLDVQLEHGERVALLGASGAGKSTLLEAL----------------RSALHEQGTPAAWCP-----QRQGLVPQ 78
Cdd:cd03229 11 GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIagleepdsgsilidgeDLTDLEDELPPLRRRigmvfQDFALFPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 79 LSVYHNIfmgrldqqssltnllnllrprpahwqavaavceplgiaglmersVEALSGGQRQRVAIARALYQGHDLFLGDE 158
Cdd:cd03229 91 LTVLENI--------------------------------------------ALGLSGGQQQRVALARALAMDPDVLLLDE 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1148626600 159 PVASVDPHQASQLIHWIHSRHA----TSVVALHQKELALTHFTRVI 200
Cdd:cd03229 127 PTSALDPITRREVRALLKSLQAqlgiTVVLVTHDLDEAARLADRVV 172
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
25-191 |
1.54e-17 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 78.73 E-value: 1.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 25 LRDLDVQLEHGERVALLGASGAGKSTLLEALRSALHEQGT-----------PA-------AWCPQRQGLVPQLSVYHNIf 86
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPGQGEillngrplsdwSAaelarhrAYLSQQQSPPFAMPVFQYL- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 87 mgRLDQQSSLtnllnllrPRPAHWQAVAAVCEPLGIAGLMERSVEALSGGQRQRVAIARALYQGHD-------LFLGDEP 159
Cdd:COG4138 91 --ALHQPAGA--------SSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQVWPtinpegqLLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1148626600 160 VASVDPHQASQLIHWI------------------HS-RHATSVVALHQKEL 191
Cdd:COG4138 161 MNSLDVAQQAALDRLLrelcqqgitvvmsshdlnHTlRHADRVWLLKQGKL 211
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
7-159 |
1.57e-17 |
|
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: 78.49 E-value: 1.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 7 SPLLHLSRHHLGHGAEVVLRDLDVQLEHGERVALLGASGAGKSTLLEALrSALHE-------------QGTPA------- 66
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAI-SGLLPprsgsirfdgediTGLPPhriarlg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 67 -AWCPQRQGLVPQLSVYHNIFMGrldqqssltnlLNLLRPRPAHWQAVAAVCE--PLgiagLMER-SVEA--LSGGQRQR 140
Cdd:COG0410 80 iGYVPEGRRIFPSLTVEENLLLG-----------AYARRDRAEVRADLERVYElfPR----LKERrRQRAgtLSGGEQQM 144
|
170
....*....|....*....
gi 1148626600 141 VAIARALYQGHDLFLGDEP 159
Cdd:COG0410 145 LAIGRALMSRPKLLLLDEP 163
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
20-193 |
2.06e-17 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 79.81 E-value: 2.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 20 GAEVVLRDLDVQLEHGERVALLGASGAGKSTLL------------------EALRSALHEQgtpaawcpQRQ-GLVPQ-- 78
Cdd:COG1118 13 GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLriiagletpdsgrivlngRDLFTNLPPR--------ERRvGFVFQhy 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 79 -----LSVYHNIFMGrldqqssltnllNLLRPRPAhwQAVAAVCEPL----GIAGLMERSVEALSGGQRQRVAIARALYQ 149
Cdd:COG1118 85 alfphMTVAENIAFG------------LRVRPPSK--AEIRARVEELlelvQLEGLADRYPSQLSGGQRQRVALARALAV 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1148626600 150 GHDLFLGDEPVASVDPHQASQLIHW---IHSR-HATSVVALHQKELAL 193
Cdd:COG1118 151 EPEVLLLDEPFGALDAKVRKELRRWlrrLHDElGGTTVFVTHDQEEAL 198
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
11-168 |
2.24e-17 |
|
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: 78.31 E-value: 2.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 11 HLS-RHHLGHGAEVVLRDLDVQLEHGERVALLGASGAGKSTLLEALrSALHE--------QGTPAAWCPQRQ-----GLV 76
Cdd:COG1124 6 NLSvSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRAL-AGLERpwsgevtfDGRPVTRRRRKAfrrrvQMV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 77 PQ---LSVyhNIFMgRLDQQSSLTNLLNLlrpRPAHWQAVAAVCEPLGI-AGLMERSVEALSGGQRQRVAIARALYQGHD 152
Cdd:COG1124 85 FQdpyASL--HPRH-TVDRILAEPLRIHG---LPDREERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALILEPE 158
|
170
....*....|....*..
gi 1148626600 153 LFLGDEPVASVDPH-QA 168
Cdd:COG1124 159 LLLLDEPTSALDVSvQA 175
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
29-215 |
2.38e-17 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 77.59 E-value: 2.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 29 DVQLEHGERVALLGASGAGKSTLL-------------------EALRSALHEQgtPAAWCPQRQGLVPQLSVYHNIFMGr 89
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLnliagfiepasgsikvndqSHTGLAPYQR--PVSMLFQENNLFAHLTVRQNIGLG- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 90 ldqqssltnLLNLLRPRPAHWQAVAAVCEPLGIAGLMERSVEALSGGQRQRVAIARALYQGHDLFLGDEPVASVDPHQAS 169
Cdd:TIGR01277 95 ---------LHPGLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLRE 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1148626600 170 QLIHWI----HSRHATSVVALHQKELALTHFTRVIGLgkdENGNGKVLLD 215
Cdd:TIGR01277 166 EMLALVkqlcSERQRTLLMVTHHLSDARAIASQIAVV---SQGKIKVVSD 212
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
17-187 |
3.75e-17 |
|
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: 77.22 E-value: 3.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 17 LGHGAEVVLRDLDVQLEHGERVALLGASGAGKSTLLEAL-RSALHEQGTPAA------------------WCPQRQGLVP 77
Cdd:cd03260 8 VYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLnRLNDLIPGAPDEgevlldgkdiydldvdvlELRRRVGMVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 78 Q------LSVYHNIFMGrldqqssltnllnlLRPRPAHWQAVAA--VCEPLGIAGLMER-----SVEALSGGQRQRVAIA 144
Cdd:cd03260 88 QkpnpfpGSIYDNVAYG--------------LRLHGIKLKEELDerVEEALRKAALWDEvkdrlHALGLSGGQQQRLCLA 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1148626600 145 RALYQGHDLFLGDEPVASVDPHQAS---QLIHWIHSRHaTSVVALH 187
Cdd:cd03260 154 RALANEPEVLLLDEPTSALDPISTAkieELIAELKKEY-TIVIVTH 198
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
23-184 |
3.93e-17 |
|
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: 77.77 E-value: 3.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 23 VVLRDLDVQLEHGERVALLGASGAGKSTLLEALrSALHE--QGT------------PAAWCpqRQGLV---------PQL 79
Cdd:COG0411 18 VAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLI-TGFYRptSGRilfdgrditglpPHRIA--RLGIArtfqnprlfPEL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 80 SVYHNIFMGRLDQQSSLTNLLNLLRPRP-----AHWQAVAAVCEPLGIAGLMERSVEALSGGQRQRVAIARALYQGHDLF 154
Cdd:COG0411 95 TVLENVLVAAHARLGRGLLAALLRLPRArreerEARERAEELLERVGLADRADEPAGNLSYGQQRRLEIARALATEPKLL 174
|
170 180 190
....*....|....*....|....*....|...
gi 1148626600 155 LGDEPVASVDP---HQASQLIHWIHSRHATSVV 184
Cdd:COG0411 175 LLDEPAAGLNPeetEELAELIRRLRDERGITIL 207
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
10-190 |
5.05e-17 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 76.75 E-value: 5.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 10 LHLSRHHLGHGAEVVLRDLDVQLEHGERVALLGASGAGKSTLLEALRSALHEQ----------GTPAAWCP--QRQ-GLV 76
Cdd:COG4136 2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsasgevllnGRRLTALPaeQRRiGIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 77 PQ-------LSVYHNIFMGrldqqssltnlLNLLRPRPAHWQAVAAVCEPLGIAGLMERSVEALSGGQRQRVAIARALYQ 149
Cdd:COG4136 82 FQddllfphLSVGENLAFA-----------LPPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1148626600 150 GHDLFLGDEPVASVDPHQASQLIHW----IHSRHATSVVALHQKE 190
Cdd:COG4136 151 EPRALLLDEPFSKLDAALRAQFREFvfeqIRQRGIPALLVTHDEE 195
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
20-165 |
5.28e-17 |
|
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: 76.80 E-value: 5.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 20 GAEVVLRDLDVQLEHGERVALLGASGAGKSTLLEALrSAL--HEQGT-------------PAAWCPQRQGLV-------P 77
Cdd:cd03262 11 GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCI-NLLeePDSGTiiidglkltddkkNINELRQKVGMVfqqfnlfP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 78 QLSVYHNIFMGrldqqssltnlLNLLRPRPAHwQAVAAVCEPLGIAGLMERSVE---ALSGGQRQRVAIARALYQGHDLF 154
Cdd:cd03262 90 HLTVLENITLA-----------PIKVKGMSKA-EAEERALELLEKVGLADKADAypaQLSGGQQQRVAIARALAMNPKVM 157
|
170
....*....|.
gi 1148626600 155 LGDEPVASVDP 165
Cdd:cd03262 158 LFDEPTSALDP 168
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
8-192 |
6.22e-17 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 79.12 E-value: 6.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 8 PLLHLSRHHLGHGAEVVLRDLDVQLEHGERVALLGASGAGKSTLLEALRSAL-------HEQGTP-----AAWCPQRQGL 75
Cdd:PRK09536 2 PMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLtptagtvLVAGDDvealsARAASRRVAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 76 VPQ-------LSVYHNIFMGRldqqssLTNLLNLLRPRPAHWQAVAAVCEPLGIAGLMERSVEALSGGQRQRVAIARALY 148
Cdd:PRK09536 82 VPQdtslsfeFDVRQVVEMGR------TPHRSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALA 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1148626600 149 QGHDLFLGDEPVASVDPHQASQ---LIHWIHSRHATSVVALHQKELA 192
Cdd:PRK09536 156 QATPVLLLDEPTASLDINHQVRtleLVRRLVDDGKTAVAAIHDLDLA 202
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
11-164 |
9.36e-17 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 76.82 E-value: 9.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 11 HLSRHHLGHGAEV-VLRDLDVQLEHGERVALLGASGAGKSTLLEALRSALheqgTPAAWC----------P--------Q 71
Cdd:COG4525 8 HVSVRYPGGGQPQpALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFL----APSSGEitldgvpvtgPgadrgvvfQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 72 RQGLVPQLSVYHNIFMG-RLdqqssltnllnLLRPRPAHWQAVAAVCEPLGIAGLMERSVEALSGGQRQRVAIARALYQG 150
Cdd:COG4525 84 KDALLPWLNVLDNVAFGlRL-----------RGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAAD 152
|
170
....*....|....
gi 1148626600 151 HDLFLGDEPVASVD 164
Cdd:COG4525 153 PRFLLMDEPFGALD 166
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
27-180 |
1.06e-16 |
|
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: 77.84 E-value: 1.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 27 DLDVQLEHGERVALLGASGAGKSTLLEAL-------RSALHEQGTpaAWCPQRQG------------------LVPQLSV 81
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIagltrpdEGEIVLNGR--TLFDSRKGiflppekrrigyvfqearLFPHLSV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 82 YHNIFMGRldqqssltnllnlLRPRPAHWQAV-AAVCEPLGIAGLMERSVEALSGGQRQRVAIARALYQGHDLFLGDEPV 160
Cdd:TIGR02142 93 RGNLRYGM-------------KRARPSERRISfERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPL 159
|
170 180
....*....|....*....|
gi 1148626600 161 ASVDPHQASQLIHWIHSRHA 180
Cdd:TIGR02142 160 AALDDPRKYEILPYLERLHA 179
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
10-187 |
1.23e-16 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 76.59 E-value: 1.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 10 LHLSRHHLGHGAEVVLRDLDVQLEHGERVALLGASGAGKSTLLEAL-------RSALHEQGTP------------AAWCP 70
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFarlltpqSGTVFLGDKPismlssrqlarrLALLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 71 QrQGLVP------QLSVY----HNIFMGRLDQQSSltnllnllrprpahwQAVAAVCEPLGIAGLMERSVEALSGGQRQR 140
Cdd:PRK11231 83 Q-HHLTPegitvrELVAYgrspWLSLWGRLSAEDN---------------ARVNQAMEQTRINHLADRRLTDLSGGQRQR 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1148626600 141 VAIARALYQGHDLFLGDEPVASVD-PHQAS--QLIHWIHSRHATSVVALH 187
Cdd:PRK11231 147 AFLAMVLAQDTPVVLLDEPTTYLDiNHQVElmRLMRELNTQGKTVVTVLH 196
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
20-164 |
1.40e-16 |
|
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: 75.74 E-value: 1.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 20 GAEVVLRDLDVQLEHGERVALLGASGAGKSTLLEAL---------RSALHEQ---GTPAAWCP-----QRQGLVPQLSVY 82
Cdd:cd03300 11 GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIagfetptsgEILLDGKditNLPPHKRPvntvfQNYALFPHLTVF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 83 HNIFMG----RLDQQSSLtnllnllrprpahwQAVAAVCEPLGIAGLMERSVEALSGGQRQRVAIARALYQGHDLFLGDE 158
Cdd:cd03300 91 ENIAFGlrlkKLPKAEIK--------------ERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDE 156
|
....*.
gi 1148626600 159 PVASVD 164
Cdd:cd03300 157 PLGALD 162
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
11-184 |
3.00e-16 |
|
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: 74.85 E-value: 3.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 11 HLSRHHLGHGAEV-VLRDLDVQLEHGERVALLGASGAGKSTLLEAL---------------RSALHEQGTPAAWCPQRQG 74
Cdd:cd03257 6 NLSVSFPTGGGSVkALDDVSFSIKKGETLGLVGESGSGKSTLARAIlgllkptsgsiifdgKDLLKLSRRLRKIRRKEIQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 75 LVPQ---------LSVYHNIfmgrldqqsslTNLLNLLRPRPAHWQAVAAVCEPL-GI---AGLMERSVEALSGGQRQRV 141
Cdd:cd03257 86 MVFQdpmsslnprMTIGEQI-----------AEPLRIHGKLSKKEARKEAVLLLLvGVglpEEVLNRYPHELSGGQRQRV 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1148626600 142 AIARALYQGHDLFLGDEPVASVDPH-QAS--QLIHWIHSRHATSVV 184
Cdd:cd03257 155 AIARALALNPKLLIADEPTSALDVSvQAQilDLLKKLQEELGLTLL 200
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
18-215 |
3.99e-16 |
|
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: 73.50 E-value: 3.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 18 GHGAEVVLRDLDVQLEHGERVALLGASGAGKSTLLEALRSALHEQ-------GTPAAwcpqrqGLVPQLSVYhnifMGRL 90
Cdd:cd03247 11 PEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQqgeitldGVPVS------DLEKALSSL----ISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 91 DQQssltnllnllrprpAHwqavaavcepLGIAGLMERSVEALSGGQRQRVAIARALYQGHDLFLGDEPVASVDPHQASQ 170
Cdd:cd03247 81 NQR--------------PY----------LFDTTLRNNLGRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQ 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1148626600 171 LIHWI--HSRHATSVVALHQKeLALTHFTRVIGLgkdenGNGKVLLD 215
Cdd:cd03247 137 LLSLIfeVLKDKTLIWITHHL-TGIEHMDKILFL-----ENGKIIMQ 177
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
23-165 |
4.89e-16 |
|
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: 74.08 E-value: 4.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 23 VVLRDLDVQLEHGERVALLGASGAGKSTLLEALRSaLHEQGTPAAW-------------------CPQRQGLVPQLSVY- 82
Cdd:cd03263 16 PAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTG-ELRPTSGTAYingysirtdrkaarqslgyCPQFDALFDELTVRe 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 83 HNIFMGRLdqqssltnllnllRPRPaHWQA---VAAVCEPLGIAGLMERSVEALSGGQRQRVAIARALYQGHDLFLGDEP 159
Cdd:cd03263 95 HLRFYARL-------------KGLP-KSEIkeeVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
....*.
gi 1148626600 160 VASVDP 165
Cdd:cd03263 161 TSGLDP 166
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
20-165 |
6.22e-16 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 73.80 E-value: 6.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 20 GAEVVLRDLDVQLEHGERVALLGASGAGKSTLLEAL---------RSALHEQGTPA--------------AWCPQRQGLV 76
Cdd:TIGR03608 9 GDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIgllekfdsgQVYLNGQETPPlnskkaskfrreklGYLFQNFALI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 77 PQLSVYHNIFMGRLDQQssltnllnllRPRPAHWQAVAAVCEPLGIAGLMERSVEALSGGQRQRVAIARALYQGHDLFLG 156
Cdd:TIGR03608 89 ENETVEENLDLGLKYKK----------LSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILA 158
|
....*....
gi 1148626600 157 DEPVASVDP 165
Cdd:TIGR03608 159 DEPTGSLDP 167
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
20-176 |
7.08e-16 |
|
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: 72.46 E-value: 7.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 20 GAEVVLRDLDVQLEHGERVALLGASGAGKSTLLEALrSALHeqgtpaawcPQRQGlvpqlSVYHNifmGRldqqssltnl 99
Cdd:cd03216 11 GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKIL-SGLY---------KPDSG-----EILVD---GK---------- 62
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1148626600 100 lNLLRPRPAHWQAvaavcepLGIAglmerSVEALSGGQRQRVAIARALYQGHDLFLGDEPVASVDPHQASQLIHWIH 176
Cdd:cd03216 63 -EVSFASPRDARR-------AGIA-----MVYQLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIR 126
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
24-200 |
7.20e-16 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 75.51 E-value: 7.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 24 VLRDLDVQLEHGERVALLGASGAGKSTLLE-----------ALR------SALHEQGTPAAWCPQRQGLVPQLSVYHNIF 86
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRiiaglehqtsgHIRfhgtdvSRLHARDRKVGFVFQHYALFRHMTVFDNIA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 87 MGrldqqssltNLLNLLRPRP---AHWQAVAAVCEPLGIAGLMERSVEALSGGQRQRVAIARALYQGHDLFLGDEPVASV 163
Cdd:PRK10851 97 FG---------LTVLPRRERPnaaAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGAL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1148626600 164 DPHQASQLIHWIHSRHA----TSVVALHQKELALTHFTRVI 200
Cdd:PRK10851 168 DAQVRKELRRWLRQLHEelkfTSVFVTHDQEEAMEVADRVV 208
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
23-200 |
7.82e-16 |
|
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: 72.43 E-value: 7.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 23 VVLRDLDVQLEHGERVALLGASGAGKSTLLEALRSAL--------------HEQGTPA----AWCPQRQGLVPQLSVYHN 84
Cdd:cd03230 14 TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLkpdsgeikvlgkdiKKEPEEVkrriGYLPEEPSLYENLTVREN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 85 IfmgrldqqssltnllnllrprpahwqavaavceplgiaglmersveALSGGQRQRVAIARALyqGHD---LFLgDEPVA 161
Cdd:cd03230 94 L----------------------------------------------KLSGGMKQRLALAQAL--LHDpelLIL-DEPTS 124
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1148626600 162 SVDPHQASQLIHWIHS---RHATSVVALHQKELALTHFTRVI 200
Cdd:cd03230 125 GLDPESRREFWELLRElkkEGKTILLSSHILEEAERLCDRVA 166
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
10-159 |
1.31e-15 |
|
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: 73.33 E-value: 1.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 10 LHLSRHHLGHGAEVVLRDLDVQLEHGERVALLGASGAGKSTLLEAL-------RSALHEQGTPA-------------AWC 69
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLmgllpvkSGSIRLDGEDItklppheraragiAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 70 PQRQGLVPQLSVYHNIFMGrldqqssLTNLLNLLRPRPAHWQAVAAVCEPLgiaglMERSVEALSGGQRQRVAIARALYQ 149
Cdd:TIGR03410 81 PQGREIFPRLTVEENLLTG-------LAALPRRSRKIPDEIYELFPVLKEM-----LGRRGGDLSGGQQQQLAIARALVT 148
|
170
....*....|
gi 1148626600 150 GHDLFLGDEP 159
Cdd:TIGR03410 149 RPKLLLLDEP 158
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
7-200 |
1.39e-15 |
|
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: 73.58 E-value: 1.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 7 SPLLHLSRHHLGHGAEVVLRDLDVQLEHGERVALLGASGAGKSTLLEALrSALHEQ--------------GTPAAWCPQR 72
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLI-TGDLPPtygndvrlfgerrgGEDVWELRKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 73 QGLV---------PQLSVYHNIFMGRLDQqssltnLLNLLRPRPAHWQAVAAVCEPLGIAGLMERSVEALSGGQRQRVAI 143
Cdd:COG1119 80 IGLVspalqlrfpRDETVLDVVLSGFFDS------IGLYREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLI 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1148626600 144 ARALYQGHDLFLGDEPVASVDPHQASQLIHWIHSRHATSVVAL----HQKELALTHFTRVI 200
Cdd:COG1119 154 ARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLvlvtHHVEEIPPGITHVL 214
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
20-165 |
1.40e-15 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 73.10 E-value: 1.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 20 GAEVVLRDLDVQLEHGERVALLGASGAGKSTLLEALrSAL--HEQGT-----------PAAWCPQRQ--GLV-------P 77
Cdd:COG1126 12 GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCI-NLLeePDSGTitvdgedltdsKKDINKLRRkvGMVfqqfnlfP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 78 QLSVYHNIFMGRLdqqssltnlLNLLRPRPahwQAVAAVCEPL---GIAGLMERSVEALSGGQRQRVAIARALYQGHDLF 154
Cdd:COG1126 91 HLTVLENVTLAPI---------KVKKMSKA---EAEERAMELLervGLADKADAYPAQLSGGQQQRVAIARALAMEPKVM 158
|
170
....*....|.
gi 1148626600 155 LGDEPVASVDP 165
Cdd:COG1126 159 LFDEPTSALDP 169
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
24-192 |
2.22e-15 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 72.38 E-value: 2.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 24 VLRDLDVQLEHGERVALLGASGAGKSTLLEAL-------------------------RSALHEQGTpaAWCPQRQGLVPQ 78
Cdd:TIGR02211 20 VLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLggldnptsgevlfngqslsklssneRAKLRNKKL--GFIYQFHHLLPD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 79 LSVYHNIFM----GRLDQQSSLtnllnllrprpahwQAVAAVCEPLGIAGLMERSVEALSGGQRQRVAIARALYQGHDLF 154
Cdd:TIGR02211 98 FTALENVAMplliGKKSVKEAK--------------ERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPSLV 163
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1148626600 155 LGDEPVASVDPHQAS---QLIHWIHSRHATS-VVALHQKELA 192
Cdd:TIGR02211 164 LADEPTGNLDNNNAKiifDLMLELNRELNTSfLVVTHDLELA 205
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
22-208 |
3.06e-15 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 74.46 E-value: 3.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 22 EVVLRDLDVQLEHGERVALLGASGAGKSTLLEALrSAL--HEQGTPAawCPQRQGL--VPQLSvYhnIFMGRLDQQsslt 97
Cdd:COG4178 376 RPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAI-AGLwpYGSGRIA--RPAGARVlfLPQRP-Y--LPLGTLREA---- 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 98 nllnLLRPRPAHW---QAVAAVCEPLGIAGLMER-SVEA-----LSGGQRQRVAIARALYQGHD-LFLgDEPVASVDPHQ 167
Cdd:COG4178 446 ----LLYPATAEAfsdAELREALEAVGLGHLAERlDEEAdwdqvLSLGEQQRLAFARLLLHKPDwLFL-DEATSALDEEN 520
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1148626600 168 ASQLIHWIHSRHA-TSVVAL-HQKELALtHFTRVIGLGKDENG 208
Cdd:COG4178 521 EAALYQLLREELPgTTVISVgHRSTLAA-FHDRVLELTGDGSW 562
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
18-204 |
3.65e-15 |
|
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: 72.23 E-value: 3.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 18 GHGAEVVLRDLDVQLEHGERVALLGASGAGKSTLLEAL-------RSALHEQGT------PAAWCPQRQ--GLVPQ---- 78
Cdd:cd03258 14 TGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCInglerptSGSVLVDGTdltllsGKELRKARRriGMIFQhfnl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 79 LS---VYHNI-FMGRLDQQssltnllnllrPRPAHWQAVAAVCEPLGIAGLMERSVEALSGGQRQRVAIARALYQGHDLF 154
Cdd:cd03258 94 LSsrtVFENVaLPLEIAGV-----------PKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1148626600 155 LGDEPVASVDP---HQASQLIHWIHSRHA-TSVVALHQKE--------LALTHFTRVIGLGK 204
Cdd:cd03258 163 LCDEATSALDPettQSILALLRDINRELGlTIVLITHEMEvvkricdrVAVMEKGEVVEEGT 224
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
25-171 |
4.45e-15 |
|
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: 74.21 E-value: 4.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 25 LRDLDVQLEHGERVALLGASGAGKSTLLEALRSAL-------HEQGTpAAWCPQrQGLVPQLSVYHNIFMGRLDQqsslt 97
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMdkveghvHMKGS-VAYVPQ-QAWIQNDSLRENILFGKALN----- 726
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 98 nllnllrprPAHWQAVAAVCEPLGIAGLM---------ERSVEaLSGGQRQRVAIARALYQGHDLFLGDEPVASVDPHQA 168
Cdd:TIGR00957 727 ---------EKYYQQVLEACALLPDLEILpsgdrteigEKGVN-LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVG 796
|
...
gi 1148626600 169 SQL 171
Cdd:TIGR00957 797 KHI 799
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
19-164 |
5.14e-15 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 73.14 E-value: 5.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 19 HGAEVVLRDLDVQLEHGERVALLGASGAGKSTLLEALrsALHEQGT---------------PA----AWCPQRQGLVPQL 79
Cdd:PRK11000 13 YGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMI--AGLEDITsgdlfigekrmndvpPAergvGMVFQSYALYPHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 80 SVYHNIFMG-RLDQQSSLTNLlnllrprpahwQAVAAVCEPLGIAGLMERSVEALSGGQRQRVAIARALYQGHDLFLGDE 158
Cdd:PRK11000 91 SVAENMSFGlKLAGAKKEEIN-----------QRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDE 159
|
....*.
gi 1148626600 159 PVASVD 164
Cdd:PRK11000 160 PLSNLD 165
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
23-188 |
8.03e-15 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 73.27 E-value: 8.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 23 VVLRDLDVQLEHGERVALLGASGAGKSTLLEALRSALhEQGTPAAWCPQRQGLVPQ------LSVYHNIFMgrLDQQssl 96
Cdd:PTZ00243 674 VLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQF-EISEGRVWAERSIAYVPQqawimnATVRGNILF--FDEE--- 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 97 tnllnllrpRPAHWQAVAAVCE------PLGiAGLM----ERSVEaLSGGQRQRVAIARALYQGHDLFLGDEPVASVDPH 166
Cdd:PTZ00243 748 ---------DAARLADAVRVSQleadlaQLG-GGLEteigEKGVN-LSGGQKARVSLARAVYANRDVYLLDDPLSALDAH 816
|
170 180
....*....|....*....|....*
gi 1148626600 167 QASQLIHWI---HSRHATSVVALHQ 188
Cdd:PTZ00243 817 VGERVVEECflgALAGKTRVLATHQ 841
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
19-171 |
1.07e-14 |
|
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: 70.79 E-value: 1.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 19 HGAEVVLRDLDVQLEHGERVALLGASGAGKSTLLEAL-RSALHEQGT-------PAAWCP-----------QRQGLVPQL 79
Cdd:cd03295 11 GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMInRLIEPTSGEifidgedIREQDPvelrrkigyviQQIGLFPHM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 80 SVYHNIfmgrldqqssltnllnLLRPRPAHW---QAVAAVCEPLGIAGL-----MERSVEALSGGQRQRVAIARALYQGH 151
Cdd:cd03295 91 TVEENI----------------ALVPKLLKWpkeKIRERADELLALVGLdpaefADRYPHELSGGQQQRVGVARALAADP 154
|
170 180
....*....|....*....|
gi 1148626600 152 DLFLGDEPVASVDPHQASQL 171
Cdd:cd03295 155 PLLLMDEPFGALDPITRDQL 174
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1-164 |
1.34e-14 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 70.86 E-value: 1.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 1 MTQATPSPLLHLSRHHlghGAEVVLRDLDVQLEHGERVALLGASGAGKSTLLEAL--------------RSALHEQGTPA 66
Cdd:PRK11247 7 LNQGTPLLLNAVSKRY---GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLagletpsagellagTAPLAEAREDT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 67 AWCPQRQGLVPQLSVYHNIFMGrldqqssltnllNLLRPRPAHWQAVAAVceplgiaGLMERSVE---ALSGGQRQRVAI 143
Cdd:PRK11247 84 RLMFQDARLLPWKKVIDNVGLG------------LKGQWRDAALQALAAV-------GLADRANEwpaALSGGQKQRVAL 144
|
170 180
....*....|....*....|.
gi 1148626600 144 ARALYQGHDLFLGDEPVASVD 164
Cdd:PRK11247 145 ARALIHRPGLLLLDEPLGALD 165
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
16-222 |
2.06e-14 |
|
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: 70.01 E-value: 2.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 16 HLGHGAEVVLRDLDVQLEHGERVALLGASGAGKSTLLEAL-----------------RSALHEQGTPAAwcPQRQGLVPQ 78
Cdd:COG1127 12 TKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIigllrpdsgeilvdgqdITGLSEKELYEL--RRRIGMLFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 79 -------LSVYHNI-----FMGRLDQQSSLtnllnllrprpahwQAVAAVCEPLGIAGLMERSVEALSGGQRQRVAIARA 146
Cdd:COG1127 90 ggalfdsLTVFENVafplrEHTDLSEAEIR--------------ELVLEKLELVGLPGAADKMPSELSGGMRKRVALARA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 147 L-----YqghdLFLgDEPVASVDPHQA---SQLIHWIH-SRHATSVVALHQKELALTHFTRVIGLgkdenGNGKVLLDAN 217
Cdd:COG1127 156 LaldpeI----LLY-DEPTAGLDPITSaviDELIRELRdELGLTSVVVTHDLDSAFAIADRVAVL-----ADGKIIAEGT 225
|
....*
gi 1148626600 218 TDDLK 222
Cdd:COG1127 226 PEELL 230
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
24-187 |
2.35e-14 |
|
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: 69.95 E-value: 2.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 24 VLRDLDVQLEHGERVALLGASGAGKSTL--------------------------LEALRSALheqgtpaawcpqrqGLVP 77
Cdd:cd03253 16 VLKDVSFTIPAGKKVAIVGPSGSGKSTIlrllfrfydvssgsilidgqdirevtLDSLRRAI--------------GVVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 78 QLSV------YHNIFMGRLDqqssltnllnllrprpAHWQAVAAVCEPLGIAGLMERSVEA-----------LSGGQRQR 140
Cdd:cd03253 82 QDTVlfndtiGYNIRYGRPD----------------ATDEEVIEAAKAAQIHDKIMRFPDGydtivgerglkLSGGEKQR 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1148626600 141 VAIARALYQGHDLFLGDEPVASVDPHQASQLIHWIH--SRHATSVVALH 187
Cdd:cd03253 146 VAIARAILKNPPILLLDEATSALDTHTEREIQAALRdvSKGRTTIVIAH 194
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
20-208 |
3.18e-14 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 69.66 E-value: 3.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 20 GAEVVLRDLDVQLEHGERVALLGASGAGKSTLLEAL------RSA----------LHEQGTPAAWCPQRQ--GLV----- 76
Cdd:COG4161 13 GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLnlletpDSGqlniaghqfdFSQKPSEKAIRLLRQkvGMVfqqyn 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 77 --PQLSVYHNIF------MGRLDQQSSLTNLLNLLRprpahwqavaavcepLGIAGLMERSVEALSGGQRQRVAIARALY 148
Cdd:COG4161 93 lwPHLTVMENLIeapckvLGLSKEQAREKAMKLLAR---------------LRLTDKADRFPLHLSGGQQQRVAIARALM 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1148626600 149 QGHDLFLGDEPVASVDPHQASQLIHWIHSRHA---TSVVALHQKELALTHFTRVIGLgkdENG 208
Cdd:COG4161 158 MEPQVLLFDEPTAALDPEITAQVVEIIRELSQtgiTQVIVTHEVEFARKVASQVVYM---EKG 217
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
24-200 |
3.20e-14 |
|
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: 69.16 E-value: 3.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 24 VLRDLDVQLEHGERVALLGASGAGKSTLL-------EALRSALHEQGTPAA-WCPQ--RQ--GLVPQ---L---SVYHNI 85
Cdd:cd03245 19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLkllaglyKPTSGSVLLDGTDIRqLDPAdlRRniGYVPQdvtLfygTLRDNI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 86 FMGRLdqqssltnllnllrprPAHWQAVAAVCEPLGIAGL-------MERSV----EALSGGQRQRVAIARALYQGHDLF 154
Cdd:cd03245 99 TLGAP----------------LADDERILRAAELAGVTDFvnkhpngLDLQIgergRGLSGGQRQAVALARALLNDPPIL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1148626600 155 LGDEPVASVDPHQASQLIH----WIhsRHATSVVALHQKELaLTHFTRVI 200
Cdd:cd03245 163 LLDEPTSAMDMNSEERLKErlrqLL--GDKTLIIITHRPSL-LDLVDRII 209
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
20-164 |
3.48e-14 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 70.90 E-value: 3.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 20 GAEVVLRDLDVQLEHGERVALLGASGAGKSTLLEaLRSALH-----------EQGTPAAW-----CP--QRQGLVPQLSV 81
Cdd:PRK11432 17 GSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLR-LVAGLEkptegqifidgEDVTHRSIqqrdiCMvfQSYALFPHMSL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 82 YHNIFMGrLDQQSsltnllnllRPRPAHWQAVAAVCEPLGIAGLMERSVEALSGGQRQRVAIARALYQGHDLFLGDEPVA 161
Cdd:PRK11432 96 GENVGYG-LKMLG---------VPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLS 165
|
...
gi 1148626600 162 SVD 164
Cdd:PRK11432 166 NLD 168
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
24-188 |
3.69e-14 |
|
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: 68.73 E-value: 3.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 24 VLRDLDVQLEHGERVALLGASGAGKSTLLEAL---RSALHEQGT--------PAAWCPQRQGLVPQlsvyHNIFMGRLdq 92
Cdd:cd03213 24 LLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagrRTGLGVSGEvlingrplDKRSFRKIIGYVPQ----DDILHPTL-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 93 qssltnllnllrprpahwqavaAVCEPLGIAGLMeRSveaLSGGQRQRVAIARALYQGHDLFLGDEPVASVDPHQASQLI 172
Cdd:cd03213 98 ----------------------TVRETLMFAAKL-RG---LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVM 151
|
170
....*....|....*....
gi 1148626600 173 HWIH---SRHATSVVALHQ 188
Cdd:cd03213 152 SLLRrlaDTGRTIICSIHQ 170
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
20-191 |
3.73e-14 |
|
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: 68.01 E-value: 3.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 20 GAEVVLRDLDVQLEHGERVALLGASGAGKSTLLEALRsalheqgtpAAWCPQrQGLVpqlsvyhnifmgRLDQQSSLTNL 99
Cdd:cd03246 13 AEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLIL---------GLLRPT-SGRV------------RLDGADISQWD 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 100 LNLLRPRpahwqavaavceplgIAGLMERsVE---------ALSGGQRQRVAIARALYQGHDLFLGDEPVASVDP---HQ 167
Cdd:cd03246 71 PNELGDH---------------VGYLPQD-DElfsgsiaenILSGGQRQRLGLARALYGNPRILVLDEPNSHLDVegeRA 134
|
170 180
....*....|....*....|....
gi 1148626600 168 ASQLIHWIHSRHATSVVALHQKEL 191
Cdd:cd03246 135 LNQAIAALKAAGATRIVIAHRPET 158
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
16-222 |
5.17e-14 |
|
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: 69.07 E-value: 5.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 16 HLGHGAEVVLRDLDVQLEHGERVALLGASGAGKSTLLEAL-----------------RSALHEQGTPAawCPQRQGLVPQ 78
Cdd:cd03261 7 TKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIvgllrpdsgevlidgedISGLSEAELYR--LRRRMGMLFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 79 -------LSVYHNI-FM----GRLDQQSSLtnllnllrprpahwQAVAAVCEPLGIAGLMERSVEALSGGQRQRVAIARA 146
Cdd:cd03261 85 sgalfdsLTVFENVaFPlrehTRLSEEEIR--------------EIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 147 LYQGHDLFLGDEPVASVDP---HQASQLIHWIH-SRHATSVVALHQKELALTHFTRVIGLgkdenGNGKVLLDANTDDLK 222
Cdd:cd03261 151 LALDPELLLYDEPTAGLDPiasGVIDDLIRSLKkELGLTSIMVTHDLDTAFAIADRIAVL-----YDGKIVAEGTPEELR 225
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
17-202 |
6.26e-14 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 69.24 E-value: 6.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 17 LGHGAEVVLRDLDVQLEHGERVALLGASGAGKSTLLEALRSAL------------HEQGTPAAWCPQRQGLVPQ------ 78
Cdd:PRK10253 15 LGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMtpahghvwldgeHIQHYASKEVARRIGLLAQnattpg 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 79 -LSVYHNIFMGRLDQQSSLTnllnllRPRPAHWQAVAAVCEPLGIAGLMERSVEALSGGQRQRVAIARALYQGHDLFLGD 157
Cdd:PRK10253 95 dITVQELVARGRYPHQPLFT------RWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLD 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1148626600 158 EPVASVD-PHQAS--QLIHWIHSRHATSVVA-LHQKELALTHFTRVIGL 202
Cdd:PRK10253 169 EPTTWLDiSHQIDllELLSELNREKGYTLAAvLHDLNQACRYASHLIAL 217
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
2-199 |
7.52e-14 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 69.86 E-value: 7.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 2 TQATPSPLLHLSRHHLGHGAEVVLRDLDVQLEHGERVALLGASGAGKSTLLEALrsALHEQGT----------------- 64
Cdd:PRK11607 12 TRKALTPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRML--AGFEQPTagqimldgvdlshvppy 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 65 --PAAWCPQRQGLVPQLSVYHNIFMGrLDQQssltnllnllrpRPAHWQAVAAVCEPLGIAGLME---RSVEALSGGQRQ 139
Cdd:PRK11607 90 qrPINMMFQSYALFPHMTVEQNIAFG-LKQD------------KLPKAEIASRVNEMLGLVHMQEfakRKPHQLSGGQRQ 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1148626600 140 RVAIARALYQGHDLFLGDEPVASVDP----HQASQLIHWIHSRHATSVVALHQKELALTHFTRV 199
Cdd:PRK11607 157 RVALARSLAKRPKLLLLDEPMGALDKklrdRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRI 220
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
18-192 |
1.06e-13 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 69.75 E-value: 1.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 18 GHGAEVVLRDLDVQLEHGERVALLGASGAGKSTLLEAL-----------RSAlheqGTPAA----------------WCP 70
Cdd:PRK10535 17 GEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILgcldkptsgtyRVA----GQDVAtldadalaqlrrehfgFIF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 71 QRQGLVPQLSVYHN-----IFMGRldqqssltnllnllrPRPAHWQAVAAVCEPLGIAGLMERSVEALSGGQRQRVAIAR 145
Cdd:PRK10535 93 QRYHLLSHLTAAQNvevpaVYAGL---------------ERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIAR 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1148626600 146 ALYQGHDLFLGDEPVASVDPHQASQ---LIHWIHSRHATSVVALHQKELA 192
Cdd:PRK10535 158 ALMNGGQVILADEPTGALDSHSGEEvmaILHQLRDRGHTVIIVTHDPQVA 207
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
19-227 |
1.36e-13 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 67.85 E-value: 1.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 19 HGaEVVLRDLDVQLEHGERVALLGASGAGKSTLLEALRsaLHEQGTP------------AAWCPQRQGLVPQL------- 79
Cdd:PRK11264 14 HG-QTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCIN--LLEQPEAgtirvgditidtARSLSQQKGLIRQLrqhvgfv 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 80 ----------SVYHNIFMGRLdqqssltnlLNLLRPRPAHWQAVAAVCEPLGIAGLMERSVEALSGGQRQRVAIARALYQ 149
Cdd:PRK11264 91 fqnfnlfphrTVLENIIEGPV---------IVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 150 GHDLFLGDEPVASVDPHQASQLIHWIHS---RHATSVVALHQKELALTHFTRVIGLGKD---ENGNGKVLLDANTDDLKP 223
Cdd:PRK11264 162 RPEVILFDEPTSALDPELVGEVLNTIRQlaqEKRTMVIVTHEMSFARDVADRAIFMDQGrivEQGPAKALFADPQQPRTR 241
|
....
gi 1148626600 224 QDLD 227
Cdd:PRK11264 242 QFLE 245
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
22-191 |
1.39e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 67.68 E-value: 1.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 22 EVVLRDLDVQLEHGERVALLGASGAGKSTLLEALRSALHEQGTPAAWCPQRQGLVPQLSVYHNIfmgrldqqssltnlln 101
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQFGREASLIDAI---------------- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 102 llrprpAHWQAVAAVCEPLGIAGL-----MERSVEALSGGQRQRVAIARALYQGHDLFLGDEPVASVDPHQASQLIHWIH 176
Cdd:COG2401 107 ------GRKGDFKDAVELLNAVGLsdavlWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQ 180
|
170
....*....|....*....
gi 1148626600 177 S----RHATSVVALHQKEL 191
Cdd:COG2401 181 KlarrAGITLVVATHHYDV 199
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
23-164 |
2.41e-13 |
|
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: 66.62 E-value: 2.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 23 VVLRDLDVQLEHGERVALLGASGAGKSTLLEALRSALH-EQG-----------TPAA------WCPQRQGLVPQLSVYHN 84
Cdd:cd03266 19 QAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEpDAGfatvdgfdvvkEPAEarrrlgFVSDSTGLYDRLTAREN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 85 I-FMGRLdqqssltnllNLLRPRPAHwQAVAAVCEPLGIAGLMERSVEALSGGQRQRVAIARALYQGHDLFLGDEPVASV 163
Cdd:cd03266 99 LeYFAGL----------YGLKGDELT-ARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGL 167
|
.
gi 1148626600 164 D 164
Cdd:cd03266 168 D 168
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
24-219 |
3.22e-13 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 68.35 E-value: 3.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 24 VLRDLDVQLEHGERVALLGASGAGKSTLLEALrSALHE--QGT-----------PAAWCPQRQGLVPQ---L---SVYHN 84
Cdd:TIGR03375 480 ALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLL-LGLYQptEGSvlldgvdirqiDPADLRRNIGYVPQdprLfygTLRDN 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 85 IFMGRL---DQqssltnllnllrprpahwqavaAVCEPLGIAGL----------MERSV----EALSGGQRQRVAIARAL 147
Cdd:TIGR03375 559 IALGAPyadDE----------------------EILRAAELAGVtefvrrhpdgLDMQIgergRSLSGGQRQAVALARAL 616
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1148626600 148 YQGHDLFLGDEPVASVDPHQASQLIH----WIHSRhaTSVVALHQKELaLTHFTRVIGLgkdenGNGKVLLDANTD 219
Cdd:TIGR03375 617 LRDPPILLLDEPTSAMDNRSEERFKDrlkrWLAGK--TLVLVTHRTSL-LDLVDRIIVM-----DNGRIVADGPKD 684
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
9-164 |
3.36e-13 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 67.03 E-value: 3.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 9 LLHLSRHHLGHGAEVVLRDLDVQLEHGERVALLGASGAGKSTLL-------EALRSALHEQGTPAAwCP--------QRQ 73
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLnliagfvPYQHGSITLDGKPVE-GPgaergvvfQNE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 74 GLVPQLSVYHNIFMGrldqqssltnLLNLLRPRPAHWQAVAAVCEPLGIAGLMERSVEALSGGQRQRVAIARALYQGHDL 153
Cdd:PRK11248 80 GLLPWRNVQDNVAFG----------LQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQL 149
|
170
....*....|.
gi 1148626600 154 FLGDEPVASVD 164
Cdd:PRK11248 150 LLLDEPFGALD 160
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
7-192 |
5.36e-13 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 65.99 E-value: 5.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 7 SPLLHLS----RHHLGHGAEVVLRDLDVQLEHGERVALLGASGAGKSTLLEAL-------------------------RS 57
Cdd:PRK11629 3 KILLQCDnlckRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLggldtptsgdvifngqpmsklssaaKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 58 AL--HEQGtpaaWCPQRQGLVPQLSVYHNIFMGRLdqqssltnlLNLLRPRPAHWQAVaavcEPLGIAGLMERS---VEA 132
Cdd:PRK11629 83 ELrnQKLG----FIYQFHHLLPDFTALENVAMPLL---------IGKKKPAEINSRAL----EMLAAVGLEHRAnhrPSE 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1148626600 133 LSGGQRQRVAIARALYQGHDLFLGDEPVASVDPHQAS---QLIHWIHSRHATS-VVALHQKELA 192
Cdd:PRK11629 146 LSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADsifQLLGELNRLQGTAfLVVTHDLQLA 209
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
18-159 |
8.83e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 67.01 E-value: 8.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 18 GHGAEVVLRDLDVQLEHGERVALLGASGAGKSTLLEALRSALH------EQGTPA--AWCPQ-RQGLVPQLSVYHNIFMG 88
Cdd:COG0488 324 SYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEpdsgtvKLGETVkiGYFDQhQEELDPDKTVLDELRDG 403
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1148626600 89 RLDQQSsltnllnllrprpahwQAVAAVCEPLGIAGLM-ERSVEALSGGQRQRVAIARALYQGHDLFLGDEP 159
Cdd:COG0488 404 APGGTE----------------QEVRGYLGRFLFSGDDaFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEP 459
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-164 |
1.14e-12 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 66.51 E-value: 1.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 1 MTQATPSPLLHLSRHHLGHGAEVVLRDLDVQLEHGERVALLGASGAGKSTLL------EALRS---ALHEQ---GTPAAw 68
Cdd:PRK09452 6 KQPSSLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLrliagfETPDSgriMLDGQditHVPAE- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 69 cpQRQ--------GLVPQLSVYHNIFMGrLDQQSSLTNLLnllRPRpahwqavaaVCEPLG---IAGLMERSVEALSGGQ 137
Cdd:PRK09452 85 --NRHvntvfqsyALFPHMTVFENVAFG-LRMQKTPAAEI---TPR---------VMEALRmvqLEEFAQRKPHQLSGGQ 149
|
170 180
....*....|....*....|....*..
gi 1148626600 138 RQRVAIARALYQGHDLFLGDEPVASVD 164
Cdd:PRK09452 150 QQRVAIARAVVNKPKVLLLDESLSALD 176
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
35-187 |
2.06e-12 |
|
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: 64.74 E-value: 2.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 35 GERVALLGASGAGKSTLLEALRSALHEQGTPAAWCPQRQGLVPQlsvYHNI-FMGRLDQQSSLTNLLNLLRPrpaHWQAv 113
Cdd:cd03237 25 SEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQ---YIKAdYEGTVRDLLSSITKDFYTHP---YFKT- 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1148626600 114 aAVCEPLGIAGLMERSVEALSGGQRQRVAIARALYQGHDLFLGDEPVASVDPHQ---ASQLI-HWIHSRHATSVVALH 187
Cdd:cd03237 98 -EIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQrlmASKVIrRFAENNEKTAFVVEH 174
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
17-159 |
2.42e-12 |
|
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: 62.47 E-value: 2.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 17 LGHGAEVVLRDLDVQLEHGERVALLGASGAGKSTLLEALRSALHE-QGTPaawcpqrqglvpqlSVYHNIFMGRLDQqss 95
Cdd:cd03221 8 KTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPdEGIV--------------TWGSTVKIGYFEQ--- 70
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1148626600 96 ltnllnllrprpahwqavaavceplgiaglmersveaLSGGQRQRVAIARALYQGHDLFLGDEP 159
Cdd:cd03221 71 -------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEP 97
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
20-165 |
2.86e-12 |
|
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: 63.84 E-value: 2.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 20 GAEVVLRDLDVQLEHGERVALLGASGAGKSTLLEAL-------RSALHEQGTPA--------AWCPQRQGLVPQLSVYHN 84
Cdd:cd03269 11 GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMIlgiilpdSGEVLFDGKPLdiaarnriGYLPEERGLYPKMKVIDQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 85 -IFMGRLdqqssLTNLLNLLRPRPAHWqavaavCEPLGIAGLMERSVEALSGGQRQRVAIARALYQGHDLFLGDEPVASV 163
Cdd:cd03269 91 lVYLAQL-----KGLKKEEARRRIDEW------LERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGL 159
|
..
gi 1148626600 164 DP 165
Cdd:cd03269 160 DP 161
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
23-207 |
2.91e-12 |
|
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: 62.94 E-value: 2.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 23 VVLRDLDVQLEHGERVALLGASGAGKSTLLEALrSALHEQGTPAAWCPQRQGL--VPQLSvyhniFM--GRLDQQssltn 98
Cdd:cd03223 15 VLLKDLSFEIKPGDRLLITGPSGTGKSSLFRAL-AGLWPWGSGRIGMPEGEDLlfLPQRP-----YLplGTLREQ----- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 99 llnllrprpahwqavaaVCEPLGiaglmersvEALSGGQRQRVAIARALYQGHDLFLGDEPVASVDPHQASQLIHWIHSR 178
Cdd:cd03223 84 -----------------LIYPWD---------DVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKEL 137
|
170 180
....*....|....*....|....*....
gi 1148626600 179 HATSVVALHQKELaLTHFTRVIGLGKDEN 207
Cdd:cd03223 138 GITVISVGHRPSL-WKFHDRVLDLDGEGG 165
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
15-166 |
3.68e-12 |
|
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: 63.61 E-value: 3.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 15 HHLGHGAEVVLRDLDVQLEHGERVALLGASGAGKSTLLEAL-RSALHEQGT-----PAAW-----CPQRQ---------G 74
Cdd:COG4778 17 HLQGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIyGNYLPDSGSilvrhDGGWvdlaqASPREilalrrrtiG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 75 LVPQ-LSVyhnifmgrldqqssltnllnllRPRPAhwqAVAAVCEPLgIAGLMERSV---------------EAL----- 133
Cdd:COG4778 97 YVSQfLRV----------------------IPRVS---ALDVVAEPL-LERGVDREEarararellarlnlpERLwdlpp 150
|
170 180 190
....*....|....*....|....*....|....*.
gi 1148626600 134 ---SGGQRQRVAIARALYQGHDLFLGDEPVASVDPH 166
Cdd:COG4778 151 atfSGGEQQRVNIARGFIADPPLLLLDEPTASLDAA 186
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
20-165 |
3.80e-12 |
|
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: 64.20 E-value: 3.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 20 GAEVVLRDLDVQLEHGERVALLGASGAGKSTLLEAL----------------------RSALHE-QGTPAAWCPQRQGLV 76
Cdd:cd03294 35 GQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCInrlieptsgkvlidgqdiaamsRKELRElRRKKISMVFQSFALL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 77 PQLSVYHNIFMGrLDQQSsltnllnllRPRPAHWQAVAAVCEPLGIAGLMERSVEALSGGQRQRVAIARALYQGHDLFLG 156
Cdd:cd03294 115 PHRTVLENVAFG-LEVQG---------VPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLM 184
|
....*....
gi 1148626600 157 DEPVASVDP 165
Cdd:cd03294 185 DEAFSALDP 193
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
24-166 |
4.21e-12 |
|
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: 63.40 E-value: 4.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 24 VLRDLDVQLEHGERVALLGASGAGKSTLLEAL-RSALHEQGT-----------PAAWCPQRQGLVPQ------LSVYHNI 85
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLmRFYDPQKGQilidgidirdiSRKSLRSMIGVVLQdtflfsGTIMENI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 86 FMGRLDQQSSLtnllnllrprpahwqaVAAVCEPLGIAGLMERSVEA-----------LSGGQRQRVAIARALYQGHDLF 154
Cdd:cd03254 98 RLGRPNATDEE----------------VIEAAKEAGAHDFIMKLPNGydtvlgenggnLSQGERQLLAIARAMLRDPKIL 161
|
170
....*....|..
gi 1148626600 155 LGDEPVASVDPH 166
Cdd:cd03254 162 ILDEATSNIDTE 173
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
4-192 |
4.49e-12 |
|
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: 63.61 E-value: 4.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 4 ATPSPLLHLS--RHHLGHGAE--VVLRDLDVQLEHGERVALLGASGAGKSTLL------------------EALrSALHE 61
Cdd:COG4181 3 SSSAPIIELRglTKTVGTGAGelTILKGISLEVEAGESVAIVGASGSGKSTLLgllagldrptsgtvrlagQDL-FALDE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 62 QGTpAAWCPQRQG-------LVPQLSVYHNIFM-----GRldqqssltnllnllrpRPAHWQAVAAvcepLGIAGLMERS 129
Cdd:COG4181 82 DAR-ARLRARHVGfvfqsfqLLPTLTALENVMLplelaGR----------------RDARARARAL----LERVGLGHRL 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 130 VEA---LSGGQRQRVAIARALYQGHDLFLGDEPVASVDPHQASQLIHWIHS----RHATSVVALHQKELA 192
Cdd:COG4181 141 DHYpaqLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFElnreRGTTLVLVTHDPALA 210
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
19-171 |
5.51e-12 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 63.56 E-value: 5.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 19 HGAEVVLRDLDVQLEHGERVALLGASGAGKSTLLeALRSALHEQ--------GTPAAWCPQRQ------------GLVPQ 78
Cdd:COG4604 11 YGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLL-SMISRLLPPdsgevlvdGLDVATTPSRElakrlailrqenHINSR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 79 LSV----------YHNifmGRLdqqssltnllnllrpRPAHWQAVAAVCEPLGIAGLMERSVEALSGGQRQRVAIARALY 148
Cdd:COG4604 90 LTVrelvafgrfpYSK---GRL---------------TAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLA 151
|
170 180
....*....|....*....|...
gi 1148626600 149 QGHDLFLGDEPVASVDPHQASQL 171
Cdd:COG4604 152 QDTDYVLLDEPLNNLDMKHSVQM 174
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
24-165 |
7.18e-12 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 62.99 E-value: 7.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 24 VLRDLDVQLEHGERVALLGASGAGKSTLLEAL-----RSA--------------LHEQGTPA-AWCPQRQGLVPQLSVYH 83
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVvgivpRDAgniiiddedisllpLHARARRGiGYLPQEASIFRRLSVYD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 84 NIfMGRLDQQSSLTNLLNLLRPRpahwqavaAVCEPLGIAGLMERSVEALSGGQRQRVAIARALYQGHDLFLGDEPVASV 163
Cdd:PRK10895 98 NL-MAVLQIRDDLSAEQREDRAN--------ELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGV 168
|
..
gi 1148626600 164 DP 165
Cdd:PRK10895 169 DP 170
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
24-173 |
8.06e-12 |
|
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: 61.68 E-value: 8.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 24 VLRDLDVQLEHGERVALLGASGAGKSTLLEALrSALHEQ--------GTPAAWCP----------------QRQGLVPQL 79
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEAL-FGLRPPasgeitldGKPVTRRSprdairagiayvpedrKREGLVLDL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 80 SVYHNIFMGRLdqqssltnllnllrprpahwqavaavceplgiaglmersveaLSGGQRQRVAIARALYQGHDLFLGDEP 159
Cdd:cd03215 94 SVAENIALSSL------------------------------------------LSGGNQQKVVLARWLARDPRVLILDEP 131
|
170
....*....|....
gi 1148626600 160 VASVDPHqASQLIH 173
Cdd:cd03215 132 TRGVDVG-AKAEIY 144
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
7-202 |
9.89e-12 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 62.42 E-value: 9.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 7 SPLLHLSRHHLGHGAEVVLRDLDVQLEHGERVALLGASGAGKSTLLEALRSALHE-------QGTP-AAWCPQ--RQGL- 75
Cdd:PRK10247 5 SPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPtsgtllfEGEDiSTLKPEiyRQQVs 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 76 ----VPQL---SVYHN-IFMGRLDQQssltnllnllRPRPAHWQAVAAVCE-PLGIaglMERSVEALSGGQRQRVAIARA 146
Cdd:PRK10247 85 ycaqTPTLfgdTVYDNlIFPWQIRNQ----------QPDPAIFLDDLERFAlPDTI---LTKNIAELSGGEKQRISLIRN 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1148626600 147 LYQGHDLFLGDEPVASVDPHQ---ASQLIHWIHSRHATSVVALHQKELALTHFTRVIGL 202
Cdd:PRK10247 152 LQFMPKVLLLDEITSALDESNkhnVNEIIHRYVREQNIAVLWVTHDKDEINHADKVITL 210
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
24-165 |
1.05e-11 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 62.68 E-value: 1.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 24 VLRDLDVQLEHGERVALLGASGAGKST-------LLEALRSALHEQGTPAAWCP----QRQGLV--PQ-------LSVYH 83
Cdd:TIGR04406 16 VVNDVSLSVKSGEIVGLLGPNGAGKTTsfymivgLVRPDAGKILIDGQDITHLPmherARLGIGylPQeasifrkLTVEE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 84 NIfMGRLDQQSSLtnllnllrPRPAHWQAVAAVCEPLGIAGLMERSVEALSGGQRQRVAIARALYQGHDLFLGDEPVASV 163
Cdd:TIGR04406 96 NI-MAVLEIRKDL--------DRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLDEPFAGV 166
|
..
gi 1148626600 164 DP 165
Cdd:TIGR04406 167 DP 168
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
20-183 |
1.06e-11 |
|
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: 62.39 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 20 GAEVVLRDLDVQLEHGERVALLGASGAGKSTLLEALRSALHEQGTPA------------------AWCPQRQGLVPQLSV 81
Cdd:cd03265 11 GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRAtvaghdvvreprevrrriGIVFQDLSVDDELTG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 82 YHNIFM-GRLdqqssltnllnLLRPRPAHWQAVAAVCEPLGIAGLMERSVEALSGGQRQRVAIARALYQGHDLFLGDEPV 160
Cdd:cd03265 91 WENLYIhARL-----------YGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPT 159
|
170 180
....*....|....*....|....*.
gi 1148626600 161 ASVDPHQASQL---IHWIHSRHATSV 183
Cdd:cd03265 160 IGLDPQTRAHVweyIEKLKEEFGMTI 185
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
25-171 |
1.07e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 64.23 E-value: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 25 LRDLDVQLEHGERVALLGASGAGKSTLLEALRSALHEQGTPAAWCPQRQGLVPQLSVyhnIFMGRLDQQSSLTNLLNLLR 104
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVVIRGSVAYVPQVSW---IFNATVRENILFGSDFESER 709
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1148626600 105 prpaHWQA--VAAVCEPLGI-AG-----LMERSVEaLSGGQRQRVAIARALYQGHDLFLGDEPVASVDPHQASQL 171
Cdd:PLN03232 710 ----YWRAidVTALQHDLDLlPGrdlteIGERGVN-ISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQV 779
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
24-188 |
1.19e-11 |
|
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: 62.29 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 24 VLRDLDVQLEHGERVALLGASGAGKSTLLEALRSALHEQGT-------------PAAW------CPQRQGLVPQLSVYHN 84
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGTtsgqilfngqprkPDQFqkcvayVRQDDILLPGLTVRET 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 85 I-FMGRLDQQSSLTNLLNLLRprpahwqAVAAVCEPLGIAGLMERSVEALSGGQRQRVAIARALYQGHDLFLGDEPVASV 163
Cdd:cd03234 102 LtYTAILRLPRKSSDAIRKKR-------VEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGL 174
|
170 180
....*....|....*....|....*....
gi 1148626600 164 DPHQASQLIHwIHSRHATS----VVALHQ 188
Cdd:cd03234 175 DSFTALNLVS-TLSQLARRnrivILTIHQ 202
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
40-221 |
1.24e-11 |
|
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: 63.28 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 40 LLGASGAGKSTLLEALrsALHEQ---------GTPAAWCP----------QRQGLVPQLSVYHNIFMGrLDQQSSltnll 100
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLL--AGFEQpdsgsimldGEDVTNVPphlrhinmvfQSYALFPHMTVEENVAFG-LKMRKV----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 101 nllrPRPAHWQAVAAVCEPLGIAGLMERSVEALSGGQRQRVAIARALYQGHDLFLGDEPVASVDPHQASQLIHWIHSRH- 179
Cdd:TIGR01187 73 ----PRAEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQe 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1148626600 180 ---ATSVVALHQKELALTHFTRVIGLgkdenGNGKVLLDANTDDL 221
Cdd:TIGR01187 149 qlgITFVFVTHDQEEAMTMSDRIAIM-----RKGKIAQIGTPEEI 188
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
118-187 |
1.75e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 63.29 E-value: 1.75e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1148626600 118 EPLGIAGLMERSVEALSGGQRQRVAIARALYQGHDLFLGDEPVASVDPHQ---ASQLI-HWIHSRHATSVVALH 187
Cdd:PRK13409 439 KPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQrlaVAKAIrRIAEEREATALVVDH 512
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
18-172 |
1.84e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 62.21 E-value: 1.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 18 GHGAevvLRDLDVQLEHGERVALLGASGAGKSTLLEALRSALH-EQGTPAAW-CPQRQGL-------VPQ---------L 79
Cdd:PRK15056 19 GHTA---LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRlASGKISILgQPTRQALqknlvayVPQseevdwsfpV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 80 SVYHNIFMGRLDQQSSLTnllnllRPRPAHWQAVAAVCEPLGIAGLMERSVEALSGGQRQRVAIARALYQGHDLFLGDEP 159
Cdd:PRK15056 96 LVEDVVMMGRYGHMGWLR------RAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEP 169
|
170
....*....|...
gi 1148626600 160 VASVDPHQASQLI 172
Cdd:PRK15056 170 FTGVDVKTEARII 182
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
25-202 |
1.90e-11 |
|
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: 61.71 E-value: 1.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 25 LRDLDVQLEHGERVALLGASGAGKSTLLEALRS--------------ALHEQGTPAAWCPQRQGLVPQLSVYHNIFMGrl 90
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGlaqptsggvilegkQITEPGPDRMVVFQNYSLLPWLTVRENIALA-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 91 dqqsslTNLLNLLRPRPAHWQAVAAVCEPLGIAGLMERSVEALSGGQRQRVAIARALYQGHDLFLGDEPVASVDP----H 166
Cdd:TIGR01184 79 ------VDRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDAltrgN 152
|
170 180 190
....*....|....*....|....*....|....*.
gi 1148626600 167 QASQLIHWIHSRHATSVVALHQKELALTHFTRVIGL 202
Cdd:TIGR01184 153 LQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVML 188
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
25-194 |
2.37e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 62.17 E-value: 2.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 25 LRDLDVQLEHGERVALLGASGAGKSTLLEALRSALHE-------QGTPAAWcpQRQGLVP--------------QL---S 80
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPssgrilfDGKPIDY--SRKGLMKlresvgmvfqdpdnQLfsaS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 81 VYHNIFMGRLDQQSsltnllnllrPRPAHWQAVAAVCEPLGIAGLMERSVEALSGGQRQRVAIARALYQGHDLFLGDEPV 160
Cdd:PRK13636 100 VYQDVSFGAVNLKL----------PEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPT 169
|
170 180 190
....*....|....*....|....*....|....
gi 1148626600 161 ASVDPHQASQLIHWIHSRhatsvvalhQKELALT 194
Cdd:PRK13636 170 AGLDPMGVSEIMKLLVEM---------QKELGLT 194
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
21-217 |
3.06e-11 |
|
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: 61.35 E-value: 3.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 21 AEVVLRDLDVQLEHGERVALLGASGAGKSTLLEAL-RSALHEQG-----------TPAAWCPQRQGLVPQ------LSVY 82
Cdd:cd03252 14 GPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIqRFYVPENGrvlvdghdlalADPAWLRRQVGVVLQenvlfnRSIR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 83 HNIFMGrlDQQSSLTNLLNLLRPRPAHwqavAAVCE-PLGIAGLMERSVEALSGGQRQRVAIARALYQGHDLFLGDEPVA 161
Cdd:cd03252 94 DNIALA--DPGMSMERVIEAAKLAGAH----DFISElPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATS 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1148626600 162 SVDPHQASQLIHWIHSRHA--TSVVALHQKElALTHFTRVIGLGKD---ENGNGKVLLDAN 217
Cdd:cd03252 168 ALDYESEHAIMRNMHDICAgrTVIIIAHRLS-TVKNADRIIVMEKGrivEQGSHDELLAEN 227
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
10-167 |
3.17e-11 |
|
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: 60.67 E-value: 3.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 10 LHLSRHHLGHGAEVVLRDLDVQLEHGeRVALLGASGAGKSTLLEAL---------RSALHEQGTPA---------AWCPQ 71
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILatltppssgTIRIDGQDVLKqpqklrrriGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 72 RQGLVPQLSVYHNI-FMGRLDqqssltnllnllrpRPAHWQAVAAVCEPLGIAGLMER---SVEALSGGQRQRVAIARAL 147
Cdd:cd03264 80 EFGVYPNFTVREFLdYIAWLK--------------GIPSKEVKARVDEVLELVNLGDRakkKIGSLSGGMRRRVGIAQAL 145
|
170 180
....*....|....*....|
gi 1148626600 148 YQGHDLFLGDEPVASVDPHQ 167
Cdd:cd03264 146 VGDPSILIVDEPTAGLDPEE 165
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
24-165 |
3.41e-11 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 61.20 E-value: 3.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 24 VLRDLDVQLEHGERVALLGASGAGKST-------LLEAlrsalhEQGT-----------P----AawcpqRQGL--VPQ- 78
Cdd:COG1137 18 VVKDVSLEVNQGEIVGLLGPNGAGKTTtfymivgLVKP------DSGRifldgedithlPmhkrA-----RLGIgyLPQe 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 79 ------LSVYHNIfMGRLDQQSsltnllnllRPRPAHWQAVAAVCEPLGIAGLMERSVEALSGGQRQRVAIARALYQGHD 152
Cdd:COG1137 87 asifrkLTVEDNI-LAVLELRK---------LSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPK 156
|
170
....*....|...
gi 1148626600 153 LFLGDEPVASVDP 165
Cdd:COG1137 157 FILLDEPFAGVDP 169
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
23-206 |
5.54e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 60.86 E-value: 5.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 23 VVLRDLDVQLEHGERVALLGASGAGKSTL-------LEALRSALHEQGTPAAW-------CPQRQGLVPQ--------LS 80
Cdd:PRK13639 16 EALKGINFKAEKGEMVALLGPNGAGKSTLflhfngiLKPTSGEVLIKGEPIKYdkkslleVRKTVGIVFQnpddqlfaPT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 81 VYHNIFMGRLDQQSSLTNLLNLLRprpahwQAVAAVceplGIAGLMERSVEALSGGQRQRVAIARALYQGHDLFLGDEPV 160
Cdd:PRK13639 96 VEEDVAFGPLNLGLSKEEVEKRVK------EALKAV----GMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPT 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1148626600 161 ASVDPHQASQ---LIHWIHSRHATSVVALHQKELALTHFTRVIGLGKDE 206
Cdd:PRK13639 166 SGLDPMGASQimkLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGK 214
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
24-164 |
6.82e-11 |
|
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: 60.32 E-value: 6.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 24 VLRDLDVQLEHGERVALLGASGAGKSTL--------------------------LEALRSALheqgtpaawcpqrqGLVP 77
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLvnliprfydvdsgrilidghdvrdytLASLRRQI--------------GLVS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 78 QL------SVYHNIFMGRLDQQSSLTNLLNllrpRPAHwqAVAAVCE-PLGI-AGLMERSVEaLSGGQRQRVAIARALYQ 149
Cdd:cd03251 83 QDvflfndTVAENIAYGRPGATREEVEEAA----RAAN--AHEFIMElPEGYdTVIGERGVK-LSGGQRQRIAIARALLK 155
|
170
....*....|....*
gi 1148626600 150 GHDLFLGDEPVASVD 164
Cdd:cd03251 156 DPPILILDEATSALD 170
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
24-164 |
7.49e-11 |
|
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: 60.64 E-value: 7.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 24 VLRDLDVQLEHGERVALLGASGAGKSTLL-------EALRSALHEQGTpAAWCPQRQGLVPQlSVYHNIFMG-RLDQQss 95
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLmlilgelEPSEGKIKHSGR-ISFSSQFSWIMPG-TIKENIIFGvSYDEY-- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 96 ltnllnllrprpaHWQAVAAVCE--------------PLGIAGLMersveaLSGGQRQRVAIARALYQGHDLFLGDEPVA 161
Cdd:cd03291 128 -------------RYKSVVKACQleeditkfpekdntVLGEGGIT------LSGGQRARISLARAVYKDADLYLLDSPFG 188
|
...
gi 1148626600 162 SVD 164
Cdd:cd03291 189 YLD 191
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
20-165 |
8.62e-11 |
|
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: 59.86 E-value: 8.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 20 GAEVVLRDLDVQLEHGERVALLGASGAGKSTL-------------------LEALRSALHEQ---GTpaAWCPQRQGLVP 77
Cdd:cd03218 11 GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTfymivglvkpdsgkilldgQDITKLPMHKRarlGI--GYLPQEASIFR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 78 QLSVYHNI-----FMGRLDQQSSltnllnllrprpahwQAVAAVCEPLGIAGLMERSVEALSGGQRQRVAIARALYQGHD 152
Cdd:cd03218 89 KLTVEENIlavleIRGLSKKERE---------------EKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPK 153
|
170
....*....|...
gi 1148626600 153 LFLGDEPVASVDP 165
Cdd:cd03218 154 FLLLDEPFAGVDP 166
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
24-164 |
8.86e-11 |
|
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: 61.27 E-value: 8.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 24 VLRDLDVQLEHGERVALLGASGAGKSTLLEAL-RSALHEQGT------PAA----WCPQRQ-GLVPQL------SVYHNI 85
Cdd:TIGR02203 347 ALDSISLVIEPGETVALVGRSGSGKSTLVNLIpRFYEPDSGQilldghDLAdytlASLRRQvALVSQDvvlfndTIANNI 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 86 FMGRLDQqssltnlLNLLRPRPAhwqAVAAVCE------PLGIAGLMERSVEALSGGQRQRVAIARALYQGHDLFLGDEP 159
Cdd:TIGR02203 427 AYGRTEQ-------ADRAEIERA---LAAAYAQdfvdklPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEA 496
|
....*
gi 1148626600 160 VASVD 164
Cdd:TIGR02203 497 TSALD 501
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
20-171 |
9.10e-11 |
|
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: 59.81 E-value: 9.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 20 GAEVVLRDLDVQLEHGERVALLGASGAGKSTL--------------------------LEALRSALheqgtpaawcpqrq 73
Cdd:cd03244 15 NLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLllalfrlvelssgsilidgvdiskigLHDLRSRI-------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 74 GLVPQLSVyhnIFMG--R--LDqqssltnllnllrPRPAH-----WQAVAAVC-------EPLGIAGLMERSVEALSGGQ 137
Cdd:cd03244 81 SIIPQDPV---LFSGtiRsnLD-------------PFGEYsdeelWQALERVGlkefvesLPGGLDTVVEEGGENLSVGQ 144
|
170 180 190
....*....|....*....|....*....|....
gi 1148626600 138 RQRVAIARALYQGHDLFLGDEPVASVDPHQASQL 171
Cdd:cd03244 145 RQLLCLARALLRKSKILVLDEATASVDPETDALI 178
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
25-176 |
9.78e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 61.10 E-value: 9.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 25 LRDLDVQLEHGERVALLGASGAGKSTLLEALrSALHEQGTpaaWC-----------------PQRQG---------LVPQ 78
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVL-SGVYPHGT---YEgeiifegeelqasnirdTERAGiaiihqelaLVKE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 79 LSVYHNIFMGRldqqssltnllnllRPRPA---HWQAVAAVCEPL----GIAGLMERSVEALSGGQRQRVAIARALYQGH 151
Cdd:PRK13549 97 LSVLENIFLGN--------------EITPGgimDYDAMYLRAQKLlaqlKLDINPATPVGNLGLGQQQLVEIAKALNKQA 162
|
170 180
....*....|....*....|....*
gi 1148626600 152 DLFLGDEPVASVDPHQASQLIHWIH 176
Cdd:PRK13549 163 RLLILDEPTASLTESETAVLLDIIR 187
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
19-196 |
9.94e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 60.59 E-value: 9.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 19 HGAEVVLRDLDVQLEHGERVALLGASGAGKSTLLEALRSALHEQGTPAAWCP-----------QRQGLVPQL-------S 80
Cdd:PRK13537 17 YGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGepvpsrarharQRVGVVPQFdnldpdfT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 81 VYHNIFM-GRLDQQSSLtnllnllrprpahwQAVAAVCEPLGIAGLMERS---VEALSGGQRQRVAIARALYQGHDLFLG 156
Cdd:PRK13537 97 VRENLLVfGRYFGLSAA--------------AARALVPPLLEFAKLENKAdakVGELSGGMKRRLTLARALVNDPDVLVL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1148626600 157 DEPVASVDPhQASQLIhWIHSRhatSVVALHQKELALTHF 196
Cdd:PRK13537 163 DEPTTGLDP-QARHLM-WERLR---SLLARGKTILLTTHF 197
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
7-171 |
1.16e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 59.79 E-value: 1.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 7 SPLLHLSRHHLGHGAEVVLRDLDVQLEHGERVALLGASGAGKSTLLEALrsalheqgtpaawcpQRQG-LVPQLSVY--- 82
Cdd:PRK14239 3 EPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSI---------------NRMNdLNPEVTITgsi 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 83 ----HNIFMGRLDQ-QSSLTNLLNLLRPRPAHWQAVAAVCEPLGIAG-----LMERSVE--------------------- 131
Cdd:PRK14239 68 vyngHNIYSPRTDTvDLRKEIGMVFQQPNPFPMSIYENVVYGLRLKGikdkqVLDEAVEkslkgasiwdevkdrlhdsal 147
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1148626600 132 ALSGGQRQRVAIARALYQGHDLFLGDEPVASVDPHQASQL 171
Cdd:PRK14239 148 GLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKI 187
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
10-167 |
1.49e-10 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 59.84 E-value: 1.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 10 LHLSRHHlghgaEVVLRDLDVQLEHGERVALLGASGAGKSTLLEALRSALHEQGTP----------------AAWCPQR- 72
Cdd:PRK13547 7 LHVARRH-----RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGAPrgarvtgdvtlngeplAAIDAPRl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 73 ---QGLVPQ-------LSVYHNIFMGRLDQqsSLTNLLNLLRPRPAHWQAVAAVceplGIAGLMERSVEALSGGQRQRVA 142
Cdd:PRK13547 82 arlRAVLPQaaqpafaFSAREIVLLGRYPH--ARRAGALTHRDGEIAWQALALA----GATALVGRDVTTLSGGELARVQ 155
|
170 180 190
....*....|....*....|....*....|....*
gi 1148626600 143 IARALYQ---------GHDLFLGDEPVASVD-PHQ 167
Cdd:PRK13547 156 FARVLAQlwpphdaaqPPRYLLLDEPTAALDlAHQ 190
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
118-164 |
1.51e-10 |
|
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: 60.57 E-value: 1.51e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1148626600 118 EPLGIAGLMERSVEALSGGQRQRVAIARALYQGHDLFLGDEPVASVD 164
Cdd:COG1245 441 KPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 487
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
23-203 |
1.55e-10 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 58.66 E-value: 1.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 23 VVLRDLDVQLEHGERVALLGASGAGKSTLL---------------------EALRSALHEQgtpAAWCPQRQGLVPQLSV 81
Cdd:PRK13538 15 ILFSGLSFTLNAGELVQIEGPNGAGKTSLLrilaglarpdagevlwqgepiRRQRDEYHQD---LLYLGHQPGIKTELTA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 82 YHNI-FMGRLDQQSSltnllnllrpRPAHWQAVAAVceplGIAGLMERSVEALSGGQRQRVAIARALYQGHDLFLGDEPV 160
Cdd:PRK13538 92 LENLrFYQRLHGPGD----------DEALWEALAQV----GLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPF 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1148626600 161 ASVDPHQASQLIHWIhSRHATS----VVALHQKELALTHFTRVIGLG 203
Cdd:PRK13538 158 TAIDKQGVARLEALL-AQHAEQggmvILTTHQDLPVASDKVRKLRLG 203
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
24-164 |
1.55e-10 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 60.24 E-value: 1.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 24 VLRDLDVQLEHGERVALLGASGAGKSTL------LEALRSalheqGT------------PA----AWCPQRQGLVPQLSV 81
Cdd:PRK11650 19 VIKGIDLDVADGEFIVLVGPSGCGKSTLlrmvagLERITS-----GEiwiggrvvnelePAdrdiAMVFQNYALYPHMSV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 82 YHNIFMGrldqqssltnllNLLR--PRPAHWQAVAAVCEPLGIAGLMERSVEALSGGQRQRVAIARALYQGHDLFLGDEP 159
Cdd:PRK11650 94 RENMAYG------------LKIRgmPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEP 161
|
....*
gi 1148626600 160 VASVD 164
Cdd:PRK11650 162 LSNLD 166
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
24-164 |
1.57e-10 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 60.69 E-value: 1.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 24 VLRDLDVQLEHGERVALLGASGAGKSTLLEALRSALH------EQGTPAAWCPQRQGLVPQlSVYHNIFMG-RLDQQssl 96
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEpsegkiKHSGRISFSPQTSWIMPG-TIKDNIIFGlSYDEY--- 516
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 97 tnllnllrprpaHWQAVAAVCE--------------PLGIAGLmersveALSGGQRQRVAIARALYQGHDLFLGDEPVAS 162
Cdd:TIGR01271 517 ------------RYTSVIKACQleedialfpekdktVLGEGGI------TLSGGQRARISLARAVYKDADLYLLDSPFTH 578
|
..
gi 1148626600 163 VD 164
Cdd:TIGR01271 579 LD 580
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
24-164 |
2.40e-10 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 59.65 E-value: 2.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 24 VLRDLDVQLEHGERVALLGASGAGKSTLLEAL-----RSA----LHEQ----GTPA-------AWCP---QRQGLVPQLS 80
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALfgadpADSgeirLDGKpvriRSPRdairagiAYVPedrKGEGLVLDLS 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 81 VYHNIFMGRLDQqssltNLLNLLRPRPAHWQAVAAVCEPLGI-AGLMERSVEALSGGQRQRVAIARALYQGHDLFLGDEP 159
Cdd:COG1129 347 IRENITLASLDR-----LSRGGLLDRRRERALAEEYIKRLRIkTPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEP 421
|
....*
gi 1148626600 160 VASVD 164
Cdd:COG1129 422 TRGID 426
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
25-170 |
2.66e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 60.14 E-value: 2.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 25 LRDLDVQLEHGERVALLGASGAGKSTLLEALRSALHEQGTPAAWCPQRQGLVPQLS------VYHNIFMGrldqqssltn 98
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVVIRGTVAYVPQVSwifnatVRDNILFG---------- 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 99 llnLLRPRPAHWQA--VAAVCEPLGI-AG-----LMERSVEaLSGGQRQRVAIARALYQGHDLFLGDEPVASVDPHQASQ 170
Cdd:PLN03130 703 ---SPFDPERYERAidVTALQHDLDLlPGgdlteIGERGVN-ISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQ 778
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
19-199 |
3.27e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 57.96 E-value: 3.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 19 HGAEVVLRDLDVQLEHGERVALLGASGAGKSTLL---------EALRSALHEQGTPAAWCPQ-------RQGLVPQLSVY 82
Cdd:PRK13539 12 RGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLrliagllppAAGTIKLDGGDIDDPDVAEachylghRNAMKPALTVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 83 HNI-FMGRLdqqssltnllnllrpRPAHWQAVAAVCEPLGIAGLMERSVEALSGGQRQRVAIARALYQGHDLFLGDEPVA 161
Cdd:PRK13539 92 ENLeFWAAF---------------LGGEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTA 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1148626600 162 SVDPHqASQLIHWIHSRHATS----VVALHQ-------KELALTHFTRV 199
Cdd:PRK13539 157 ALDAA-AVALFAELIRAHLAQggivIAATHIplglpgaRELDLGPFAAE 204
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
32-188 |
3.38e-10 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 59.68 E-value: 3.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 32 LEHGERVALLGASGAGKSTLLEAL--RSALHEQGTPA---------AWCPQRQG--------LVPQLSVY-HNIFMGRLD 91
Cdd:TIGR00955 48 AKPGELLAVMGSSGAGKTTLMNALafRSPKGVKGSGSvllngmpidAKEMRAISayvqqddlFIPTLTVReHLMFQAHLR 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 92 QQSSLTNLLNLLRprpahwqaVAAVCEPLG-------IAGLMERsVEALSGGQRQRVAIA-RALYQGHDLFLgDEPVASV 163
Cdd:TIGR00955 128 MPRRVTKKEKRER--------VDEVLQALGlrkcantRIGVPGR-VKGLSGGERKRLAFAsELLTDPPLLFC-DEPTSGL 197
|
170 180
....*....|....*....|....*...
gi 1148626600 164 DPHQASQLIHWIHS---RHATSVVALHQ 188
Cdd:TIGR00955 198 DSFMAYSVVQVLKGlaqKGKTIICTIHQ 225
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
31-226 |
3.49e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 58.41 E-value: 3.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 31 QLEHGERVALLGASGAGKSTLLEALRSAL------HEQGTPA------------AWCPQRQGLVPQLSVYHNIFMGRLDQ 92
Cdd:PRK03695 18 EVRAGEILHLVGPNGAGKSTLLARMAGLLpgsgsiQFAGQPLeawsaaelarhrAYLSQQQTPPFAMPVFQYLTLHQPDK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 93 QSSLTNLLnllrprpahwqAVAAVCEPLGIAGLMERSVEALSGGQRQRVAIARALYQGH-------DLFLGDEPVASVDP 165
Cdd:PRK03695 98 TRTEAVAS-----------ALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQVWpdinpagQLLLLDEPMNSLDV 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1148626600 166 HQAS---QLIHWIHSRHATSVVALHQKELALTHFTRVIGLgkdenGNGKVLLDANTDD-LKPQDL 226
Cdd:PRK03695 167 AQQAaldRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLL-----KQGKLLASGRRDEvLTPENL 226
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
23-164 |
3.54e-10 |
|
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: 58.11 E-value: 3.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 23 VVLRDLDVQLEHGERVALLGASGAGKSTLLEALRSALH-EQGTP--AAWCP--QRQGLVPQLSVyhniFMGRLDQ----- 92
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQpTSGEVrvAGLVPwkRRKKFLRRIGV----VFGQKTQlwwdl 110
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1148626600 93 --QSSLTNLLNLLRPRPAHWQA-VAAVCEPLGIAGLMERSVEALSGGQRQRVAIARALYqgHD---LFLgDEPVASVD 164
Cdd:cd03267 111 pvIDSFYLLAAIYDLPPARFKKrLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALL--HEpeiLFL-DEPTIGLD 185
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
25-200 |
4.21e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 58.21 E-value: 4.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 25 LRDLDVQLEHGERVALLGASGAGKSTLLEALRSA-LHEQG---------TPAA--WCPQRQGLVPQ--------LSVYHN 84
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIyLPQRGrvkvmgrevNAENekWVRSKVGLVFQdpddqvfsSTVWDD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 85 IFMGRLDQQSSLTNLLNLLRprpahwQAVAAVceplGIAGLMERSVEALSGGQRQRVAIARALYQGHDLFLGDEPVASVD 164
Cdd:PRK13647 101 VAFGPVNMGLDKDEVERRVE------EALKAV----RMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLD 170
|
170 180 190
....*....|....*....|....*....|....*....
gi 1148626600 165 PHQASQL--IHW-IHSRHATSVVALHQKELALTHFTRVI 200
Cdd:PRK13647 171 PRGQETLmeILDrLHNQGKTVIVATHDVDLAAEWADQVI 209
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-165 |
4.57e-10 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 58.27 E-value: 4.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 1 MTQATPsPLLHLSRHHLGHGAEVVLRDLDVQLEHGERVALLGASGAGKSTLLEAL-------RSALHEQGTPAAWCPQRQ 73
Cdd:COG4598 1 MTDTAP-PALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCInlletpdSGEIRVGGEEIRLKPDRD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 74 G-------------------------LVPQLSVYHNIFMGRLDQQSsltnllnllRPRPahwQAVA---AVCEPLGIAGL 125
Cdd:COG4598 80 GelvpadrrqlqrirtrlgmvfqsfnLWSHMTVLENVIEAPVHVLG---------RPKA---EAIEraeALLAKVGLADK 147
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1148626600 126 MERSVEALSGGQRQRVAIARALYQGHDLFLGDEPVASVDP 165
Cdd:COG4598 148 RDAYPAHLSGGQQQRAAIARALAMEPEVMLFDEPTSALDP 187
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
24-164 |
6.46e-10 |
|
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: 57.55 E-value: 6.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 24 VLRDLDVQLEHGERVALLGASGAGKST---LLEalRSALHEQGT-----------PAAWCPQRQGLVPQ------LSVYH 83
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTvvsLLE--RFYDPTSGEilldgvdirdlNLRWLRSQIGLVSQepvlfdGTIAE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 84 NIFMGRLDQQSSLTNLLnllrprpahwqAVAAVCEPLgIAGLM--------ERSVEaLSGGQRQRVAIARALYQGHDLFL 155
Cdd:cd03249 96 NIRYGKPDATDEEVEEA-----------AKKANIHDF-IMSLPdgydtlvgERGSQ-LSGGQKQRIAIARALLRNPKILL 162
|
....*....
gi 1148626600 156 GDEPVASVD 164
Cdd:cd03249 163 LDEATSALD 171
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
11-165 |
7.35e-10 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 58.17 E-value: 7.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 11 HLS-RHHLGHGAEVVLRDLDVQLEHGERVALLGASGAGKSTLLealR--------------------SALheqgTPAAWC 69
Cdd:COG1135 6 NLSkTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLI---RcinllerptsgsvlvdgvdlTAL----SERELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 70 PQRQ--GLVPQ----LS---VYHNI-----FMGRldqqssltnllnllrPRPAHWQAVAAVCEPLGIAGLMERSVEALSG 135
Cdd:COG1135 79 AARRkiGMIFQhfnlLSsrtVAENValpleIAGV---------------PKAEIRKRVAELLELVGLSDKADAYPSQLSG 143
|
170 180 190
....*....|....*....|....*....|
gi 1148626600 136 GQRQRVAIARALYQGHDLFLGDEPVASVDP 165
Cdd:COG1135 144 GQKQRVGIARALANNPKVLLCDEATSALDP 173
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
116-184 |
7.92e-10 |
|
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: 57.38 E-value: 7.92e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1148626600 116 VCEPLGIAGLMERSVEALSGGQRQRVAIARALYQGHDLFLGDEPVASVDPHQ---ASQLIHWIhSRHATSVV 184
Cdd:cd03236 123 LVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQrlnAARLIREL-AEDDNYVL 193
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
23-172 |
9.77e-10 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 58.11 E-value: 9.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 23 VVLRDLDVQLEHGERVALLGASGAGKSTL-------LEA------LRSALHEQGTPAAwcPQRQG---------LVPQLS 80
Cdd:COG3845 19 VANDDVSLTVRPGEIHALLGENGAGKSTLmkilyglYQPdsgeilIDGKPVRIRSPRD--AIALGigmvhqhfmLVPNLT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 81 VYHNIFMGRldqqsslTNLLNLLRPRPAHWQAVAAVCEPLGIAGLMERSVEALSGGQRQRVAIARALYQGHDLFLGDEPV 160
Cdd:COG3845 97 VAENIVLGL-------EPTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGARILILDEPT 169
|
170
....*....|..
gi 1148626600 161 ASVDPHQASQLI 172
Cdd:COG3845 170 AVLTPQEADELF 181
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
20-165 |
1.21e-09 |
|
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: 56.21 E-value: 1.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 20 GAEVVLRDLDVQLEHGERVALLGASGAGKSTLLEALRSALHE-------QGTPA-----------AWCPQRQGLVPQLSV 81
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPdsgevrwNGTPLaeqrdepheniLYLGHLPGLKPELSA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 82 YHNI-FMGRLDQQSsltnllnllrpRPAHWQAVAAVceplGIAGLMERSVEALSGGQRQRVAIARALYQGHDLFLGDEPV 160
Cdd:TIGR01189 91 LENLhFWAAIHGGA-----------QRTIEDALAAV----GLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPT 155
|
....*
gi 1148626600 161 ASVDP 165
Cdd:TIGR01189 156 TALDK 160
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-172 |
1.93e-09 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 56.23 E-value: 1.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 1 MTQATPSPLLHLSRHH---LGHGAEVVLRDLDVQLEHGERVALLGASGAGKSTL---------------------LEALR 56
Cdd:PRK10419 1 MTLLNVSGLSHHYAHGglsGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLarllvglespsqgnvswrgepLAKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 57 SALHE----------QGTPAAWCPQRQ-GLVPQLSVYHNIFMGRLDQQSSltnllnllrprpahwqaVAAVCEPLGIA-G 124
Cdd:PRK10419 81 RAQRKafrrdiqmvfQDSISAVNPRKTvREIIREPLRHLLSLDKAERLAR-----------------ASEMLRAVDLDdS 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1148626600 125 LMERSVEALSGGQRQRVAIARALYQGHDLFLGDEPVASVDPHQASQLI 172
Cdd:PRK10419 144 VLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVI 191
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
16-171 |
2.51e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 56.00 E-value: 2.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 16 HLGHGAEVVLRDLDVQLEHGERVALLGASGAGKSTLLEALRSAL-------------------HEQGTPAAWCPQRQGLV 76
Cdd:PRK14267 11 RVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLelneearvegevrlfgrniYSPDVDPIEVRREVGMV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 77 -------PQLSVYHNIFMG-----RLDQQSSLTNLLNLLRPRPAHWQAVAavceplgiaGLMERSVEALSGGQRQRVAIA 144
Cdd:PRK14267 91 fqypnpfPHLTIYDNVAIGvklngLVKSKKELDERVEWALKKAALWDEVK---------DRLNDYPSNLSGGQRQRLVIA 161
|
170 180
....*....|....*....|....*..
gi 1148626600 145 RALYQGHDLFLGDEPVASVDPHQASQL 171
Cdd:PRK14267 162 RALAMKPKILLMDEPTANIDPVGTAKI 188
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
12-90 |
2.73e-09 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 55.86 E-value: 2.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 12 LSRHHLGHGAEVVLRDLDVQLEHGERVALLGASGAGKSTLLEAL----------------RSALHEQGTpaawcpqrqGL 75
Cdd:COG1134 29 LRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIagileptsgrvevngrVSALLELGA---------GF 99
|
90
....*....|....*.
gi 1148626600 76 VPQLSVYHNIFM-GRL 90
Cdd:COG1134 100 HPELTGRENIYLnGRL 115
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
20-165 |
2.99e-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: 56.84 E-value: 2.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 20 GAEVVLRDLDVQLEHGERVALLGASGAGKSTLLEALRSALHEQG------------TPAAWcpqRQ--GLVPQ-LSVYHN 84
Cdd:TIGR01271 1230 AGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTEGeiqidgvswnsvTLQTW---RKafGVIPQkVFIFSG 1306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 85 IFMGRLDQQssltnllnllrprpAHW--QAVAAVCEPLGIAGLMERSVE-----------ALSGGQRQRVAIARALYQGH 151
Cdd:TIGR01271 1307 TFRKNLDPY--------------EQWsdEEIWKVAEEVGLKSVIEQFPDkldfvlvdggyVLSNGHKQLMCLARSILSKA 1372
|
170
....*....|....
gi 1148626600 152 DLFLGDEPVASVDP 165
Cdd:TIGR01271 1373 KILLLDEPSAHLDP 1386
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
21-196 |
4.11e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 55.51 E-value: 4.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 21 AEVVLRDLDVQLEHGERVALLGASGAGKSTLLEALRSALH-EQGTP-----AAWCPQRQGLVPQLSVYHNIFMGRLDQQS 94
Cdd:PRK13643 18 ASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQpTEGKVtvgdiVVSSTSKQKEIKPVRKKVGVVFQFPESQL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 95 SLTNLLNLLRPRPAHW-----QAVAAVCEPLGIAGL----MERSVEALSGGQRQRVAIARALYQGHDLFLGDEPVASVDP 165
Cdd:PRK13643 98 FEETVLKDVAFGPQNFgipkeKAEKIAAEKLEMVGLadefWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDP 177
|
170 180 190
....*....|....*....|....*....|.
gi 1148626600 166 HQASQLIHWIHSRHATSvvalhQKELALTHF 196
Cdd:PRK13643 178 KARIEMMQLFESIHQSG-----QTVVLVTHL 203
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
9-209 |
6.50e-09 |
|
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: 54.46 E-value: 6.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 9 LLHLSRHHLGHGAEVVLRDLDVQLEHGERVALLGASGAGKSTLLEALR----------------SALHEQGTpaawcpqr 72
Cdd:cd03220 22 KLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAgiyppdsgtvtvrgrvSSLLGLGG-------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 73 qGLVPQLSVYHNI-FMGRLdqqssltnLLNLLRPRPAHWQAVAAVCEpLGiaGLMERSVEALSGGQRQRVAIARALYQGH 151
Cdd:cd03220 94 -GFNPELTGRENIyLNGRL--------LGLSRKEIDEKIDEIIEFSE-LG--DFIDLPVKTYSSGMKARLAFAIATALEP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1148626600 152 DLFLGDEPVASVDPH---QASQLIHWIHSRHATSVVALHQKELALTHFTRVIGLgkdENGN 209
Cdd:cd03220 162 DILLIDEVLAVGDAAfqeKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVL---EKGK 219
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
7-164 |
6.72e-09 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 54.73 E-value: 6.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 7 SPLLHLSRHHLGHGAEVVLRDLDVQLEHGERVALLGASGAGKSTLLEAL--------RSALHEQGTPAAWCPQRQGLVPQ 78
Cdd:PRK09544 2 TSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVlglvapdeGVIKRNGKLRIGYVPQKLYLDTT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 79 LSVYHNIFMgrldqqssltnllnllRPRPAHWQA-VAAVCEPLGIAGLMERSVEALSGGQRQRVAIARALYQGHDLFLGD 157
Cdd:PRK09544 82 LPLTVNRFL----------------RLRPGTKKEdILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLD 145
|
....*..
gi 1148626600 158 EPVASVD 164
Cdd:PRK09544 146 EPTQGVD 152
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
19-209 |
7.08e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 54.79 E-value: 7.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 19 HGAEVVLRDLDVQLEHGERVALLGASGAGKSTLL----------EALR---------SALHEQGTPAAWCPQRQGLVPQL 79
Cdd:PRK14243 20 YGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILrcfnrlndliPGFRvegkvtfhgKNLYAPDVDPVEVRRRIGMVFQK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 80 ------SVYHNI--------FMGRLDQQSSLTNLlnllrpRPAHWQAVAavcEPLGIAGLmersveALSGGQRQRVAIAR 145
Cdd:PRK14243 100 pnpfpkSIYDNIaygaringYKGDMDELVERSLR------QAALWDEVK---DKLKQSGL------SLSGGQQQRLCIAR 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1148626600 146 ALYQGHDLFLGDEPVASVDP---HQASQLIHWIHSRHaTSVVALH--QKELALTHFTRVIGLGKDENGN 209
Cdd:PRK14243 165 AIAVQPEVILMDEPCSALDPistLRIEELMHELKEQY-TIIIVTHnmQQAARVSDMTAFFNVELTEGGG 232
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
20-164 |
7.09e-09 |
|
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: 55.52 E-value: 7.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 20 GAEVVLRDLDVQLEHGERVALLGASGAGKSTLLEALRSALheqgTPAA------------WCPQRQ----GLVPQ---L- 79
Cdd:COG4618 343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVW----PPTAgsvrldgadlsqWDREELgrhiGYLPQdveLf 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 80 --SVYHNIfmGRLDQqssltnllnllrPRPAhwQAVAA-----VCE-----------PLGIAGLMersveaLSGGQRQRV 141
Cdd:COG4618 419 dgTIAENI--ARFGD------------ADPE--KVVAAaklagVHEmilrlpdgydtRIGEGGAR------LSGGQRQRI 476
|
170 180
....*....|....*....|...
gi 1148626600 142 AIARALYQGHDLFLGDEPVASVD 164
Cdd:COG4618 477 GLARALYGDPRLVVLDEPNSNLD 499
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
20-187 |
7.28e-09 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 55.43 E-value: 7.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 20 GAEVVLRDLDVQLEHGERVALLGASGAGKSTLLEALRSA-LHEQGT----PAA---WCPQ----RQGLVPQL------SV 81
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIwPPTSGSvrldGADlkqWDREtfgkHIGYLPQDvelfpgTV 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 82 YHNIfmGRLDQQSSLTNLLNLLRPRPAHwQAVAAVcePLGIAGLMERSVEALSGGQRQRVAIARALYQGHDLFLGDEPVA 161
Cdd:TIGR01842 409 AENI--ARFGENADPEKIIEAAKLAGVH-ELILRL--PDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNS 483
|
170 180 190
....*....|....*....|....*....|
gi 1148626600 162 SVDP--HQA--SQLIHwIHSRHATSVVALH 187
Cdd:TIGR01842 484 NLDEegEQAlaNAIKA-LKARGITVVVITH 512
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
120-164 |
7.43e-09 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 55.27 E-value: 7.43e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1148626600 120 LGIAGLMERSVEALSGGQRQRVAIARALYQGHDLFLGDEPVASVD 164
Cdd:PRK11144 116 LGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLD 160
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
9-165 |
8.17e-09 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 54.81 E-value: 8.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 9 LLHLSRHHLGHGAEVV-LRDLDVQLEHGERVALLGASGAGKSTLLEALR-----------------SALHEQGTPAAwcp 70
Cdd:PRK11153 4 LKNISKVFPQGGRTIHaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINllerptsgrvlvdgqdlTALSEKELRKA--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 71 QRQ-GLVPQ----LS---VYHNIFMG-RLDqqssltnllnlLRPRPAHWQAVAAVCEPLGIAGLMERSVEALSGGQRQRV 141
Cdd:PRK11153 81 RRQiGMIFQhfnlLSsrtVFDNVALPlELA-----------GTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRV 149
|
170 180
....*....|....*....|....
gi 1148626600 142 AIARALYQGHDLFLGDEPVASVDP 165
Cdd:PRK11153 150 AIARALASNPKVLLCDEATSALDP 173
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
16-166 |
8.96e-09 |
|
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: 55.21 E-value: 8.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 16 HLGHGAE-VVLRDLDVQLEHGERVALLGASGAGKSTL--------------------------LEALRSALheqgtpaaw 68
Cdd:COG5265 364 SFGYDPErPILKGVSFEVPAGKTVAIVGPSGAGKSTLarllfrfydvtsgrilidgqdirdvtQASLRAAI--------- 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 69 cpqrqGLVPQ---L---SVYHNIFMGRLDqqssltnllnllrprpAHWQAVAAVCE-----------PLGIAGLM-ERSV 130
Cdd:COG5265 435 -----GIVPQdtvLfndTIAYNIAYGRPD----------------ASEEEVEAAARaaqihdfieslPDGYDTRVgERGL 493
|
170 180 190
....*....|....*....|....*....|....*.
gi 1148626600 131 EaLSGGQRQRVAIARALYQGHDLFLGDEPVASVDPH 166
Cdd:COG5265 494 K-LSGGEKQRVAIARTLLKNPPILIFDEATSALDSR 528
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
25-189 |
1.02e-08 |
|
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: 54.83 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 25 LRDLDVQLEHGERVALLGASGAGKSTLLEALrSALHEQGTPAA---WCPQ-----------RQG---------LVPQLSV 81
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKIL-SGVYPHGTWDGeiyWSGSplkasnirdteRAGiviihqeltLVPELSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 82 YHNIFMGRldqqssltnlLNLLRPRPAHWQAVAAVCEPLgiagLME---------RSVEALSGGQRQRVAIARALYQGHD 152
Cdd:TIGR02633 96 AENIFLGN----------EITLPGGRMAYNAMYLRAKNL----LRElqldadnvtRPVGDYGGGQQQLVEIAKALNKQAR 161
|
170 180 190
....*....|....*....|....*....|....*....
gi 1148626600 153 LFLGDEPVASVDPHQASQLIHWIH--SRHATSVVALHQK 189
Cdd:TIGR02633 162 LLILDEPSSSLTEKETEILLDIIRdlKAHGVACVYISHK 200
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
20-164 |
1.22e-08 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 54.71 E-value: 1.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 20 GAEVVLRDLDVQLEHGERVALLGASGAGKST----LLEALRS---------ALHeQGTPAAWCPQRQ-----------GL 75
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINSqgeiwfdgqPLH-NLNRRQLLPVRHriqvvfqdpnsSL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 76 VPQLSVYHNIFMGRLDQQSSLTNLLNLLRprpahwqaVAAVCEPLGI-AGLMERSVEALSGGQRQRVAIARALYQGHDLF 154
Cdd:PRK15134 376 NPRLNVLQIIEEGLRVHQPTLSAAQREQQ--------VIAVMEEVGLdPETRHRYPAEFSGGQRQRIAIARALILKPSLI 447
|
170
....*....|
gi 1148626600 155 LGDEPVASVD 164
Cdd:PRK15134 448 ILDEPTSSLD 457
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
11-192 |
1.76e-08 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 53.24 E-value: 1.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 11 HLSRHhLGHGAEV--VLRDLDVQLEHGERVALLGASGAGKSTLLEALR-----------------SALHEQGTPA----- 66
Cdd:PRK10584 11 HLKKS-VGQGEHElsILTGVELVVKRGETIALIGESGSGKSTLLAILAglddgssgevslvgqplHQMDEEARAKlrakh 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 67 -AWCPQRQGLVPQLSVYHNIFMGRLdqqssltnlLNLLRPRPAHWQAVAaVCEPLGIAGLMERSVEALSGGQRQRVAIAR 145
Cdd:PRK10584 90 vGFVFQSFMLIPTLNALENVELPAL---------LRGESSRQSRNGAKA-LLEQLGLGKRLDHLPAQLSGGEQQRVALAR 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1148626600 146 ALYQGHDLFLGDEPVASVDPHQASQLIHWIHS---RHATSVVAL-HQKELA 192
Cdd:PRK10584 160 AFNGRPDVLFADEPTGNLDRQTGDKIADLLFSlnrEHGTTLILVtHDLQLA 210
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-200 |
1.89e-08 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 54.06 E-value: 1.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 2 TQATPSPLLHLSRHHLG--HGAEVVLRDLDVQLEHGERVALLGASGAGKSTLLEALRSALHEQ-------GTP-AAWCPQ 71
Cdd:PRK11160 331 TAAADQVSLTLNNVSFTypDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQqgeillnGQPiADYSEA 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 72 --RQG--LVPQlSVYhnIFMGRLDQQSSLTNLLnllrprpAHWQAVAAVCEPLGIAGLME-------------RsveALS 134
Cdd:PRK11160 411 alRQAisVVSQ-RVH--LFSATLRDNLLLAAPN-------ASDEALIEVLQQVGLEKLLEddkglnawlgeggR---QLS 477
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1148626600 135 GGQRQRVAIARALYQGHDLFLGDEPVASVDPHQASQLIHWI--HSRHATSVVALHqKELALTHFTRVI 200
Cdd:PRK11160 478 GGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLaeHAQNKTVLMITH-RLTGLEQFDRIC 544
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
25-172 |
1.94e-08 |
|
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: 52.33 E-value: 1.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 25 LRDLDVQLEHGERVALLGASGAGKSTLLealrsalhEQGTPAAWCPQRQGLVPQLSVYHNIFMGRLdqqssltnllnllr 104
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLV--------NEGLYASGKARLISFLPKFSRNKLIFIDQL-------------- 68
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1148626600 105 prpahwQAVAAVceplGIAGL-MERSVEALSGGQRQRVAIARALYQG--HDLFLGDEPVASVDPHQASQLI 172
Cdd:cd03238 69 ------QFLIDV----GLGYLtLGQKLSTLSGGELQRVKLASELFSEppGTLFILDEPSTGLHQQDINQLL 129
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
20-164 |
2.00e-08 |
|
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: 52.88 E-value: 2.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 20 GAEVVLRDLDVQLEHGERVALLGASGAGKSTLLEAL--------------RSALHEQGTPAA----WCPQRQGLVPQLSV 81
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILaglspplagrvllnGGPLDFQRDSIArgllYLGHAPGIKTTLSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 82 YHNIFMGRLDQQssltnllnllrpRPAHWQAVAAVceplGIAGLMERSVEALSGGQRQRVAIARALYQGHDLFLGDEPVA 161
Cdd:cd03231 91 LENLRFWHADHS------------DEQVEEALARV----GLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTT 154
|
...
gi 1148626600 162 SVD 164
Cdd:cd03231 155 ALD 157
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
2-183 |
2.20e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 53.90 E-value: 2.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 2 TQATPSPLLHLSRHHLGHGAEVVLRDLDVQLEHGERVALLGASGAGKSTLLEAL-------RSALHEQGTPAA------- 67
Cdd:PRK15439 4 SDTTAPPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIagivppdSGTLEIGGNPCArltpaka 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 68 ------WCPQRQGLVPQLSVYHNIFMGrldqqssltnllnllRPRPAHWQA-VAAVCEPLGIAGLMERSVEALSGGQRQR 140
Cdd:PRK15439 84 hqlgiyLVPQEPLLFPNLSVKENILFG---------------LPKRQASMQkMKQLLAALGCQLDLDSSAGSLEVADRQI 148
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1148626600 141 VAIARALYQGHDLFLGDEPVASVDPHQASQLIHWIHSRHATSV 183
Cdd:PRK15439 149 VEILRGLMRDSRILILDEPTASLTPAETERLFSRIRELLAQGV 191
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
15-165 |
2.34e-08 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 53.98 E-value: 2.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 15 HHLGH--GAEVVLRDLDVQLEHGERVALLGASGAGKSTLL--------------EAL----RSALH-EQGTPA-AWCPQR 72
Cdd:NF033858 5 EGVSHryGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLsliagarkiqqgrvEVLggdmADARHrRAVCPRiAYMPQG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 73 QG--LVPQLSVYHNI-FMGRLDQQssltnllnllrPRPAHWQAVAAVCEPLGIAGLMERSVEALSGGQRQRVAIARALYQ 149
Cdd:NF033858 85 LGknLYPTLSVFENLdFFGRLFGQ-----------DAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIH 153
|
170
....*....|....*.
gi 1148626600 150 GHDLFLGDEPVASVDP 165
Cdd:NF033858 154 DPDLLILDEPTTGVDP 169
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
19-196 |
2.48e-08 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 53.68 E-value: 2.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 19 HGAEVVLRDLDVQLEHGERVALLGASGAGKSTLLEAL-------RSALHEQGTP----AAWCPQRQGLVPQLSvyhnifm 87
Cdd:PRK13536 51 YGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMIlgmtspdAGKITVLGVPvparARLARARIGVVPQFD------- 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 88 gRLDQQ-SSLTNLLNLLRPRPAHWQAVAAVCEPLGIAGLMERSVEA----LSGGQRQRVAIARALYQGHDLFLGDEPVAS 162
Cdd:PRK13536 124 -NLDLEfTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADArvsdLSGGMKRRLTLARALINDPQLLILDEPTTG 202
|
170 180 190
....*....|....*....|....*....|....
gi 1148626600 163 VDPHqASQLIhWIHSRhatSVVALHQKELALTHF 196
Cdd:PRK13536 203 LDPH-ARHLI-WERLR---SLLARGKTILLTTHF 231
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
17-171 |
2.83e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 52.99 E-value: 2.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 17 LGHGAEVVLRDLDVQLEHGERVALLGASGAGKSTLLEAL------------RSALHEQG-----TPAAWCPQRQGLV--- 76
Cdd:PRK14247 11 VSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFnrlielypearvSGEVYLDGqdifkMDVIELRRRVQMVfqi 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 77 ----PQLSVYHNIFMGRLDQQSSLTNLLNLLRPRPAH-----WQAVA-AVCEPLGiaglmersveALSGGQRQRVAIARA 146
Cdd:PRK14247 91 pnpiPNLSIFENVALGLKLNRLVKSKKELQERVRWALekaqlWDEVKdRLDAPAG----------KLSGGQQQRLCIARA 160
|
170 180
....*....|....*....|....*
gi 1148626600 147 LYQGHDLFLGDEPVASVDPHQASQL 171
Cdd:PRK14247 161 LAFQPEVLLADEPTANLDPENTAKI 185
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
25-205 |
2.98e-08 |
|
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: 52.33 E-value: 2.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 25 LRDLDVQLEHGERVALLGASGAGKSTLLEA-------LRSALHEQGT----------------PAAWCPQRQGLVpQLSV 81
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAilgemqtLEGKVHWSNKnesepsfeatrsrnrySVAYAAQKPWLL-NATV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 82 YHNIFMGR-LDQQssltnllnllrprpaHWQAVAAVCE--------PLG-IAGLMERSVEaLSGGQRQRVAIARALYQGH 151
Cdd:cd03290 96 EENITFGSpFNKQ---------------RYKAVTDACSlqpdidllPFGdQTEIGERGIN-LSGGQRQRICVARALYQNT 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1148626600 152 DLFLGDEPVASVDPHQASQLIH-----WIHSRHATSVVALHQKELaLTHFTRVIGLgKD 205
Cdd:cd03290 160 NIVFLDDPFSALDIHLSDHLMQegilkFLQDDKRTLVLVTHKLQY-LPHADWIIAM-KD 216
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
10-204 |
3.10e-08 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 52.66 E-value: 3.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 10 LHLSRHHLGHGAEVVLRDLDVQLEHGERVALLGASGAGKSTLLEAL-------RSALHEQGTPAAWCPQRQGlvpQLSVY 82
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCInflekpsEGSIVVNGQTINLVRDKDG---QLKVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 83 HNIFMGRLDQQSSLTNLLNLLRprpAHWQAVAAVCE-PLGIAGLM-----ERSVE-----------------ALSGGQRQ 139
Cdd:PRK10619 83 DKNQLRLLRTRLTMVFQHFNLW---SHMTVLENVMEaPIQVLGLSkqearERAVKylakvgideraqgkypvHLSGGQQQ 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1148626600 140 RVAIARALYQGHDLFLGDEPVASVDPH---QASQLIHWIHSRHATSVVALHQKELALTHFTRVIGLGK 204
Cdd:PRK10619 160 RVSIARALAMEPEVLLFDEPTSALDPElvgEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQ 227
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
25-165 |
3.25e-08 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 52.71 E-value: 3.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 25 LRDLDVQLEHGERVALLGASGAGKSTLLEALRSALH-EQGT----------PAAWCPQRQ-GLVPQLSvyHNIFMGRLDQ 92
Cdd:PRK13635 23 LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLpEAGTitvggmvlseETVWDVRRQvGMVFQNP--DNQFVGATVQ 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1148626600 93 QSSLTNLLNLLRPRPAHWQAVAAVCEPLGIAGLMERSVEALSGGQRQRVAIARALYQGHDLFLGDEPVASVDP 165
Cdd:PRK13635 101 DDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDP 173
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
126-220 |
3.32e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 53.17 E-value: 3.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 126 MERSVEALSGGQRQRVAIARALYQGHDLFLGDEPVASVDPHQASQ---LIHWIHSRHATSVVALHQKELALTHFTRVIGL 202
Cdd:PRK13651 159 LQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEileIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFF 238
|
90
....*....|....*...
gi 1148626600 203 gkdenGNGKVLLDANTDD 220
Cdd:PRK13651 239 -----KDGKIIKDGDTYD 251
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
24-166 |
3.59e-08 |
|
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: 52.03 E-value: 3.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 24 VLRDLDVQLEHGERVALLGASGAGKSTLLEALRSALH-EQGT-----------PAAWCPQRQGLVPQLSVyhnIFMG--- 88
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEaEEGKieidgidistiPLEDLRSSLTIIPQDPT---LFSGtir 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1148626600 89 -RLDqqssltnllnllrprPAHWQAVAAVCEPLGIAGlmerSVEALSGGQRQRVAIARALYQGHDLFLGDEPVASVDPH 166
Cdd:cd03369 100 sNLD---------------PFDEYSDEEIYGALRVSE----GGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYA 159
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
24-187 |
3.88e-08 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 53.41 E-value: 3.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 24 VLRDLDVQLEHGERVALLGASGAGKSTLLEaLRSALHEQ--------GTPAAWCPQRQ-----GLVPQ------LSVYHN 84
Cdd:TIGR03796 494 LIENFSLTLQPGQRVALVGGSGSGKSTIAK-LVAGLYQPwsgeilfdGIPREEIPREVlansvAMVDQdiflfeGTVRDN 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 85 IFMgrLDQQSSLTNLLNLLRPRPAHwQAVAAVcePLGIAGLMERSVEALSGGQRQRVAIARALYQGHDLFLGDEPVASVD 164
Cdd:TIGR03796 573 LTL--WDPTIPDADLVRACKDAAIH-DVITSR--PGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALD 647
|
170 180
....*....|....*....|...
gi 1148626600 165 PHQASQLIHWIHSRHATSVVALH 187
Cdd:TIGR03796 648 PETEKIIDDNLRRRGCTCIIVAH 670
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
25-164 |
4.21e-08 |
|
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: 53.15 E-value: 4.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 25 LRDLDVQLEHGERVALLGASGAGKSTLLEALRSALHEQGT------------PAAWCPQRQG-----------LVPQLSV 81
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPSEGEirfdgqdldglsRRALRPLRRRmqvvfqdpfgsLSPRMTV 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 82 Y---------HNIFMGRLDQQssltnllnllrprpahwQAVAAVCEPLGI-AGLMERSVEALSGGQRQRVAIARALYQGH 151
Cdd:COG4172 382 GqiiaeglrvHGPGLSAAERR-----------------ARVAEALEEVGLdPAARHRYPHEFSGGQRQRIAIARALILEP 444
|
170
....*....|...
gi 1148626600 152 DLFLGDEPVASVD 164
Cdd:COG4172 445 KLLVLDEPTSALD 457
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-165 |
6.56e-08 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 51.96 E-value: 6.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 1 MTQATPSPLLHLSRHHLG--HGAEVVLRDLDVQLEHGERVALLGASGAGKSTLLEAL-RsaLHE---------------- 61
Cdd:COG1117 1 MTAPASTLEPKIEVRNLNvyYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLnR--MNDlipgarvegeilldge 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 62 ----QGTPAAWCPQRQGLVPQ------LSVYHNIFMG----------RLDQqssltnllnllrprpahwqavaAVCEPLG 121
Cdd:COG1117 79 diydPDVDVVELRRRVGMVFQkpnpfpKSIYDNVAYGlrlhgiksksELDE----------------------IVEESLR 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1148626600 122 IAGLME-------RSVEALSGGQRQRVAIARALYQGHDLFLGDEPVASVDP 165
Cdd:COG1117 137 KAALWDevkdrlkKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDP 187
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
4-164 |
9.04e-08 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 51.66 E-value: 9.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 4 ATPSPLL---HLSRHH------LGHGAEVV--LRDLDVQLEHGERVALLGASGAGKST-------LLEALRSALHEQGT- 64
Cdd:COG4608 2 AMAEPLLevrDLKKHFpvrgglFGRTVGVVkaVDGVSFDIRRGETLGLVGESGCGKSTlgrlllrLEEPTSGEILFDGQd 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 65 -----PAAWCPQRQGLvpQLsvyhnIF---MGRLDqqssltnllnllrPRpahwQAVAA-VCEPLGIAGLM------ERS 129
Cdd:COG4608 82 itglsGRELRPLRRRM--QM-----VFqdpYASLN-------------PR----MTVGDiIAEPLRIHGLAskaerrERV 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1148626600 130 VEAL-----------------SGGQRQRVAIARALYQGHDLFLGDEPVASVD 164
Cdd:COG4608 138 AELLelvglrpehadryphefSGGQRQRIGIARALALNPKLIVCDEPVSALD 189
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
24-216 |
1.10e-07 |
|
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: 50.68 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 24 VLRDLDVQLEHGERVALLGASGAGKSTLLEALRSALH-EQGTPAAW---------CPQR-------QGLVPQLSVYHNIF 86
Cdd:cd03268 15 VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKpDSGEITFDgksyqknieALRRigalieaPGFYPNLTARENLR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 87 MGRLdqqssltnllNLLRPRpahwQAVAAVCEPLGIAGLMERSVEALSGGQRQRVAIARALYQGHDLFLGDEPVASVDP- 165
Cdd:cd03268 95 LLAR----------LLGIRK----KRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPd 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1148626600 166 --HQASQLIHWIHSRHATSVVALHQ-KELALTHfTRVIGLGKdengnGKVLLDA 216
Cdd:cd03268 161 giKELRELILSLRDQGITVLISSHLlSEIQKVA-DRIGIINK-----GKLIEEG 208
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
23-173 |
1.32e-07 |
|
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: 51.73 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 23 VVLRDLDVQLEHGERVALLGASGAGKSTLLEALRSAlhEQGTP--------AAWCPQRQGLVPQLSVYHN--IFMGRLDQ 92
Cdd:TIGR03269 14 EVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGM--DQYEPtsgriiyhVALCEKCGYVERPSKVGEPcpVCGGTLEP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 93 QS-----SLTNLLNLLRPRPA-HWQAVAA----------VCEPLGIAGL-----MERSVEA----------------LSG 135
Cdd:TIGR03269 92 EEvdfwnLSDKLRRRIRKRIAiMLQRTFAlygddtvldnVLEALEEIGYegkeaVGRAVDLiemvqlshrithiardLSG 171
|
170 180 190
....*....|....*....|....*....|....*...
gi 1148626600 136 GQRQRVAIARALYQGHDLFLGDEPVASVDPhQASQLIH 173
Cdd:TIGR03269 172 GEKQRVVLARQLAKEPFLFLADEPTGTLDP-QTAKLVH 208
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
23-164 |
1.43e-07 |
|
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: 51.50 E-value: 1.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 23 VVLRDLDVQLEHGERVALLGASGAGKSTLLEALR-----------------SALHEQGTpaawcpQRQ-GLVPQ------ 78
Cdd:TIGR03797 467 LILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLgfetpesgsvfydgqdlAGLDVQAV------RRQlGVVLQngrlms 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 79 LSVYHNIFMG---RLDQQssltnllnllrprpahWQAV--AAVCE-----PLGIAGLMERSVEALSGGQRQRVAIARALY 148
Cdd:TIGR03797 541 GSIFENIAGGaplTLDEA----------------WEAArmAGLAEdiramPMGMHTVISEGGGTLSGGQRQRLLIARALV 604
|
170
....*....|....*.
gi 1148626600 149 QGHDLFLGDEPVASVD 164
Cdd:TIGR03797 605 RKPRILLFDEATSALD 620
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
23-241 |
1.62e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 50.85 E-value: 1.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 23 VVLRDLDVQLEHGERVALLGASGAGKSTLLEALRSALH-EQGT-----------PAAwcpQRQGLV------------PQ 78
Cdd:COG1101 20 RALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPpDSGSilidgkdvtklPEY---KRAKYIgrvfqdpmmgtaPS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 79 LSVYHNIFM--GRldqqssltnllnlLRPRPAHW-------QAVAAVCEPLGIaGL---MERSVEALSGGQRQRVAIARA 146
Cdd:COG1101 97 MTIEENLALayRR-------------GKRRGLRRgltkkrrELFRELLATLGL-GLenrLDTKVGLLSGGQRQALSLLMA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 147 LYQGHDLFLGDEPVASVDPHQASQLIH----WIHSRHATSVVALHQKELALTHFTRVIGLGKdengnGKVLLDANTDD-- 220
Cdd:COG1101 163 TLTKPKLLLLDEHTAALDPKTAALVLEltekIVEENNLTTLMVTHNMEQALDYGNRLIMMHE-----GRIILDVSGEEkk 237
|
250 260
....*....|....*....|..
gi 1148626600 221 -LKPQDLDCLYPAASSEPLDVD 241
Cdd:COG1101 238 kLTVEDLLELFEEIRGEELADD 259
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
5-159 |
1.65e-07 |
|
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: 51.22 E-value: 1.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 5 TPSPLL---HLS-RHHLGHGAEVVLRDLDVQLEHGERVALLGASGAGKS-TLLEALR----SALHEQG------------ 63
Cdd:COG4172 2 MSMPLLsveDLSvAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILRllpdPAAHPSGsilfdgqdllgl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 64 TPAAWCP---QRQGLVPQ-----LSVYHNIfmGRldqQSSLTNLLNLLRPRPAHWQAVAAVCEPLGIAGLmERSVEA--- 132
Cdd:COG4172 82 SERELRRirgNRIAMIFQepmtsLNPLHTI--GK---QIAEVLRLHRGLSGAAARARALELLERVGIPDP-ERRLDAyph 155
|
170 180
....*....|....*....|....*...
gi 1148626600 133 -LSGGQRQRVAIARALYQGHDLFLGDEP 159
Cdd:COG4172 156 qLSGGQRQRVMIAMALANEPDLLIADEP 183
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
8-204 |
1.86e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 50.23 E-value: 1.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 8 PLLHLSRHHLGHGAEVVLRDLDVQLEHGERVALLGASGAGKSTLLEALRSALHEQ-------GTPA---------AWCPQ 71
Cdd:PRK13543 10 PLLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVEsgqiqidGKTAtrgdrsrfmAYLGH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 72 RQGLVPQLSVYHNI-FMGRLDQQssltnllnllRPRPAHWQAVAAVceplGIAGLMERSVEALSGGQRQRVAIARALYQG 150
Cdd:PRK13543 90 LPGLKADLSTLENLhFLCGLHGR----------RAKQMPGSALAIV----GLAGYEDTLVRQLSAGQKKRLALARLWLSP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1148626600 151 HDLFLGDEPVASVDPHQASQLIHWI----HSRHATsVVALHQKELALTHFTRVIGLGK 204
Cdd:PRK13543 156 APLWLLDEPYANLDLEGITLVNRMIsahlRGGGAA-LVTTHGAYAAPPVRTRMLTLEA 212
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
24-175 |
1.96e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 50.57 E-value: 1.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 24 VLRDLDVQLEHGERVALLGASGAGKST---LLEAL-------RSALHEQGT----PAAW-CPQRQGLVPQLSvyHNIFMG 88
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLllpddnpNSKITVDGItltaKTVWdIREKVGIVFQNP--DNQFVG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 89 RLDQQSSLTNLLNLLRPRPAHWQAVAAVCEPLGIAGLMERSVEALSGGQRQRVAIARALYQGHDLFLGDEPVASVDPHQA 168
Cdd:PRK13640 100 ATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGK 179
|
....*..
gi 1148626600 169 SQLIHWI 175
Cdd:PRK13640 180 EQILKLI 186
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
9-159 |
2.02e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 51.10 E-value: 2.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 9 LLHLSRHHLGHGAEVVLRDLDVQLEHGERVALLGASGAGKSTLLEALR------------------SAL------HEQGT 64
Cdd:PRK11147 3 LISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNgevllddgriiyeqdlivARLqqdpprNVEGT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 65 PAAWCPQR-QGLVPQLSVYHNIF--------------MGRLDQQSSLTNLlnllrprpahWQ---AVAAVCEPLGIAGlm 126
Cdd:PRK11147 83 VYDFVAEGiEEQAEYLKRYHDIShlvetdpseknlneLAKLQEQLDHHNL----------WQlenRINEVLAQLGLDP-- 150
|
170 180 190
....*....|....*....|....*....|...
gi 1148626600 127 ERSVEALSGGQRQRVAIARALYQGHDLFLGDEP 159
Cdd:PRK11147 151 DAALSSLSGGWLRKAALGRALVSNPDVLLLDEP 183
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
20-227 |
2.35e-07 |
|
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: 50.12 E-value: 2.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 20 GAEVVLRDLDVQLEHGERVALLGASGAGKSTL---LEALrsALHEQGT----------PAAWCPQRQ--GLV---P--QL 79
Cdd:TIGR04520 13 SEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLaklLNGL--LLPTSGKvtvdgldtldEENLWEIRKkvGMVfqnPdnQF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 80 ---SVYHNIFMGRLDQQSsltnllnllrPRPAHWQAVAAVCEPLGIAGLMERSVEALSGGQRQRVAIARALYQGHDLFLG 156
Cdd:TIGR04520 91 vgaTVEDDVAFGLENLGV----------PREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDIIIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 157 DEPVASVDP---HQASQLIHWIHSRHATSVValhqkelALTHFT-------RVIGLGKdengnGKVLLD-------ANTD 219
Cdd:TIGR04520 161 DEATSMLDPkgrKEVLETIRKLNKEEGITVI-------SITHDMeeavladRVIVMNK-----GKIVAEgtpreifSQVE 228
|
....*...
gi 1148626600 220 DLKPQDLD 227
Cdd:TIGR04520 229 LLKEIGLD 236
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
20-165 |
2.69e-07 |
|
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: 50.24 E-value: 2.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 20 GAEVVLRDLDVQLEHGERVALLGASGAGKSTLLEALRSALHEQGT----PAAW--CPQRQ-----GLVPQlSVYhnIFMG 88
Cdd:cd03289 15 GGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGDiqidGVSWnsVPLQKwrkafGVIPQ-KVF--IFSG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 89 RLDQQSSltnllnllrPRPAHW-QAVAAVCEPLGIAGLMERSVE-----------ALSGGQRQRVAIARALYQGHDLFLG 156
Cdd:cd03289 92 TFRKNLD---------PYGKWSdEEIWKVAEEVGLKSVIEQFPGqldfvlvdggcVLSHGHKQLMCLARSVLSKAKILLL 162
|
....*....
gi 1148626600 157 DEPVASVDP 165
Cdd:cd03289 163 DEPSAHLDP 171
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
20-206 |
2.86e-07 |
|
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: 51.10 E-value: 2.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 20 GAEVVLRDLDVQLEHGERVALLGASGAGKSTL-------LEALRSALHEQGTPAAwcpqRQGL---------VPQLSVyh 83
Cdd:TIGR00957 1297 DLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLtlglfriNESAEGEIIIDGLNIA----KIGLhdlrfkitiIPQDPV-- 1370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 84 nIFMG----RLDQQSSLTNLLNLLRPRPAHWQAVAAvCEPLGIAGLMERSVEALSGGQRQRVAIARALYQGHDLFLGDEP 159
Cdd:TIGR00957 1371 -LFSGslrmNLDPFSQYSDEEVWWALELAHLKTFVS-ALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEA 1448
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1148626600 160 VASVDPHQASQLIHWIHSRHAT-SVVALHQKELALTHFTRVIGLGKDE 206
Cdd:TIGR00957 1449 TAAVDLETDNLIQSTIRTQFEDcTVLTIAHRLNTIMDYTRVIVLDKGE 1496
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
24-181 |
3.03e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 49.99 E-value: 3.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 24 VLRDLDVQLEHGERVALLGASGAGKSTLLEALRSALHEQ-------GTPAAWCPQRQ-----GLVPQ--------LSVYH 83
Cdd:PRK13632 24 ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQsgeikidGITISKENLKEirkkiGIIFQnpdnqfigATVED 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 84 NIFMGRLDQQSsltnllnllrPRPAHWQAVAAVCEPLGIAGLMERSVEALSGGQRQRVAIARALYQGHDLFLGDEPVASV 163
Cdd:PRK13632 104 DIAFGLENKKV----------PPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSML 173
|
170
....*....|....*...
gi 1148626600 164 DPHQASQLIHWIHSRHAT 181
Cdd:PRK13632 174 DPKGKREIKKIMVDLRKT 191
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
35-188 |
3.24e-07 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 50.65 E-value: 3.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 35 GERVALLGASGAGKSTLLEALRSALH----------EQGTPAAWCPQRQGLVPQlsvyHNIFMGRLDQQSSLTNLLNLLR 104
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQgnnftgtilaNNRKPTKQILKRTGFVTQ----DDILYPHLTVRETLVFCSLLRL 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 105 PRPAHWQ----AVAAVCEPLGIAG-----LMERSVEALSGGQRQRVAIARALYQGHDLFLGDEPVASVDPHQASQLIHWI 175
Cdd:PLN03211 170 PKSLTKQekilVAESVISELGLTKcentiIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTL 249
|
170
....*....|....*.
gi 1148626600 176 HS---RHATSVVALHQ 188
Cdd:PLN03211 250 GSlaqKGKTIVTSMHQ 265
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
126-206 |
3.98e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 49.85 E-value: 3.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 126 MERSVEALSGGQRQRVAIARALYQGHDLFLGDEPVASVDP---HQASQLIHWIHSRHATSVVALHQKELALTHFTRVIGL 202
Cdd:PRK13631 170 LERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPkgeHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVM 249
|
....
gi 1148626600 203 GKDE 206
Cdd:PRK13631 250 DKGK 253
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
24-188 |
4.46e-07 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 50.11 E-value: 4.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 24 VLRDLDVQLEHGERVALLGASGAGKST---LLEALRSALHEQ----GTPAA-----WCPQRQGLV---PQL---SVYHNI 85
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTvaaLLQNLYQPTGGQvlldGVPLVqydhhYLHRQVALVgqePVLfsgSVRENI 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 86 FMGrLDQQSSLTNLLNllrprpahwqAVAAVCE------PLGIAGLMERSVEALSGGQRQRVAIARALYQGHDLFLGDEP 159
Cdd:TIGR00958 576 AYG-LTDTPDEEIMAA----------AKAANAHdfimefPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEA 644
|
170 180
....*....|....*....|....*....
gi 1148626600 160 VASVDPHQASQLIHWIHSRHATSVVALHQ 188
Cdd:TIGR00958 645 TSALDAECEQLLQESRSRASRTVLLIAHR 673
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
8-182 |
4.78e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 49.26 E-value: 4.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 8 PLLHLSRHHLGHGAEVVLRDLDVQLEHGERVALLGASGAGKSTLLEALRSALHEQGTPAAwcpqrQGLVPQL--SVYHN- 84
Cdd:PRK14258 6 PAIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRV-----EGRVEFFnqNIYERr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 85 IFMGRLDQQSSLTNllnllrPRP-----AHWQAVAAVCEPLG------IAGLMERSVEA-----------------LSGG 136
Cdd:PRK14258 81 VNLNRLRRQVSMVH------PKPnlfpmSVYDNVAYGVKIVGwrpkleIDDIVESALKDadlwdeikhkihksaldLSGG 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1148626600 137 QRQRVAIARALYQGHDLFLGDEPVASVDPHQASQLIHWIHSRHATS 182
Cdd:PRK14258 155 QQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRS 200
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
116-159 |
6.50e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 49.42 E-value: 6.50e-07
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1148626600 116 VCEPLGIAGLMERSVEALSGGQRQRVAIARALYQGHDLFLGDEP 159
Cdd:PRK13409 196 VVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEP 239
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
25-190 |
6.51e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 49.25 E-value: 6.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 25 LRDLDVQLEHGERVALLGASGAGKSTLLEALRSALH-EQGT-------------PAAWCPQRQ--GLVPQL--------S 80
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQpTSGTvtigervitagkkNKKLKPLRKkvGIVFQFpehqlfeeT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 81 VYHNIFMGrldqqssltnllnllrprPAHW-----QAVAAVCEPLGIAGL----MERSVEALSGGQRQRVAIARALYQGH 151
Cdd:PRK13634 103 VEKDICFG------------------PMNFgvseeDAKQKAREMIELVGLpeelLARSPFELSGGQMRRVAIAGVLAMEP 164
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1148626600 152 DLFLGDEPVASVDP---HQASQLIHWIHSRHA-TSVVALHQKE 190
Cdd:PRK13634 165 EVLVLDEPTAGLDPkgrKEMMEMFYKLHKEKGlTTVLVTHSME 207
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
11-164 |
6.65e-07 |
|
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: 49.28 E-value: 6.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 11 HLSRH-HLGHGAEVVLRDLDVQLEHGERVALLGASGAGKSTLLealRSALheqgtpaawcpqrqGLVPQLSV------YH 83
Cdd:COG0444 6 NLKVYfPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLA---RAIL--------------GLLPPPGItsgeilFD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 84 NIFMGRLDQQssltnllnllRPRPAHWQAVAAV------------------CEPLGIAGLM------ERSVEAL------ 133
Cdd:COG0444 69 GEDLLKLSEK----------ELRKIRGREIQMIfqdpmtslnpvmtvgdqiAEPLRIHGGLskaearERAIELLervglp 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1148626600 134 -------------SGGQRQRVAIARALYQGHDLFLGDEPVASVD 164
Cdd:COG0444 139 dperrldryphelSGGMRQRVMIARALALEPKLLIADEPTTALD 182
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
17-64 |
7.73e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 49.51 E-value: 7.73e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1148626600 17 LGHG--AEVVLRDLDVQLEHGERVALLGASGAGKSTLLEALRSAL-HEQGT 64
Cdd:PRK15064 325 LTKGfdNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELePDSGT 375
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
25-227 |
1.13e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 48.19 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 25 LRDLDVQLEHGERVALLGASGAGKST-------LLEALRSALHEQG---TPA-AWCPQRQ-GLVPQLSvyHNIFMGR--- 89
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTtvrlidgLLEAESGQIIIDGdllTEEnVWDIRHKiGMVFQNP--DNQFVGAtve 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 90 ------LDQQSSltnllnllrprpAHWQAVAAVCEPLGIAGLM---ERSVEALSGGQRQRVAIARALYQGHDLFLGDEPV 160
Cdd:PRK13650 101 ddvafgLENKGI------------PHEEMKERVNEALELVGMQdfkEREPARLSGGQKQRVAIAGAVAMRPKIIILDEAT 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1148626600 161 ASVDPHQASQLIHWIHS---RHATSVVAL-HQ-KELALTHFTRVIGLGKDENGNGKVLLDANTDDLKPQDLD 227
Cdd:PRK13650 169 SMLDPEGRLELIKTIKGirdDYQMTVISItHDlDEVALSDRVLVMKNGQVESTSTPRELFSRGNDLLQLGLD 240
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
35-171 |
1.23e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 48.75 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 35 GERVALLGASGAGKSTLLEALRSA-------LHEQGTPAAWCPQRQG-------------LVPQLSVYHNIFMGRLDQQS 94
Cdd:PRK11288 30 GQVHALMGENGAGKSTLLKILSGNyqpdagsILIDGQEMRFASTTAAlaagvaiiyqelhLVPEMTVAENLYLGQLPHKG 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1148626600 95 SLTNLLNLLRprpahwqAVAAVCEPLGIAGLMERSVEALSGGQRQRVAIARALYQGHDLFLGDEPVASVDPHQASQL 171
Cdd:PRK11288 110 GIVNRRLLNY-------EAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQL 179
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
25-232 |
1.49e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 48.06 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 25 LRDLDVQLEHGERVALLGASGAGKSTLLEALRSALHEQ-------GTPAAWCPQRQGLVPQLS-VYHNI---FMGRLDQQ 93
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQkgkvlvsGIDTGDFSKLQGIRKLVGiVFQNPetqFVGRTVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 94 SSLTNLLNLLRPRPAHWQAVAAVCEPLGIAGLMERSVEALSGGQRQRVAIARALYQGHDLFLGDEPVASVDPHQASQLIH 173
Cdd:PRK13644 98 DLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLE 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1148626600 174 WI---HSRHATSVVALHQKElALTHFTRVIGLGKdengnGKVLLDANTD----DLKPQDLDCLYPA 232
Cdd:PRK13644 178 RIkklHEKGKTIVYITHNLE-ELHDADRIIVMDR-----GKIVLEGEPEnvlsDVSLQTLGLTPPS 237
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
22-175 |
1.87e-06 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 47.69 E-value: 1.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 22 EVVLRDLDVQLEHGERVALLGASGAGKSTLLEALRSALHEQGTPAAWCPQ-----RQGLVP---QL-SVYHN----IFMG 88
Cdd:PRK13638 14 EPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKpldysKRGLLAlrqQVaTVFQDpeqqIFYT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 89 RLDQQSSLTNLLNLLrprpAHWQAVAAVCEPLGIA---GLMERSVEALSGGQRQRVAIARALYQGHDLFLGDEPVASVDP 165
Cdd:PRK13638 94 DIDSDIAFSLRNLGV----PEAEITRRVDEALTLVdaqHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDP 169
|
170
....*....|
gi 1148626600 166 HQASQLIHWI 175
Cdd:PRK13638 170 AGRTQMIAII 179
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
134-164 |
1.99e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 47.65 E-value: 1.99e-06
10 20 30
....*....|....*....|....*....|.
gi 1148626600 134 SGGQRQRVAIARALYQGHDLFLGDEPVASVD 164
Cdd:PRK11308 156 SGGQRQRIAIARALMLDPDVVVADEPVSALD 186
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
24-173 |
2.12e-06 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 48.17 E-value: 2.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 24 VLRDLDVQLEHGERVALLGASGAGKSTLLEALRS---------ALHEQGTPA----AWcPQRQGLVPQL------SVYHN 84
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRhfdvsegdiRFHDIPLTKlqldSW-RSRLAVVSQTpflfsdTVANN 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 85 IFMGRLDQQSSLTNllnllrprpaHWQAVAAVCE-----PLGI-AGLMERSVeALSGGQRQRVAIARALYQGHDLFLGDE 158
Cdd:PRK10789 409 IALGRPDATQQEIE----------HVARLASVHDdilrlPQGYdTEVGERGV-MLSGGQKQRISIARALLLNAEILILDD 477
|
170
....*....|....*
gi 1148626600 159 PVASVDPHQASQLIH 173
Cdd:PRK10789 478 ALSAVDGRTEHQILH 492
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
9-164 |
2.18e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 47.35 E-value: 2.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 9 LLHLSRHHLGHGAEVVLRDLDVQLEHGERVALLGASGAGKSTLLEALR-------SALHEQGT-----------PAAWCP 70
Cdd:PRK14246 10 VFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNrlieiydSKIKVDGKvlyfgkdifqiDAIKLR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 71 QRQGLV-------PQLSVYHNIFM-----GRLDQQSSLTNLLNLLRpRPAHWQAVAavceplgiaGLMERSVEALSGGQR 138
Cdd:PRK14246 90 KEVGMVfqqpnpfPHLSIYDNIAYplkshGIKEKREIKKIVEECLR-KVGLWKEVY---------DRLNSPASQLSGGQQ 159
|
170 180
....*....|....*....|....*.
gi 1148626600 139 QRVAIARALYQGHDLFLGDEPVASVD 164
Cdd:PRK14246 160 QRLTIARALALKPKVLLMDEPTSMID 185
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
118-159 |
2.48e-06 |
|
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: 47.86 E-value: 2.48e-06
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1148626600 118 EPLGIAGLMERSVEALSGGQRQRVAIARALYQGHDLFLGDEP 159
Cdd:COG1245 198 EKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEP 239
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
16-191 |
2.68e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 47.11 E-value: 2.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 16 HLGHGAEVVLRDLDVQLEHGERVALLGASGAGKSTLLEALRSALH----------EQGTPAAWCPQRQ--GLVPQ----- 78
Cdd:PRK13652 11 YSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKptsgsvlirgEPITKENIREVRKfvGLVFQnpddq 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 79 ---LSVYHNIFMGR----LDQQSSltnllnllrprpAHwqAVAAVCEPLGIAGLMERSVEALSGGQRQRVAIARALYQGH 151
Cdd:PRK13652 91 ifsPTVEQDIAFGPinlgLDEETV------------AH--RVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEP 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1148626600 152 DLFLGDEPVASVDPHQASQLIHWIHS---RHATSVV-ALHQKEL 191
Cdd:PRK13652 157 QVLVLDEPTAGLDPQGVKELIDFLNDlpeTYGMTVIfSTHQLDL 200
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
25-222 |
2.92e-06 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 47.39 E-value: 2.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 25 LRDLDVQLEHGERVALLGASGAGKSTLLEALRSALHeqgtP-------AAWCPQRQ--------GLV----PQL------ 79
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILV----PtsgevrvLGYVPFKRrkefarriGVVfgqrSQLwwdlpa 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 80 --------SVYhNIfmgrldqqssltnllnllrPRPAHWQAVAAVCEPLGIAGLMERSVEALSGGQRQRVAIARALYqgH 151
Cdd:COG4586 114 idsfrllkAIY-RI-------------------PDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALL--H 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 152 D---LFLgDEP-----VASvdphQAS--QLIHWIHSRHATSVValhqkelaLT-HF--------TRVIGLGKdengnGKV 212
Cdd:COG4586 172 RpkiLFL-DEPtigldVVS----KEAirEFLKEYNRERGTTIL--------LTsHDmddiealcDRVIVIDH-----GRI 233
|
250
....*....|
gi 1148626600 213 LLDANTDDLK 222
Cdd:COG4586 234 IYDGSLEELK 243
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
20-187 |
2.98e-06 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 47.07 E-value: 2.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 20 GAEVVLRDLDVQLEHGERVALLGASGAGKSTLLEAL----------------------RSALHEQGTPAAWCPQRQGLVP 77
Cdd:PRK11831 18 GNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIggqiapdhgeilfdgenipamsRSRLYTVRKRMSMLFQSGALFT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 78 QLSVYHNI-FMGRLDQQSsltnllnllrPRPAHWQAVAAVCEPLGIAGLMERSVEALSGGQRQRVAIARALYQGHDLFLG 156
Cdd:PRK11831 98 DMNVFDNVaYPLREHTQL----------PAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMF 167
|
170 180 190
....*....|....*....|....*....|....*
gi 1148626600 157 DEPVASVDPHQASQLIHWI----HSRHATSVVALH 187
Cdd:PRK11831 168 DEPFVGQDPITMGVLVKLIselnSALGVTCVVVSH 202
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
23-192 |
4.47e-06 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 46.32 E-value: 4.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 23 VVLRDLDVQLEHGERVALLGASGAGKSTLLEAL---------RSALHEQ----------GTPAAWCPQRQGLVPQLSVYH 83
Cdd:PRK10575 25 TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLgrhqppsegEILLDAQpleswsskafARKVAYLPQQLPAAEGMTVRE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 84 NIFMGRLDQQSSLTNLLNLLRPRPAhwQAVAAVceplGIAGLMERSVEALSGGQRQRVAIARALYQGHDLFLGDEPVASV 163
Cdd:PRK10575 105 LVAIGRYPWHGALGRFGAADREKVE--EAISLV----GLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSAL 178
|
170 180 190
....*....|....*....|....*....|...
gi 1148626600 164 D-PHQAS--QLIHWIHSRHATSVVA-LHQKELA 192
Cdd:PRK10575 179 DiAHQVDvlALVHRLSQERGLTVIAvLHDINMA 211
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
23-173 |
4.83e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 46.94 E-value: 4.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 23 VVLRDLDVQLEHGERVALLGASGAGKSTLLEAL---RSAlhEQG------------TPAAWC----------PQRQGLVP 77
Cdd:COG3845 272 PALKDVSLEVRAGEILGIAGVAGNGQSELAEALaglRPP--ASGsirldgeditglSPRERRrlgvayipedRLGRGLVP 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 78 QLSVYHNIFMGRLDQQSSLTNLLNllrprpaHWQAVAAVCEplgiaGLMER----------SVEALSGGQRQRVAIARAL 147
Cdd:COG3845 350 DMSVAENLILGRYRRPPFSRGGFL-------DRKAIRAFAE-----ELIEEfdvrtpgpdtPARSLSGGNQQKVILAREL 417
|
170 180
....*....|....*....|....*.
gi 1148626600 148 YQGHDLFLGDEPVASVDPHqASQLIH 173
Cdd:COG3845 418 SRDPKLLIAAQPTRGLDVG-AIEFIH 442
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
21-165 |
5.19e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 46.58 E-value: 5.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 21 AEVVLRDLDVQLEHGERVALLGASGAGKSTLLEALRSALH--------------EQGTPAAWCPQRQGLVPQL------- 79
Cdd:PRK13637 19 EKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKptsgkiiidgvditDKKVKLSDIRKKVGLVFQYpeyqlfe 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 80 -SVYHNIFMGrlDQQSSLTNLLNLLRPRpahwQAVAAVcePLGIAGLMERSVEALSGGQRQRVAIARALYQGHDLFLGDE 158
Cdd:PRK13637 99 eTIEKDIAFG--PINLGLSEEEIENRVK----RAMNIV--GLDYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDE 170
|
....*..
gi 1148626600 159 PVASVDP 165
Cdd:PRK13637 171 PTAGLDP 177
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
25-171 |
6.37e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 46.70 E-value: 6.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 25 LRDLDVQLEHGERVALLGASGAGKSTLLEALrSALHE--------------QGTPAAWCP-------QRQGLVPQLSVYH 83
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVL-SGIHEptkgtitinninynKLDHKLAAQlgigiiyQELSVIDELTVLE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 84 NIFMGRLDQQSSLTNLLNLLRprpaHWQAVAAV-CEPLGIAGLMERSVEALSGGQRQRVAIARALYQGHDLFLGDEPVAS 162
Cdd:PRK09700 100 NLYIGRHLTKKVCGVNIIDWR----EMRVRAAMmLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSS 175
|
....*....
gi 1148626600 163 VDPHQASQL 171
Cdd:PRK09700 176 LTNKEVDYL 184
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
24-185 |
7.16e-06 |
|
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: 46.47 E-value: 7.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 24 VLRDLDVQLEHGERVALLGASGAGKSTLL--------EALRSALHEQGTPAAWCPQRQGLVPQLSVYHNIFMG------- 88
Cdd:TIGR03719 20 ILKDISLSFFPGAKIGVLGLNGAGKSTLLrimagvdkDFNGEARPQPGIKVGYLPQEPQLDPTKTVRENVEEGvaeikda 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 89 --RLDQQSSL----TNLLNLLRPRPAHWQAVAAVCEPLGIAGLMERSVEAL------------SGGQRQRVAIARALYQG 150
Cdd:TIGR03719 100 ldRFNEISAKyaepDADFDKLAAEQAELQEIIDAADAWDLDSQLEIAMDALrcppwdadvtklSGGERRRVALCRLLLSK 179
|
170 180 190
....*....|....*....|....*....|....*
gi 1148626600 151 HDLFLGDEPVASVDPHQASQLIHWIHsRHATSVVA 185
Cdd:TIGR03719 180 PDMLLLDEPTNHLDAESVAWLERHLQ-EYPGTVVA 213
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
131-195 |
8.27e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 45.90 E-value: 8.27e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1148626600 131 EALSGGQRQRVAIARALYQGHDLFLGDEPVASVDPHQASQLIHWIHSRHATSVVALhqkeLALTH 195
Cdd:PRK13648 141 NALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITI----ISITH 201
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
133-172 |
1.04e-05 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 45.21 E-value: 1.04e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1148626600 133 LSGGQRQRVAIARALYQGHDLFLGDEPVASVDPHQASQLI 172
Cdd:COG4167 150 LSSGQKQRVALARALILQPKIIIADEALAALDMSVRSQII 189
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
25-176 |
1.17e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 45.47 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 25 LRDLDVQLEHGERVALLGASGAGKST-------LLEALRSALHEQG----TPAAWCPQRQ-GLVPQLSvyHNIFMGRLDQ 92
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTtarlidgLFEEFEGKVKIDGelltAENVWNLRRKiGMVFQNP--DNQFVGATVE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 93 QSSLTNLLNLLRPRPAHWQAVAAVCEPLGIAGLMERSVEALSGGQRQRVAIARALYQGHDLFLGDEPVASVDPHQASQLI 172
Cdd:PRK13642 101 DDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIM 180
|
....
gi 1148626600 173 HWIH 176
Cdd:PRK13642 181 RVIH 184
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
35-173 |
1.20e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 46.00 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 35 GERVALLGASGAGKSTLLEALRSALHEQGTPAAWCPQRQGLVP--QLSVYhnifmgRLDQQSSLTNLLNLLRPRpahwQA 112
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgKLQAL------RRDIQFIFQDPYASLDPR----QT 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 113 VA-AVCEPLGIAGLME-----------------------RSVEALSGGQRQRVAIARALYQGHDLFLGDEPVASVDPHQA 168
Cdd:PRK10261 420 VGdSIMEPLRVHGLLPgkaaaarvawllervgllpehawRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIR 499
|
....*
gi 1148626600 169 SQLIH 173
Cdd:PRK10261 500 GQIIN 504
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
24-204 |
1.26e-05 |
|
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: 44.77 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 24 VLRDLDVQLEHGERVALLGASGAGKSTLLEALRSALHEQ-------GTPAAWCPQRQ--------GLVPQL---SVYHNI 85
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQggqvlldGKPISQYEHKYlhskvslvGQEPVLfarSLQDNI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 86 FMGRldQQSSLTNLLNLLRPRPAHwqavAAVCE-PLGIAGLMERSVEALSGGQRQRVAIARALYQGHDLFLGDEPVASVD 164
Cdd:cd03248 109 AYGL--QSCSFECVKEAAQKAHAH----SFISElASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALD 182
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1148626600 165 ---PHQASQLIHWIHSRHATSVVALHQKELALTHFTRVIGLGK 204
Cdd:cd03248 183 aesEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGR 225
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
35-159 |
1.45e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 45.38 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 35 GERVALLGASGAGKSTLLEAL-----RSA--LHEQGTPAAW----CPQRQG---------LVPQLSVYHNIFMGR----- 89
Cdd:PRK10762 30 GRVMALVGENGAGKSTMMKVLtgiytRDAgsILYLGKEVTFngpkSSQEAGigiihqelnLIPQLTIAENIFLGRefvnr 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1148626600 90 ---LDQQSSltnllnllrprpahWQAVAAVCEPLGIAGLMERSVEALSGGQRQRVAIARALYQGHDLFLGDEP 159
Cdd:PRK10762 110 fgrIDWKKM--------------YAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEP 168
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
8-165 |
1.47e-05 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 44.87 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 8 PLLHLSRHHLGHGAEVVLRDLDVQLEHGERVALLGASGAGKSTLLEALRSALH-EQGT-------------------PAA 67
Cdd:PRK11614 4 VMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRaTSGRivfdgkditdwqtakimreAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 68 WCPQRQGLVPQLSVYHNIFMGRLDQQssltnllnllrpRPAHWQAVAAVCEPLgiAGLMERSVE---ALSGGQRQRVAIA 144
Cdd:PRK11614 84 IVPEGRRVFSRMTVEENLAMGGFFAE------------RDQFQERIKWVYELF--PRLHERRIQragTMSGGEQQMLAIG 149
|
170 180
....*....|....*....|.
gi 1148626600 145 RALYQGHDLFLGDEPVASVDP 165
Cdd:PRK11614 150 RALMSQPRLLLLDEPSLGLAP 170
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
3-62 |
1.65e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 45.55 E-value: 1.65e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 3 QATPSPLLHLSRHHLGHGAEVVLRDLDVQLEHGERVALLGASGAGKSTLLEALRSALHEQ 62
Cdd:PRK10636 306 ESLPNPLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPV 365
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
25-206 |
1.74e-05 |
|
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: 44.18 E-value: 1.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 25 LRDLDVQLEHGERVALLGASGAGKSTLLEALRSALHEQGTP---------------------AAWCPQRQGLVPQLSVYH 83
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVSVegdihyngipykefaekypgeIIYVSEEDVHFPTLTVRE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 84 NI-FmgrldqqssltnllnllrprpahwqavAAVCEplGiaglmERSVEALSGGQRQRVAIARALYQGHDLFLGDEPVAS 162
Cdd:cd03233 103 TLdF---------------------------ALRCK--G-----NEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRG 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1148626600 163 VDPHQASQLIHWI----HSRHATSVVALHQKELALTH-FTRVIGLGKDE 206
Cdd:cd03233 149 LDSSTALEILKCIrtmaDVLKTTTFVSLYQASDEIYDlFDKVLVLYEGR 197
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
20-165 |
2.68e-05 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 44.64 E-value: 2.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 20 GAEVVLRDLDVQLEHGERVALLGASGAGKST-------LLEALRSALHEQGTPAAWCP----------------QRQGLV 76
Cdd:PRK10070 39 GLSLGVKDASLAIEEGEIFVIMGLSGSGKSTmvrllnrLIEPTRGQVLIDGVDIAKISdaelrevrrkkiamvfQSFALM 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 77 PQLSVYHNIFMGrldqqssltnLLNLLRPRPAHWQAVAAVCEPLGIAGLMERSVEALSGGQRQRVAIARALYQGHDLFLG 156
Cdd:PRK10070 119 PHMTVLDNTAFG----------MELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLM 188
|
....*....
gi 1148626600 157 DEPVASVDP 165
Cdd:PRK10070 189 DEAFSALDP 197
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
11-164 |
4.17e-05 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 43.32 E-value: 4.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 11 HLSRHHLGhgAEVVLRDLDVQLEHGERVALLGASGAGKSTLLEaLRSALHEQGTPAAW-------------CP--QRQ-G 74
Cdd:PRK10908 6 HVSKAYLG--GRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLK-LICGIERPSAGKIWfsghditrlknreVPflRRQiG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 75 LVPQ-------LSVYHNIFMGRLdqqsSLTNLLNLLRPRpahwqaVAAVCEPLGIAGLMERSVEALSGGQRQRVAIARAL 147
Cdd:PRK10908 83 MIFQdhhllmdRTVYDNVAIPLI----IAGASGDDIRRR------VSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAV 152
|
170
....*....|....*..
gi 1148626600 148 YQGHDLFLGDEPVASVD 164
Cdd:PRK10908 153 VNKPAVLLADEPTGNLD 169
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
21-164 |
5.16e-05 |
|
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: 43.96 E-value: 5.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 21 AEVVLRDLDVQLEHGERVALLGASGAGKSTLLEAL-RSALHEQG-----------TPAAWCPQRQGLVPQ------LSVY 82
Cdd:TIGR01846 469 SPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLqRLYTPQHGqvlvdgvdlaiADPAWLRRQMGVVLQenvlfsRSIR 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 83 HNIFMGRldQQSSLTNLLNLLRPRPAHWQAVAavcEPLGIAGLMERSVEALSGGQRQRVAIARALYQGHDLFLGDEPVAS 162
Cdd:TIGR01846 549 DNIALCN--PGAPFEHVIHAAKLAGAHDFISE---LPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSA 623
|
..
gi 1148626600 163 VD 164
Cdd:TIGR01846 624 LD 625
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
25-164 |
7.45e-05 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 43.47 E-value: 7.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 25 LRDLDVQLEHGERVALLGASGAGKST----------------LLEA--LR----SALHEQgtpaawcpqrQGLVPQL--- 79
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTianlltrfydidegeiLLDGhdLRdytlASLRNQ----------VALVSQNvhl 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 80 ---SVYHNIFMGRLDQQSSltnllnllrprpAHWQAVAAVCEPLGIAGLMERSVEA--------LSGGQRQRVAIARALY 148
Cdd:PRK11176 429 fndTIANNIAYARTEQYSR------------EQIEEAARMAYAMDFINKMDNGLDTvigengvlLSGGQRQRIAIARALL 496
|
170
....*....|....*.
gi 1148626600 149 QGHDLFLGDEPVASVD 164
Cdd:PRK11176 497 RDSPILILDEATSALD 512
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
128-202 |
8.03e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 43.31 E-value: 8.03e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1148626600 128 RSVEALSGGQRQRVAIARALYQGHDLFLGDEPVASVDPHQASQLIHWIHSRHATSVVALHQKELALTHFTRVIGL 202
Cdd:PLN03073 340 KATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDILHL 414
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
8-172 |
8.56e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 43.31 E-value: 8.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 8 PLLHLSRHHLGH-GAEVVLRDLDVQLEHGERVALLGASGAGKSTLLEALRSALHeqgtPAAWCPQRQGLVpQLSVYHNIF 86
Cdd:PLN03073 507 PIISFSDASFGYpGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQ----PSSGTVFRSAKV-RMAVFSQHH 581
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 87 MGRLDQQSSLTNLLNLLRPRPAHwQAVAAVCEPLGIAG-LMERSVEALSGGQRQRVAIARALYQGHDLFLGDEPVASVDP 165
Cdd:PLN03073 582 VDGLDLSSNPLLYMMRCFPGVPE-QKLRAHLGSFGVTGnLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDL 660
|
....*..
gi 1148626600 166 HQASQLI 172
Cdd:PLN03073 661 DAVEALI 667
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
25-164 |
1.10e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 42.68 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 25 LRDLDVQLEHGERVALLGASGAGKSTLLEALRSAL-HEQG-------TPAAWCPQ---------------RQGLVPQLSV 81
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALpRTSGyvtldghEVVTRSPQdglangivyisedrkRDGLVLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 82 YHNI----------FMGRLDQQssltnllnllrprpAHWQAVAAVCEPLGI-AGLMERSVEALSGGQRQRVAIARALYQG 150
Cdd:PRK10762 348 KENMsltalryfsrAGGSLKHA--------------DEQQAVSDFIRLFNIkTPSMEQAIGLLSGGNQQKVAIARGLMTR 413
|
170
....*....|....
gi 1148626600 151 HDLFLGDEPVASVD 164
Cdd:PRK10762 414 PKVLILDEPTRGVD 427
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
133-187 |
1.41e-04 |
|
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: 41.40 E-value: 1.41e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1148626600 133 LSGGQRQRVAIARALYQGHDLFLGDEPVASVDPHQ---ASQLI-HWIHSRHATSVVALH 187
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQrlnAARAIrRLSEEGKKTALVVEH 130
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
131-164 |
1.49e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 42.71 E-value: 1.49e-04
10 20 30
....*....|....*....|....*....|....
gi 1148626600 131 EALSGGQRQRVAIARALYQGHDLFLGDEPVASVD 164
Cdd:PTZ00265 1357 KSLSGGQKQRIAIARALLREPKILLLDEATSSLD 1390
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
18-164 |
1.51e-04 |
|
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: 42.23 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 18 GHGAEVVLRDLDVQLEHGERVALLGASGAGKSTLLEALRSalheQGTP------------AAWCPQ-RQGLVPQLSVYHN 84
Cdd:TIGR03719 331 AFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITG----QEQPdsgtieigetvkLAYVDQsRDALDPNKTVWEE 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 85 IFMGrLDQqssltnLLNLLRPRPAHwqavaAVCEPLGIAGL-MERSVEALSGGQRQRVAIARALYQGHDLFLGDEPVASV 163
Cdd:TIGR03719 407 ISGG-LDI------IKLGKREIPSR-----AYVGRFNFKGSdQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDL 474
|
.
gi 1148626600 164 D 164
Cdd:TIGR03719 475 D 475
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
25-172 |
1.57e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 42.12 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 25 LRDLDVQLEHGERVALLGASGAGKSTLLEALRSALH----------EQGTPAAWCP------QRQGLVPQLS-------- 80
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKpssgtitiagYHITPETGNKnlkklrKKVSLVFQFPeaqlfent 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 81 VYHNIFMGRLDqqssLTNLLNLLRPRPAHWQAVAAVCEPLgiaglMERSVEALSGGQRQRVAIARALYQGHDLFLGDEPV 160
Cdd:PRK13641 103 VLKDVEFGPKN----FGFSEDEAKEKALKWLKKVGLSEDL-----ISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPA 173
|
170
....*....|..
gi 1148626600 161 ASVDPHQASQLI 172
Cdd:PRK13641 174 AGLDPEGRKEMM 185
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
111-165 |
1.79e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 41.65 E-value: 1.79e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1148626600 111 QAVAAVCEPLGIAG----LMERSVEALSGGQRQRVAIARALYQGHDLFLGDEPVASVDP 165
Cdd:PRK13649 120 EAEALAREKLALVGisesLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDP 178
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
24-164 |
1.81e-04 |
|
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: 41.36 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 24 VLRDLDVQLEHGERVALLGASGAGKSTLLEALrsALHEQGTPAawcpqrQGLV-------PQLSVYH----NIFMGrldq 92
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTI--MGHPKYEVT------EGEIlfkgediTDLPPEErarlGIFLA---- 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1148626600 93 qssltnllnllrprpahWQavaavcEPLGIAGL----MERSV-EALSGGQRQRVAIARALYQGHDLFLGDEPVASVD 164
Cdd:cd03217 83 -----------------FQ------YPPEIPGVknadFLRYVnEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLD 136
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
20-190 |
1.96e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 42.08 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 20 GAEVVLRDLDVQLEHGERVALLGASGAGKSTLLEALRSALHEQGTPA--------AWCPQRQGLVPQLSVYHNIFMGRLD 91
Cdd:PRK10636 12 GVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYtfpgnwqlAWVNQETPALPQPALEYVIDGDREY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 92 QQSSLTNLLNLLRpRPAHwqAVAAVCEPLG--------------IAGL------MERSVEALSGGQRQRVAIARALYQGH 151
Cdd:PRK10636 92 RQLEAQLHDANER-NDGH--AIATIHGKLDaidawtirsraaslLHGLgfsneqLERPVSDFSGGWRMRLNLAQALICRS 168
|
170 180 190
....*....|....*....|....*....|....*....
gi 1148626600 152 DLFLGDEPVASVDPHQASQLIHWIHSRHATSVVALHQKE 190
Cdd:PRK10636 169 DLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRD 207
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
23-165 |
2.56e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 41.23 E-value: 2.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 23 VVLRDLDVQLEHGERVALLGASGAGKSTLLEALRSALheqgTPAA----------------W-CPQRQGLVPQlsvyhni 85
Cdd:PRK13633 24 LALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALL----IPSEgkvyvdgldtsdeenlWdIRNKAGMVFQ------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 86 fmgrldqqssltnllnllrpRPAHwQAVAAVCE-------------PLGIAGLMERSVEA-------------LSGGQRQ 139
Cdd:PRK13633 93 --------------------NPDN-QIVATIVEedvafgpenlgipPEEIRERVDESLKKvgmyeyrrhaphlLSGGQKQ 151
|
170 180
....*....|....*....|....*.
gi 1148626600 140 RVAIARALYQGHDLFLGDEPVASVDP 165
Cdd:PRK13633 152 RVAIAGILAMRPECIIFDEPTAMLDP 177
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
24-164 |
4.62e-04 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 40.84 E-value: 4.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 24 VLRDLDVQLEHGERVALLGASGAGKStlLEALrSALHEQGTPAAWCPQRQGLVPQLSVYHN---------------IF-- 86
Cdd:PRK15134 24 VVNDVSLQIEAGETLALVGESGSGKS--VTAL-SILRLLPSPPVVYPSGDIRFHGESLLHAseqtlrgvrgnkiamIFqe 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 87 -------MGRLDQQSSLTNLLNLLRPRPAHWQAVAAVCEPLGI---AGLMERSVEALSGGQRQRVAIARALYQGHDLFLG 156
Cdd:PRK15134 101 pmvslnpLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIrqaAKRLTDYPHQLSGGERQRVMIAMALLTRPELLIA 180
|
....*...
gi 1148626600 157 DEPVASVD 164
Cdd:PRK15134 181 DEPTTALD 188
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
20-164 |
5.20e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 40.70 E-value: 5.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 20 GAEVVLRDLDVQLEHGERVALLGASGAGKSTLLEALRSALHEQ------GTP--AAWCPQ-RQGLVPQLSVYHNIFMGRL 90
Cdd:PRK11147 330 DGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADsgrihcGTKleVAYFDQhRAELDPEKTVMDNLAEGKQ 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 91 DqqssltnLLNLLRPRpaHwqavaavceplgIAGLME-------RS---VEALSGGQRQRVAIARALYQGHDLFLGDEPV 160
Cdd:PRK11147 410 E-------VMVNGRPR--H------------VLGYLQdflfhpkRAmtpVKALSGGERNRLLLARLFLKPSNLLILDEPT 468
|
....
gi 1148626600 161 ASVD 164
Cdd:PRK11147 469 NDLD 472
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
25-203 |
5.21e-04 |
|
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: 39.93 E-value: 5.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 25 LRDLDVQLEHGERVALLGASGAGKSTL-------------LEAL----RSALHEQGTPAAwcPQRQGLVPQLSVyhnifm 87
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLafdtiyaegqrryVESLsayaRQFLGQMDKPDV--DSIEGLSPAIAI------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 88 grlDQQSSLTNllnllrPRpahwQAVAAVCE----------PLGI---------AGL----MERSVEALSGGQRQRVAIA 144
Cdd:cd03270 83 ---DQKTTSRN------PR----STVGTVTEiydylrllfaRVGIrerlgflvdVGLgyltLSRSAPTLSGGEAQRIRLA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1148626600 145 RALYQGHD--LFLGDEPVASVDPHQASQLIHWIHS-RHA--TSVVALHQKELALtHFTRVIGLG 203
Cdd:cd03270 150 TQIGSGLTgvLYVLDEPSIGLHPRDNDRLIETLKRlRDLgnTVLVVEHDEDTIR-AADHVIDIG 212
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
9-172 |
5.43e-04 |
|
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: 41.15 E-value: 5.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 9 LLHLSRHHLGHGAEVVLRdLDVQLEHGERVALLGASGAGKSTLLEAL---------------RSALheqgTPAAWCPQRQ 73
Cdd:TIGR01257 1940 LNELTKVYSGTSSPAVDR-LCVGVRPGECFGLLGVNGAGKTTTFKMLtgdttvtsgdatvagKSIL----TNISDVHQNM 2014
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 74 GLVPQLSVYHNIFMGR--LDQQSSLTNLLNLLRPRPAHWQavaavCEPLGIAGLMERSVEALSGGQRQRVAIARALYQGH 151
Cdd:TIGR01257 2015 GYCPQFDAIDDLLTGRehLYLYARLRGVPAEEIEKVANWS-----IQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCP 2089
|
170 180
....*....|....*....|.
gi 1148626600 152 DLFLGDEPVASVDPhQASQLI 172
Cdd:TIGR01257 2090 PLVLLDEPTTGMDP-QARRML 2109
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
125-194 |
7.38e-04 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 40.07 E-value: 7.38e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 125 LMERSVEALSGGQRQRVAIARALYQGHDLFLGDEPVASVDPHQASQLIHWIHSRhatsvvalhQKELALT 194
Cdd:PRK15079 154 LINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQL---------QREMGLS 214
|
|
| ExeA |
COG3267 |
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ... |
3-66 |
7.59e-04 |
|
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 442498 [Multi-domain] Cd Length: 261 Bit Score: 39.77 E-value: 7.59e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1148626600 3 QATPSP-LLHLSRHHlghgaEVVLRDLDVQLEHGERVALL-GASGAGKSTLLEALRSALHEQGTPA 66
Cdd:COG3267 14 SLTPDPrFLFLSPSH-----REALARLEYALAQGGGFVVLtGEVGTGKTTLLRRLLERLPDDVKVA 74
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
130-159 |
1.08e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 39.72 E-value: 1.08e-03
10 20 30
....*....|....*....|....*....|
gi 1148626600 130 VEALSGGQRQRVAIARALYQGHDLFLGDEP 159
Cdd:PRK11819 161 VTKLSGGERRRVALCRLLLEKPDMLLLDEP 190
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
4-164 |
1.18e-03 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 39.14 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 4 ATPSPLLhlSRHHLGH--GAEVVLRDLDVQLEHGERVALLGASGAGKSTLLEALRSALHEQGTPAAWCPQRQGLVP--QL 79
Cdd:PRK11701 1 MMDQPLL--SVRGLTKlyGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDlyAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 80 SVYHNIFMGRLD----QQSsltnllnllrPRPAHWQAVAA---VCEPLGIAGL-------------MERsVE-------- 131
Cdd:PRK11701 79 SEAERRRLLRTEwgfvHQH----------PRDGLRMQVSAggnIGERLMAVGArhygdiratagdwLER-VEidaaridd 147
|
170 180 190
....*....|....*....|....*....|....*.
gi 1148626600 132 ---ALSGGQRQRVAIARALYQGHDLFLGDEPVASVD 164
Cdd:PRK11701 148 lptTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLD 183
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
132-172 |
1.36e-03 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 39.00 E-value: 1.36e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1148626600 132 ALSGGQRQRVAIARALYQGHDLFLGDEPVASVDPHQASQLI 172
Cdd:PRK15112 149 MLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLI 189
|
|
| PRK03846 |
PRK03846 |
adenylylsulfate kinase; Provisional |
31-63 |
1.76e-03 |
|
adenylylsulfate kinase; Provisional
Pssm-ID: 179661 Cd Length: 198 Bit Score: 38.38 E-value: 1.76e-03
10 20 30
....*....|....*....|....*....|....*.
gi 1148626600 31 QLEHGERVALL---GASGAGKSTLLEALRSALHEQG 63
Cdd:PRK03846 17 EQLHGHKGVVLwftGLSGSGKSTVAGALEEALHELG 52
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
22-193 |
1.82e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 38.39 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 22 EVVLRDLDVQLEHGERVALLGASGAGKSTLLEALRSALHEQGTP------------AAWCPQ------RQGLVPQLSVYH 83
Cdd:PRK13540 14 QPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEilferqsikkdlCTYQKQlcfvghRSGINPYLTLRE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 84 NIFmgrLDQQSSLTNLlnllrprpahwqAVAAVCEPLGIAGLMERSVEALSGGQRQRVAIARALYQGHDLFLGDEPVASV 163
Cdd:PRK13540 94 NCL---YDIHFSPGAV------------GITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVAL 158
|
170 180 190
....*....|....*....|....*....|..
gi 1148626600 164 DPHQASQLIHWI--HSRHATSVVALHQKELAL 193
Cdd:PRK13540 159 DELSLLTIITKIqeHRAKGGAVLLTSHQDLPL 190
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
25-79 |
2.20e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 38.76 E-value: 2.20e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1148626600 25 LRDLDVQLehGERVALLGASGAGKSTLLEALR--SALHEQGTPAAWcpQRQGLVPQL 79
Cdd:COG4637 13 LRDLELPL--GPLTVLIGANGSGKSNLLDALRflSDAARGGLQDAL--ARRGGLEEL 65
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
20-165 |
2.39e-03 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 38.99 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 20 GAEVVLRDLDVQLEHGERVALLGASGAGKSTLL-------EALRSALHEQGTPAAWCPQRQ-----GLVPQLSVyhnIFM 87
Cdd:PTZ00243 1321 GLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLltfmrmvEVCGGEIRVNGREIGAYGLRElrrqfSMIPQDPV---LFD 1397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 88 GRLDQQSSltnllnllrprPAHWQAVAAVCEPLGIAGLMERsVEALSG---------------GQRQRVAIARALYQ-GH 151
Cdd:PTZ00243 1398 GTVRQNVD-----------PFLEASSAEVWAALELVGLRER-VASESEgidsrvleggsnysvGQRQLMCMARALLKkGS 1465
|
170
....*....|....
gi 1148626600 152 DLFLGDEPVASVDP 165
Cdd:PTZ00243 1466 GFILMDEATANIDP 1479
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
25-59 |
2.51e-03 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 37.86 E-value: 2.51e-03
10 20 30
....*....|....*....|....*....|....*
gi 1148626600 25 LRDLDVQLEHGErVALLGASGAGKSTLLEALRSAL 59
Cdd:pfam13476 9 FRDQTIDFSKGL-TLITGPNGSGKTTILDAIKLAL 42
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
25-147 |
2.52e-03 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 38.79 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 25 LRDLDVQLEHGERVALLGASGAGKSTLLeALrsaLHEqgtpaAWCPQ---------------RQGLVPQL---------- 79
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLI-NL---LQR-----VFDPQsgrilidgtdirtvtRASLRRNIavvfqdaglf 421
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1148626600 80 --SVYHNIFMGRLDQQSSLTNLLNLlrpRPAHWQAVAAvcEPLG---IAGlmERSvEALSGGQRQRVAIARAL 147
Cdd:PRK13657 422 nrSIEDNIRVGRPDATDEEMRAAAE---RAQAHDFIER--KPDGydtVVG--ERG-RQLSGGERQRLAIARAL 486
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
24-207 |
2.70e-03 |
|
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: 38.63 E-value: 2.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 24 VLRDLD-VQLE--HGERVALLGASGAGKSTLLEALRSALHeqgtPAA----------WC------PQRQG--------LV 76
Cdd:TIGR03269 296 VVKAVDnVSLEvkEGEIFGIVGTSGAGKTTLSKIIAGVLE----PTSgevnvrvgdeWVdmtkpgPDGRGrakryigiLH 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 77 PQLSVY-HNIFMGRLDQQSSLTNLLNLLRPRPAHWQAVAAVCEPLGIAgLMERSVEALSGGQRQRVAIARALYQGHDLFL 155
Cdd:TIGR03269 372 QEYDLYpHRTVLDNLTEAIGLELPDELARMKAVITLKMVGFDEEKAEE-ILDKYPDELSEGERHRVALAQVLIKEPRIVI 450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1148626600 156 GDEPVASVDPHQASQLIHWI-HSR---HATSVVALHQKEL--------ALTHFTRVIGLGKDEN 207
Cdd:TIGR03269 451 LDEPTGTMDPITKVDVTHSIlKAReemEQTFIIVSHDMDFvldvcdraALMRDGKIVKIGDPEE 514
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
23-172 |
2.75e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 38.22 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 23 VVLRDLDVQLEHGERVALLGASGAGKSTLLEALRSAL--------------HEQGTPAAWCPQRQ--GLVPQL------- 79
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLkpttgtvtvdditiTHKTKDKYIRPVRKriGMVFQFpesqlfe 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 80 -SVYHNIFMG------RLDQqssltnllnllrprpAHWQAVAAVCEpLGIA-GLMERSVEALSGGQRQRVAIARALYQGH 151
Cdd:PRK13646 101 dTVEREIIFGpknfkmNLDE---------------VKNYAHRLLMD-LGFSrDVMSQSPFQMSGGQMRKIAIVSILAMNP 164
|
170 180
....*....|....*....|.
gi 1148626600 152 DLFLGDEPVASVDPHQASQLI 172
Cdd:PRK13646 165 DIIVLDEPTAGLDPQSKRQVM 185
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
28-166 |
2.84e-03 |
|
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: 38.84 E-value: 2.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 28 LDVQLEHGERVALLGASGAGKSTLLEALRSALH-EQGT-----------------PAAWCPQRQGLVPQLSVY-HNIFMG 88
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPpTSGTvlvggkdietnldavrqSLGMCPQHNILFHHLTVAeHILFYA 1028
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1148626600 89 RLDQQSSLTNLLNllrprpahwqaVAAVCEPLGIAGLMERSVEALSGGQRQRVAIARALYQGHDLFLGDEPVASVDPH 166
Cdd:TIGR01257 1029 QLKGRSWEEAQLE-----------MEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPY 1095
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
125-164 |
3.21e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 38.47 E-value: 3.21e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1148626600 125 LMERSVEALSGGQRQRVAIARALYQGHDLFLGDEPVASVD 164
Cdd:PTZ00265 572 LVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
35-55 |
4.22e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 37.61 E-value: 4.22e-03
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
133-177 |
5.12e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 37.38 E-value: 5.12e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1148626600 133 LSGGQRQRVAIARALYQGHDLFLGDEPVASVDPHQASQLIHWIHS 177
Cdd:PRK14271 164 LSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRS 208
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
35-55 |
5.61e-03 |
|
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: 36.84 E-value: 5.61e-03
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
11-164 |
6.59e-03 |
|
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: 37.50 E-value: 6.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 11 HLSRHHLGHGAEVVLRDLDVQLEHGERVALLGASGAGKSTLLEAL---------------------RSALHEQGTPAAWC 69
Cdd:TIGR02633 262 NLTCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALfgaypgkfegnvfingkpvdiRNPAQAIRAGIAMV 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 70 PQ---RQGLVPQLSVYHNIFMGRLDQQSSLTNLLNLlrprpAHWQAVAAVCEPLGI-AGLMERSVEALSGGQRQRVAIAR 145
Cdd:TIGR02633 342 PEdrkRHGIVPILGVGKNITLSVLKSFCFKMRIDAA-----AELQIIGSAIQRLKVkTASPFLPIGRLSGGNQQKAVLAK 416
|
170
....*....|....*....
gi 1148626600 146 ALYQGHDLFLGDEPVASVD 164
Cdd:TIGR02633 417 MLLTNPRVLILDEPTRGVD 435
|
|
| PRK08903 |
PRK08903 |
DnaA regulatory inactivator Hda; Validated |
18-75 |
6.62e-03 |
|
DnaA regulatory inactivator Hda; Validated
Pssm-ID: 236347 [Multi-domain] Cd Length: 227 Bit Score: 36.88 E-value: 6.62e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 18 GHGAEVV--LRDLDVQLEHGERVALLGASGAGKSTLLEALRSALHEQGTPAAWCPQRQGL 75
Cdd:PRK08903 23 GENAELVarLRELAAGPVADRFFYLWGEAGSGRSHLLQALVADASYGGRNARYLDAASPL 82
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
16-224 |
7.55e-03 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 37.02 E-value: 7.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 16 HLGHGAEVVLRDLDVQleHGERVALLGASGAGKStllealRSAL--HEQGTPAA--------WCPQRQGLVPQLSVYHNI 85
Cdd:NF000106 22 HFGEVKAVDGVDLDVR--EGTVLGVLGP*GAA**------RGALpaHV*GPDAGrrpwrf*tWCANRRALRRTIG*HRPV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 86 FMGRLDQQSSLTNLLNLLR----PRPAHWQAVAAVCEPLGIAGLMERSVEALSGGQRQRVAIARALYQGHDLFLGDEPVA 161
Cdd:NF000106 94 R*GRRESFSGRENLYMIGR*ldlSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTT 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1148626600 162 SVDPHQASQLIHWIHS--RHATSVVALHQ---KELALTHFTRVIglgkdenGNGKVLLDANTDDLKPQ 224
Cdd:NF000106 174 GLDPRTRNEVWDEVRSmvRDGATVLLTTQymeEAEQLAHELTVI-------DRGRVIADGKVDELKTK 234
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
27-183 |
8.55e-03 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 36.51 E-value: 8.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 27 DLDVQleHGERVALLGASGAGKSTLLEALrSALHE--------QGTPAAWCP----QRQGLV---------PQLSVYHNI 85
Cdd:PRK11300 25 NLEVR--EQEIVSLIGPNGAGKTTVFNCL-TGFYKptggtillRGQHIEGLPghqiARMGVVrtfqhvrlfREMTVIENL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 86 FMGRLDQQSSLTNLLNLLRP-----------RPAHWqavaavCEPLGIAGLMERSVEALSGGQRQRVAIARALYQGHDLF 154
Cdd:PRK11300 102 LVAQHQQLKTGLFSGLLKTPafrraesealdRAATW------LERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEIL 175
|
170 180 190
....*....|....*....|....*....|..
gi 1148626600 155 LGDEPVASVDPHQA---SQLIHWIHSRHATSV 183
Cdd:PRK11300 176 MLDEPAAGLNPKETkelDELIAELRNEHNVTV 207
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
25-65 |
8.94e-03 |
|
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: 36.90 E-value: 8.94e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1148626600 25 LRDLDVQLEHGeRVALLGASGAGKSTLLEALRSALHEQGTP 65
Cdd:COG3593 14 IKDLSIELSDD-LTVLVGENNSGKSSILEALRLLLGPSSSR 53
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
38-59 |
9.03e-03 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 36.14 E-value: 9.03e-03
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
39-171 |
9.08e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 37.02 E-value: 9.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 39 ALLGASGAGKSTLLEAL-----------------------RSALhEQGTpaAWCPQRQGLVPQLSVYHNIFMGR------ 89
Cdd:PRK10982 28 ALMGENGAGKSTLLKCLfgiyqkdsgsilfqgkeidfkssKEAL-ENGI--SMVHQELNLVLQRSVMDNMWLGRyptkgm 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626600 90 -LDQQSSltnllnllrprpahWQAVAAVCEPLGIAGLMERSVEALSGGQRQRVAIARALYQGHDLFLGDEPVASVDPHQA 168
Cdd:PRK10982 105 fVDQDKM--------------YRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEV 170
|
...
gi 1148626600 169 SQL 171
Cdd:PRK10982 171 NHL 173
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
130-159 |
9.26e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 37.02 E-value: 9.26e-03
10 20 30
....*....|....*....|....*....|
gi 1148626600 130 VEALSGGQRQRVAIARALYQGHDLFLGDEP 159
Cdd:PRK11819 443 VGVLSGGERNRLHLAKTLKQGGNVLLLDEP 472
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
34-55 |
9.62e-03 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 36.22 E-value: 9.62e-03
|
| |
