|
Name |
Accession |
Description |
Interval |
E-value |
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-236 |
1.73e-113 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 324.71 E-value: 1.73e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 4 LVVKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKMPD--KEVLARVGYMPQ 81
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARdpAEVRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 82 ELALYLNLTVEENLWFYSRLYGLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLILDEPTV 161
Cdd:COG1131 81 EPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1828880889 162 GVDPGLRASFWRYFRELTDEGASILITTHYMDEAVN-CDRVAIVIAGRVLVTATPEEIMAEtgsaTLEEAVLKLTG 236
Cdd:COG1131 161 GLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERlCDRVAIIDKGRIVADGTPDELKAR----LLEDVFLELTG 232
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
4-234 |
1.61e-85 |
|
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: 254.01 E-value: 1.61e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 4 LVVKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGR--KMPDKEVLARVGYMPQ 81
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEdvRKEPREARRQIGVLPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 82 ELALYLNLTVEENLWFYSRLYGLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLILDEPTV 161
Cdd:COG4555 82 ERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTN 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1828880889 162 GVDPGLRASFWRYFRELTDEGASILITTHYMDEAVN-CDRVAIVIAGRVLVTATPEEIMAETGSATLEEAVLKL 234
Cdd:COG4555 162 GLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIGEENLEDAFVAL 235
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-209 |
1.05e-82 |
|
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: 244.23 E-value: 1.05e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 4 LVVKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKMPD--KEVLARVGYMPQ 81
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKepEEVKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 82 ELALYLNLTVEENLwfysrlyglpreeferrkeevlrfvgleefrdrlvaELSGGMQRRASLACALVHEPEFLILDEPTV 161
Cdd:cd03230 81 EPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTS 124
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1828880889 162 GVDPGLRASFWRYFRELTDEGASILITTHYMDEAVN-CDRVAIVIAGRV 209
Cdd:cd03230 125 GLDPESRREFWELLRELKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
4-218 |
1.93e-82 |
|
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: 245.36 E-value: 1.93e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 4 LVVKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLG---RKMPDkEVLARVGYMP 80
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGhdvVREPR-EVRRRIGIVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 81 QELALYLNLTVEENLWFYSRLYGLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLILDEPT 160
Cdd:cd03265 80 QDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 161 VGVDPGLRASFWRYFRELTDE-GASILITTHYMDEAVN-CDRVAIVIAGRVLVTATPEEI 218
Cdd:cd03265 160 IGLDPQTRAHVWEYIEKLKEEfGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-218 |
8.81e-80 |
|
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: 238.56 E-value: 8.81e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 4 LVVKELRKSYGDFE--AVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGR--KMPDKEVLARVGYM 79
Cdd:cd03263 1 LQIRNLTKTYKKGTkpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYsiRTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 80 PQELALYLNLTVEENLWFYSRLYGLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLILDEP 159
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 160 TVGVDPGLRASFWRYFRELTdEGASILITTHYMDEAVN-CDRVAIVIAGRVLVTATPEEI 218
Cdd:cd03263 161 TSGLDPASRRAIWDLILEVR-KGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
2-230 |
2.26e-76 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 247.35 E-value: 2.26e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 2 PALVVKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKMP--DKEVLARVGYM 79
Cdd:NF033858 265 PAIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDagDIATRRRVGYM 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 80 PQELALYLNLTVEENLWFYSRLYGLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLILDEP 159
Cdd:NF033858 345 SQAFSLYGELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEP 424
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1828880889 160 TVGVDPGLRASFWRYFRELT-DEGASILITTHYMDEAVNCDRVAIVIAGRVLVTATPEEIMAETGSATLEEA 230
Cdd:NF033858 425 TSGVDPVARDMFWRLLIELSrEDGVTIFISTHFMNEAERCDRISLMHAGRVLASDTPAALVAARGAATLEEA 496
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
11-228 |
2.42e-76 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 232.67 E-value: 2.42e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 11 KSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKM---PDKeVLARVGYMPQELALYL 87
Cdd:TIGR01188 1 KVYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVvrePRK-VRRSIGIVPQYASVDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 88 NLTVEENLWFYSRLYGLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLILDEPTVGVDPGL 167
Cdd:TIGR01188 80 DLTGRENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1828880889 168 RASFWRYFRELTDEGASILITTHYMDEAVN-CDRVAIVIAGRVLVTATPEEIMAETGSATLE 228
Cdd:TIGR01188 160 RRAIWDYIRALKEEGVTILLTTHYMEEADKlCDRIAIIDHGRIIAEGTPEELKRRLGKDTLE 221
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-228 |
6.07e-76 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 231.54 E-value: 6.07e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 3 ALVVKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKMpDKEVLARVGYMPQE 82
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPL-DPEDRRRIGYLPEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 83 LALYLNLTVEENLWFYSRLYGLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLILDEPTVG 162
Cdd:COG4152 80 RGLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSG 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1828880889 163 VDPGLRASFWRYFRELTDEGASILITTHYMD--EAVnCDRVAIVIAGRVLVTATPEEIMAETGSATLE 228
Cdd:COG4152 160 LDPVNVELLKDVIRELAAKGTTVIFSSHQMElvEEL-CDRIVIINKGRKVLSGSVDEIRRQFGRNTLR 226
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
2-220 |
2.21e-68 |
|
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: 210.22 E-value: 2.21e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 2 PALVVKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKMPD------KEVLAR 75
Cdd:COG1127 4 PMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGlsekelYELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 76 VGYMPQELALYLNLTVEENLWFYSRLY-GLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFL 154
Cdd:COG1127 84 IGMLFQGGALFDSLTVFENVAFPLREHtDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEIL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1828880889 155 ILDEPTVGVDPGLRASFWRYFRELTDE-GASILITTHYMDEAVN-CDRVAIVIAGRVLVTATPEEIMA 220
Cdd:COG1127 164 LYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEELLA 231
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-221 |
6.77e-67 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 206.86 E-value: 6.77e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 1 MPALVVKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRkmPDKEVLARVGYMP 80
Cdd:COG1121 4 MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGK--PPRRARRRIGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 81 QELALYLN--LTVEE----NLWFYSRLYGLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFL 154
Cdd:COG1121 82 QRAEVDWDfpITVRDvvlmGRYGRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1828880889 155 ILDEPTVGVDPGLRASFWRYFRELTDEGASILITTHYMDEAV-NCDRVaIVIAGRVLVTATPEEIMAE 221
Cdd:COG1121 162 LLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVReYFDRV-LLLNRGLVAHGPPEEVLTP 228
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-209 |
4.29e-66 |
|
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: 203.67 E-value: 4.29e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 4 LVVKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKMpDKEVLARVGYMPQEL 83
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPL-DIAARNRIGYLPEER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 84 ALYLNLTVEENLWFYSRLYGLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLILDEPTVGV 163
Cdd:cd03269 80 GLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1828880889 164 DPGLRASFWRYFRELTDEGASILITTHYMDEAVN-CDRVAIVIAGRV 209
Cdd:cd03269 160 DPVNVELLKDVIRELARAGKTVILSTHQMELVEElCDRVLLLNKGRA 206
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
3-234 |
1.43e-63 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 212.68 E-value: 1.43e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 3 ALVVKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKMPDK----EVLARVGY 78
Cdd:NF033858 1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADArhrrAVCPRIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 79 MPQELA--LYLNLTVEENLWFYSRLYGLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLIL 156
Cdd:NF033858 81 MPQGLGknLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 157 DEPTVGVDPGLRASFWryfrELTDE------GASILITTHYMDEAVNCDRVAIVIAGRVLVTATPEEIMAETGSATLEEA 230
Cdd:NF033858 161 DEPTTGVDPLSRRQFW----ELIDRiraerpGMSVLVATAYMEEAERFDWLVAMDAGRVLATGTPAELLARTGADTLEAA 236
|
....
gi 1828880889 231 VLKL 234
Cdd:NF033858 237 FIAL 240
|
|
| PQQ_ABC_ATP |
TIGR03864 |
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of ... |
3-235 |
5.59e-63 |
|
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of this protein family are the ATP-binding subunit of an ABC transporter system that is associated with PQQ biosynthesis and PQQ-dependent alcohol dehydrogenases. While this family shows homology to several efflux ABC transporter subunits, the presence of a periplasmic substrate-binding protein and association with systems for catabolism of alcohols suggests a role in import rather than detoxification. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 274822 [Multi-domain] Cd Length: 236 Bit Score: 196.36 E-value: 5.59e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 3 ALVVKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKMPD--KEVLARVGYMP 80
Cdd:TIGR03864 1 ALEVAGLSFRYGARRALDDVSFTVRPGRFVALLGPNGAGKSTLFSLLTRLYVAQSGQISVAGHDLRRapRAALARLGVVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 81 QELALYLNLTVEENLWFYSRLYGLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLILDEPT 160
Cdd:TIGR03864 81 QQPTLDLDLSVRQNLRYHAALHGLSRAEARARIAELLARLGLAERADDKVRELNGGHRRRVEIARALLHRPALLLLDEPT 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1828880889 161 VGVDPGLRASFWRYFRELT-DEGASILITTHYMDEAVNCDRVAIVIAGRVLVTATPEEIMAETGSATLEEAVLKLT 235
Cdd:TIGR03864 161 VGLDPASRAAITAHVRALArDQGLSVLWATHLVDEIEASDRLVVLHRGRVLADGAAAELRGATGGADLEAAFLALT 236
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
3-221 |
8.48e-62 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 196.98 E-value: 8.48e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 3 ALVVKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKMPDKEVLAR--VGYMP 80
Cdd:PRK13536 41 AIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARarIGVVP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 81 QELALYLNLTVEENLWFYSRLYGLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLILDEPT 160
Cdd:PRK13536 121 QFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPT 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1828880889 161 VGVDPGLRASFWRYFRELTDEGASILITTHYMDEAVN-CDRVAIVIAGRVLVTATPEEIMAE 221
Cdd:PRK13536 201 TGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERlCDRLCVLEAGRKIAEGRPHALIDE 262
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-228 |
1.07e-61 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 195.41 E-value: 1.07e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 2 PALVVKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKMPDKEVLAR--VGYM 79
Cdd:PRK13537 6 APIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARqrVGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 80 PQELALYLNLTVEENLWFYSRLYGLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLILDEP 159
Cdd:PRK13537 86 PQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEP 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1828880889 160 TVGVDPGLRASFWRYFRELTDEGASILITTHYMDEAVN-CDRVAIVIAGRVLVTATPEE-IMAETGSATLE 228
Cdd:PRK13537 166 TTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERlCDRLCVIEEGRKIAEGAPHAlIESEIGCDVIE 236
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-210 |
1.46e-60 |
|
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: 189.35 E-value: 1.46e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 4 LVVKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKMPD-KEVLARVGYMPQE 82
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKnIEALRRIGALIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 83 LALYLNLTVEENLWFYSRLYGLPreefERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLILDEPTVG 162
Cdd:cd03268 81 PGFYPNLTARENLRLLARLLGIR----KKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNG 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1828880889 163 VDPGLRASFWRYFRELTDEGASILITTHYMDE-AVNCDRVAIVIAGRVL 210
Cdd:cd03268 157 LDPDGIKELRELILSLRDQGITVLISSHLLSEiQKVADRIGIINKGKLI 205
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-210 |
3.53e-60 |
|
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: 188.56 E-value: 3.53e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 4 LVVKELRKSYGDFEAVRGLSFEVEKGeIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKMPD--KEVLARVGYMPQ 81
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKqpQKLRRRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 82 ELALYLNLTVEENLWFYSRLYGLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLILDEPTV 161
Cdd:cd03264 80 EFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1828880889 162 GVDPGLRASFWRYFRELTdEGASILITTHYM-DEAVNCDRVAIVIAGRVL 210
Cdd:cd03264 160 GLDPEERIRFRNLLSELG-EDRIVILSTHIVeDVESLCNQVAVLNKGKLV 208
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-221 |
7.94e-60 |
|
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: 188.31 E-value: 7.94e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 4 LVVKELRKSY-GDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKMPDK---EVLARVGYM 79
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKnlrELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 80 PQ--ELALyLNLTVEENLWFYSRLYGLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLILD 157
Cdd:COG1122 81 FQnpDDQL-FAPTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLD 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1828880889 158 EPTVGVDPGLRASFWRYFRELTDEGASILITTHYMDEAV-NCDRVAIVIAGRVLVTATPEEIMAE 221
Cdd:COG1122 160 EPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAeLADRVIVLDDGRIVADGTPREVFSD 224
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
6-222 |
2.66e-59 |
|
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: 186.94 E-value: 2.66e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 6 VKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKMPD------KEVLARVGYM 79
Cdd:cd03261 3 LRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGlseaelYRLRRRMGML 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 80 PQELALYLNLTVEENLWFYSRLYG-LPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLILDE 158
Cdd:cd03261 83 FQSGALFDSLTVFENVAFPLREHTrLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1828880889 159 PTVGVDPGLRASFWRYFRELTDE-GASILITTHYMDEAVN-CDRVAIVIAGRVLVTATPEEIMAET 222
Cdd:cd03261 163 PTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEELRASD 228
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-220 |
2.93e-59 |
|
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: 187.55 E-value: 2.93e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 1 MPALVVKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGR----KMPDKEVLARV 76
Cdd:COG0411 2 DPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRditgLPPHRIARLGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 77 GYMPQELALYLNLTVEENL----------WFYSRLYGLPREEFERRKEE-----VLRFVGLEEFRDRLVAELSGGMQRRA 141
Cdd:COG0411 82 ARTFQNPRLFPELTVLENVlvaaharlgrGLLAALLRLPRARREEREAReraeeLLERVGLADRADEPAGNLSYGQQRRL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 142 SLACALVHEPEFLILDEPTVGVDPGLRASFWRYFRELTDE-GASILITTHYMDeAVN--CDRVAIVIAGRVLVTATPEEI 218
Cdd:COG0411 162 EIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDErGITILLIEHDMD-LVMglADRIVVLDFGRVIAEGTPAEV 240
|
..
gi 1828880889 219 MA 220
Cdd:COG0411 241 RA 242
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
6-210 |
5.32e-59 |
|
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: 185.43 E-value: 5.32e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 6 VKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRkmPDKEVLARVGYMPQ--EL 83
Cdd:cd03235 2 VEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGK--PLEKERKRIGYVPQrrSI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 84 ALYLNLTVEE----NLWFYSRLYGLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLILDEP 159
Cdd:cd03235 80 DRDFPISVRDvvlmGLYGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1828880889 160 TVGVDPGLRASFWRYFRELTDEGASILITTHYMDEAVN-CDRVaIVIAGRVL 210
Cdd:cd03235 160 FAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEyFDRV-LLLNRTVV 210
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-230 |
3.53e-58 |
|
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: 184.86 E-value: 3.53e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 3 ALVVKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGR---KMPDKEVLARVGYM 79
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRdlaSLSRRELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 80 PQELALYLNLTVEENLWF----YSRLYGLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLI 155
Cdd:COG1120 81 PQEPPAPFGLTVRELVALgrypHLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1828880889 156 LDEPTVGVDPGLRASFWRYFRELTDE-GASILITTHYMDEAVN-CDRVAIVIAGRVLVTATPEEIMAEtgsATLEEA 230
Cdd:COG1120 161 LDEPTSHLDLAHQLEVLELLRRLARErGRTVVMVLHDLNLAARyADRLVLLKDGRIVAQGPPEEVLTP---ELLEEV 234
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
4-210 |
1.02e-57 |
|
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: 182.57 E-value: 1.02e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 4 LVVKELRKSYGD----FEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLG---RKMPdKEVLARV 76
Cdd:cd03266 2 ITADALTKRFRDvkktVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfdvVKEP-AEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 77 GYMPQELALYLNLTVEENLWFYSRLYGLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLIL 156
Cdd:cd03266 81 GFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1828880889 157 DEPTVGVDPGLRASFWRYFRELTDEGASILITTHYMDEAVN-CDRVAIVIAGRVL 210
Cdd:cd03266 161 DEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERlCDRVVVLHRGRVV 215
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-218 |
3.21e-57 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 185.30 E-value: 3.21e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 1 MPALVVKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKMPDKEVLAR-VGYM 79
Cdd:COG3842 3 MPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRnVGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 80 PQELALYLNLTVEENLWFYSRLYGLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLILDEP 159
Cdd:COG3842 83 FQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1828880889 160 TVGVDPGLRASFWRYFRELTDE-GASILITTHYMDEAVN-CDRVAIVIAGRVLVTATPEEI 218
Cdd:COG3842 163 LSALDAKLREEMREELRRLQRElGITFIYVTHDQEEALAlADRIAVMNDGRIEQVGTPEEI 223
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-220 |
4.09e-57 |
|
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: 181.20 E-value: 4.09e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 4 LVVKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGR---KMP-DKEVLARVGYM 79
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQditKLPmHKRARLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 80 PQELALYLNLTVEENLWFYSRLYGLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLILDEP 159
Cdd:cd03218 81 PQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1828880889 160 TVGVDPGLRASFWRYFRELTDEGASILITTHYMDEAVN-CDRVAIVIAGRVLVTATPEEIMA 220
Cdd:cd03218 161 FAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSiTDRAYIIYEGKVLAEGTPEEIAA 222
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
5-208 |
8.19e-57 |
|
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: 179.97 E-value: 8.19e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 5 VVKELRKSYGDFE--AVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLG---RKMPDKEVLARVGYM 79
Cdd:cd03225 1 ELKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGkdlTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 80 PQ--ELALyLNLTVEENLWFYSRLYGLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLILD 157
Cdd:cd03225 81 FQnpDDQF-FGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1828880889 158 EPTVGVDPGLRASFWRYFRELTDEGASILITTHYMDEAVN-CDRVAIVIAGR 208
Cdd:cd03225 160 EPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-220 |
1.19e-56 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 180.23 E-value: 1.19e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 1 MPALVVKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGR---KMP-DKEvlAR- 75
Cdd:COG1137 1 MMTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEditHLPmHKR--ARl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 76 -VGYMPQELALYLNLTVEENLWFYSRLYGLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFL 154
Cdd:COG1137 79 gIGYLPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFI 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1828880889 155 ILDEPTVGVDPGLRASFWRYFRELTDEGASILITTHYMDEAVN-CDRVAIVIAGRVLVTATPEEIMA 220
Cdd:COG1137 159 LLDEPFAGVDPIAVADIQKIIRHLKERGIGVLITDHNVRETLGiCDRAYIISEGKVLAEGTPEEILN 225
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-210 |
1.23e-56 |
|
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: 179.64 E-value: 1.23e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 4 LVVKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKMPDKEVLAR-VGYMPQE 82
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRnIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 83 LALYLNLTVEENLWFYSRLYGLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLILDEPTVG 162
Cdd:cd03259 81 YALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1828880889 163 VDPGLRASFWRYFRELTDE-GASILITTHYMDEAVN-CDRVAIVIAGRVL 210
Cdd:cd03259 161 LDAKLREELREELKELQRElGITTIYVTHDQEEALAlADRIAVMNEGRIV 210
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
2-203 |
1.49e-56 |
|
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: 178.83 E-value: 1.49e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 2 PALVVKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGR--KMPDKEVLARVGYM 79
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEpiRDAREDYRRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 80 PQELALYLNLTVEENLWFYSRLYGLPREEFERRKeeVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLILDEP 159
Cdd:COG4133 81 GHADGLKPELTVRENLRFWAALYGLRADREAIDE--ALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEP 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1828880889 160 TVGVDPGLRASFWRYFRELTDEGASILITTHYMDEAVNCDRVAI 203
Cdd:COG4133 159 FTALDAAGVALLAELIAAHLARGGAVLLTTHQPLELAAARVLDL 202
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-220 |
7.64e-56 |
|
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: 178.01 E-value: 7.64e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 4 LVVKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGR----KMPDKEVLARVGYM 79
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEditgLPPHEIARLGIGRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 80 PQELALYLNLTVEENL----------WFYSRLYGLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVH 149
Cdd:cd03219 81 FQIPRLFPELTVLENVmvaaqartgsGLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALAT 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1828880889 150 EPEFLILDEPTVGVDPGLRASFWRYFRELTDEGASILITTHYMDeAVN--CDRVAIVIAGRVLVTATPEEIMA 220
Cdd:cd03219 161 DPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMD-VVMslADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
4-220 |
5.15e-55 |
|
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: 176.31 E-value: 5.15e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 4 LVVKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKMPDKEVLAR----VGYM 79
Cdd:TIGR04406 2 LVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERarlgIGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 80 PQELALYLNLTVEENLW-FYSRLYGLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLILDE 158
Cdd:TIGR04406 82 PQEASIFRKLTVEENIMaVLEIRKDLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLDE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1828880889 159 PTVGVDPGLRASFWRYFRELTDEGASILITTHYMDEAVN-CDRVAIVIAGRVLVTATPEEIMA 220
Cdd:TIGR04406 162 PFAGVDPIAVGDIKKIIKHLKERGIGVLITDHNVRETLDiCDRAYIISDGKVLAEGTPAEIVA 224
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-208 |
1.76e-54 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 175.66 E-value: 1.76e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 1 MPALVVKELRKSY----GDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRkmPDKEVLARV 76
Cdd:COG1116 5 APALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGK--PVTGPGPDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 77 GYMPQELALYLNLTVEENLWFYSRLYGLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLIL 156
Cdd:COG1116 83 GVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLLM 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1828880889 157 DEPTVGVDPGLRASFWRYFREL-TDEGASILITTHYMDEAVN-CDRVaIVIAGR 208
Cdd:COG1116 163 DEPFGALDALTRERLQDELLRLwQETGKTVLFVTHDVDEAVFlADRV-VVLSAR 215
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
4-221 |
2.41e-51 |
|
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: 166.07 E-value: 2.41e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 4 LVVKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKM----PDKEVLARVGYM 79
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDItglpPHERARAGIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 80 PQELALYLNLTVEENLwfysRL--YGLPREEFERRKEEVL-RFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLIL 156
Cdd:cd03224 81 PEGRRIFPELTVEENL----LLgaYARRRAKRKARLERVYeLFPRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1828880889 157 DEPTVGVDPGLRASFWRYFRELTDEGASILITTHYMDEAVN-CDRVAIVIAGRVLVTATPEEIMAE 221
Cdd:cd03224 157 DEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELLAD 222
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-218 |
3.32e-51 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 169.87 E-value: 3.32e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 1 MPALVVKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKMPDKEVLAR-VGYM 79
Cdd:COG3839 1 MASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRnIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 80 PQELALYLNLTVEENLWFYSRLYGLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLILDEP 159
Cdd:COG3839 81 FQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1828880889 160 TVGVDPGLRASFWRYFRELTDE-GASILITTHYMDEAVN-CDRVAIVIAGRVLVTATPEEI 218
Cdd:COG3839 161 LSNLDAKLRVEMRAEIKRLHRRlGTTTIYVTHDQVEAMTlADRIAVMNDGRIQQVGTPEEL 221
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
6-208 |
2.06e-50 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 161.64 E-value: 2.06e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 6 VKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGR---KMPDKEVLARVGYMPQe 82
Cdd:cd00267 2 IENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKdiaKLPLEELRRRIGYVPQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 83 lalylnltveenlwfysrlyglpreeferrkeevlrfvgleefrdrlvaeLSGGMQRRASLACALVHEPEFLILDEPTVG 162
Cdd:cd00267 81 --------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSG 110
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1828880889 163 VDPGLRASFWRYFRELTDEGASILITTHYMDEAVN-CDRVAIVIAGR 208
Cdd:cd00267 111 LDPASRERLLELLRELAEEGRTVIIVTHDPELAELaADRVIVLKDGK 157
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-220 |
5.08e-50 |
|
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: 170.47 E-value: 5.08e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 2 PALVVKELRKSY-----GDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKMPD------K 70
Cdd:COG1123 259 PLLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKlsrrslR 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 71 EVLARVGYMPQELALYLN--LTVEENLWFYSRLYG-LPREEFERRKEEVLRFVGL-EEFRDRLVAELSGGMQRRASLACA 146
Cdd:COG1123 339 ELRRRVQMVFQDPYSSLNprMTVGDIIAEPLRLHGlLSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIARA 418
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1828880889 147 LVHEPEFLILDEPTVGVDPGLRASFWRYFRELTDE-GASILITTHYMDEAVN-CDRVAIVIAGRVLVTATPEEIMA 220
Cdd:COG1123 419 LALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPTEEVFA 494
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-218 |
1.93e-49 |
|
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: 161.64 E-value: 1.93e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 4 LVVKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKMPDKEVLAR-VGYMPQE 82
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRpVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 83 LALYLNLTVEENLWFYSRLYGLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLILDEPTVG 162
Cdd:cd03300 81 YALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1828880889 163 VDPGLRASFWRYFRELTDE-GASILITTHYMDEAVN-CDRVAIVIAGRVLVTATPEEI 218
Cdd:cd03300 161 LDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTmSDRIAVMNKGKIQQIGTPEEI 218
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-208 |
2.30e-49 |
|
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: 161.10 E-value: 2.30e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 4 LVVKELRKSYGD----FEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRkmPDKEVLARVGYM 79
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGE--PVTGPGPDRGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 80 PQELALYLNLTVEENLWFYSRLYGLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLILDEP 159
Cdd:cd03293 79 FQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1828880889 160 TVGVDPGLRASFWRYFREL-TDEGASILITTHYMDEAVN-CDRVaIVIAGR 208
Cdd:cd03293 159 FSALDALTREQLQEELLDIwRETGKTVLLVTHDIDEAVFlADRV-VVLSAR 208
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
6-210 |
3.24e-49 |
|
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: 159.52 E-value: 3.24e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 6 VKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGR---KMPDKEVLARVGYMPQe 82
Cdd:cd03214 2 VENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKdlaSLSPKELARKIAYVPQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 83 lalylnltveenlwfysrlyglpreeferrkeeVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLILDEPTVG 162
Cdd:cd03214 81 ---------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSH 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1828880889 163 VDPGLRASFWRYFRELTDE-GASILITTHYMDEAVN-CDRVAIVIAGRVL 210
Cdd:cd03214 128 LDIAHQIELLELLRRLARErGKTVVMVLHDLNLAARyADRVILLKDGRIV 177
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-220 |
4.02e-49 |
|
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: 160.92 E-value: 4.02e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 1 MPALVVKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKM----PDKEVLARV 76
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDItglpPHRIARLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 77 GYMPQELALYLNLTVEENLwfysRLyGLPREEFERRKEEVLRFVG-----LEEFRDRLVAELSGGMQRRASLACALVHEP 151
Cdd:COG0410 81 GYVPEGRRIFPSLTVEENL----LL-GAYARRDRAEVRADLERVYelfprLKERRRQRAGTLSGGEQQMLAIGRALMSRP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 152 EFLILDEPTVGVDPGLRASFWRYFRELTDEGASILITTHYMDEAVN-CDRVAIVIAGRVLVTATPEEIMA 220
Cdd:COG0410 156 KLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEiADRAYVLERGRIVLEGTAAELLA 225
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
4-209 |
4.19e-49 |
|
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: 160.75 E-value: 4.19e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 4 LVVKELRKSY----GDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGR---KMPDKEVLAR- 75
Cdd:cd03257 2 LEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKdllKLSRRLRKIRr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 76 --VGYMPQELALYLN--LTVEENLWFYSRLYGLPREEFERRKEEVLRFVGL---EEFRDRLVAELSGGMQRRASLACALV 148
Cdd:cd03257 82 keIQMVFQDPMSSLNprMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVglpEEVLNRYPHELSGGQRQRVAIARALA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1828880889 149 HEPEFLILDEPTVGVDPGLRASFWRYFRELTDE-GASILITTHymDEAVN---CDRVAIVIAGRV 209
Cdd:cd03257 162 LNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITH--DLGVVakiADRVAVMYAGKI 224
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
10-210 |
5.60e-49 |
|
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: 160.58 E-value: 5.60e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 10 RKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRkMP---DKEVLARVGY-MPQELAL 85
Cdd:cd03267 28 KRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGL-VPwkrRKKFLRRIGVvFGQKTQL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 86 YLNLTVEENLWFYSRLYGLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLILDEPTVGVDP 165
Cdd:cd03267 107 WWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDV 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1828880889 166 GLRASFWRYFRELT-DEGASILITTHYM-DEAVNCDRVAIVIAGRVL 210
Cdd:cd03267 187 VAQENIRNFLKEYNrERGTTVLLTSHYMkDIEALARRVLVIDKGRLL 233
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-220 |
2.43e-48 |
|
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: 166.23 E-value: 2.43e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 2 PALVVKELRKSY--GDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPD---SGEIELLGR---KMPDKEVL 73
Cdd:COG1123 3 PLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRdllELSEALRG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 74 ARVGYMPQELALYLN-LTVEENLWFYSRLYGLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPE 152
Cdd:COG1123 83 RRIGMVFQDPMTQLNpVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPD 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 153 FLILDEPTVGVDPGLRASFWRYFRELTDE-GASILITTHYMDEAVN-CDRVAIVIAGRVLVTATPEEIMA 220
Cdd:COG1123 163 LLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEILA 232
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
4-238 |
7.52e-48 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 161.08 E-value: 7.52e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 4 LVVKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKMP-DKEVLAR-VGYMPQ 81
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFtNLPPRERrVGFVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 82 ELALYLNLTVEENLWFYSRLYGLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLILDEPTV 161
Cdd:COG1118 83 HYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 162 GVDPGLRASFWRYFRELTDE--GASILItTHYMDEAV-NCDRVAIVIAGRVLVTATPEEIMAETGSAtleeAVLKLTGVK 238
Cdd:COG1118 163 ALDAKVRKELRRWLRRLHDElgGTTVFV-THDQEEALeLADRVVVMNQGRIEQVGTPDEVYDRPATP----FVARFLGCV 237
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
11-193 |
8.65e-48 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 157.14 E-value: 8.65e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 11 KSY-GDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGR---KMPDKEVLA---RVGYMPQEL 83
Cdd:COG2884 9 KRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQdlsRLKRREIPYlrrRIGVVFQDF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 84 ALYLNLTVEENLWFYSRLYGLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLILDEPTVGV 163
Cdd:COG2884 89 RLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLADEPTGNL 168
|
170 180 190
....*....|....*....|....*....|
gi 1828880889 164 DPGLRASFWRYFRELTDEGASILITTHYMD 193
Cdd:COG2884 169 DPETSWEIMELLEEINRRGTTVLIATHDLE 198
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
11-220 |
1.57e-47 |
|
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: 157.08 E-value: 1.57e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 11 KSYGD-FEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLG---RKMPDKEVLARVGYMPQELALY 86
Cdd:cd03295 8 KRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGediREQDPVELRRKIGYVIQQIGLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 87 LNLTVEENLWFYSRLYGLPREEFERRKEEVLRFVGLE--EFRDRLVAELSGGMQRRASLACALVHEPEFLILDEPTVGVD 164
Cdd:cd03295 88 PHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDpaEFADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALD 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1828880889 165 PGLRASFWRYFRELTDE-GASILITTHYMDEAVN-CDRVAIVIAGRVLVTATPEEIMA 220
Cdd:cd03295 168 PITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRlADRIAIMKNGEIVQVGTPDEILR 225
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-232 |
2.08e-47 |
|
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: 156.89 E-value: 2.08e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 3 ALVVKELRKSYG----DFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGR---KMPDKEVLAR 75
Cdd:COG1124 1 MLEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRpvtRRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 76 VGYMPQELALYLN--LTVEENLWFYSRLYGLPREEFERRKeeVLRFVGL-EEFRDRLVAELSGGMQRRASLACALVHEPE 152
Cdd:COG1124 81 VQMVFQDPYASLHprHTVDRILAEPLRIHGLPDREERIAE--LLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALILEPE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 153 FLILDEPTVGVDPGLRASFWRYFRELTDE-GASILITTHymDEAVN---CDRVAIVIAGRVLVTATPEEIMAETGSA--- 225
Cdd:COG1124 159 LLLLDEPTSALDVSVQAEILNLLKDLREErGLTYLFVSH--DLAVVahlCDRVAVMQNGRIVEELTVADLLAGPKHPytr 236
|
....*..
gi 1828880889 226 TLEEAVL 232
Cdd:COG1124 237 ELLAASL 243
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
4-218 |
1.44e-46 |
|
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: 154.42 E-value: 1.44e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 4 LVVKELRKSYGDFEaVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKM----PDKEvlaRVGYM 79
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDItnlpPEKR---DISYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 80 PQELALYLNLTVEENLWFYSRLYGLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLILDEP 159
Cdd:cd03299 77 PQNYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1828880889 160 TVGVDPGLRASFWRYFRELTDE-GASILITTHYMDEA-VNCDRVAIVIAGRVLVTATPEEI 218
Cdd:cd03299 157 FSALDVRTKEKLREELKKIRKEfGVTVLHVTHDFEEAwALADKVAIMLNGKLIQVGKPEEV 217
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-201 |
2.79e-46 |
|
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: 153.03 E-value: 2.79e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 4 LVVKELRKSYGD----FEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGR---KMPDKEvLAR- 75
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTdisKLSEKE-LAAf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 76 ----VGYMPQELALYLNLTVEENLWFYSRLYGLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEP 151
Cdd:cd03255 80 rrrhIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1828880889 152 EFLILDEPTVGVDPGLRASFWRYFRELTDE-GASILITTHYMDEAVNCDRV 201
Cdd:cd03255 160 KIILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHDPELAEYADRI 210
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-208 |
3.88e-46 |
|
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: 151.57 E-value: 3.88e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 4 LVVKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKMPDKEVL-----ARVGY 78
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDElpplrRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 79 MPQELALYLNLTVEENLwfysrlyGLPreeferrkeevlrfvgleefrdrlvaeLSGGMQRRASLACALVHEPEFLILDE 158
Cdd:cd03229 81 VFQDFALFPHLTVLENI-------ALG---------------------------LSGGQQQRVALARALAMDPDVLLLDE 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1828880889 159 PTVGVDPGLRASFWRYFRELTDE-GASILITTHYMDEAVN-CDRVAIVIAGR 208
Cdd:cd03229 127 PTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
9-210 |
7.76e-46 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 155.25 E-value: 7.76e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 9 LRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKmP---DKEVLARVGY-MPQELA 84
Cdd:COG4586 28 FRREYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYV-PfkrRKEFARRIGVvFGQRSQ 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 85 LYLNLTVEENLWFYSRLYGLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGmQR-RASLACALVHEPEFLILDEPTVGV 163
Cdd:COG4586 107 LWWDLPAIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLG-QRmRCELAAALLHRPKILFLDEPTIGL 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1828880889 164 DPGLRASFWRYFREL-TDEGASILITTHYMD--EAVnCDRVaIVIA-GRVL 210
Cdd:COG4586 186 DVVSKEAIREFLKEYnRERGTTILLTSHDMDdiEAL-CDRV-IVIDhGRII 234
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
2-209 |
8.27e-46 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 152.12 E-value: 8.27e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 2 PALVVKELRKSYGD----FEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGR---KMPDKEvLA 74
Cdd:COG1136 3 PLLELRNLTKSYGTgegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQdisSLSERE-LA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 75 R-----VGYMPQELALYLNLTVEENLWFYSRLYGLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVH 149
Cdd:COG1136 82 RlrrrhIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1828880889 150 EPEFLILDEPTVGVDPGLRASFWRYFRELTDE-GASILITTHymDEAV--NCDRVAIVIAGRV 209
Cdd:COG1136 162 RPKLILADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTH--DPELaaRADRVIRLRDGRI 222
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
19-161 |
1.18e-45 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 149.34 E-value: 1.18e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 19 VRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKMPDKE---VLARVGYMPQELALYLNLTVEENL 95
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDErksLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 96 WFYSRLYGLPREEFERRKEEVLRFVGLEEFRDRLV----AELSGGMQRRASLACALVHEPEFLILDEPTV 161
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVgerpGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
3-218 |
3.06e-45 |
|
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: 151.34 E-value: 3.06e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 3 ALVVKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKMPDKEVLAR-VGYMPQ 81
Cdd:cd03296 2 SIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERnVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 82 ELALYLNLTVEENLWF----YSRLYGLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLILD 157
Cdd:cd03296 82 HYALFRHMTVFDNVAFglrvKPRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1828880889 158 EPTVGVDPGLRASFWRYFRELTDE-GASILITTHYMDEAVN-CDRVAIVIAGRVLVTATPEEI 218
Cdd:cd03296 162 EPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEvADRVVVMNKGRIEQVGTPDEV 224
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
7-221 |
8.32e-43 |
|
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: 145.86 E-value: 8.32e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 7 KELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGR---KMPDKEVLA----RVGYM 79
Cdd:cd03294 28 EEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQdiaAMSRKELRElrrkKISMV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 80 PQELALYLNLTVEENLWFYSRLYGLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLILDEP 159
Cdd:cd03294 108 FQSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEA 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1828880889 160 TVGVDPGLRASFWRYFRELTDE-GASILITTHYMDEAVNC-DRVAIVIAGRVLVTATPEEIMAE 221
Cdd:cd03294 188 FSALDPLIRREMQDELLRLQAElQKTIVFITHDLDEALRLgDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-209 |
1.14e-41 |
|
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: 141.24 E-value: 1.14e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 4 LVVKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKMPDKEVLAR-VGYMPQE 82
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRdIAMVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 83 LALYLNLTVEENLWFYSRLYGLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLILDEPTVG 162
Cdd:cd03301 81 YALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSN 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1828880889 163 VDPGLRASFWRYFRELTDE-GASILITTHYMDEAVN-CDRVAIVIAGRV 209
Cdd:cd03301 161 LDAKLRVQMRAELKRLQQRlGTTTIYVTHDQVEAMTmADRIAVMNDGQI 209
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
5-220 |
2.98e-41 |
|
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: 140.79 E-value: 2.98e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 5 VVKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGR---KMPDKEVLA---RVGY 78
Cdd:cd03258 7 VSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTdltLLSGKELRKarrRIGM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 79 MPQELALYLNLTVEENLWFYSRLYGLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLILDE 158
Cdd:cd03258 87 IFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1828880889 159 PTVGVDPGLRASFWRYFRELTDE-GASILITTHYMdEAVN--CDRVAIVIAGRVLVTATPEEIMA 220
Cdd:cd03258 167 ATSALDPETTQSILALLRDINRElGLTIVLITHEM-EVVKriCDRVAVMEKGEVVEEGTVEEVFA 230
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-221 |
8.72e-41 |
|
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: 139.63 E-value: 8.72e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 4 LVVKELRKSYGD-FEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLG---RKMPDKE---VLARV 76
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGtdiNKLKGKAlrqLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 77 GYMPQELALYLNLTVEENLW--------FYSRLYGLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALV 148
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLsgrlgrrsTWRSLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1828880889 149 HEPEFLILDEPTVGVDPGLRASFWRYFRELTDE-GASILITTHYMDEAV-NCDRVAIVIAGRVLVTATPEEIMAE 221
Cdd:cd03256 161 QQPKLILADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDLAReYADRIVGLKDGRIVFDGPPAELTDE 235
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
6-218 |
6.04e-40 |
|
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: 137.31 E-value: 6.04e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 6 VKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLK-----PDSGEIELLGRKMPDK-----EVLAR 75
Cdd:cd03260 3 LRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLdvdvlELRRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 76 VGYMPQELALyLNLTVEENLWFYSRLYG-LPREEFERRKEEVLRFVGL-EEFRDRLVA-ELSGGMQRRASLACALVHEPE 152
Cdd:cd03260 83 VGMVFQKPNP-FPGSIYDNVAYGLRLHGiKLKEELDERVEEALRKAALwDEVKDRLHAlGLSGGQQQRLCLARALANEPE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1828880889 153 FLILDEPTVGVDPGLRASFWRYFRELTDEgASILITTHYMDEAVNC-DRVAIVIAGRVLVTATPEEI 218
Cdd:cd03260 162 VLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVaDRTAFLLNGRLVEFGPTEQI 227
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-221 |
1.65e-39 |
|
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: 138.65 E-value: 1.65e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 4 LVVKELRKSY----GDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKP---DSGEIELLGR---KMPDKEVL 73
Cdd:COG0444 2 LEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEdllKLSEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 74 A----RVGYMPQELALYLN--LTVEENLW-FYSRLYGLPREEFERRKEEVLRFVGLEEFRDRLVA---ELSGGMQRRASL 143
Cdd:COG0444 82 KirgrEIQMIFQDPMTSLNpvMTVGDQIAePLRIHGGLSKAEARERAIELLERVGLPDPERRLDRyphELSGGMRQRVMI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 144 ACALVHEPEFLILDEPTVGVDPGLRASFWRYFRELTDE-GASILITTHymDEAV---NCDRVAIVIAGRVLVTATPEEIM 219
Cdd:COG0444 162 ARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFITH--DLGVvaeIADRVAVMYAGRIVEEGPVEELF 239
|
..
gi 1828880889 220 AE 221
Cdd:COG0444 240 EN 241
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
4-218 |
2.39e-39 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 135.89 E-value: 2.39e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 4 LVVKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKMPDKE-----VLARVGY 78
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKkdinkLRRKVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 79 MPQELALYLNLTVEENL-----WfysrLYGLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEF 153
Cdd:COG1126 82 VFQQFNLFPHLTVLENVtlapiK----VKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1828880889 154 LILDEPTVGVDPGLRASFWRYFRELTDEGASILITTHYMDEAVN-CDRVAIVIAGRVLVTATPEEI 218
Cdd:COG1126 158 MLFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGFAREvADRVVFMDGGRIVEEGPPEEF 223
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
4-221 |
1.59e-38 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 134.05 E-value: 1.59e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 4 LVVKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRkmpdkeVLA----RVGYM 79
Cdd:COG1134 27 LLLRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR------VSAllelGAGFH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 80 PQelalylnLTVEENLWFYSRLYGLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLILDEP 159
Cdd:COG1134 101 PE-------LTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1828880889 160 TVGVDPGLRASFWRYFRELTDEGASILITTHYMDEAVN-CDRVAIVIAGRVLVTATPEEIMAE 221
Cdd:COG1134 174 LAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGDPEEVIAA 236
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
6-201 |
2.14e-38 |
|
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: 132.65 E-value: 2.14e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 6 VKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKMPDK-----EVLARVGYMP 80
Cdd:cd03262 3 IKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDkkninELRQKVGMVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 81 QELALYLNLTVEENLWFYSR-LYGLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLILDEP 159
Cdd:cd03262 83 QQFNLFPHLTVLENITLAPIkVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEP 162
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1828880889 160 TVGVDPGLRASFWRYFRELTDEGASILITTHYMDEAVN-CDRV 201
Cdd:cd03262 163 TSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREvADRV 205
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
4-234 |
3.21e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 134.05 E-value: 3.21e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 4 LVVKELRKSYGD-FEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKMP-DK----EVLARVG 77
Cdd:PRK13639 2 LETRDLKYSYPDgTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKyDKksllEVRKTVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 78 YMPQELALYL-NLTVEENLWFYSRLYGLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLIL 156
Cdd:PRK13639 82 IVFQNPDDQLfAPTVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1828880889 157 DEPTVGVDPGLRASFWRYFRELTDEGASILITTHYMDEA-VNCDRVAIVIAGRVLVTATPEEIMAEtgSATLEEAVLKL 234
Cdd:PRK13639 162 DEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVpVYADKVYVMSDGKIIKEGTPKEVFSD--IETIRKANLRL 238
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
12-201 |
5.53e-38 |
|
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: 131.61 E-value: 5.53e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 12 SYGDF-EAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKMPDKEVLARVGYMPQELALYL-NL 89
Cdd:cd03226 8 SYKKGtEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERRKSIGYVMQDVDYQLfTD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 90 TVEENLwfysrLYGLPREEFERRKE-EVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLILDEPTVGVDPGLR 168
Cdd:cd03226 88 SVREEL-----LLGLKELDAGNEQAeTVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNM 162
|
170 180 190
....*....|....*....|....*....|....
gi 1828880889 169 ASFWRYFRELTDEGASILITTHYMDEAVN-CDRV 201
Cdd:cd03226 163 ERVGELIRELAAQGKAVIVITHDYEFLAKvCDRV 196
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-221 |
1.78e-37 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 131.17 E-value: 1.78e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 1 MPALVVKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKMPDKEVLAR----V 76
Cdd:PRK10895 1 MATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARarrgI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 77 GYMPQELALYLNLTVEENLWFYSRL-YGLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLI 155
Cdd:PRK10895 81 GYLPQEASIFRRLSVYDNLMAVLQIrDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1828880889 156 LDEPTVGVDPGLRASFWRYFRELTDEGASILITTHYMDEAVN-CDRVAIVIAGRVLVTATPEEIMAE 221
Cdd:PRK10895 161 LDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAvCERAYIVSQGHLIAHGTPTEILQD 227
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1-215 |
4.38e-37 |
|
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: 138.22 E-value: 4.38e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 1 MPALVVKELRKSYGDF--EAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKMPDKEVLAR--V 76
Cdd:TIGR01257 926 VPGVCVKNLVKIFEPSgrPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRqsL 1005
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 77 GYMPQELALYLNLTVEENLWFYSRLYGLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLIL 156
Cdd:TIGR01257 1006 GMCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVL 1085
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 157 DEPTVGVDPGLRASFWRYFRELTdEGASILITTHYMDEA-VNCDRVAIVIAGRVLVTATP 215
Cdd:TIGR01257 1086 DEPTSGVDPYSRRSIWDLLLKYR-SGRTIIMSTHHMDEAdLLGDRIAIISQGRLYCSGTP 1144
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
12-230 |
5.91e-37 |
|
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: 130.20 E-value: 5.91e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 12 SYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSG-EIELLGRKMPDKEVL---ARVGYMPQELALYL 87
Cdd:COG1119 12 RRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWelrKRIGLVSPALQLRF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 88 --NLTVEENLW--FYS--RLYGLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLILDEPTV 161
Cdd:COG1119 92 prDETVLDVVLsgFFDsiGLYREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTA 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1828880889 162 GVDPGLRASFWRYFRELTDEGA-SILITTHYMDEAVNC-DRVAIVIAGRVLVTATPEEIMAetgSATLEEA 230
Cdd:COG1119 172 GLDLGARELLLALLDKLAAEGApTLVLVTHHVEEIPPGiTHVLLLKDGRVVAAGPKEEVLT---SENLSEA 239
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
6-226 |
6.88e-37 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 132.12 E-value: 6.88e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 6 VKELRKSY----GDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGR---KMPDKEVLA---R 75
Cdd:COG1135 4 LENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVdltALSERELRAarrK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 76 VGYMPQELALYLNLTVEENLWFYSRLYGLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLI 155
Cdd:COG1135 84 IGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKVLL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1828880889 156 LDEPTVGVDPGLRASFWRYFRELTDE-GASILITTHYMD--EAVnCDRVAIVIAGRVLVTATPEEIMAETGSAT 226
Cdd:COG1135 164 CDEATSALDPETTRSILDLLKDINRElGLTIVLITHEMDvvRRI-CDRVAVLENGRIVEQGPVLDVFANPQSEL 236
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
10-209 |
7.34e-37 |
|
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: 129.19 E-value: 7.34e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 10 RKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKMPdkeVLA-RVGYMPqelalylN 88
Cdd:cd03220 29 KGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSS---LLGlGGGFNP-------E 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 89 LTVEENLWFYSRLYGLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLILDEPTVGVDPGLR 168
Cdd:cd03220 99 LTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQ 178
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1828880889 169 ASFWRYFRELTDEGASILITTHYMDEAVN-CDRVAIVIAGRV 209
Cdd:cd03220 179 EKCQRRLRELLKQGKTVILVSHDPSSIKRlCDRALVLEKGKI 220
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4-209 |
7.83e-37 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 128.40 E-value: 7.83e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 4 LVVKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKMPDKEVLA---RVGYMP 80
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEwrrQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 81 QELALYLNlTVEENLWFYSRLYGLPREEFERRKeeVLRFVGL-EEFRDRLVAELSGGMQRRASLACALVHEPEFLILDEP 159
Cdd:COG4619 81 QEPALWGG-TVRDNLPFPFQLRERKFDRERALE--LLERLGLpPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1828880889 160 TVGVDPGLRASFWRYFREL-TDEGASILITTHYMDEAVN-CDRVAIVIAGRV 209
Cdd:COG4619 158 TSALDPENTRRVEELLREYlAEEGRAVLWVSHDPEQIERvADRVLTLEAGRL 209
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2-220 |
1.98e-36 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 133.99 E-value: 1.98e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 2 PALVVKELRKSygdfEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKM----PDKEVLARVG 77
Cdd:COG1129 255 VVLEVEGLSVG----GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVrirsPRDAIRAGIA 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 78 YMP---QELALYLNLTVEENLWF--YSRLYGLPREEFERRKEEVLRFVglEEFR------DRLVAELSGGMQRRASLACA 146
Cdd:COG1129 331 YVPedrKGEGLVLDLSIRENITLasLDRLSRGGLLDRRRERALAEEYI--KRLRiktpspEQPVGNLSGGNQQKVVLAKW 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 147 LVHEPEFLILDEPTVGVDPGLRASFWRYFRELTDEGASILITTHYMDEAV-NCDRVAIVIAGRVlV------TATPEEIM 219
Cdd:COG1129 409 LATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSELPELLgLSDRILVMREGRI-VgeldreEATEEAIM 487
|
.
gi 1828880889 220 A 220
Cdd:COG1129 488 A 488
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-209 |
2.68e-36 |
|
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: 126.39 E-value: 2.68e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 2 PALVVKELRKSYgdfeAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKM----PDKEVLARVG 77
Cdd:cd03215 3 PVLEVRGLSVKG----AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVtrrsPRDAIRAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 78 YMP---QELALYLNLTVEENLwfysrlyglpreeferrkeeVLRFVgleefrdrlvaeLSGGMQRRASLACALVHEPEFL 154
Cdd:cd03215 79 YVPedrKREGLVLDLSVAENI--------------------ALSSL------------LSGGNQQKVVLARWLARDPRVL 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1828880889 155 ILDEPTVGVDPGLRASFWRYFRELTDEGASILITTHYMDEAVN-CDRVAIVIAGRV 209
Cdd:cd03215 127 ILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGlCDRILVMYEGRI 182
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
4-221 |
4.18e-36 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 128.21 E-value: 4.18e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 4 LVVKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGR---KMPDKEVLARVGYMP 80
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKpisMLSSRQLARRLALLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 81 QELALYLNLTVEEnLWFYSR-----LYGLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLI 155
Cdd:PRK11231 83 QHHLTPEGITVRE-LVAYGRspwlsLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1828880889 156 LDEPTVGVDPGLRASFWRYFRELTDEGASILITTHYMDEAVN-CDRVAIVIAGRVLVTATPEEIMAE 221
Cdd:PRK11231 162 LDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRyCDHLVVLANGHVMAQGTPEEVMTP 228
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
4-227 |
1.38e-35 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 126.02 E-value: 1.38e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 4 LVVKELRKSYGDFEAvrGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKMPDKEVLAR-VGYMPQE 82
Cdd:COG3840 2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERpVSMLFQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 83 LALYLNLTVEENLWFysrlyGL-----PREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLILD 157
Cdd:COG3840 80 NNLFPHLTVAQNIGL-----GLrpglkLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLD 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1828880889 158 EPTVGVDPGLRASFWRYFRELTDE-GASILITTHYMDEAVN-CDRVAIVIAGRVLVTATPEEIMAETGSATL 227
Cdd:COG3840 155 EPFSALDPALRQEMLDLVDELCRErGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLDGEPPPAL 226
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-208 |
2.96e-35 |
|
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: 123.26 E-value: 2.96e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 4 LVVKELRKSYGDF--EAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLG---RKMPDKEVLARVGY 78
Cdd:cd03228 1 IEFKNVSFSYPGRpkPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGvdlRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 79 MPQELALYlNLTVEENLwfysrlyglpreeferrkeevlrfvgleefrdrlvaeLSGGMQRRASLACALVHEPEFLILDE 158
Cdd:cd03228 81 VPQDPFLF-SGTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1828880889 159 PTVGVDPGLRASFWRYFRELTDEGASILItTHYMDEAVNCDRVAIVIAGR 208
Cdd:cd03228 123 ATSALDPETEALILEALRALAKGKTVIVI-AHRLSTIRDADRIIVLDDGR 171
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-212 |
3.55e-35 |
|
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: 122.92 E-value: 3.55e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 4 LVVKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKmpdkevlarvgympqel 83
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKE----------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 84 alylnltveenlwfysrlyglpreeferrkeevLRFVGLEEFRD---RLVAELSGGMQRRASLACALVHEPEFLILDEPT 160
Cdd:cd03216 64 ---------------------------------VSFASPRDARRagiAMVYQLSVGERQMVEIARALARNARLLILDEPT 110
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1828880889 161 VGVDPGLRASFWRYFRELTDEGASILITTHYMDEAVN-CDRVAIVIAGRVLVT 212
Cdd:cd03216 111 AALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEiADRVTVLRDGRVVGT 163
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-218 |
5.13e-35 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 130.14 E-value: 5.13e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 1 MPALVVKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKMPDKEVL----ARV 76
Cdd:COG1129 2 EPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRdaqaAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 77 GYMPQELALYLNLTVEENLWF---YSRLYGLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEF 153
Cdd:COG1129 82 AIIHQELNLVPNLSVAENIFLgrePRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1828880889 154 LILDEPTVGVDPGLRASFWRYFRELTDEGASILITTHYMDEAVN-CDRVAIVIAGRVLVTATPEEI 218
Cdd:COG1129 162 LILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEiADRVTVLRDGRLVGTGPVAEL 227
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
4-223 |
5.51e-35 |
|
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: 132.06 E-value: 5.51e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 4 LVVKELRKSYGDFE--AVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKMPDK--EVLARVGYM 79
Cdd:TIGR01257 1938 LRLNELTKVYSGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNisDVHQNMGYC 2017
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 80 PQELALYLNLTVEENLWFYSRLYGLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLILDEP 159
Cdd:TIGR01257 2018 PQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEP 2097
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1828880889 160 TVGVDPGLRASFWRYFRELTDEGASILITTHYMDEA-VNCDRVAIVIAGRVLVTATPEEIMAETG 223
Cdd:TIGR01257 2098 TTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECeALCTRLAIMVKGAFQCLGTIQHLKSKFG 2162
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-217 |
9.71e-35 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 129.38 E-value: 9.71e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 1 MPALVVKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKM----PDKEVLARV 76
Cdd:COG3845 3 PPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVrirsPRDAIALGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 77 GYMPQELALYLNLTVEENLWfysrlYGLPREEFERRKEEVLRfvglEEFR------------DRLVAELSGGMQRRASLA 144
Cdd:COG3845 83 GMVHQHFMLVPNLTVAENIV-----LGLEPTKGGRLDRKAAR----ARIRelserygldvdpDAKVEDLSVGEQQRVEIL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1828880889 145 CALVHEPEFLILDEPTVGVDPGLRASFWRYFRELTDEGASILITTHYMDE--AVnCDRVAIVIAGRVLVTATPEE 217
Cdd:COG3845 154 KALYRGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREvmAI-ADRVTVLRRGKVVGTVDTAE 227
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-221 |
1.49e-34 |
|
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: 129.15 E-value: 1.49e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 2 PALVVKELRKSY-----GDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIE-LLGRK---MPDKEV 72
Cdd:TIGR03269 278 PIIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvRVGDEwvdMTKPGP 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 73 LAR------VGYMPQELALYLNLTVEENLWFYSRLyGLPREEFERRKEEVLRFVGLEEFR-----DRLVAELSGGMQRRA 141
Cdd:TIGR03269 358 DGRgrakryIGILHQEYDLYPHRTVLDNLTEAIGL-ELPDELARMKAVITLKMVGFDEEKaeeilDKYPDELSEGERHRV 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 142 SLACALVHEPEFLILDEPTVGVDPGLRASFWRYFRELTDE-GASILITTHYMDEAVN-CDRVAIVIAGRVLVTATPEEIM 219
Cdd:TIGR03269 437 ALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEmEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIV 516
|
..
gi 1828880889 220 AE 221
Cdd:TIGR03269 517 EE 518
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-220 |
3.39e-34 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 123.59 E-value: 3.39e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 2 PALVVKELRKSYGDFE--AVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKMPDK---EVLARV 76
Cdd:PRK13635 4 EIIRVEHISFRYPDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEEtvwDVRRQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 77 GYMPQEL-ALYLNLTVEENLWFYSRLYGLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLI 155
Cdd:PRK13635 84 GMVFQNPdNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIII 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1828880889 156 LDEPTVGVDPGLRASFWRYFRELTDE-GASILITTHYMDEAVNCDRVAIVIAGRVLVTATPEEIMA 220
Cdd:PRK13635 164 LDEATSMLDPRGRREVLETVRQLKEQkGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFK 229
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-230 |
3.57e-34 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 122.92 E-value: 3.57e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 4 LVVKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKMPD--KEVLARV-GYMP 80
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAwsPWELARRrAVLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 81 QELALYLNLTVEENLwfysRL----YGLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACAL--VHEPE-- 152
Cdd:COG4559 82 QHSSLAFPFTVEEVV----ALgrapHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLaqLWEPVdg 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 153 ---FLILDEPTVGVDPG-----LRASfwryfRELTDEGASILITTHymDeaVN-----CDRVAIVIAGRVLVTATPEEIM 219
Cdd:COG4559 158 gprWLFLDEPTSALDLAhqhavLRLA-----RQLARRGGGVVAVLH--D--LNlaaqyADRILLLHQGRLVAQGTPEEVL 228
|
250
....*....|.
gi 1828880889 220 AEtgsATLEEA 230
Cdd:COG4559 229 TD---ELLERV 236
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
12-203 |
4.28e-34 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 120.80 E-value: 4.28e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 12 SYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRkmpdkevlARVGYMPQELAL--YLNL 89
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGG--------ARVAYVPQRSEVpdSLPL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 90 TVEE----NLWFYSRLYGLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLILDEPTVGVDP 165
Cdd:NF040873 73 TVRDlvamGRWARRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDA 152
|
170 180 190
....*....|....*....|....*....|....*...
gi 1828880889 166 GLRASFWRYFRELTDEGASILITTHYMDEAVNCDRVAI 203
Cdd:NF040873 153 ESRERIIALLAEEHARGATVVVVTHDLELVRRADPCVL 190
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
22-210 |
4.93e-34 |
|
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: 121.63 E-value: 4.93e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 22 LSFEVEkGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKMPDKEVLA-------RVGYMPQELALYLNLTVEEN 94
Cdd:cd03297 17 IDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKInlppqqrKIGLVFQQYALFPHLNVREN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 95 LwfysrLYGLPREEFERRKEEV---LRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLILDEPTVGVDPGLRASF 171
Cdd:cd03297 96 L-----AFGLKRKRNREDRISVdelLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1828880889 172 WRYFREL-TDEGASILITTHYMDEAVN-CDRVAIVIAGRVL 210
Cdd:cd03297 171 LPELKQIkKNLNIPVIFVTHDLSEAEYlADRIVVMEDGRLQ 211
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
9-220 |
7.06e-34 |
|
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: 124.84 E-value: 7.06e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 9 LRKSYGDFEAvrGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKMPDKEVLA-------RVGYMPQ 81
Cdd:TIGR02142 5 FSKRLGDFSL--DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIflppekrRIGYVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 82 ELALYLNLTVEENLwfysrLYGLP---REEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLILDE 158
Cdd:TIGR02142 83 EARLFPHLSVRGNL-----RYGMKrarPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1828880889 159 PTVGVDPGLRASFWRYFRELTDE-GASILITTHYMDE-AVNCDRVAIVIAGRVLVTATPEEIMA 220
Cdd:TIGR02142 158 PLAALDDPRKYEILPYLERLHAEfGIPILYVSHSLQEvLRLADRVVVLEDGRVAAAGPIAEVWA 221
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-223 |
7.62e-34 |
|
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: 127.57 E-value: 7.62e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 2 PALVVKELRKSY--GDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLG---RKMPDKEVLARV 76
Cdd:COG4987 332 PSLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGvdlRDLDEDDLRRRI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 77 GYMPQELALyLNLTVEENLwfysrLYGLPREEFERRKEeVLRFVGLEEFRDRL-------VAE----LSGGMQRRASLAC 145
Cdd:COG4987 412 AVVPQRPHL-FDTTLRENL-----RLARPDATDEELWA-ALERVGLGDWLAALpdgldtwLGEggrrLSGGERRRLALAR 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1828880889 146 ALVHEPEFLILDEPTVGVDPGLRASFWRYFRELTdEGASILITTHYMDEAVNCDRVAIVIAGRVLVTATPEEIMAETG 223
Cdd:COG4987 485 ALLRDAPILLLDEPTEGLDAATEQALLADLLEAL-AGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQNG 561
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
6-229 |
1.06e-33 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 121.73 E-value: 1.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 6 VKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGR---KMPDKEVLARVGYMPQE 82
Cdd:COG4604 4 IKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLdvaTTPSRELAKRLAILRQE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 83 LALYLNLTVEENLWF----YSRlyGLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGmQR-RASLACALVHEPEFLILD 157
Cdd:COG4604 84 NHINSRLTVRELVAFgrfpYSK--GRLTAEDREIIDEAIAYLDLEDLADRYLDELSGG-QRqRAFIAMVLAQDTDYVLLD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1828880889 158 EPTVGVDPGLRASFWRYFRELTDE-GASILITTHYMDEAVN-CDRVAIVIAGRVLVTATPEEIMAEtgsATLEE 229
Cdd:COG4604 161 EPLNNLDMKHSVQMMKLLRRLADElGKTVVIVLHDINFASCyADHIVAMKDGRVVAQGTPEEIITP---EVLSD 231
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-230 |
1.39e-33 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 124.95 E-value: 1.39e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 1 MPALVVKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKMPD---KEVLARVG 77
Cdd:PRK09536 1 MPMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEAlsaRAASRRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 78 YMPQELALYLNLTVEENLWF-----YSRLYGLPREEFERRKEEVLRfVGLEEFRDRLVAELSGGMQRRASLACALVHEPE 152
Cdd:PRK09536 81 SVPQDTSLSFEFDVRQVVEMgrtphRSRFDTWTETDRAAVERAMER-TGVAQFADRPVTSLSGGERQRVLLARALAQATP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1828880889 153 FLILDEPTVGVDPGLRASFWRYFRELTDEGASILITTHYMDEAVN-CDRVAIVIAGRVLVTATPEEIMAetgSATLEEA 230
Cdd:PRK09536 160 VLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARyCDELVLLADGRVRAAGPPADVLT---ADTLRAA 235
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
4-190 |
1.83e-33 |
|
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: 119.39 E-value: 1.83e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 4 LVVKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELlgrkmpDKEVLARVGYMPQEL 83
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRW------NGTPLAEQRDEPHEN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 84 ALYLN--------LTVEENLWFYSRLYGlpreEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLI 155
Cdd:TIGR01189 75 ILYLGhlpglkpeLSALENLHFWAAIHG----GAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWI 150
|
170 180 190
....*....|....*....|....*....|....*
gi 1828880889 156 LDEPTVGVDPGLRASFWRYFRELTDEGASILITTH 190
Cdd:TIGR01189 151 LDEPTTALDKAGVALLAGLLRAHLARGGIVLLTTH 185
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
4-190 |
2.24e-33 |
|
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: 119.82 E-value: 2.24e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 4 LVVKELRKSY-GDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGR---KMPDKEV--LAR-V 76
Cdd:cd03292 1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQdvsDLRGRAIpyLRRkI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 77 GYMPQELALYLNLTVEENLWFYSRLYGLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLIL 156
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160
|
170 180 190
....*....|....*....|....*....|....
gi 1828880889 157 DEPTVGVDPGLRASFWRYFRELTDEGASILITTH 190
Cdd:cd03292 161 DEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATH 194
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
19-190 |
3.11e-33 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 118.81 E-value: 3.11e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 19 VRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKP--DSGEIELLGRKMPDKEVLARVGYMPQELALYLNLTVEENLW 96
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRPLDKRSFRKIIGYVPQDDILHPTLTVRETLM 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 97 FYSRLYGlpreeferrkeevlrfvgleefrdrlvaeLSGGMQRRASLACALVHEPEFLILDEPTVGVDPGLRASFWRYFR 176
Cdd:cd03213 105 FAAKLRG-----------------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLR 155
|
170
....*....|....
gi 1828880889 177 ELTDEGASILITTH 190
Cdd:cd03213 156 RLADTGRTIICSIH 169
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
21-190 |
3.81e-33 |
|
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: 119.68 E-value: 3.81e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 21 GLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPD---SGEIELLGRKMPDKEVLARVGYMPQELALYLNLTVEENLWF 97
Cdd:cd03234 25 DVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQPRKPDQFQKCVAYVRQDDILLPGLTVRETLTY 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 98 YSRLyGLP-----REEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLILDEPTVGVDPGLRASFW 172
Cdd:cd03234 105 TAIL-RLPrkssdAIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNLV 183
|
170
....*....|....*...
gi 1828880889 173 RYFRELTDEGASILITTH 190
Cdd:cd03234 184 STLSQLARRNRIVILTIH 201
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-233 |
1.30e-32 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 121.87 E-value: 1.30e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 1 MPALVVKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKMPDKEVLAR-VGYM 79
Cdd:PRK11607 17 TPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRpINMM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 80 PQELALYLNLTVEENLWFYSRLYGLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLILDEP 159
Cdd:PRK11607 97 FQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 160 TVGVDPGLRAsfwRYFRELTD----EGASILITTHYMDEAVN-CDRVAIVIAGRVLVTATPEEIM--------AE-TGSA 225
Cdd:PRK11607 177 MGALDKKLRD---RMQLEVVDilerVGVTCVMVTHDQEEAMTmAGRIAIMNRGKFVQIGEPEEIYehpttrysAEfIGSV 253
|
....*...
gi 1828880889 226 TLEEAVLK 233
Cdd:PRK11607 254 NVFEGVLK 261
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
17-229 |
1.49e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 119.77 E-value: 1.49e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 17 EAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEI-----ELLGRKMPDKEVLARVGYMPQ--ELALYLNl 89
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIiidgvDITDKKVKLSDIRKKVGLVFQypEYQLFEE- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 90 TVEENLWFYSRLYGLPREEFERRKEEVLRFVGL--EEFRDRLVAELSGGMQRRASLACALVHEPEFLILDEPTVGVDPGL 167
Cdd:PRK13637 100 TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLdyEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKG 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1828880889 168 RASFWRYFRELTDE-GASILITTHYM-DEAVNCDRVAIVIAGRVLVTATPEEIMAETgsATLEE 229
Cdd:PRK13637 180 RDEILNKIKELHKEyNMTIILVSHSMeDVAKLADRIIVMNKGKCELQGTPREVFKEV--ETLES 241
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
2-219 |
2.07e-32 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 118.34 E-value: 2.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 2 PALVVKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGR---KMPDKEVLARVGY 78
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRplaDWSPAELARRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 79 MPQELALYLNLTVEENLWFYSRLYGLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALV------HEPE 152
Cdd:PRK13548 81 LPQHSSLSFPFTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPPR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1828880889 153 FLILDEPTVGVDPG-----LRASfwryfRELTDE-GASILITTHYMDEAVN-CDRVAIVIAGRVLVTATPEEIM 219
Cdd:PRK13548 161 WLLLDEPTSALDLAhqhhvLRLA-----RQLAHErGLAVIVVLHDLNLAARyADRIVLLHQGRLVADGTPAEVL 229
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
6-222 |
2.50e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 119.42 E-value: 2.50e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 6 VKELRKSYG-----DFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELL----------------- 63
Cdd:PRK13651 5 VKNIVKIFNkklptELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIfkdeknkkktkekekvl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 64 ---------GRKMPD-KEVLARVGYMPQ--ELALYlNLTVEENLWFYSRLYGLPREEFERRKEEVLRFVGL-EEFRDRLV 130
Cdd:PRK13651 85 eklviqktrFKKIKKiKEIRRRVGVVFQfaEYQLF-EQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLdESYLQRSP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 131 AELSGGMQRRASLACALVHEPEFLILDEPTVGVDPGLRASFWRYFRELTDEGASILITTHYMDEAVN-CDRVAIVIAGRV 209
Cdd:PRK13651 164 FELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEwTKRTIFFKDGKI 243
|
250
....*....|...
gi 1828880889 210 LVTATPEEIMAET 222
Cdd:PRK13651 244 IKDGDTYDILSDN 256
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
4-217 |
2.54e-32 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 116.81 E-value: 2.54e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 4 LVVKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPD---SGEIELLGRKMPDKEVLAR-VGYM 79
Cdd:COG4136 2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPAEQRrIGIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 80 PQELALYLNLTVEENLWFysrlyGLPREEFE----RRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLI 155
Cdd:COG4136 82 FQDDLLFPHLSVGENLAF-----ALPPTIGRaqrrARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1828880889 156 LDEPTVGVDPGLRASFWRY-FRELTDEGASILITTHymDEAvncDRVAiviAGRVLVTATPEE 217
Cdd:COG4136 157 LDEPFSKLDAALRAQFREFvFEQIRQRGIPALLVTH--DEE---DAPA---AGRVLDLGNWQH 211
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-223 |
6.06e-32 |
|
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: 122.17 E-value: 6.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 2 PALVVKELRKSYGD-FEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKMPD---KEVLARVG 77
Cdd:COG4988 335 PSIELEDVSFSYPGgRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDldpASWRRQIA 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 78 YMPQELALyLNLTVEENLWFYSRlyglprEEFERRKEEVLRFVGLEEFRDRL-------VAE----LSGGMQRRASLACA 146
Cdd:COG4988 415 WVPQNPYL-FAGTIRENLRLGRP------DASDEELEAALEAAGLDEFVAALpdgldtpLGEggrgLSGGQAQRLALARA 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1828880889 147 LVHEPEFLILDEPTVGVDPGLRASFWRYFRELTdEGASILITTHYMDEAVNCDRVAIVIAGRVLVTATPEEIMAETG 223
Cdd:COG4988 488 LLRDAPLLLLDEPTAHLDAETEAEILQALRRLA-KGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
2-218 |
7.50e-32 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 117.01 E-value: 7.50e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 2 PALVVKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRK---MPDKEVlARVGY 78
Cdd:PRK11300 4 PLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHiegLPGHQI-ARMGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 79 MP--QELALYLNLTVEENLW----------FYSRLYGLPR-----EEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRA 141
Cdd:PRK11300 83 VRtfQHVRLFREMTVIENLLvaqhqqlktgLFSGLLKTPAfrraeSEALDRAATWLERVGLLEHANRQAGNLAYGQQRRL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1828880889 142 SLACALVHEPEFLILDEPTVGVDPGLRASFWRYFRELTDE-GASILITTHYMDEAVN-CDRVAIVIAGRVLVTATPEEI 218
Cdd:PRK11300 163 EIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEI 241
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
4-190 |
1.26e-31 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 114.97 E-value: 1.26e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 4 LVVKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKMPDKEVLARVGYMPQEL 83
Cdd:PRK13539 3 LEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLGHRN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 84 ALYLNLTVEENLWFYSRLYGlpreEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLILDEPTVGV 163
Cdd:PRK13539 83 AMKPALTVAENLEFWAAFLG----GEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAAL 158
|
170 180
....*....|....*....|....*..
gi 1828880889 164 DPGLRASFWRYFRELTDEGASILITTH 190
Cdd:PRK13539 159 DAAAVALFAELIRAHLAQGGIVIAATH 185
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
19-220 |
1.36e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 116.75 E-value: 1.36e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 19 VRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKMPDKEVLA---RVGYMPQEL-ALYLNLTVEEN 94
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDirhKIGMVFQNPdNQFVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 95 LWFYSRLYGLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLILDEPTVGVDPGLRASFWRY 174
Cdd:PRK13650 103 VAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKT 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1828880889 175 FRELTDE-GASILITTHYMDEAVNCDRVAIVIAGRVLVTATPEEIMA 220
Cdd:PRK13650 183 IKGIRDDyQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFS 229
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
4-229 |
2.72e-31 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 115.45 E-value: 2.72e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 4 LVVKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGR------------KMPDKE 71
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQtinlvrdkdgqlKVADKN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 72 VL----ARVGYMPQELALYLNLTVEENLWFYS-RLYGLPREEFERRKEEVLRFVGLEE-FRDRLVAELSGGMQRRASLAC 145
Cdd:PRK10619 86 QLrllrTRLTMVFQHFNLWSHMTVLENVMEAPiQVLGLSKQEARERAVKYLAKVGIDErAQGKYPVHLSGGQQQRVSIAR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 146 ALVHEPEFLILDEPTVGVDPGLRASFWRYFRELTDEGASILITTHYMDEAVNCDRVAIVI-AGRVLVTATPEEIMAETGS 224
Cdd:PRK10619 166 ALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLhQGKIEEEGAPEQLFGNPQS 245
|
....*
gi 1828880889 225 ATLEE 229
Cdd:PRK10619 246 PRLQQ 250
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-221 |
2.87e-31 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 118.13 E-value: 2.87e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 1 MPALVVKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKMPDKEVLAR-VGYM 79
Cdd:PRK09452 12 SPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRhVNTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 80 PQELALYLNLTVEENLWFYSRLYGLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLILDEP 159
Cdd:PRK09452 92 FQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDES 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1828880889 160 TVGVDPGLRASFWRYFRELTDE-GASILITTHYMDEAVN-CDRVAIVIAGRVLVTATPEEIMAE 221
Cdd:PRK09452 172 LSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTmSDRIVVMRDGRIEQDGTPREIYEE 235
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
6-210 |
4.05e-31 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 114.72 E-value: 4.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 6 VKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLG------RKMPDKEVLA---RV 76
Cdd:COG4161 5 LKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsQKPSEKAIRLlrqKV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 77 GYMPQELALYLNLTVEENLWFYS-RLYGLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLI 155
Cdd:COG4161 85 GMVFQQYNLWPHLTVMENLIEAPcKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1828880889 156 LDEPTVGVDPGLRASFWRYFRELTDEGASILITTHYMDeavncdrVAIVIAGRVL 210
Cdd:COG4161 165 FDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVE-------FARKVASQVV 212
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-223 |
1.16e-30 |
|
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: 119.17 E-value: 1.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 2 PALVVKELRKSYGDFE--AVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLG---RKMPDKEVLARV 76
Cdd:COG2274 472 GDIELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGidlRQIDPASLRRQI 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 77 GYMPQELALYlNLTVEENLWFYSRLYGLpreefeRRKEEVLRFVGLEEFRDRL-------VAE----LSGGMQRRASLAC 145
Cdd:COG2274 552 GVVLQDVFLF-SGTIRENITLGDPDATD------EEIIEAARLAGLHDFIEALpmgydtvVGEggsnLSGGQRQRLAIAR 624
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1828880889 146 ALVHEPEFLILDEPTVGVDPGLRASFWRYFRELTdEGASILITTHYMDEAVNCDRVAIVIAGRVLVTATPEEIMAETG 223
Cdd:COG2274 625 ALLRNPRILILDEATSALDAETEAIILENLRRLL-KGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKG 701
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
7-229 |
1.58e-30 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 113.26 E-value: 1.58e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 7 KELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGE-----IELLGRKMPDKEVLARVGYMPQ 81
Cdd:PRK09493 5 KNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDlivdgLKVNDPKVDERLIRQEAGMVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 82 ELALYLNLTVEENLWFYS-RLYGLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLILDEPT 160
Cdd:PRK09493 85 QFYLFPHLTALENVMFGPlRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPT 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1828880889 161 VGVDPGLRASFWRYFRELTDEGASILITTHYMDEAvncDRVA---IVI-AGRVLVTATPEEIMAETGSATLEE 229
Cdd:PRK09493 165 SALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFA---EKVAsrlIFIdKGRIAEDGDPQVLIKNPPSQRLQE 234
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
6-210 |
1.73e-30 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 113.19 E-value: 1.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 6 VKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIEL------LGRKMPDKEVLA---RV 76
Cdd:PRK11124 5 LNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIagnhfdFSKTPSDKAIRElrrNV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 77 GYMPQELALYLNLTVEENLWFYS-RLYGLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLI 155
Cdd:PRK11124 85 GMVFQQYNLWPHLTVQQNLIEAPcRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1828880889 156 LDEPTVGVDPGLRASFWRYFRELTDEGASILITTHYMDeavncdrVAIVIAGRVL 210
Cdd:PRK11124 165 FDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVE-------VARKTASRVV 212
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-221 |
2.05e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 113.55 E-value: 2.05e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 2 PALVVKELRKSYGDFE--AVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKMPD---KEVLARV 76
Cdd:PRK13632 6 VMIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKenlKEIRKKI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 77 GYMPQEL-ALYLNLTVEENLWFysrlyGL-----PREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHE 150
Cdd:PRK13632 86 GIIFQNPdNQFIGATVEDDIAF-----GLenkkvPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALN 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1828880889 151 PEFLILDEPTVGVDPGLRASFWRYFRELTDEGASILIT-THYMDEAVNCDRVAIVIAGRVLVTATPEEIMAE 221
Cdd:PRK13632 161 PEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISiTHDMDEAILADKVIVFSEGKLIAQGKPKEILNN 232
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
3-234 |
2.34e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 113.68 E-value: 2.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 3 ALVVKELRKSYGD-FEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGR---KMPDKEVLARVGY 78
Cdd:PRK13647 4 IIEVEDLHFRYKDgTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGRevnAENEKWVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 79 MPQELALYL-NLTVEENLWFYSRLYGLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLILD 157
Cdd:PRK13647 84 VFQDPDDQVfSSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLD 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1828880889 158 EPTVGVDPGLRASFWRYFRELTDEGASILITTHYMDEAVN-CDRVAIVIAGRVLVTATPEEIMAEtgsATLEEAVLKL 234
Cdd:PRK13647 164 EPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEwADQVIVLKEGRVLAEGDKSLLTDE---DIVEQAGLRL 238
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
9-220 |
3.73e-30 |
|
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: 114.81 E-value: 3.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 9 LRKSYGDFE-AVRglsFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKMPDKE----VLA---RVGYMP 80
Cdd:COG4148 7 FRLRRGGFTlDVD---FTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSArgifLPPhrrRIGYVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 81 QELALYLNLTVEENLwfysrLYGL---PREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLILD 157
Cdd:COG4148 84 QEARLFPHLSVRGNL-----LYGRkraPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1828880889 158 EPTVGVDPGLRASFWRYFRELTDEGA-SILITTHYMDEAVN-CDRVAIVIAGRVLVTATPEEIMA 220
Cdd:COG4148 159 EPLAALDLARKAEILPYLERLRDELDiPILYVSHSLDEVARlADHVVLLEQGRVVASGPLAEVLS 223
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
4-235 |
4.33e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 113.02 E-value: 4.33e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 4 LVVKELRKSYGD-FEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIeLLGRKMPDkevLARVGYMPQE 82
Cdd:PRK13636 6 LKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRI-LFDGKPID---YSRKGLMKLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 83 LALYLNLTVEENLWFYSRLY----------GLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPE 152
Cdd:PRK13636 82 ESVGMVFQDPDNQLFSASVYqdvsfgavnlKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 153 FLILDEPTVGVDPGLRASFWRYFRELTDE-GASILITTHYMDE-AVNCDRVAIVIAGRVLVTATPEEIMAEtgSATLEEA 230
Cdd:PRK13636 162 VLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIvPLYCDNVFVMKEGRVILQGNPKEVFAE--KEMLRKV 239
|
....*
gi 1828880889 231 VLKLT 235
Cdd:PRK13636 240 NLRLP 244
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
2-160 |
6.79e-30 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 116.32 E-value: 6.79e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 2 PALVVKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIElLGRKMpdkevlaRVGYMPQ 81
Cdd:COG0488 314 KVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVK-LGETV-------KIGYFDQ 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 82 ELA-LYLNLTVEENLWFYSRlyglpreefERRKEEVLRFVGLEEFR----DRLVAELSGGMQRRASLACALVHEPEFLIL 156
Cdd:COG0488 386 HQEeLDPDKTVLDELRDGAP---------GGTEQEVRGYLGRFLFSgddaFKPVGVLSGGEKARLALAKLLLSPPNVLLL 456
|
....
gi 1828880889 157 DEPT 160
Cdd:COG0488 457 DEPT 460
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-218 |
8.33e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 112.20 E-value: 8.33e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 1 MPALVVKELRKSY-GDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGR---KMPDKEVLARV 76
Cdd:PRK13652 1 MHLIETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEpitKENIREVRKFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 77 GYMPQELA-LYLNLTVEENLWFYSRLYGLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLI 155
Cdd:PRK13652 81 GLVFQNPDdQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1828880889 156 LDEPTVGVDPGLRASFWRYFRELTDE-GASILITTHYMD-EAVNCDRVAIVIAGRVLVTATPEEI 218
Cdd:PRK13652 161 LDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDlVPEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
4-218 |
1.14e-29 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 113.28 E-value: 1.14e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 4 LVVKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKMPDKEVLAR-VGYMPQE 82
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRdICMVFQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 83 LALYLNLTVEENLWFYSRLYGLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLILDEPTVG 162
Cdd:PRK11432 87 YALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSN 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1828880889 163 VDPGLRASFWRYFRELTDE-GASILITTHYMDEAVNC-DRVAIVIAGRVLVTATPEEI 218
Cdd:PRK11432 167 LDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVsDTVIVMNKGKIMQIGSPQEL 224
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
7-220 |
1.59e-29 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 112.97 E-value: 1.59e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 7 KELRKSY----GDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGR---KMPDKE-VLAR--V 76
Cdd:PRK11153 5 KNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQdltALSEKElRKARrqI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 77 GYMPQELALYLNLTVEENLWFYSRLYGLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLIL 156
Cdd:PRK11153 85 GMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLLC 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1828880889 157 DEPTVGVDPGLRASFWRYFRELTDE-GASILITTHYMD--EAVnCDRVAIVIAGRVLVTATPEEIMA 220
Cdd:PRK11153 165 DEATSALDPATTRSILELLKDINRElGLTIVLITHEMDvvKRI-CDRVAVIDAGRLVEQGTVSEVFS 230
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
22-221 |
1.70e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 111.46 E-value: 1.70e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 22 LSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKMPD-------KEVLARVGYMPQ--ELALYLNlTVE 92
Cdd:PRK13641 26 ISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPetgnknlKKLRKKVSLVFQfpEAQLFEN-TVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 93 ENLWFYSRLYGLPREEFERRKEEVLRFVGL-EEFRDRLVAELSGGMQRRASLACALVHEPEFLILDEPTVGVDPGLRASF 171
Cdd:PRK13641 105 KDVEFGPKNFGFSEDEAKEKALKWLKKVGLsEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEM 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1828880889 172 WRYFRELTDEGASILITTHYMDE-AVNCDRVAIVIAGRVLVTATPEEIMAE 221
Cdd:PRK13641 185 MQLFKDYQKAGHTVILVTHNMDDvAEYADDVLVLEHGKLIKHASPKEIFSD 235
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-196 |
2.78e-29 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 110.34 E-value: 2.78e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 1 MPALVVKELRKSYGDF----EAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKM--PDkevlA 74
Cdd:COG4525 1 MSMLTVRHVSVRYPGGgqpqPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVtgPG----A 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 75 RVGYMPQELALYLNLTVEENLWFYSRLYGLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFL 154
Cdd:COG4525 77 DRGVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1828880889 155 ILDEPTVGVDPGLRASF-------WRyfreltDEGASILITTHYMDEAV 196
Cdd:COG4525 157 LMDEPFGALDALTREQMqellldvWQ------RTGKGVFLITHSVEEAL 199
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
18-221 |
2.99e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 110.95 E-value: 2.99e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 18 AVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKMPDKE----VLARVGYMPQELALYLNLT-VE 92
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEnlwdIRNKAGMVFQNPDNQIVATiVE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 93 ENLWFYSRLYGLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLILDEPTVGVDPGLRASFW 172
Cdd:PRK13633 105 EDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVV 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1828880889 173 RYFRELTDE-GASILITTHYMDEAVNCDRVAIVIAGRVLVTATPEEIMAE 221
Cdd:PRK13633 185 NTIKELNKKyGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-160 |
3.26e-29 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 114.39 E-value: 3.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 6 VKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRkmpdkevlARVGYMPQELAL 85
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKG--------LRIGYLPQEPPL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 86 YLNLTVEENLW-----------FYSRLYGLPREEFERRKE---------------------EVLRFVGL-EEFRDRLVAE 132
Cdd:COG0488 73 DDDLTVLDTVLdgdaelraleaELEELEAKLAEPDEDLERlaelqeefealggweaearaeEILSGLGFpEEDLDRPVSE 152
|
170 180
....*....|....*....|....*...
gi 1828880889 133 LSGGMQRRASLACALVHEPEFLILDEPT 160
Cdd:COG0488 153 LSGGWRRRVALARALLSEPDLLLLDEPT 180
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
4-190 |
8.86e-29 |
|
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: 107.58 E-value: 8.86e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 4 LVVKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKmpdkevLARVGYMPQEL 83
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGP------LDFQRDSIARG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 84 ALYLN--------LTVEENLWFYSRLYGlpreefERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLI 155
Cdd:cd03231 75 LLYLGhapgikttLSVLENLRFWHADHS------DEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWI 148
|
170 180 190
....*....|....*....|....*....|....*
gi 1828880889 156 LDEPTVGVDPGLRASFWRYFRELTDEGASILITTH 190
Cdd:cd03231 149 LDEPTTALDKAGVARFAEAMAGHCARGGMVVLTTH 183
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
3-222 |
3.61e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 107.96 E-value: 3.61e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 3 ALVVKELRKSYGDFE--AVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGE---IELLGRKMPDK---EVLA 74
Cdd:PRK13640 5 IVEFKHVSFTYPDSKkpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLTAKtvwDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 75 RVGYMPQEL-ALYLNLTVEENLWFYSRLYGLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEF 153
Cdd:PRK13640 85 KVGIVFQNPdNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKI 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 154 LILDEPTVGVDPGLRASFWRYFREL-TDEGASILITTHYMDEAVNCDRVAIVIAGRVLVTATPEEIMAET 222
Cdd:PRK13640 165 IILDESTSMLDPAGKEQILKLIRKLkKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSKV 234
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
4-222 |
3.65e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 107.87 E-value: 3.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 4 LVVKELRKSygDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKMPDKEVL---ARVGYMP 80
Cdd:PRK13642 10 LVFKYEKES--DVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWnlrRKIGMVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 81 QEL-ALYLNLTVEENLWFYSRLYGLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLILDEP 159
Cdd:PRK13642 88 QNPdNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDES 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1828880889 160 TVGVDPGLRASFWRYFRELTDE-GASILITTHYMDEAVNCDRVAIVIAGRVLVTATPEEIMAET 222
Cdd:PRK13642 168 TSMLDPTGRQEIMRVIHEIKEKyQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFATS 231
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
18-227 |
3.78e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 107.77 E-value: 3.78e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 18 AVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKMPD----KEVLARVGYMPQELAL-YLNLTVE 92
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDfsklQGIRKLVGIVFQNPETqFVGRTVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 93 ENLWFYSRLYGLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLILDEPTVGVDPGLRASFW 172
Cdd:PRK13644 97 EDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1828880889 173 RYFRELTDEGASILITTHYMDEAVNCDRVAIVIAGRVLVTATPEEIMAETGSATL 227
Cdd:PRK13644 177 ERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSDVSLQTL 231
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
2-162 |
7.13e-28 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 106.35 E-value: 7.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 2 PALVVKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGR---KMPDKEVlAR--V 76
Cdd:COG4674 9 PILYVEDLTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTdltGLDEHEI-ARlgI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 77 GYMPQELALYLNLTVEENL---------WFYSRLYGLPrEEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACAL 147
Cdd:COG4674 88 GRKFQKPTVFEELTVFENLelalkgdrgVFASLFARLT-AEERDRIEEVLETIGLTDKADRLAGLLSHGQKQWLEIGMLL 166
|
170
....*....|....*
gi 1828880889 148 VHEPEFLILDEPTVG 162
Cdd:COG4674 167 AQDPKLLLLDEPVAG 181
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
11-224 |
8.36e-28 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 108.25 E-value: 8.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 11 KSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKMpdKEVLAR---VGYMPQELALYL 87
Cdd:PRK10851 10 KSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDV--SRLHARdrkVGFVFQHYALFR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 88 NLTVEENLWFYSRLygLP------REEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLILDEPTV 161
Cdd:PRK10851 88 HMTVFDNIAFGLTV--LPrrerpnAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFG 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1828880889 162 GVDPGLRASFWRYFRELTDE--GASILItTHYMDEAVN-CDRVAIVIAGRVLVTATPEEIMAETGS 224
Cdd:PRK10851 166 ALDAQVRKELRRWLRQLHEElkFTSVFV-THDQEEAMEvADRVVVMSQGNIEQAGTPDQVWREPAT 230
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
3-228 |
1.60e-27 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 107.90 E-value: 1.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 3 ALVVKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAG--KTTTIKTIVGllkPDSGEIEL-LGRKMPDKEVLARV--G 77
Cdd:NF000106 13 AVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G---PDAGRRPWrF*TWCANRRALRRTig* 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 78 YMPQELALYLNLTVEENLWFYSRLYGLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLILD 157
Cdd:NF000106 90 HRPVR*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLD 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1828880889 158 EPTVGVDPGLRASFWRYFRELTDEGASILITTHYMDEAVN-CDRVAIVIAGRVLVTATPEEIMAETGSATLE 228
Cdd:NF000106 170 EPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQlAHELTVIDRGRVIADGKVDELKTKVGGRTLQ 241
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
18-221 |
3.71e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 105.59 E-value: 3.71e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 18 AVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIEL-------LGRKMPDKEVLARVGYMPQ--ELALYLN 88
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVgdivvssTSKQKEIKPVRKKVGVVFQfpESQLFEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 89 lTVEENLWFYSRLYGLPREEFERRKEEVLRFVGL-EEFRDRLVAELSGGMQRRASLACALVHEPEFLILDEPTVGVDPGL 167
Cdd:PRK13643 101 -TVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLaDEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKA 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1828880889 168 RASFWRYFRELTDEGASILITTHYMDEAVN-CDRVAIVIAGRVLVTATPEEIMAE 221
Cdd:PRK13643 180 RIEMMQLFESIHQSGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDVFQE 234
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-217 |
4.36e-27 |
|
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: 104.05 E-value: 4.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 2 PALVVKELRKSYGDFEAV----RGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKMP--DKEVLAR 75
Cdd:COG4181 7 PIIELRGLTKTVGTGAGEltilKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFalDEDARAR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 76 -----VGYMPQELALYLNLTVEENLwfysrlyGLP-----REEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLAC 145
Cdd:COG4181 87 lrarhVGFVFQSFQLLPTLTALENV-------MLPlelagRRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALAR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1828880889 146 ALVHEPEFLILDEPTVGVDPGLRASFWRYFRELTDE-GASILITTHYMDEAVNCDRVAIVIAGRVLVTATPEE 217
Cdd:COG4181 160 AFATEPAILFADEPTGNLDAATGEQIIDLLFELNRErGTTLVLVTHDPALAARCDRVLRLRAGRLVEDTAATA 232
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
4-232 |
4.67e-27 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 104.70 E-value: 4.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 4 LVVKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKM--------PDKEVLAR 75
Cdd:PRK13638 2 LATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLdyskrgllALRQQVAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 76 VGYMPQELALYLNltVEENLWFYSRLYGLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLI 155
Cdd:PRK13638 82 VFQDPEQQIFYTD--IDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1828880889 156 LDEPTVGVDPGLRASFWRYFRELTDEGASILITTHYMDEAVN-CDRVAIVIAGRVLVTATPEEIMAETgsATLEEAVL 232
Cdd:PRK13638 160 LDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEiSDAVYVLRQGQILTHGAPGEVFACT--EAMEQAGL 235
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
12-223 |
5.24e-27 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 108.33 E-value: 5.24e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 12 SY-GDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLG---RKMPDKEVLARVGYMPQELALYl 87
Cdd:COG1132 348 SYpGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGvdiRDLTLESLRRQIGVVPQDTFLF- 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 88 NLTVEENLwfysrLYGLPrEEFERRKEEVLRFVGLEEFRDRL-------VAE----LSGGmQR-RASLACALVHEPEFLI 155
Cdd:COG1132 427 SGTIRENI-----RYGRP-DATDEEVEEAAKAAQAHEFIEALpdgydtvVGErgvnLSGG-QRqRIAIARALLKDPPILI 499
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1828880889 156 LDEPTVGVDPGLRASFWRYFRELTdEGASILITTHYMDEAVNCDRVAIVIAGRVLVTATPEEIMAETG 223
Cdd:COG1132 500 LDEATSALDTETEALIQEALERLM-KGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLARGG 566
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-211 |
8.23e-27 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 103.68 E-value: 8.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 1 MPALVVKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIEL------LGRKMPDKEVLA 74
Cdd:PRK11264 1 MSAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgditidTARSLSQQKGLI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 75 R-----VGYMPQELALYLNLTVEENLWFYSRLY-GLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALV 148
Cdd:PRK11264 81 RqlrqhVGFVFQNFNLFPHRTVLENIIEGPVIVkGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1828880889 149 HEPEFLILDEPTVGVDPGLRASFWRYFRELTDEGASILITTHYMDEAVNCDRVAIVIAGRVLV 211
Cdd:PRK11264 161 MRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIV 223
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
22-209 |
1.80e-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: 101.80 E-value: 1.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 22 LSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKMPDKEVLAR-VGYMPQELALYLNLTVEENLWFySR 100
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRpVSMLFQENNLFAHLTVEQNVGL-GL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 101 LYGLPREEF-ERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLILDEPTVGVDPGLRASFWRYFRELT 179
Cdd:cd03298 96 SPGLKLTAEdRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLH 175
|
170 180 190
....*....|....*....|....*....|..
gi 1828880889 180 DE-GASILITTHYMDEAVNCDRVAIVIA-GRV 209
Cdd:cd03298 176 AEtKMTVLMVTHQPEDAKRLAQRVVFLDnGRI 207
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
2-239 |
1.90e-26 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 103.04 E-value: 1.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 2 PALVVKELRKSYGD-FEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGrkMPDKEVLAR--VGY 78
Cdd:PRK15056 5 AGIVVNDVTVTWRNgHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILG--QPTRQALQKnlVAY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 79 MPQElalylnltvEENLWFYSRL---------YG------LPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASL 143
Cdd:PRK15056 83 VPQS---------EEVDWSFPVLvedvvmmgrYGhmgwlrRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 144 ACALVHEPEFLILDEPTVGVDPGLRASFWRYFRELTDEGASILITTHYMDEAVN-CDrVAIVIAGRVLVTATPEEIMAet 222
Cdd:PRK15056 154 ARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEfCD-YTVMVKGTVLASGPTETTFT-- 230
|
250 260
....*....|....*....|
gi 1828880889 223 gSATLEEA---VLKLTGVKG 239
Cdd:PRK15056 231 -AENLELAfsgVLRHVALNG 249
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
17-209 |
1.93e-26 |
|
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: 101.90 E-value: 1.93e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 17 EAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLG---RKMPDKEVLARVGYMPQELALYlNLTVEE 93
Cdd:cd03245 18 PALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGtdiRQLDPADLRRNIGYVPQDVTLF-YGTLRD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 94 NLwfysrLYGLPrEEFERRKEEVLRFVGLEEFR-------DRLVAE----LSGGmQRRA-SLACALVHEPEFLILDEPTV 161
Cdd:cd03245 97 NI-----TLGAP-LADDERILRAAELAGVTDFVnkhpnglDLQIGErgrgLSGG-QRQAvALARALLNDPPILLLDEPTS 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1828880889 162 GVDPGLRASFWRYFRELTdEGASILITTHYMDEAVNCDRVAIVIAGRV 209
Cdd:cd03245 170 AMDMNSEERLKERLRQLL-GDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
26-222 |
2.39e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 103.18 E-value: 2.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 26 VEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIEL------LGRKMPD-KEVLARVGYMPQ--ELALYlNLTVEENLW 96
Cdd:PRK13634 30 IPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgervitAGKKNKKlKPLRKKVGIVFQfpEHQLF-EETVEKDIC 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 97 FYSRLYGLPREEFERRKEEVLRFVGL-EEFRDRLVAELSGGMQRRASLACALVHEPEFLILDEPTVGVDPGLRASFWRYF 175
Cdd:PRK13634 109 FGPMNFGVSEEDAKQKAREMIELVGLpEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMF 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1828880889 176 RELTDE-GASILITTHYMDEAVN-CDRVAIVIAGRVLVTATPEEIMAET 222
Cdd:PRK13634 189 YKLHKEkGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREIFADP 237
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
6-222 |
3.18e-26 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 102.54 E-value: 3.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 6 VKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKMPD------KEVLARVGYM 79
Cdd:PRK11831 10 MRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAmsrsrlYTVRKRMSML 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 80 PQELALYLNLTVEENLWFYSRLYG-LPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLILDE 158
Cdd:PRK11831 90 FQSGALFTDMNVFDNVAYPLREHTqLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1828880889 159 PTVGVDPGLRASFWRYFRELTDE-GASILITTHYMDEAVNCDRVAIVIAG-RVLVTATPEEIMAET 222
Cdd:PRK11831 170 PFVGQDPITMGVLVKLISELNSAlGVTCVVVSHDVPEVLSIADHAYIVADkKIVAHGSAQALQANP 235
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
20-190 |
3.74e-26 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 100.65 E-value: 3.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 20 RGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKmpdkevLARVG--YMpQELaLYLN--------L 89
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEP------IRRQRdeYH-QDL-LYLGhqpgikteL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 90 TVEENLWFYSRLYGLPreeFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLILDEPTVGVDPGLRA 169
Cdd:PRK13538 90 TALENLRFYQRLHGPG---DDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVA 166
|
170 180
....*....|....*....|.
gi 1828880889 170 SFWRYFRELTDEGASILITTH 190
Cdd:PRK13538 167 RLEALLAQHAEQGGMVILTTH 187
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
18-221 |
4.24e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 102.52 E-value: 4.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 18 AVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKMPD-------KEVLARVGYMPQ--ELALYlN 88
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITStsknkdiKQIRKKVGLVFQfpESQLF-E 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 89 LTVEENLWFYSRLYGLPREEFERRKEEVLRFVGL-EEFRDRLVAELSGGMQRRASLACALVHEPEFLILDEPTVGVDPGL 167
Cdd:PRK13649 101 ETVLKDVAFGPQNFGVSQEEAEALAREKLALVGIsESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKG 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1828880889 168 RASFWRYFRELTDEGASILITTHYMDEAVN-CDRVAIVIAGRVLVTATPEEIMAE 221
Cdd:PRK13649 181 RKELMTLFKKLHQSGMTIVLVTHLMDDVANyADFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
21-230 |
7.43e-26 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 101.07 E-value: 7.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 21 GLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLkPDSGEIELLGRKMPD--KEVLARV-GYMPQELALYLNLTVeenlWF 97
Cdd:COG4138 14 PISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDwsAAELARHrAYLSQQQSPPFAMPV----FQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 98 YSRLY---GLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACAL--VH-----EPEFLILDEPTVGVDPGL 167
Cdd:COG4138 89 YLALHqpaGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLlqVWptinpEGQLLLLDEPMNSLDVAQ 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1828880889 168 RASFWRYFRELTDEGASILITTHYMDEAV-NCDRVAIVIAGRVLVTATPEEIMAEtgsATLEEA 230
Cdd:COG4138 169 QAALDRLLRELCQQGITVVMSSHDLNHTLrHADRVWLLKQGKLVASGETAEVMTP---ENLSEV 229
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-201 |
1.55e-25 |
|
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: 103.91 E-value: 1.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 2 PALVVKELRKSYGD-FEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKMPD---KEVLARVG 77
Cdd:TIGR02857 320 SSLEFSGVSVAYPGrRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADadaDSWRDQIA 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 78 YMPQELALYlNLTVEENLWFYSRlyglprEEFERRKEEVLRFVGLEEF-------RDRLVAE----LSGGMQRRASLACA 146
Cdd:TIGR02857 400 WVPQHPFLF-AGTIAENIRLARP------DASDAEIREALERAGLDEFvaalpqgLDTPIGEggagLSGGQAQRLALARA 472
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1828880889 147 LVHEPEFLILDEPTVGVDPGLRASFWRYFRELTdEGASILITTHYMDEAVNCDRV 201
Cdd:TIGR02857 473 FLRDAPLLLLDEPTAHLDAETEAEVLEALRALA-QGRTVLLVTHRLALAALADRI 526
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
11-218 |
4.22e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 100.70 E-value: 4.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 11 KSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIEL------------------LGRKMPD-KE 71
Cdd:PRK13631 34 KQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigdkknnhelitnpYSKKIKNfKE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 72 VLARVGYMPQ--ELALYLNlTVEENLWFYSRLYGLPREEFERRKEEVLRFVGLEE-FRDRLVAELSGGMQRRASLACALV 148
Cdd:PRK13631 114 LRRRVSMVFQfpEYQLFKD-TIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDDsYLERSPFGLSGGQKRRVAIAGILA 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1828880889 149 HEPEFLILDEPTVGVDPGLRASFWRYFRELTDEGASILITTHYMDEAVNCDRVAIVIA-GRVLVTATPEEI 218
Cdd:PRK13631 193 IQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDkGKILKTGTPYEI 263
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
23-225 |
1.03e-24 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 97.73 E-value: 1.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 23 SFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLG----RKMPDKEvlaRVGYMPQELALYLNLTVEENLwfy 98
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGqdhtTTPPSRR---PVSMLFQENNLFSHLTVAQNI--- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 99 srlyGL---P----REEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLILDEPTVGVDPGLRASF 171
Cdd:PRK10771 93 ----GLglnPglklNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEM 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1828880889 172 WRYFRELTDE-GASILITTHYMDEAVNCDRVAIVIA-GRVLVTATPEEIMAETGSA 225
Cdd:PRK10771 169 LTLVSQVCQErQLTLLMVSHSLEDAARIAPRSLVVAdGRIAWDGPTDELLSGKASA 224
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
18-219 |
2.69e-24 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 99.72 E-value: 2.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 18 AVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLG---RKMPDKEVL----ARVGYMPQELALYLNLT 90
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiAKISDAELRevrrKKIAMVFQSFALMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 91 VEENLWFYSRLYGLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLILDEPTVGVDPGLRAS 170
Cdd:PRK10070 123 VLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1828880889 171 FWRYFREL-TDEGASILITTHYMDEAVNC-DRVAIVIAGRVLVTATPEEIM 219
Cdd:PRK10070 203 MQDELVKLqAKHQRTIVFISHDLDEAMRIgDRIAIMQNGEVVQVGTPDEIL 253
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
19-221 |
3.05e-24 |
|
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: 100.59 E-value: 3.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 19 VRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKMP--DKEVLAR-VGYMPQELALyLNLTVEENL 95
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSqwDREELGRhIGYLPQDVEL-FDGTIAENI 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 96 wfySRLYGLPreeferrKEEVL---RFVGLEEFRDRL-------VAE----LSGGMQRRASLACALVHEPEFLILDEPTV 161
Cdd:COG4618 427 ---ARFGDAD-------PEKVVaaaKLAGVHEMILRLpdgydtrIGEggarLSGGQRQRIGLARALYGDPRLVVLDEPNS 496
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 162 GVDPGLRASFWRYFRELTDEGASILITTHYMDEAVNCDRVAIVIAGRVLVTATPEEIMAE 221
Cdd:COG4618 497 NLDDEGEAALAAAIRALKARGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-220 |
3.34e-24 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 100.10 E-value: 3.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 2 PALVVKELR-KSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKMPDKEVLAR----V 76
Cdd:COG3845 256 VVLEVENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERrrlgV 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 77 GYMPQE---LALYLNLTVEENL---WFYSRLYGlpreeferrKEEVLRFVGLEEFRDRLVAE--------------LSGG 136
Cdd:COG3845 336 AYIPEDrlgRGLVPDMSVAENLilgRYRRPPFS---------RGGFLDRKAIRAFAEELIEEfdvrtpgpdtparsLSGG 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 137 MQRRASLACALVHEPEFLILDEPTVGVDPGLRASFWRYFRELTDEGASILITTHYMDEAVN-CDRVAIVIAGRvLV---- 211
Cdd:COG3845 407 NQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILAlSDRIAVMYEGR-IVgevp 485
|
250
....*....|....
gi 1828880889 212 --TATPEEI---MA 220
Cdd:COG3845 486 aaEATREEIgllMA 499
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
15-222 |
4.32e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 97.16 E-value: 4.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 15 DFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIEL----LGRKMPDKE---VLARVGYMPQ--ELAL 85
Cdd:PRK13646 19 EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVdditITHKTKDKYirpVRKRIGMVFQfpESQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 86 YLNlTVEENLWFYSRLYGLPREEFERRKEEVLRFVGLEefRDRLVA---ELSGGMQRRASLACALVHEPEFLILDEPTVG 162
Cdd:PRK13646 99 FED-TVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFS--RDVMSQspfQMSGGQMRKIAIVSILAMNPDIIVLDEPTAG 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1828880889 163 VDPGLRASFWRYFREL-TDEGASILITTHYMDE-AVNCDRVAIVIAGRVLVTATPEEIMAET 222
Cdd:PRK13646 176 LDPQSKRQVMRLLKSLqTDENKTIILVSHDMNEvARYADEVIVMKEGSIVSQTSPKELFKDK 237
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
6-210 |
4.54e-24 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 96.62 E-value: 4.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 6 VKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDS---GEIELLGRKMPDKEVLAR------- 75
Cdd:PRK09984 7 VEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsagSHIELLGRTVQREGRLARdirksra 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 76 -VGYMPQELALYLNLTVEENLW--------FYSRLYGLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACA 146
Cdd:PRK09984 87 nTGYIFQQFNLVNRLSVLENVLigalgstpFWRTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1828880889 147 LVHEPEFLILDEPTVGVDPGLRASFWRYFRELT-DEGASILITTHYMDEAVN-CDRVAIVIAGRVL 210
Cdd:PRK09984 167 LMQQAKVILADEPIASLDPESARIVMDTLRDINqNDGITVVVTLHQVDYALRyCERIVALRQGHVF 232
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
4-216 |
4.68e-24 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 94.90 E-value: 4.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 4 LVVKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGL--LKPDSGEIELLGRKMPDKEVLAR----VG 77
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPEERarlgIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 78 YMPQELALYLNLTVEEnlwfysrlyglpreeferrkeeVLRFVGlEEFrdrlvaelSGGMQRRASLACALVHEPEFLILD 157
Cdd:cd03217 81 LAFQYPPEIPGVKNAD----------------------FLRYVN-EGF--------SGGEKKRNEILQLLLLEPDLAILD 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1828880889 158 EPTVGVD-PGLRASFwRYFRELTDEGASILITTHY--MDEAVNCDRVAIVIAGRVLVTATPE 216
Cdd:cd03217 130 EPDSGLDiDALRLVA-EVINKLREEGKSVLIITHYqrLLDYIKPDRVHVLYDGRIVKSGDKE 190
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-160 |
5.79e-24 |
|
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: 93.28 E-value: 5.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 4 LVVKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRkmpdkevlARVGYMPQel 83
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST--------VKIGYFEQ-- 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1828880889 84 alylnltveenlwfysrlyglpreeferrkeevlrfvgleefrdrlvaeLSGGMQRRASLACALVHEPEFLILDEPT 160
Cdd:cd03221 71 -------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPT 98
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
18-226 |
1.19e-23 |
|
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 94.74 E-value: 1.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 18 AVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPD----SGEIELLGRKMPDKEVLAR-VGYMPQELALYLN--LT 90
Cdd:TIGR02770 1 LVQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPGltqtSGEILLDGRPLLPLSIRGRhIATIMQNPRTAFNplFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 91 VEENLWFYSRLYGLPREEFERRKEEVLRFVGLEEFRDRLVA---ELSGGMQRRASLACALVHEPEFLILDEPTVGVDPGL 167
Cdd:TIGR02770 81 MGNHAIETLRSLGKLSKQARALILEALEAVGLPDPEEVLKKypfQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVVN 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1828880889 168 RASFWRYFREL-TDEGASILITTHYMDEAVNC-DRVAIVIAGRVLVTATPEEIMAETGSAT 226
Cdd:TIGR02770 161 QARVLKLLRELrQLFGTGILLITHDLGVVARIaDEVAVMDDGRIVERGTVKEIFYNPKHET 221
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-190 |
2.66e-23 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 94.41 E-value: 2.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 1 MPALV-VKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIEllgrkmpdKEVLARVGYM 79
Cdd:PRK09544 1 MTSLVsLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK--------RNGKLRIGYV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 80 PQELAL--YLNLTVeenlwfySRLYGLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLILD 157
Cdd:PRK09544 73 PQKLYLdtTLPLTV-------NRFLRLRPGTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLD 145
|
170 180 190
....*....|....*....|....*....|....
gi 1828880889 158 EPTVGVDPGLRASFWRYFRELTDE-GASILITTH 190
Cdd:PRK09544 146 EPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSH 179
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-190 |
4.01e-23 |
|
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: 97.05 E-value: 4.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 2 PALVVKELRKSY-GDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLG---RKMPDKEVLARVG 77
Cdd:TIGR02868 333 PTLELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGvpvSSLDQDEVRRRVS 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 78 YMPQELALYlNLTVEENLwfysrLYGLPREEFERRKEeVLRFVGLEEFRDRLV-----------AELSGGMQRRASLACA 146
Cdd:TIGR02868 413 VCAQDAHLF-DTTVRENL-----RLARPDATDEELWA-ALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALARA 485
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1828880889 147 LVHEPEFLILDEPTVGVDPGLRASFWRYFRELTDEGASILITTH 190
Cdd:TIGR02868 486 LLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHH 529
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
2-210 |
6.04e-23 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 93.36 E-value: 6.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 2 PALVVKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEI----------ELLGRKMPDKE 71
Cdd:TIGR02323 2 PLLQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTAtyimrsgaelELYQLSEAERR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 72 VLARV--GYMPQELALYLNLTV-------EENLWFYSRLYGlpreEFERRKEEVLRFVGLEEFR-DRLVAELSGGMQRRA 141
Cdd:TIGR02323 82 RLMRTewGFVHQNPRDGLRMRVsaganigERLMAIGARHYG----NIRATAQDWLEEVEIDPTRiDDLPRAFSGGMQQRL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1828880889 142 SLACALVHEPEFLILDEPTVGVDPGLRASFWRYFREL-TDEGASILITTHymDEAVN---CDRVAIVIAGRVL 210
Cdd:TIGR02323 158 QIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLvRDLGLAVIIVTH--DLGVArllAQRLLVMQQGRVV 228
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-218 |
6.54e-23 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 93.56 E-value: 6.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 2 PALVVKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGL--LKPD---SGEIEL-----LGRKMPDKE 71
Cdd:COG1117 10 PKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndLIPGarvEGEILLdgediYDPDVDVVE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 72 VLARVGYMPQElalyLN---LTVEENLWFYSRLYGL-PREEFERRKEEVLRFVGL-EEFRDRL---VAELSGGMQRRASL 143
Cdd:COG1117 90 LRRRVGMVFQK----PNpfpKSIYDNVAYGLRLHGIkSKSELDEIVEESLRKAALwDEVKDRLkksALGLSGGQQQRLCI 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1828880889 144 ACALVHEPEFLILDEPTVGVDPGLRASFWRYFRELTDEgASILITTHYMDEAVNC-DRVAIVIAGRVLVTATPEEI 218
Cdd:COG1117 166 ARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD-YTIVIVTHNMQQAARVsDYTAFFYLGELVEFGPTEQI 240
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
2-226 |
8.38e-23 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 96.27 E-value: 8.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 2 PALVVKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKM----PDKEVLARVG 77
Cdd:PRK15439 10 PLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCarltPAKAHQLGIY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 78 YMPQELALYLNLTVEENLwfysrLYGLPREEFERRKEEVL-----------RFVGLEEFRDRLVAELSGGMQRRASLaca 146
Cdd:PRK15439 90 LVPQEPLLFPNLSVKENI-----LFGLPKRQASMQKMKQLlaalgcqldldSSAGSLEVADRQIVEILRGLMRDSRI--- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 147 lvhepefLILDEPTVGVDPGLRASFWRYFRELTDEGASILITTHYMDEAVN-CDRV------AIVIAGRVLVTATPEEIM 219
Cdd:PRK15439 162 -------LILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQlADRIsvmrdgTIALSGKTADLSTDDIIQ 234
|
....*..
gi 1828880889 220 AETGSAT 226
Cdd:PRK15439 235 AITPAAR 241
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
4-209 |
1.05e-22 |
|
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: 90.74 E-value: 1.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 4 LVVKELRKSYGDFEA--VRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLG---RKMPDKEVLARVGY 78
Cdd:cd03246 1 LEVENVSFRYPGAEPpvLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGadiSQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 79 MPQELALyLNLTVEENLwfysrlyglpreeferrkeevlrfvgleefrdrlvaeLSGGMQRRASLACALVHEPEFLILDE 158
Cdd:cd03246 81 LPQDDEL-FSGSIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILVLDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1828880889 159 PTVGVDPGLRASFWRYFRELTDEGASILITTHYMDEAVNCDRVAIVIAGRV 209
Cdd:cd03246 123 PNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-218 |
1.07e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 92.67 E-value: 1.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 1 MPALVVKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGL--LKPD---SGEIELLGR---KMPDKEV 72
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLieLYPEarvSGEVYLDGQdifKMDVIEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 73 LARVGYMPQELALYLNLTVEENLWFYSRLYGL--PREEFERRKEEVLRFVGL-EEFRDRL---VAELSGGMQRRASLACA 146
Cdd:PRK14247 81 RRRVQMVFQIPNPIPNLSIFENVALGLKLNRLvkSKKELQERVRWALEKAQLwDEVKDRLdapAGKLSGGQQQRLCIARA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1828880889 147 LVHEPEFLILDEPTVGVDPGLRASFWRYFRELTDEgASILITTHYMDEAVNC-DRVAIVIAGRVLVTATPEEI 218
Cdd:PRK14247 161 LAFQPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARIsDYVAFLYKGQIVEWGPTREV 232
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
18-223 |
1.26e-22 |
|
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: 91.90 E-value: 1.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 18 AVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLG---RKMPDKEVLARVGYMPQELALyLNLTVEEN 94
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGidiRDISRKSLRSMIGVVLQDTFL-FSGTIMEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 95 LwfysrLYGLPrEEFERRKEEVLRFVGLEEFRDRL-------VAE----LSGGMQRRASLACALVHEPEFLILDEPTVGV 163
Cdd:cd03254 97 I-----RLGRP-NATDEEVIEAAKEAGAHDFIMKLpngydtvLGEnggnLSQGERQLLAIARAMLRDPKILILDEATSNI 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 164 DPGLRASFWRYFRELTDEGASILItTHYMDEAVNCDRVAIVIAGRVLVTATPEEIMAETG 223
Cdd:cd03254 171 DTETEKLIQEALEKLMKGRTSIII-AHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-220 |
2.59e-22 |
|
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: 94.75 E-value: 2.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 1 MPALVVKELRKSYGD----FEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLkPD-----SGEIELLGR---KMP 68
Cdd:COG4172 4 MPLLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLL-PDpaahpSGSILFDGQdllGLS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 69 DKEVLA----RVGYMPQELALYLN--LTVE----ENLwfysRLY-GLPREEFERRKEEVLRFVGLEEFRDRLVA---ELS 134
Cdd:COG4172 83 ERELRRirgnRIAMIFQEPMTSLNplHTIGkqiaEVL----RLHrGLSGAAARARALELLERVGIPDPERRLDAyphQLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 135 GGMQRRASLACALVHEPEFLILDEPTVGVDPGLRASFWRYFRELTDE-GASILITTHymDEAV---NCDRVAIVIAGRVL 210
Cdd:COG4172 159 GGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRElGMALLLITH--DLGVvrrFADRVAVMRQGEIV 236
|
250
....*....|
gi 1828880889 211 VTATPEEIMA 220
Cdd:COG4172 237 EQGPTAELFA 246
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
15-220 |
2.61e-22 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 94.85 E-value: 2.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 15 DFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKMPDKEVLARV----GYMPQ---ELALYL 87
Cdd:PRK09700 275 DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVkkgmAYITEsrrDNGFFP 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 88 NLTVEENLWFYSRLY--GLPREEFERRKEEVLRFVglEEFRDRL----------VAELSGGMQRRASLACALVHEPEFLI 155
Cdd:PRK09700 355 NFSIAQNMAISRSLKdgGYKGAMGLFHEVDEQRTA--ENQRELLalkchsvnqnITELSGGNQQKVLISKWLCCCPEVII 432
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1828880889 156 LDEPTVGVDPGLRASFWRYFRELTDEGASILITTHYMDEAVN-CDRVAIVIAGRV------LVTATPEEIMA 220
Cdd:PRK09700 433 FDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITvCDRIAVFCEGRLtqiltnRDDMSEEEIMA 504
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
3-196 |
2.91e-22 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 91.68 E-value: 2.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 3 ALVVKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKMPDKEvlARVGYMPQE 82
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPG--AERGVVFQN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 83 LALYLNLTVEENLWFYSRLYGLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLILDEPTVG 162
Cdd:PRK11248 79 EGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGA 158
|
170 180 190
....*....|....*....|....*....|....*
gi 1828880889 163 VDPGLRASFWRYFREL-TDEGASILITTHYMDEAV 196
Cdd:PRK11248 159 LDAFTREQMQTLLLKLwQETGKQVLLITHDIEEAV 193
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-231 |
3.23e-22 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 91.09 E-value: 3.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 1 MPALVVKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKMPD-------KEVL 73
Cdd:PRK11614 3 KVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDwqtakimREAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 74 ARVgymPQELALYLNLTVEENL---WFYS----------RLYGLpreeferrkeevlrFVGLEEFRDRLVAELSGGMQRR 140
Cdd:PRK11614 83 AIV---PEGRRVFSRMTVEENLamgGFFAerdqfqerikWVYEL--------------FPRLHERRIQRAGTMSGGEQQM 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 141 ASLACALVHEPEFLILDEPTVGVDPGLRASFWRYFRELTDEGASILITTHYMDEAVN-CDRVAIVIAGRVlvtatpeeIM 219
Cdd:PRK11614 146 LAIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKlADRGYVLENGHV--------VL 217
|
250
....*....|...
gi 1828880889 220 AETGSATL-EEAV 231
Cdd:PRK11614 218 EDTGDALLaNEAV 230
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
2-221 |
3.46e-22 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 92.87 E-value: 3.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 2 PALVVKELRKSY----GDFE-------AVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKMpdk 70
Cdd:COG4608 6 PLLEVRDLKKHFpvrgGLFGrtvgvvkAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDI--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 71 evlarVGYMPQELALY--------------LN--LTVEENLWFYSRLYGL-PREEFERRKEEVLRFVGL-EEFRDRLVAE 132
Cdd:COG4608 83 -----TGLSGRELRPLrrrmqmvfqdpyasLNprMTVGDIIAEPLRIHGLaSKAERRERVAELLELVGLrPEHADRYPHE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 133 LSGGmQR-RASLACALVHEPEFLILDEPTVGVDPGLRASFWRYFRELTDE-GASILITTHymDEAVN---CDRVAIVIAG 207
Cdd:COG4608 158 FSGG-QRqRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDElGLTYLFISH--DLSVVrhiSDRVAVMYLG 234
|
250
....*....|....
gi 1828880889 208 RVLVTATPEEIMAE 221
Cdd:COG4608 235 KIVEIAPRDELYAR 248
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
8-192 |
3.56e-22 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 94.49 E-value: 3.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 8 ELRKSYGDFeavrglSFEVE-----KGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIellgrkmpDKEVlaRVGYMPQE 82
Cdd:PRK13409 345 DLTKKLGDF------SLEVEggeiyEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV--------DPEL--KISYKPQY 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 83 LALYLNLTVEENL----------WFYSRLyglpreeferrkeevLRFVGLEEFRDRLVAELSGG-MQRRASLACaLVHEP 151
Cdd:PRK13409 409 IKPDYDGTVEDLLrsitddlgssYYKSEI---------------IKPLQLERLLDKNVKDLSGGeLQRVAIAAC-LSRDA 472
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1828880889 152 EFLILDEPTVGVDPGLRASFWRYFRELTDE-GASILITTH--YM 192
Cdd:PRK13409 473 DLYLLDEPSAHLDVEQRLAVAKAIRRIAEErEATALVVDHdiYM 516
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
8-190 |
4.88e-22 |
|
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: 94.08 E-value: 4.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 8 ELRKSYGDF--EAVRGlsfEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIellgrkmpDKEVlaRVGYMPQELAL 85
Cdd:COG1245 346 DLTKSYGGFslEVEGG---EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV--------DEDL--KISYKPQYISP 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 86 YLNLTVEENL-----------WFYSRlyglpreeferrkeeVLRFVGLEEFRDRLVAELSGG-MQRRASLACaLVHEPEF 153
Cdd:COG1245 413 DYDGTVEEFLrsantddfgssYYKTE---------------IIKPLGLEKLLDKNVKDLSGGeLQRVAIAAC-LSRDADL 476
|
170 180 190
....*....|....*....|....*....|....*...
gi 1828880889 154 LILDEPTVGVDPGLRASFWRYFRELTDE-GASILITTH 190
Cdd:COG1245 477 YLLDEPSAHLDVEQRLAVAKAIRRFAENrGKTAMVVDH 514
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
4-209 |
6.66e-22 |
|
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: 88.91 E-value: 6.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 4 LVVKELRKSYGDFE--AVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKMPDKEVLAR--VGYM 79
Cdd:cd03247 1 LSINNVSFSYPEQEqqVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSslISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 80 PQELALYlNLTVEENLwfysrlyGLPreeferrkeevlrfvgleefrdrlvaeLSGGMQRRASLACALVHEPEFLILDEP 159
Cdd:cd03247 81 NQRPYLF-DTTLRNNL-------GRR---------------------------FSGGERQRLALARILLQDAPIVLLDEP 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1828880889 160 TVGVDPGLRASFWRYFRELTdEGASILITTHYMDEAVNCDRVAIVIAGRV 209
Cdd:cd03247 126 TVGLDPITERQLLSLIFEVL-KDKTLIWITHHLTGIEHMDKILFLENGKI 174
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
19-207 |
7.65e-22 |
|
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: 89.83 E-value: 7.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 19 VRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKM----PDKEVLArvgympQELALYLNLTVEEN 94
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQItepgPDRMVVF------QNYSLLPWLTVREN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 95 --LWFYSRLYGLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLILDEPTVGVDPGLRASFW 172
Cdd:TIGR01184 75 iaLAVDRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQ 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 1828880889 173 RYFRELTDE-GASILITTHYMDEAVN-CDRVAIVIAG 207
Cdd:TIGR01184 155 EELMQIWEEhRVTVLMVTHDVDEALLlSDRVVMLTNG 191
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
19-221 |
9.03e-22 |
|
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: 93.18 E-value: 9.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 19 VRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGR--KMPDKEVLAR-VGYMPQELALYLNlTVEENL 95
Cdd:TIGR01842 334 LRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGAdlKQWDRETFGKhIGYLPQDVELFPG-TVAENI 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 96 wfySRlYGLPREEFERRKEEVLRFV-----GLEEFRDRLVAE----LSGGMQRRASLACALVHEPEFLILDEPTVGVDPG 166
Cdd:TIGR01842 413 ---AR-FGENADPEKIIEAAKLAGVhelilRLPDGYDTVIGPggatLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEE 488
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1828880889 167 LRASFWRYFRELTDEGASILITTHYMdEAVNC-DRVAIVIAGRVLVTATPEEIMAE 221
Cdd:TIGR01842 489 GEQALANAIKALKARGITVVVITHRP-SLLGCvDKILVLQDGRIARFGERDEVLAK 543
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-218 |
2.08e-21 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 91.24 E-value: 2.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 1 MPALVVKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKMPDKEVLAR-VGYM 79
Cdd:PRK11000 1 MASVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERgVGMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 80 PQELALYLNLTVEENLWFYSRLYGLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLILDEP 159
Cdd:PRK11000 81 FQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1828880889 160 TVGVDPGL----RASFWRYFRELtdeGASILITTHYMDEAVN-CDRVAIVIAGRVLVTATPEEI 218
Cdd:PRK11000 161 LSNLDAALrvqmRIEISRLHKRL---GRTMIYVTHDQVEAMTlADKIVVLDAGRVAQVGKPLEL 221
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
2-203 |
2.52e-21 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 91.99 E-value: 2.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 2 PALVVKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGR----KMPDKEVLARVG 77
Cdd:PRK10762 3 ALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKevtfNGPKSSQEAGIG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 78 YMPQELALYLNLTVEENLW----FYSRLYGLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEF 153
Cdd:PRK10762 83 IIHQELNLIPQLTIAENIFlgreFVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1828880889 154 LILDEPTVGVDPGLRASFWRYFRELTDEGASILITTHYMDEAVN-CDRVAI 203
Cdd:PRK10762 163 IIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEiCDDVTV 213
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
2-207 |
2.60e-21 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 91.77 E-value: 2.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 2 PALVVKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKMP--DKEVLAR--VG 77
Cdd:PRK09700 4 PYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNklDHKLAAQlgIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 78 YMPQELALYLNLTVEENLwFYSRL-----YGLPR---EEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVH 149
Cdd:PRK09700 84 IIYQELSVIDELTVLENL-YIGRHltkkvCGVNIidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLML 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1828880889 150 EPEFLILDEPTVGVDPGLRASFWRYFRELTDEGASILITTHYMDEAVN-CDRVAIVIAG 207
Cdd:PRK09700 163 DAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRiCDRYTVMKDG 221
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
17-223 |
2.66e-21 |
|
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: 88.70 E-value: 2.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 17 EAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKMP--DKEVLAR-VGYMPQELALyLNLTVEE 93
Cdd:cd03252 16 VILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLAlaDPAWLRRqVGVVLQENVL-FNRSIRD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 94 NLWFYSRlyGLPreefERRKEEVLRFVGLEEF-------RDRLVAE----LSGGMQRRASLACALVHEPEFLILDEPTVG 162
Cdd:cd03252 95 NIALADP--GMS----MERVIEAAKLAGAHDFiselpegYDTIVGEqgagLSGGQRQRIAIARALIHNPRILIFDEATSA 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1828880889 163 VDPGLRASFWRYFRELTDeGASILITTHYMDEAVNCDRVAIVIAGRVLVTATPEEIMAETG 223
Cdd:cd03252 169 LDYESEHAIMRNMHDICA-GRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENG 228
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
10-220 |
3.55e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 89.30 E-value: 3.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 10 RKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKMPD--------KEVLARVGYMPQ 81
Cdd:PRK13645 18 KKTPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPAnlkkikevKRLRKEIGLVFQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 82 --ELALYLNlTVEENLWFYSRLYGLPREEFERRKEEVLRFVGL-EEFRDRLVAELSGGMQRRASLACALVHEPEFLILDE 158
Cdd:PRK13645 98 fpEYQLFQE-TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDE 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1828880889 159 PTVGVDPGLRASFWRYFRELTDE-GASILITTHYMDEAVN-CDRVAIVIAGRVLVTATPEEIMA 220
Cdd:PRK13645 177 PTGGLDPKGEEDFINLFERLNKEyKKRIIMVTHNMDQVLRiADEVIVMHEGKVISIGSPFEIFS 240
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
22-221 |
4.33e-21 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 88.45 E-value: 4.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 22 LSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLkPDSGEIELLGRKMPDKEV--LARV-GYMPQELALYLNLTVeenlWFY 98
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAaeLARHrAYLSQQQTPPFAMPV----FQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 99 SRLY---GLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACAL--VH-----EPEFLILDEPTVGVDPGLR 168
Cdd:PRK03695 90 LTLHqpdKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVlqVWpdinpAGQLLLLDEPMNSLDVAQQ 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1828880889 169 ASFWRYFRELTDEGASILITTH----YMDEAvncDRVAIVIAGRVLVTATPEEIMAE 221
Cdd:PRK03695 170 AALDRLLSELCQQGIAVVMSSHdlnhTLRHA---DRVWLLKQGKLLASGRRDEVLTP 223
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-218 |
6.29e-21 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 89.40 E-value: 6.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 1 MPALVVKELRKSY----GDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPD---SGEIELLGRK---MPDK 70
Cdd:PRK09473 10 DALLDVKDLRVTFstpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREilnLPEK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 71 EvLARVgyMPQELALY-------LN--LTVEENLWFYSRLY-GLPREEFERRKEEVLRFVGLEEFRDRLVA---ELSGGM 137
Cdd:PRK09473 90 E-LNKL--RAEQISMIfqdpmtsLNpyMRVGEQLMEVLMLHkGMSKAEAFEESVRMLDAVKMPEARKRMKMyphEFSGGM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 138 QRRASLACALVHEPEFLILDEPTVGVDPGLRASFWRYFRELTDE-GASILITTHymDEAV---NCDRVAIVIAGRVLVTA 213
Cdd:PRK09473 167 RQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITH--DLGVvagICDKVLVMYAGRTMEYG 244
|
....*
gi 1828880889 214 TPEEI 218
Cdd:PRK09473 245 NARDV 249
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
8-221 |
7.36e-21 |
|
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: 87.85 E-value: 7.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 8 ELRKSYGDFeavrglSFEVEKG-----EIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKmpdkevlarVGYMPQE 82
Cdd:cd03237 5 TMKKTLGEF------TLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDT---------VSYKPQY 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 83 LALYLNLTVEENLW-----FYSRLYglpreeferRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLILD 157
Cdd:cd03237 70 IKADYEGTVRDLLSsitkdFYTHPY---------FKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLD 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1828880889 158 EPTVGVDPGLR---ASFWRYFRELTDEGASILITTHYMDEAVNcDRVaIVIAGR--VLVTATPEEIMAE 221
Cdd:cd03237 141 EPSAYLDVEQRlmaSKVIRRFAENNEKTAFVVEHDIIMIDYLA-DRL-IVFEGEpsVNGVANPPQSLRS 207
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
21-217 |
7.73e-21 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 90.88 E-value: 7.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 21 GLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPD---SGEIELLGRKMPDKEVLARVGYMPQELALYLNLTVEENLWF 97
Cdd:TIGR00955 43 NVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIDAKEMRAISAYVQQDDLFIPTLTVREHLMF 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 98 YSRLY---GLPREEFERRKEEVLRFVGLEEFRDRL------VAELSGGMQRRASLACALVHEPEFLILDEPTVGVDPGLR 168
Cdd:TIGR00955 123 QAHLRmprRVTKKEKRERVDEVLQALGLRKCANTRigvpgrVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMA 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1828880889 169 ASFWRYFRELTDEGASILITTHYMDEAVNC--DRVAIVIAGRVLVTATPEE 217
Cdd:TIGR00955 203 YSVVQVLKGLAQKGKTIICTIHQPSSELFElfDKIILMAEGRVAYLGSPDQ 253
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
4-231 |
8.27e-21 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 87.43 E-value: 8.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 4 LVVKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGL--LKPDSGEIELLGR---KM-PDKEVLARVG 77
Cdd:COG0396 1 LEIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEdilELsPDERARAGIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 78 Y---MPQE-----LALYLNLTVEENlwfysRLYGLPREEFERRKEEVLRFVGL-EEFRDRLVAE-LSGGMQRRASLACAL 147
Cdd:COG0396 81 LafqYPVEipgvsVSNFLRTALNAR-----RGEELSAREFLKLLKEKMKELGLdEDFLDRYVNEgFSGGEKKRNEILQML 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 148 VHEPEFLILDEPTVGVD-PGLRA-SfwRYFRELTDEGASILITTHY--MDEAVNCDRVAIVIAGRVLVTATPE---EIMA 220
Cdd:COG0396 156 LLEPKLAILDETDSGLDiDALRIvA--EGVNKLRSPDRGILIITHYqrILDYIKPDFVHVLVDGRIVKSGGKElalELEE 233
|
250
....*....|.
gi 1828880889 221 EtGSATLEEAV 231
Cdd:COG0396 234 E-GYDWLKEEA 243
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
7-192 |
1.66e-20 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 86.47 E-value: 1.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 7 KELRKSY-GDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGR---KMPDKEV--LAR-VGYM 79
Cdd:PRK10908 5 EHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHditRLKNREVpfLRRqIGMI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 80 PQELALYLNLTVEENLWFYSRLYGLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLILDEP 159
Cdd:PRK10908 85 FQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEP 164
|
170 180 190
....*....|....*....|....*....|...
gi 1828880889 160 TVGVDPGLRASFWRYFRELTDEGASILITTHYM 192
Cdd:PRK10908 165 TGNLDDALSEGILRLFEEFNRVGVTVLMATHDI 197
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
19-220 |
2.12e-20 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 89.29 E-value: 2.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 19 VRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGrkmpdKEVLARvgyMPQE-LA------------- 84
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDG-----HEVVTR---SPQDgLAngivyisedrkrd 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 85 -LYLNLTVEEN-----LWFYSRLYGlpREEFERRKEEVLRFVGLeeF------RDRLVAELSGGMQRRASLACALVHEPE 152
Cdd:PRK10762 340 gLVLGMSVKENmsltaLRYFSRAGG--SLKHADEQQAVSDFIRL--FniktpsMEQAIGLLSGGNQQKVAIARGLMTRPK 415
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1828880889 153 FLILDEPTVGVDPGLRASFWRYFRELTDEGASILITTHYMDEAVN-CDRVAIVIAGRV-----LVTATPEEIMA 220
Cdd:PRK10762 416 VLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGmSDRILVMHEGRIsgeftREQATQEKLMA 489
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-218 |
2.54e-20 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 87.98 E-value: 2.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 1 MPALVVKELRKSY-GDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKMPDKEVLARVGYM 79
Cdd:PRK11650 1 MAGLKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRDIAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 80 P-QELALYLNLTVEENLWFYSRLYGLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLILDE 158
Cdd:PRK11650 81 VfQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1828880889 159 PTVGVDPGLRASFWRYFRELTDE-GASILITTHYMDEAVN-CDRVAIVIAGRVLVTATPEEI 218
Cdd:PRK11650 161 PLSNLDAKLRVQMRLEIQRLHRRlKTTSLYVTHDQVEAMTlADRVVVMNGGVAEQIGTPVEV 222
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-211 |
2.70e-20 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 86.52 E-value: 2.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 1 MPALVVKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEI----------ELLGRKMPDK 70
Cdd:PRK11701 4 QPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVhyrmrdgqlrDLYALSEAER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 71 EVLARV--GYMPQELALYLNLTVE------ENL----WfysRLYGlpreEFERRKEEVLRFVGLEEFR-DRLVAELSGGM 137
Cdd:PRK11701 84 RRLLRTewGFVHQHPRDGLRMQVSaggnigERLmavgA---RHYG----DIRATAGDWLERVEIDAARiDDLPTTFSGGM 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1828880889 138 QRRASLACALVHEPEFLILDEPTVGVDPGLRASFWRYFRELTDE-GASILITTHymDEAvncdrVAIVIAGRVLV 211
Cdd:PRK11701 157 QQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRElGLAVVIVTH--DLA-----VARLLAHRLLV 224
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1-208 |
3.98e-20 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 88.43 E-value: 3.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 1 MPALVVKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKMPDKEV----LARV 76
Cdd:PRK11288 2 SPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTtaalAAGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 77 GYMPQELALYLNLTVEENLWfysrLYGLPREEFERRKEEVLRFVG--LEEFRDRL-----VAELSGGMQRRASLACALVH 149
Cdd:PRK11288 82 AIIYQELHLVPEMTVAENLY----LGQLPHKGGIVNRRLLNYEAReqLEHLGVDIdpdtpLKYLSIGQRQMVEIAKALAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 150 EPEFLILDEPTVGVDPGLRASFWRYFRELTDEGASILITTHYMDEAVN-CDRVAIVIAGR 208
Cdd:PRK11288 158 NARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFAlCDAITVFKDGR 217
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
22-218 |
6.40e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 85.57 E-value: 6.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 22 LSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKMPD---KEVLARVGYMPQELA-LYLNLTVEENLWF 97
Cdd:PRK13648 28 VSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDdnfEKLRKHIGIVFQNPDnQFVGSIVKYDVAF 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 98 YSRLYGLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLILDEPTVGVDPGLRASFWRYFRE 177
Cdd:PRK13648 108 GLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRK 187
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1828880889 178 LTDE-GASILITTHYMDEAVNCDRVAIVIAGRVLVTATPEEI 218
Cdd:PRK13648 188 VKSEhNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEI 229
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
7-219 |
6.73e-20 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 85.42 E-value: 6.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 7 KELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLG---RKMPDKEVLARVGYMPQEL 83
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGehiQHYASKEVARRIGLLAQNA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 84 ALYLNLTVEE----NLWFYSRLYGLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLILDEP 159
Cdd:PRK10253 91 TTPGDITVQElvarGRYPHQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1828880889 160 TVGVDPGLRASFWRYFRELTDE-GASILITTHYMDEAvnCDRVAIVIA---GRVLVTATPEEIM 219
Cdd:PRK10253 171 TTWLDISHQIDLLELLSELNREkGYTLAAVLHDLNQA--CRYASHLIAlreGKIVAQGAPKEIV 232
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
9-220 |
1.50e-19 |
|
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: 86.66 E-value: 1.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 9 LRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLkPDSGEIELLGR---KMPDKEVLARVGYM------ 79
Cdd:COG4172 292 FRRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQdldGLSRRALRPLRRRMqvvfqd 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 80 PqelalY--LN--LTVE----ENLWFYSRlyGLPREEFERRKEEVLRFVGL-EEFRDRLVAELSGGmQR-RASLACALVH 149
Cdd:COG4172 371 P-----FgsLSprMTVGqiiaEGLRVHGP--GLSAAERRARVAEALEEVGLdPAARHRYPHEFSGG-QRqRIAIARALIL 442
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1828880889 150 EPEFLILDEPTVGVDPGLRASFWRYFRELTDE-GASILITTHymDEAVN---CDRVAIVIAGRVLVTATPEEIMA 220
Cdd:COG4172 443 EPKLLVLDEPTSALDVSVQAQILDLLRDLQREhGLAYLFISH--DLAVVralAHRVMVMKDGKVVEQGPTEQVFD 515
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
2-190 |
2.38e-19 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 82.97 E-value: 2.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 2 PALVVKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKMPDKEVLARVGYMPQ 81
Cdd:PRK13543 10 PLLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAYLGH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 82 ELALYLNLTVEENLWFYSRLYGlprEEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLILDEPTV 161
Cdd:PRK13543 90 LPGLKADLSTLENLHFLCGLHG---RRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYA 166
|
170 180
....*....|....*....|....*....
gi 1828880889 162 GVDPGLRASFWRYFRELTDEGASILITTH 190
Cdd:PRK13543 167 NLDLEGITLVNRMISAHLRGGGAALVTTH 195
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-239 |
3.76e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 83.35 E-value: 3.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 3 ALVVKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPD-----SGEIELLGR-----KMPDKEV 72
Cdd:PRK14267 4 AIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRniyspDVDPIEV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 73 LARVGYMPQELALYLNLTVEENLWFYSRLYGL--PREEFERRKEEVLRFVGL-EEFRDRL---VAELSGGMQRRASLACA 146
Cdd:PRK14267 84 RREVGMVFQYPNPFPHLTIYDNVAIGVKLNGLvkSKKELDERVEWALKKAALwDEVKDRLndyPSNLSGGQRQRLVIARA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 147 LVHEPEFLILDEPTVGVDPGLRASFWRYFRELTDEGASILITTHYMDEAVNCDRVAIVIAGRvLVTATPEEIMAETGSAT 226
Cdd:PRK14267 164 LAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARVSDYVAFLYLGK-LIEVGPTRKVFENPEHE 242
|
250
....*....|...
gi 1828880889 227 LEEAVlkLTGVKG 239
Cdd:PRK14267 243 LTEKY--VTGALG 253
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
15-223 |
4.29e-19 |
|
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: 82.59 E-value: 4.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 15 DFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKMPD---KEVLARVGYMPQELALYlNLTV 91
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDlnlRWLRSQIGLVSQEPVLF-DGTI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 92 EENLwfysrLYGLPrEEFERRKEEVLRFVGLEEF-------RDRLVAE----LSGGMQRRASLACALVHEPEFLILDEPT 160
Cdd:cd03249 94 AENI-----RYGKP-DATDEEVEEAAKKANIHDFimslpdgYDTLVGErgsqLSGGQKQRIAIARALLRNPKILLLDEAT 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1828880889 161 VGVDP--------GL-RASfwryfreltdEGASILITTHYMDEAVNCDRVAIVIAGRVLVTATPEEIMAETG 223
Cdd:cd03249 168 SALDAeseklvqeALdRAM----------KGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKG 229
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
12-223 |
5.81e-19 |
|
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: 82.28 E-value: 5.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 12 SYGD-FEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLG---RKMPDKEVLARVGYMPQELALYl 87
Cdd:cd03253 9 AYDPgRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGqdiREVTLDSLRRAIGVVPQDTVLF- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 88 NLTVEENLwfysrLYGLPREEFERRKEEVL------RFVGLEEFRDRLVAE----LSGGMQRRASLACALVHEPEFLILD 157
Cdd:cd03253 88 NDTIGYNI-----RYGRPDATDEEVIEAAKaaqihdKIMRFPDGYDTIVGErglkLSGGEKQRVAIARAILKNPPILLLD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1828880889 158 EPTVGVDPGLRASFWRYFRELTDEGASILItTHYMDEAVNCDRVaIVIA-GRVLVTATPEEIMAETG 223
Cdd:cd03253 163 EATSALDTHTEREIQAALRDVSKGRTTIVI-AHRLSTIVNADKI-IVLKdGRIVERGTHEELLAKGG 227
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
18-217 |
6.51e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 82.83 E-value: 6.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 18 AVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGR---KMPDKE---VLARV------GYMPqelal 85
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKdvtKLPEYKrakYIGRVfqdpmmGTAP----- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 86 ylNLTVEENL----------------------WFYSRLYGLPReeferrkeevlrfvGLEefrDRL---VAELSGGmQRR 140
Cdd:COG1101 96 --SMTIEENLalayrrgkrrglrrgltkkrreLFRELLATLGL--------------GLE---NRLdtkVGLLSGG-QRQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 141 A-SLACALVHEPEFLILDEPTVGVDPGlRASFwryFRELTDE-----GASILITTHYMDEAVNC-DRVAIVIAGRVLVTA 213
Cdd:COG1101 156 AlSLLMATLTKPKLLLLDEHTAALDPK-TAAL---VLELTEKiveenNLTTLMVTHNMEQALDYgNRLIMMHEGRIILDV 231
|
....
gi 1828880889 214 TPEE 217
Cdd:COG1101 232 SGEE 235
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
18-223 |
1.55e-18 |
|
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: 81.12 E-value: 1.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 18 AVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKMPD---KEVLARVGYMPQELALYlNLTVEEN 94
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDytlASLRRQIGLVSQDVFLF-NDTVAEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 95 LwfysrLYGLPrEEFERRKEEVLRFVGLEEFRDRL-------VAE----LSGGMQRRASLACALVHEPEFLILDEPTVGV 163
Cdd:cd03251 96 I-----AYGRP-GATREEVEEAARAANAHEFIMELpegydtvIGErgvkLSGGQRQRIAIARALLKDPPILILDEATSAL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 164 DPGLRASFWRYFRELTdEGASILITTHYMDEAVNCDRVAIVIAGRVLVTATPEEIMAETG 223
Cdd:cd03251 170 DTESERLVQAALERLM-KNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGG 228
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
17-209 |
1.63e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 83.95 E-value: 1.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 17 EAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKMPDKEVLARVG----YMP---QELALYLNL 89
Cdd:PRK15439 277 EGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLArglvYLPedrQSSGLYLDA 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 90 TVEENLwfYSRLYGLPREEFERRKEEVLrfvgLEEFR----------DRLVAELSGGMQRRASLACALVHEPEFLILDEP 159
Cdd:PRK15439 357 PLAWNV--CALTHNRRGFWIKPARENAV----LERYRralnikfnhaEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEP 430
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1828880889 160 TVGVDPGLRASFWRYFRELTDEGASILITTHYMDEAVN-CDRVAIVIAGRV 209
Cdd:PRK15439 431 TRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQmADRVLVMHQGEI 481
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1-200 |
2.50e-18 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 80.59 E-value: 2.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 1 MPA---LVVKELRKSYGDFEA----VRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKMP--DKE 71
Cdd:PRK10584 1 MPAeniVEVHHLKKSVGQGEHelsiLTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHqmDEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 72 VLAR-----VGYMPQELALYLNLTVEENLWFYSRLYGLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACA 146
Cdd:PRK10584 81 ARAKlrakhVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1828880889 147 LVHEPEFLILDEPTVGVDPGLRASFWRYFRELTDEGASILI-TTHYMDEAVNCDR 200
Cdd:PRK10584 161 FNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLIlVTHDLQLAARCDR 215
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-209 |
5.88e-18 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 80.11 E-value: 5.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 4 LVVKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEieLLGRKMPDKEVLARVGYMPQEL 83
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGE--LLAGTAPLAEAREDTRLMFQDA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 84 ALYLNLTVEENLwfysrlyGLPREEF-ERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLILDEPTVG 162
Cdd:PRK11247 91 RLLPWKKVIDNV-------GLGLKGQwRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1828880889 163 VDP-------GLRASFWRyfreltDEGASILITTHYMDEAVN-CDRVAIVIAGRV 209
Cdd:PRK11247 164 LDAltriemqDLIESLWQ------QHGFTVLLVTHDVSEAVAmADRVLLIEEGKI 212
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
2-208 |
6.66e-18 |
|
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: 79.40 E-value: 6.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 2 PALVVKELRKSY-----GD--FEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGR-------KM 67
Cdd:COG4778 3 TLLEVENLSKTFtlhlqGGkrLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvdlaQA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 68 PDKEVLA----RVGYMPQEL-------ALYLnltVEENLwfysRLYGLPREEFERRKEEVLRFVGLEEfrdRL----VAE 132
Cdd:COG4778 83 SPREILAlrrrTIGYVSQFLrviprvsALDV---VAEPL----LERGVDREEARARARELLARLNLPE---RLwdlpPAT 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1828880889 133 LSGGMQRRASLACALVHEPEFLILDEPTVGVDPGLRASFWRYFRELTDEGASILITTHYMD--EAVnCDRVAIVIAGR 208
Cdd:COG4778 153 FSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEvrEAV-ADRVVDVTPFS 229
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
4-190 |
6.84e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 78.84 E-value: 6.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 4 LVVKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKMpDKEVLA---RVGYMP 80
Cdd:PRK13540 2 LDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI-KKDLCTyqkQLCFVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 81 QELALYLNLTVEENLwfysrLYGLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLILDEPT 160
Cdd:PRK13540 81 HRSGINPYLTLRENC-----LYDIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPL 155
|
170 180 190
....*....|....*....|....*....|
gi 1828880889 161 VGVDPGLRASFWRYFRELTDEGASILITTH 190
Cdd:PRK13540 156 VALDELSLLTIITKIQEHRAKGGAVLLTSH 185
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
6-220 |
8.68e-18 |
|
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: 81.77 E-value: 8.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 6 VKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGL--LKPDSGEI----------------ELLGRKM 67
Cdd:TIGR03269 3 VKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalcekcgyverpSKVGEPC 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 68 PD--------------------KEVLARVGYMPQE-LALYLNLTVEENLWFYSRLYGLPREEFERRKEEVLRFVGLEEFR 126
Cdd:TIGR03269 83 PVcggtlepeevdfwnlsdklrRRIRKRIAIMLQRtFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSHRI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 127 DRLVAELSGGMQRRASLACALVHEPEFLILDEPTVGVDPGLRASFWRYFRELT-DEGASILITTHYMDEAVNCDRVAIVI 205
Cdd:TIGR03269 163 THIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVkASGISMVLTSHWPEVIEDLSDKAIWL 242
|
250
....*....|....*.
gi 1828880889 206 A-GRVLVTATPEEIMA 220
Cdd:TIGR03269 243 EnGEIKEEGTPDEVVA 258
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
21-232 |
1.08e-17 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 79.46 E-value: 1.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 21 GLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGR---KMPDKEVLA-----RVGYMPQELALYLNLTVE 92
Cdd:TIGR02769 29 NVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQdlyQLDRKQRRAfrrdvQLVFQDSPSAVNPRMTVR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 93 ENLWFYSR-LYGLPREEFERRKEEVLRFVGLE-EFRDRLVAELSGGMQRRASLACALVHEPEFLILDEPTVGVDPGLRAS 170
Cdd:TIGR02769 109 QIIGEPLRhLTSLDESEQKARIAELLDMVGLRsEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMVLQAV 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1828880889 171 FWRYFRELTDE-GASILITTHYMDEAVN-CDRVAIVIAGRVLVTATPEEI--MAETGSATLEEAVL 232
Cdd:TIGR02769 189 ILELLRKLQQAfGTAYLFITHDLRLVQSfCQRVAVMDKGQIVEECDVAQLlsFKHPAGRNLQSAVL 254
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
22-229 |
1.64e-17 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 79.06 E-value: 1.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 22 LSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKMP--DKEVLAR-VGYMPQELALYLNLTVEENL--- 95
Cdd:PRK10575 30 LSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLEswSSKAFARkVAYLPQQLPAAEGMTVRELVaig 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 96 -WFYSRLYGLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLILDEPTVGVDPGLRASFWRY 174
Cdd:PRK10575 110 rYPWHGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLAL 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1828880889 175 FRELTDE-GASILITTHYMDEAVN-CDRVAIVIAGRVLVTATPEEIMAetgSATLEE 229
Cdd:PRK10575 190 VHRLSQErGLTVIAVLHDINMAARyCDYLVALRGGEMIAQGTPAELMR---GETLEQ 243
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4-221 |
1.65e-17 |
|
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: 81.02 E-value: 1.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 4 LVVKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDS--GEI-----ELLGRKMPDKEVlARV 76
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIywsgsPLKASNIRDTER-AGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 77 GYMPQELALYLNLTVEENLwFYSRLYGLPREEFERRKE-----EVLRFVGLEEFRD-RLVAELSGGMQRRASLACALVHE 150
Cdd:TIGR02633 81 VIIHQELTLVPELSVAENI-FLGNEITLPGGRMAYNAMylrakNLLRELQLDADNVtRPVGDYGGGQQQLVEIAKALNKQ 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1828880889 151 PEFLILDEPTVGVDPGLRASFWRYFRELTDEGASILITTHYMDE-AVNCDRVAIVIAGRVLVTaTPEEIMAE 221
Cdd:TIGR02633 160 ARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEvKAVCDTICVIRDGQHVAT-KDMSTMSE 230
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
6-215 |
2.12e-17 |
|
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: 77.45 E-value: 2.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 6 VKELRKSYG-DFEAV-RGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLG---RKMPDKEVLARVGYMP 80
Cdd:cd03369 9 VENLSVRYApDLPPVlKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGidiSTIPLEDLRSSLTIIP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 81 QELALYLNlTVEENLWFYSR-----LYGlpreeferrkeeVLRfvgleefrdrlVAE----LSGGMQRRASLACALVHEP 151
Cdd:cd03369 89 QDPTLFSG-TIRSNLDPFDEysdeeIYG------------ALR-----------VSEgglnLSQGQRQLLCLARALLKRP 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1828880889 152 EFLILDEPTVGVDPGLRASFWRYFRELTdEGASILITTHYMDEAVNCDRVAIVIAGRVLVTATP 215
Cdd:cd03369 145 RVLVLDEATASIDYATDALIQKTIREEF-TNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
4-216 |
2.58e-17 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 78.07 E-value: 2.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 4 LVVKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGllKPD----SGEIELLGRKMPDKEV--LARVG 77
Cdd:TIGR01978 1 LKIKDLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAG--HPSyevtSGTILFKGQDLLELEPdeRARAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 78 Y-----MPQELAlylNLTVEEnlwFYSRLYGLPREEFERRKEEVLRFVGL-----------EEFRDRLVAE-LSGGMQRR 140
Cdd:TIGR01978 79 LflafqYPEEIP---GVSNLE---FLRSALNARRSARGEEPLDLLDFEKLlkeklalldmdEEFLNRSVNEgFSGGEKKR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1828880889 141 ASLACALVHEPEFLILDEPTVGVD-PGLRASFwRYFRELTDEGASILITTHY--MDEAVNCDRVAIVIAGRVLVTATPE 216
Cdd:TIGR01978 153 NEILQMALLEPKLAILDEIDSGLDiDALKIVA-EGINRLREPDRSFLIITHYqrLLNYIKPDYVHVLLDGRIVKSGDVE 230
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
20-223 |
3.02e-17 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 80.15 E-value: 3.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 20 RGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKMPDKE---VLARVGYMPQELALYlNLTVEENLW 96
Cdd:TIGR00958 498 KGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDhhyLHRQVALVGQEPVLF-SGSVRENIA 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 97 FYSRLYGLPREEFERRKEEVLRFV-GLEEFRDRLVAE----LSGGMQRRASLACALVHEPEFLILDEPTVGVDPGLRASF 171
Cdd:TIGR00958 577 YGLTDTPDEEIMAAAKAANAHDFImEFPNGYDTEVGEkgsqLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLL 656
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1828880889 172 --WRYFRELTdegasILITTHYMDEAVNCDRVAIVIAGRVLVTATPEEIMAETG 223
Cdd:TIGR00958 657 qeSRSRASRT-----VLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQG 705
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
6-160 |
4.44e-17 |
|
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: 79.59 E-value: 4.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 6 VKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIElLGRKMpdkevlaRVGYMPQEL-A 84
Cdd:TIGR03719 325 AENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIE-IGETV-------KLAYVDQSRdA 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 85 LYLNLTVEE------------NLWFYSRLYglpreeferrkeeVLRFvgleEFR----DRLVAELSGGMQRRASLACALV 148
Cdd:TIGR03719 397 LDPNKTVWEeisggldiiklgKREIPSRAY-------------VGRF----NFKgsdqQKKVGQLSGGERNRVHLAKTLK 459
|
170
....*....|..
gi 1828880889 149 HEPEFLILDEPT 160
Cdd:TIGR03719 460 SGGNVLLLDEPT 471
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
2-190 |
4.63e-17 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 77.16 E-value: 4.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 2 PALVVKELRKSYGD----FEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKMPDKEVLAR-- 75
Cdd:PRK11629 4 ILLQCDNLCKRYQEgsvqTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKae 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 76 -----VGYMPQELALYLNLTVEENLWFYSRLYGLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHE 150
Cdd:PRK11629 84 lrnqkLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNN 163
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1828880889 151 PEFLILDEPTVGVDPGLRASFWRYFRELT-DEGASILITTH 190
Cdd:PRK11629 164 PRLVLADEPTGNLDARNADSIFQLLGELNrLQGTAFLVVTH 204
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
29-220 |
4.94e-17 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 79.54 E-value: 4.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 29 GEIFGLIGPNGAGKTTTIKTIVGLLKPDS--GEIELLGRKmPDKEVLARVGYMPQELALYLNLTVEENLWFYSRLY---G 103
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRK-PTKQILKRTGFVTQDDILYPHLTVRETLVFCSLLRlpkS 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 104 LPREEFERRKEEVLRFVGLEEFRDRLVAE-----LSGGMQRRASLACALVHEPEFLILDEPTVGVDPGLRASFWRYFREL 178
Cdd:PLN03211 173 LTKQEKILVAESVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSL 252
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1828880889 179 TDEGASILITTHYMDEAV--NCDRVAIVIAGRVLVTATPEEIMA 220
Cdd:PLN03211 253 AQKGKTIVTSMHQPSSRVyqMFDSVLVLSEGRCLFFGKGSDAMA 296
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
15-223 |
5.24e-17 |
|
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: 79.38 E-value: 5.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 15 DFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKMPD---KEVLARVGYMPQELALYlNLTV 91
Cdd:TIGR02203 344 DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADytlASLRRQVALVSQDVVLF-NDTI 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 92 EENLwfysrLYGLPREEFERRKEEVLRFVGLEEFRDRL-------VAE----LSGGMQRRASLACALVHEPEFLILDEPT 160
Cdd:TIGR02203 423 ANNI-----AYGRTEQADRAEIERALAAAYAQDFVDKLplgldtpIGEngvlLSGGQRQRLAIARALLKDAPILILDEAT 497
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1828880889 161 VGVDP----GLRASFWRYFRELTDegasiLITTHYMDEAVNCDRVAIVIAGRVLVTATPEEIMAETG 223
Cdd:TIGR02203 498 SALDNeserLVQAALERLMQGRTT-----LVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARNG 559
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
31-218 |
6.44e-17 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 78.38 E-value: 6.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 31 IFGLigpNGAGKTTTIKTIVGLLKPDSGEIELLGRKMPDKE---VLA----RVGYMPQELALYLNLTVEENLwfysrLYG 103
Cdd:PRK11144 29 IFGR---SGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEkgiCLPpekrRIGYVFQDARLFPHYKVRGNL-----RYG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 104 LpREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLILDEPTVGVDPGLRASFWRYFRELTDE-G 182
Cdd:PRK11144 101 M-AKSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREiN 179
|
170 180 190
....*....|....*....|....*....|....*..
gi 1828880889 183 ASILITTHYMDEAVN-CDRVAIVIAGRVLVTATPEEI 218
Cdd:PRK11144 180 IPILYVSHSLDEILRlADRVVVLEQGKVKAFGPLEEV 216
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-201 |
6.67e-17 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 79.38 E-value: 6.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 1 MPALV-VKELRKSY----GDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTtIKTIVGLL-KPDSGEIELLGRKMP--DKEV 72
Cdd:PRK10535 1 MTALLeLKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKST-LMNILGCLdKPTSGTYRVAGQDVAtlDADA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 73 LARV-----GYMPQELALYLNLTVEENLWFYSRLYGLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACAL 147
Cdd:PRK10535 80 LAQLrrehfGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARAL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1828880889 148 VHEPEFLILDEPTVGVDPGLRASFWRYFRELTDEGASILITTHYMDEAVNCDRV 201
Cdd:PRK10535 160 MNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQAERV 213
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
6-62 |
2.71e-16 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 77.47 E-value: 2.71e-16
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1828880889 6 VKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIEL 62
Cdd:PRK11819 327 AENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI 383
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
15-232 |
4.04e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 75.08 E-value: 4.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 15 DFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGR---------KMPDKEVLARVGYMPQELAL 85
Cdd:PRK14246 22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkdifQIDAIKLRKEVGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 86 YLNLTVEENLWFYSRLYGLPRE-EFERRKEEVLRFVGL-EEFRDRL---VAELSGGMQRRASLACALVHEPEFLILDEPT 160
Cdd:PRK14246 102 FPHLSIYDNIAYPLKSHGIKEKrEIKKIVEECLRKVGLwKEVYDRLnspASQLSGGQQQRLTIARALALKPKVLLMDEPT 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1828880889 161 VGVDPGLRASFWRYFRELTDEGASILITTHYMDEAVNCDRVAIVIAGRVLVTATPEEIMAETGSATLEEAVL 232
Cdd:PRK14246 182 SMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKYVI 253
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
19-190 |
4.64e-16 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 76.77 E-value: 4.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 19 VRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELlgrkmPDkevLARVGYMPQELalYLNL-TVEENLwf 97
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIAR-----PA---GARVLFLPQRP--YLPLgTLREAL-- 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 98 ysrLY-GLPREEFERRKEEVLRFVGLEEFRDRLVAE------LSGGMQRRASLACALVHEPEFLILDEPTVGVDPGLRAS 170
Cdd:COG4178 447 ---LYpATAEAFSDAELREALEAVGLGHLAERLDEEadwdqvLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAA 523
|
170 180
....*....|....*....|
gi 1828880889 171 FWRYFRElTDEGASILITTH 190
Cdd:COG4178 524 LYQLLRE-ELPGTTVISVGH 542
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
3-81 |
5.73e-16 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 76.47 E-value: 5.73e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1828880889 3 ALVVKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIellgrKMPDKevlARVGYMPQ 81
Cdd:PRK15064 319 ALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV-----KWSEN---ANIGYYAQ 389
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
2-210 |
1.06e-15 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 74.04 E-value: 1.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 2 PALVVKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTI--VGLLKPD---SGEI-----ELLGRKMPDKE 71
Cdd:PRK14239 4 PILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtiTGSIvynghNIYSPRTDTVD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 72 VLARVGYMPQELALYlNLTVEENLWFYSRLYGLPREEFE-RRKEEVLRFVGL-EEFRDRLVAE---LSGGMQRRASLACA 146
Cdd:PRK14239 84 LRKEIGMVFQQPNPF-PMSIYENVVYGLRLKGIKDKQVLdEAVEKSLKGASIwDEVKDRLHDSalgLSGGQQQRVCIARV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1828880889 147 LVHEPEFLILDEPTVGVDPGLRASFWRYFRELTDEgASILITTHYMDEAVN-CDRVAIVIAGRVL 210
Cdd:PRK14239 163 LATSPKIILLDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTRSMQQASRiSDRTGFFLDGDLI 226
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-221 |
2.91e-15 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 74.20 E-value: 2.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 1 MPALVVKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLkPD---SGEI-----ELLGRKMPDKEV 72
Cdd:PRK13549 3 EYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIifegeELQASNIRDTER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 73 lARVGYMPQELALYLNLTVEENLWF-----------YSRLYglpreefeRRKEEVLRFVGLEEFRDRLVAELSGGMQRRA 141
Cdd:PRK13549 82 -AGIAIIHQELALVKELSVLENIFLgneitpggimdYDAMY--------LRAQKLLAQLKLDINPATPVGNLGLGQQQLV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 142 SLACALVHEPEFLILDEPTVGVDPGLRASFWRYFRELTDEGASILITTHYMDE--AVnCDRVAIVIAGRVLVTaTPEEIM 219
Cdd:PRK13549 153 EIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEvkAI-SDTICVIRDGRHIGT-RPAAGM 230
|
..
gi 1828880889 220 AE 221
Cdd:PRK13549 231 TE 232
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
20-208 |
3.12e-15 |
|
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: 71.73 E-value: 3.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 20 RGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGrkmpdkevlaRVGYMPQElALYLNLTVEEN-LW-- 96
Cdd:cd03250 22 KDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG----------SIAYVSQE-PWIQNGTIRENiLFgk 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 97 -FYSRLYglpreeferrkEEVLRFVGLE------EFRDR-LVAE----LSGGMQRRASLACALVHEPEFLILDEPTVGVD 164
Cdd:cd03250 91 pFDEERY-----------EKVIKACALEpdleilPDGDLtEIGEkginLSGGQKQRISLARAVYSDADIYLLDDPLSAVD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1828880889 165 PGLRASFWRY-FRELTDEGASILITTHYMDEAVNCDRVAIVIAGR 208
Cdd:cd03250 160 AHVGRHIFENcILGLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-165 |
7.25e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 71.61 E-value: 7.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 1 MPALVVKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDS-----GEIELLGRKMPDKEV--- 72
Cdd:PRK14258 5 IPAIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIYERRVnln 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 73 -LARVGYMPQELALYLNLTVEENLWFYSRLYGL-PREEFERRKEEVLRFVGL-EEFRDRL---VAELSGGMQRRASLACA 146
Cdd:PRK14258 85 rLRRQVSMVHPKPNLFPMSVYDNVAYGVKIVGWrPKLEIDDIVESALKDADLwDEIKHKIhksALDLSGGQQQRLCIARA 164
|
170
....*....|....*....
gi 1828880889 147 LVHEPEFLILDEPTVGVDP 165
Cdd:PRK14258 165 LAVKPKVLLMDEPCFGLDP 183
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
19-226 |
7.45e-15 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 71.65 E-value: 7.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 19 VRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPdsGEIELLGRKMPDKEVLArvgymPQELALYLNLTVEEN---- 94
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPA--GVRQTAGRVLLDGKPVA-----PCALRGRKIATIMQNprsa 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 95 ------LWFYSR--LYGLPREEFERRKEEVLRFVGLEEfRDRLVA----ELSGGMQRRASLACALVHEPEFLILDEPTVG 162
Cdd:PRK10418 92 fnplhtMHTHARetCLALGKPADDATLTAALEAVGLEN-AARVLKlypfEMSGGMLQRMMIALALLCEAPFIIADEPTTD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1828880889 163 VDPGLRASFWRYFRELTDE-GASILITTHYMDEAVNC-DRVAIVIAGRVLVTATPEEIMAETGSAT 226
Cdd:PRK10418 171 LDVVAQARILDLLESIVQKrALGMLLVTHDMGVVARLaDDVAVMSHGRIVEQGDVETLFNAPKHAV 236
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
19-220 |
9.71e-15 |
|
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: 72.94 E-value: 9.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 19 VRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPD-SGEIELLGR----KMPDKEVLARVGYMPQE---------LA 84
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKpvdiRNPAQAIRAGIAMVPEDrkrhgivpiLG 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 85 LYLNLTVEEnLWFYSRLYGLPREEFERRKEEVLRFVGLEEFRDRL-VAELSGGMQRRASLACALVHEPEFLILDEPTVGV 163
Cdd:TIGR02633 356 VGKNITLSV-LKSFCFKMRIDAAAELQIIGSAIQRLKVKTASPFLpIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGV 434
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1828880889 164 DPGLRASFWRYFRELTDEGASILITTHYMDEAVN-CDRVAIVIAGRV---LVTA--TPEEIMA 220
Cdd:TIGR02633 435 DVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGlSDRVLVIGEGKLkgdFVNHalTQEQVLA 497
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
18-219 |
1.34e-14 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 72.45 E-value: 1.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 18 AVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKMPDKEVL-------ARVGYMPQELALYLNLT 90
Cdd:PRK10982 263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANeainhgfALVTEERRSTGIYAYLD 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 91 VE-----ENLWFYSRLYGL-PREEFERRKEEVLRFVGLEEFRDR-LVAELSGGMQRRASLACALVHEPEFLILDEPTVGV 163
Cdd:PRK10982 343 IGfnsliSNIRNYKNKVGLlDNSRMKSDTQWVIDSMRVKTPGHRtQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGI 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1828880889 164 DPGLRASFWRYFRELTDEGASILITTHYMDEAVN-CDRVAIVIAGRV-----LVTATPEEIM 219
Cdd:PRK10982 423 DVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGiTDRILVMSNGLVagivdTKTTTQNEIL 484
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-236 |
1.56e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 70.90 E-value: 1.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 2 PALVVKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKP-----DSGEIELLGRKMPD-KEVLA- 74
Cdd:PRK14271 20 PAMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIFNyRDVLEf 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 75 --RVGYMPQELALYlNLTVEENLWFYSRLYGL-PREEFERRKEEVLRFVGL-EEFRDRLVA---ELSGGMQRRASLACAL 147
Cdd:PRK14271 100 rrRVGMLFQRPNPF-PMSIMDNVLAGVRAHKLvPRKEFRGVAQARLTEVGLwDAVKDRLSDspfRLSGGQQQLLCLARTL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 148 VHEPEFLILDEPTVGVDPGLRASFWRYFRELTDEGASILITTHYMDEAVNCDRVAIVIAGRVLVTATPEEIMAETGSATL 227
Cdd:PRK14271 179 AVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAET 258
|
....*....
gi 1828880889 228 EEAVLKLTG 236
Cdd:PRK14271 259 ARYVAGLSG 267
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
22-201 |
1.58e-14 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 70.13 E-value: 1.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 22 LSFEVEKGEiFGLI-GPNGAGKTTTIKTIVGLLKPDSGEIELLGR---KMPDKEVLARVGYMPQELALYLNlTVEENLWF 97
Cdd:PRK10247 26 ISFSLRAGE-FKLItGPSGCGKSTLLKIVASLISPTSGTLLFEGEdisTLKPEIYRQQVSYCAQTPTLFGD-TVYDNLIF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 98 YSRLYGlPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLILDEPTVGVDPGLRAS----FWR 173
Cdd:PRK10247 104 PWQIRN-QQPDPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNvneiIHR 182
|
170 180
....*....|....*....|....*...
gi 1828880889 174 YFReltDEGASILITTHYMDEAVNCDRV 201
Cdd:PRK10247 183 YVR---EQNIAVLWVTHDKDEINHADKV 207
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-232 |
1.72e-14 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 70.87 E-value: 1.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 1 MPALVVKELRKSY---------GDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGR-----K 66
Cdd:PRK10419 1 MTLLNVSGLSHHYahgglsgkhQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEplaklN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 67 MPDKEVLARVGYM----------PQElalylnlTVEENLWFYSR-LYGLPREEFERRKEEVLRFVGL-EEFRDRLVAELS 134
Cdd:PRK10419 81 RAQRKAFRRDIQMvfqdsisavnPRK-------TVREIIREPLRhLLSLDKAERLARASEMLRAVDLdDSVLDKRPPQLS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 135 GGMQRRASLACALVHEPEFLILDEPTVGVDPGLRASFWRYFRELTDE-GASILITTHYMdEAVN--CDRVAIVIAGRVLV 211
Cdd:PRK10419 154 GGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDL-RLVErfCQRVMVMDNGQIVE 232
|
250 260
....*....|....*....|...
gi 1828880889 212 TAT--PEEIMAETGSATLEEAVL 232
Cdd:PRK10419 233 TQPvgDKLTFSSPAGRVLQNAVL 255
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
27-190 |
1.88e-14 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 72.12 E-value: 1.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 27 EKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIEllgrKMPDK-EVLA-------------------RVGYMPQ---EL 83
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPNLGDYD----EEPSWdEVLKrfrgtelqdyfkklangeiKVAHKPQyvdLI 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 84 ALYLNLTVEEnlwfysrLygLPREEFERRKEEVLRFVGLEEFRDRLVAELSGG-MQRRAsLACALVHEPEFLILDEPTVG 162
Cdd:COG1245 173 PKVFKGTVRE-------L--LEKVDERGKLDELAEKLGLENILDRDISELSGGeLQRVA-IAAALLRDADFYFFDEPSSY 242
|
170 180
....*....|....*....|....*...
gi 1828880889 163 VDPGLRASFWRYFRELTDEGASILITTH 190
Cdd:COG1245 243 LDIYQRLNVARLIRELAEEGKYVLVVEH 270
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
19-220 |
2.03e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 71.88 E-value: 2.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 19 VRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDS-GEIELLGRKM----PDKEVLARVGYMPQEL---ALYLNLT 90
Cdd:PRK13549 278 VDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRWeGEIFIDGKPVkirnPQQAIAQGIAMVPEDRkrdGIVPVMG 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 91 VEEN--LWFYSRLYGLPREEFERRKEEVLRFVgleefrDRL----------VAELSGGMQRRASLACALVHEPEFLILDE 158
Cdd:PRK13549 358 VGKNitLAALDRFTGGSRIDDAAELKTILESI------QRLkvktaspelaIARLSGGNQQKAVLAKCLLLNPKILILDE 431
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1828880889 159 PTVGVDPGLRASFWRYFRELTDEGASILITTHYMDEAVN-CDRVAIVIAGRV---LV--TATPEEIMA 220
Cdd:PRK13549 432 PTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGlSDRVLVMHEGKLkgdLInhNLTQEQVME 499
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
4-223 |
2.43e-14 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 71.69 E-value: 2.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 4 LVVKELRKSYG-DFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKMP--DKEVLAR-VGYM 79
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKdiDRHTLRQfINYL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 80 PQELALYLNlTVEENLwfysrLYGLPREEFERRKEEVLRFVGLEE--------FRDRLVAE---LSGGMQRRASLACALV 148
Cdd:TIGR01193 554 PQEPYIFSG-SILENL-----LLGAKENVSQDEIWAACEIAEIKDdienmplgYQTELSEEgssISGGQKQRIALARALL 627
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1828880889 149 HEPEFLILDEPTVGVDPGLRASFWRYFRELTDEgaSILITTHYMDEAVNCDRVAIVIAGRVLVTATPEEIMAETG 223
Cdd:TIGR01193 628 TDSKVLILDESTSNLDTITEKKIVNNLLNLQDK--TIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNG 700
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
15-209 |
2.62e-14 |
|
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: 69.42 E-value: 2.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 15 DFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKMPD------KEVLARVGYMPQELAlyln 88
Cdd:cd03248 26 DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQyehkylHSKVSLVGQEPVLFA---- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 89 LTVEENLwfysrLYGLPREEFERRKEEVLR-----FV-GLEEFRDRLVAE----LSGGMQRRASLACALVHEPEFLILDE 158
Cdd:cd03248 102 RSLQDNI-----AYGLQSCSFECVKEAAQKahahsFIsELASGYDTEVGEkgsqLSGGQKQRVAIARALIRNPQVLILDE 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1828880889 159 PTVGVDPGLRASFWRYFRElTDEGASILITTHYMDEAVNCDRVAIVIAGRV 209
Cdd:cd03248 177 ATSALDAESEQQVQQALYD-WPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
26-190 |
2.89e-14 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 71.68 E-value: 2.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 26 VEKGEIFGLIGPNGAGKTTTIKTIVGLLKP---DSGEIELLGRKMpDKEVLARVGYMPQELALYLNLTVEENLWFYSRLY 102
Cdd:TIGR00956 786 VKPGTLTALMGASGAGKTTLLNVLAERVTTgviTGGDRLVNGRPL-DSSFQRSIGYVQQQDLHLPTSTVRESLRFSAYLR 864
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 103 ---GLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGM---QR-RASLACALVHEPEFLI-LDEPTVGVDPGLRASFWRY 174
Cdd:TIGR00956 865 qpkSVSKSEKMEYVEEVIKLLEMESYADAVVGVPGEGLnveQRkRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKL 944
|
170
....*....|....*.
gi 1828880889 175 FRELTDEGASILITTH 190
Cdd:TIGR00956 945 MRKLADHGQAILCTIH 960
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
16-239 |
5.03e-14 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 70.65 E-value: 5.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 16 FEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIE----LLGRKmpDKEVL---------------ARV 76
Cdd:PRK10261 29 IAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQcdkmLLRRR--SRQVIelseqsaaqmrhvrgADM 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 77 GYMPQELALYLN--LTVEENLWFYSRLY-GLPREEFERRKEEVLRFVGLEEFR---DRLVAELSGGMQRRASLACALVHE 150
Cdd:PRK10261 107 AMIFQEPMTSLNpvFTVGEQIAESIRLHqGASREEAMVEAKRMLDQVRIPEAQtilSRYPHQLSGGMRQRVMIAMALSCR 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 151 PEFLILDEPTVGVDPGLRASFWRYFRELTDEGA-SILITTHYMDEAVN-CDRVAIVIAGRVLVTATPEEIM---AETGSA 225
Cdd:PRK10261 187 PAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmGVIFITHDMGVVAEiADRVLVMYQGEAVETGSVEQIFhapQHPYTR 266
|
250
....*....|....
gi 1828880889 226 TLEEAVLKLTGVKG 239
Cdd:PRK10261 267 ALLAAVPQLGAMKG 280
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-209 |
5.70e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 70.50 E-value: 5.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 1 MPALVVKEL----RKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPD-----SGEIELLGRKM--PD 69
Cdd:PRK15134 3 QPLLAIENLsvafRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPpvvypSGDIRFHGESLlhAS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 70 KEVLA-----RVGYMPQELALYLN--LTVEENLWFYSRLY-GLPREEFERRKEEVLRFVGLEEFRDRLVA---ELSGGMQ 138
Cdd:PRK15134 83 EQTLRgvrgnKIAMIFQEPMVSLNplHTLEKQLYEVLSLHrGMRREAARGEILNCLDRVGIRQAAKRLTDyphQLSGGER 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1828880889 139 RRASLACALVHEPEFLILDEPTVGVDPGLRASFWRYFRELTDE-GASILITTHYMDEAVN-CDRVAIVIAGRV 209
Cdd:PRK15134 163 QRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKlADRVAVMQNGRC 235
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-218 |
7.03e-14 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 69.77 E-value: 7.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 1 MPALVVKELRKSYGD----FEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLL----KPDSGEIELLGR---KMPD 69
Cdd:PRK11022 1 MALLNVDKLSVHFGDesapFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIdypgRVMAEKLEFNGQdlqRISE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 70 KE----VLARVGYMPQELALYLN--LTVEENLWFYSRLY-GLPREEFERRKEEVLRFVGLEEFRDRLVA---ELSGGMQR 139
Cdd:PRK11022 81 KErrnlVGAEVAMIFQDPMTSLNpcYTVGFQIMEAIKVHqGGNKKTRRQRAIDLLNQVGIPDPASRLDVyphQLSGGMSQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 140 RASLACALVHEPEFLILDEPTVGVDPGLRASFWRYFRELT--DEGASILITTHYMDEAVNCDRVAIVIAGRVLVTATPEE 217
Cdd:PRK11022 161 RVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQqkENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHD 240
|
.
gi 1828880889 218 I 218
Cdd:PRK11022 241 I 241
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
26-190 |
7.74e-14 |
|
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: 67.65 E-value: 7.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 26 VEKGEIFGLIGPNGAGKTTTI-----KTIVGLLKpdsGEIELLGRKmPDKEVLARVGYMPQELALYLNLTVEENLWFYSR 100
Cdd:cd03232 30 VKPGTLTALMGESGAGKTTLLdvlagRKTAGVIT---GEILINGRP-LDKNFQRSTGYVEQQDVHSPNLTVREALRFSAL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 101 LYGLpreeferrkeevlrfvGLEEfrdrlvaelsggmQRRASLACALVHEPEFLILDEPTVGVDPGLRASFWRYFRELTD 180
Cdd:cd03232 106 LRGL----------------SVEQ-------------RKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLAD 156
|
170
....*....|
gi 1828880889 181 EGASILITTH 190
Cdd:cd03232 157 SGQAILCTIH 166
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
2-227 |
8.14e-14 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 68.51 E-value: 8.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 2 PALVVKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGllKPD----SGEIELLGRKMPDK--EVLAR 75
Cdd:CHL00131 6 PILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPAykilEGDILFKGESILDLepEERAH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 76 VGYM-----PQEL-----ALYLNLTVEENLWFysrlYGLPREEFERRKEEV---LRFVGLEE-FRDRLVAE-LSGGMQRR 140
Cdd:CHL00131 84 LGIFlafqyPIEIpgvsnADFLRLAYNSKRKF----QGLPELDPLEFLEIInekLKLVGMDPsFLSRNVNEgFSGGEKKR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 141 ASLACALVHEPEFLILDEPTVGVDPGLRASFWRYFRELTDEGASILITTHY--MDEAVNCDRVAIVIAGRVLvtatpeei 218
Cdd:CHL00131 160 NEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHYqrLLDYIKPDYVHVMQNGKII-------- 231
|
....*....
gi 1828880889 219 maETGSATL 227
Cdd:CHL00131 232 --KTGDAEL 238
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
9-164 |
9.93e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 69.73 E-value: 9.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 9 LRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLkPDSGEI-------ELLGRK--MPdkeVLARVGYM 79
Cdd:PRK15134 292 LKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIwfdgqplHNLNRRqlLP---VRHRIQVV 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 80 PQELALYLN--LTV----EENLWFYSRlyGLPREEFERRKEEVLRFVGLE-EFRDRLVAELSGGMQRRASLACALVHEPE 152
Cdd:PRK15134 368 FQDPNSSLNprLNVlqiiEEGLRVHQP--TLSAAQREQQVIAVMEEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPS 445
|
170
....*....|..
gi 1828880889 153 FLILDEPTVGVD 164
Cdd:PRK15134 446 LIILDEPTSSLD 457
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
21-225 |
1.40e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 69.77 E-value: 1.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 21 GLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLG---RKMPDKEVLARVGYMPQELALYLNlTVEENLWF 97
Cdd:PLN03130 1257 GLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGcdiSKFGLMDLRKVLGIIPQAPVLFSG-TVRFNLDP 1335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 98 YSRL--YGLPREEFERRKEEVLR--FVGLeefrDRLVAE----LSGGMQRRASLACALVHEPEFLILDEPTVGVDPGLRA 169
Cdd:PLN03130 1336 FNEHndADLWESLERAHLKDVIRrnSLGL----DAEVSEagenFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDA 1411
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1828880889 170 SFWRYFRElTDEGASILITTHYMDEAVNCDRVAIVIAGRVLVTATPEEIMAETGSA 225
Cdd:PLN03130 1412 LIQKTIRE-EFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSA 1466
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
19-225 |
2.02e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 69.23 E-value: 2.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 19 VRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLG---RKMPDKEVLARVGYMPQELALYLNlTVEENL 95
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDcdvAKFGLTDLRRVLSIIPQSPVLFSG-TVRFNI 1330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 96 WFYSRL--YGLPREEFERRKEEVLR----------FVGLEEFrdrlvaelSGGMQRRASLACALVHEPEFLILDEPTVGV 163
Cdd:PLN03232 1331 DPFSEHndADLWEALERAHIKDVIDrnpfgldaevSEGGENF--------SVGQRQLLSLARALLRRSKILVLDEATASV 1402
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1828880889 164 DPGLRASFWRYFRElTDEGASILITTHYMDEAVNCDRVAIVIAGRVLVTATPEEIMAETGSA 225
Cdd:PLN03232 1403 DVRTDSLIQRTIRE-EFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSA 1463
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
16-204 |
2.08e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 66.91 E-value: 2.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 16 FEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLK--PDSGEIELlgrkmpdkevlarvgympQELALYLNLTVEE 93
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDV------------------PDNQFGREASLID 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 94 NLwfysrlyglPREEFERRKEEVLRFVGLEE---FRdRLVAELSGGMQRRASLACALVHEPEFLILDEPTVGVDPGLRAS 170
Cdd:COG2401 105 AI---------GRKGDFKDAVELLNAVGLSDavlWL-RRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKR 174
|
170 180 190
....*....|....*....|....*....|....*..
gi 1828880889 171 FWRYFRELTDE-GASILITTHYMD--EAVNCDRVAIV 204
Cdd:COG2401 175 VARNLQKLARRaGITLVVATHHYDviDDLQPDLLIFV 211
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
11-218 |
3.98e-13 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 67.83 E-value: 3.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 11 KSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKM---PDKEVLAR-VGYMPQELALY 86
Cdd:PRK10982 6 KSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfkSSKEALENgISMVHQELNLV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 87 LNLTVEENLWfysrLYGLPREEFERRKEEVLR-----FVGLE---EFRDRlVAELSGGMQRRASLACALVHEPEFLILDE 158
Cdd:PRK10982 86 LQRSVMDNMW----LGRYPTKGMFVDQDKMYRdtkaiFDELDidiDPRAK-VATLSVSQMQMIEIAKAFSYNAKIVIMDE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1828880889 159 PTVGVDPGLRASFWRYFRELTDEGASILITTHYMDEAVN-CDRVAIVIAGRVLVTATPEEI 218
Cdd:PRK10982 161 PTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQlCDEITILRDGQWIATQPLAGL 221
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-223 |
4.07e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 67.93 E-value: 4.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 2 PALVVKELRKSYGD--FEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKMPD---KEVLARV 76
Cdd:PRK11160 337 VSLTLNNVSFTYPDqpQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADyseAALRQAI 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 77 GYMPQELALYlNLTVEENLwfysrLYGLPREEFERRKEeVLRFVGLE---EFRDRLVA-------ELSGGMQRRASLACA 146
Cdd:PRK11160 417 SVVSQRVHLF-SATLRDNL-----LLAAPNASDEALIE-VLQQVGLEkllEDDKGLNAwlgeggrQLSGGEQRRLGIARA 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1828880889 147 LVHEPEFLILDEPTVGVDPGLRASFWRYFRELTdEGASILITTHYMDEAVNCDRVAIVIAGRVLVTATPEEIMAETG 223
Cdd:PRK11160 490 LLHDAPLLLLDEPTEGLDAETERQILELLAEHA-QNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQG 565
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
13-195 |
4.87e-13 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 66.73 E-value: 4.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 13 YGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGL--LKPD---SGEIELLGRKMPDK-----EVLARVGYMPQE 82
Cdd:PRK14243 20 YGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLndLIPGfrvEGKVTFHGKNLYAPdvdpvEVRRRIGMVFQK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 83 LALYLNlTVEENLWFYSRLYGLPREEFERRKEEVLRFVGLEEFRDRLVAE---LSGGMQRRASLACALVHEPEFLILDEP 159
Cdd:PRK14243 100 PNPFPK-SIYDNIAYGARINGYKGDMDELVERSLRQAALWDEVKDKLKQSglsLSGGQQQRLCIARAIAVQPEVILMDEP 178
|
170 180 190
....*....|....*....|....*....|....*.
gi 1828880889 160 TVGVDPGLRASFWRYFRELTdEGASILITTHYMDEA 195
Cdd:PRK14243 179 CSALDPISTLRIEELMHELK-EQYTIIIVTHNMQQA 213
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
18-222 |
7.89e-13 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 66.65 E-value: 7.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 18 AVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGR---KMPDKEVLAR---VGYMPQELALYLN--L 89
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKdllGMKDDEWRAVrsdIQMIFQDPLASLNprM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 90 TVEENLWFYSRLY--GLPREEFERRKEEVLRFVGL-EEFRDRLVAELSGGMQRRASLACALVHEPEFLILDEPTVGVDPG 166
Cdd:PRK15079 116 TIGEIIAEPLRTYhpKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVS 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 167 LRASFWRYFRELTDE-GASILITTHymDEAVN---CDRVAIVIAGRVLVTATPEEIMAET 222
Cdd:PRK15079 196 IQAQVVNLLQQLQREmGLSLIFIAH--DLAVVkhiSDRVLVMYLGHAVELGTYDEVYHNP 253
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
22-190 |
1.54e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 64.12 E-value: 1.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 22 LSFEVEKGEIFGLI------------GPNGAGKTTTIKTIVGLLKPDSGEIELlgrKMPDKEVLAR--VGYMPQELALYL 87
Cdd:PRK13541 7 LQFNIEQKNLFDLSitflpsaityikGANGCGKSSLLRMIAGIMQPSSGNIYY---KNCNINNIAKpyCTYIGHNLGLKL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 88 NLTVEENLWFYSRLYGlpreeFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLILDEPTVGVDPGL 167
Cdd:PRK13541 84 EMTVFENLKFWSEIYN-----SAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKEN 158
|
170 180
....*....|....*....|...
gi 1828880889 168 RASFWRYFRELTDEGASILITTH 190
Cdd:PRK13541 159 RDLLNNLIVMKANSGGIVLLSSH 181
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
26-198 |
1.93e-12 |
|
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: 64.70 E-value: 1.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 26 VEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSG------------------EIELLGRKMPDKEVlaRVGYMPQelalYL 87
Cdd:cd03236 23 PREGQVLGLVGPNGIGKSTALKILAGKLKPNLGkfddppdwdeildefrgsELQNYFTKLLEGDV--KVIVKPQ----YV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 88 NL-------TVEENLwfysrlyglPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLILDEPT 160
Cdd:cd03236 97 DLipkavkgKVGELL---------KKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPS 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1828880889 161 VGVDPGLRASFWRYFRELTDEGASILITTH------YMDEAVNC 198
Cdd:cd03236 168 SYLDIKQRLNAARLIRELAEDDNYVLVVEHdlavldYLSDYIHC 211
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
26-190 |
2.43e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 65.60 E-value: 2.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 26 VEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEI----------------ELLG--RKMPDKEVlaRVGYMPQ---ELA 84
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDYeeepswdevlkrfrgtELQNyfKKLYNGEI--KVVHKPQyvdLIP 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 85 LYLNLTVEENLwfysrlyglPREEFERRKEEVLRFVGLEEFRDRLVAELSGG-MQRRAsLACALVHEPEFLILDEPTVGV 163
Cdd:PRK13409 174 KVFKGKVRELL---------KKVDERGKLDEVVERLGLENILDRDISELSGGeLQRVA-IAAALLRDADFYFFDEPTSYL 243
|
170 180
....*....|....*....|....*..
gi 1828880889 164 DPGLRASFWRYFRELTdEGASILITTH 190
Cdd:PRK13409 244 DIRQRLNVARLIRELA-EGKYVLVVEH 269
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
19-190 |
3.10e-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: 62.56 E-value: 3.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 19 VRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIEllgrkMPDKEvlaRVGYMPQelalylnltveenlwfy 98
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIG-----MPEGE---DLLFLPQ----------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 99 sRLYgLPREEferrkeevlrfvgleeFRDRLV----AELSGGMQRRASLACALVHEPEFLILDEPTVGVDPGLRAsfwRY 174
Cdd:cd03223 72 -RPY-LPLGT----------------LREQLIypwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESED---RL 130
|
170
....*....|....*.
gi 1828880889 175 FRELTDEGASILITTH 190
Cdd:cd03223 131 YQLLKELGITVISVGH 146
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
12-198 |
5.41e-12 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 64.65 E-value: 5.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 12 SYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGllkpD-----SGEIELLGRKMPDKEVL----ARVGYMPQE 82
Cdd:PRK10938 269 SYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG----DhpqgySNDLTLFGRRRGSGETIwdikKHIGYVSSS 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 83 LAL-Y-LNLTVEENL---WFYS-RLYGLPREEFERRKEEVLRFVGLEE------FRDrlvaeLSGGMQRRASLACALVHE 150
Cdd:PRK10938 345 LHLdYrVSTSVRNVIlsgFFDSiGIYQAVSDRQQKLAQQWLDILGIDKrtadapFHS-----LSWGQQRLALIVRALVKH 419
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1828880889 151 PEFLILDEPTVGVDPGLRASFWRYFRELTDEGAS-ILITTHYMDEAVNC 198
Cdd:PRK10938 420 PTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETqLLFVSHHAEDAPAC 468
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
18-223 |
5.51e-12 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 64.60 E-value: 5.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 18 AVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLG---RKMPDKEVLARVGYMPQElALYLNLTVEEN 94
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGtdiRTVTRASLRRNIAVVFQD-AGLFNRSIEDN 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 95 LwfysRLyGLPREEFERRKEEVLR-----FVGLEEFR-DRLVAE----LSGGMQRRASLACALVHEPEFLILDEPTVGVD 164
Cdd:PRK13657 429 I----RV-GRPDATDEEMRAAAERaqahdFIERKPDGyDTVVGErgrqLSGGERQRLAIARALLKDPPILILDEATSALD 503
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1828880889 165 PGLRASFWRYFRELTdEGASILITTHYMDEAVNCDRVAIVIAGRVLVTATPEEIMAETG 223
Cdd:PRK13657 504 VETEAKVKAALDELM-KGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGG 561
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
6-194 |
6.52e-12 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 64.53 E-value: 6.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 6 VKEL--RKSYGDFE-AVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGrkmpdKEVLARVGYmpqe 82
Cdd:PRK13545 24 LKDLffRSKDGEYHyALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG-----SAALIAISS---- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 83 lALYLNLTVEENLWFYSRLYGLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLILDEP-TV 161
Cdd:PRK13545 95 -GLNGQLTGIENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEAlSV 173
|
170 180 190
....*....|....*....|....*....|...
gi 1828880889 162 GvDPGLRASFWRYFRELTDEGASILITTHYMDE 194
Cdd:PRK13545 174 G-DQTFTKKCLDKMNEFKEQGKTIFFISHSLSQ 205
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
1-221 |
7.96e-12 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 63.77 E-value: 7.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 1 MPALVVK----ELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDS---------GEIELLgrKM 67
Cdd:COG4170 1 MPLLDIRnltiEIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNWhvtadrfrwNGIDLL--KL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 68 PDKE---VLAR-VGYMPQELALYL--NLTVEENL-----------WFYSRLyglprEEFERRKEEVLRFVGLEEFRDRLV 130
Cdd:COG4170 79 SPRErrkIIGReIAMIFQEPSSCLdpSAKIGDQLieaipswtfkgKWWQRF-----KWRKKRAIELLHRVGIKDHKDIMN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 131 A---ELSGGMQRRASLACALVHEPEFLILDEPTVGVDPGLRASFWRYFRELTD-EGASILITTHYMdEAV--NCDRVAIV 204
Cdd:COG4170 154 SyphELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQlQGTSILLISHDL-ESIsqWADTITVL 232
|
250
....*....|....*..
gi 1828880889 205 IAGRVLVTATPEEIMAE 221
Cdd:COG4170 233 YCGQTVESGPTEQILKS 249
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
23-209 |
1.00e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 63.78 E-value: 1.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 23 SFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKMPDKEVLA--RVGYM--PQ---ELALYLNLTVEENL 95
Cdd:PRK11288 273 SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDaiRAGIMlcPEdrkAEGIIPVHSVADNI 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 96 WFYSRLYGLPREE---FERRKEEVLRFVGLEEF----RDRLVAELSGGMQRRASLACALVHEPEFLILDEPTVGVDPGLR 168
Cdd:PRK11288 353 NISARRHHLRAGClinNRWEAENADRFIRSLNIktpsREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAK 432
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1828880889 169 ASFWRYFRELTDEGASILITTHYMDEAVN-CDRVAIVIAGRV 209
Cdd:PRK11288 433 HEIYNVIYELAAQGVAVLFVSSDLPEVLGvADRIVVMREGRI 474
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
19-219 |
2.41e-11 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 62.88 E-value: 2.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 19 VRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLL--KPDSGEIELLGRKMPDKEV-------LARVGYMPQELALYLNL 89
Cdd:NF040905 276 VDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRSygRNISGTVFKDGKEVDVSTVsdaidagLAYVTEDRKGYGLNLID 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 90 TVEENLwfysRLYGLPREEFERRKEEVLRFVGLEEFRDRL----------VAELSGGMQRRASLACALVHEPEFLILDEP 159
Cdd:NF040905 356 DIKRNI----TLANLGKVSRRGVIDENEEIKVAEEYRKKMniktpsvfqkVGNLSGGNQQKVVLSKWLFTDPDVLILDEP 431
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1828880889 160 TVGVDPGlrASFWRY--FRELTDEGASILITTHYMDEAVN-CDRVAIVIAGRVL--VT---ATPEEIM 219
Cdd:NF040905 432 TRGIDVG--AKYEIYtiINELAAEGKGVIVISSELPELLGmCDRIYVMNEGRITgeLPreeASQERIM 497
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
6-160 |
2.52e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 62.66 E-value: 2.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 6 VKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIElLGRKMpdkevlaRVGYMPQ-ELA 84
Cdd:PRK11147 322 MENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIH-CGTKL-------EVAYFDQhRAE 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 85 LYLNLTVEENLwfysrLYGLPREEFERRKEEVLRFvgLEEF-----RDRL-VAELSGGMQRRASLACALVHEPEFLILDE 158
Cdd:PRK11147 394 LDPEKTVMDNL-----AEGKQEVMVNGRPRHVLGY--LQDFlfhpkRAMTpVKALSGGERNRLLLARLFLKPSNLLILDE 466
|
..
gi 1828880889 159 PT 160
Cdd:PRK11147 467 PT 468
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
33-188 |
2.77e-11 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 62.65 E-value: 2.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 33 GLIGPNGAGKTTTIKTIVGLLKPDSGEIellgRKMPDkevlARVGYMPQELALYLNLTVEEN--------------LWFY 98
Cdd:TIGR03719 35 GVLGLNGAGKSTLLRIMAGVDKDFNGEA----RPQPG----IKVGYLPQEPQLDPTKTVRENveegvaeikdaldrFNEI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 99 SRLYGLPREEFERRKEEVLRF-----------------VGLEEFR----DRLVAELSGGMQRRASLACALVHEPEFLILD 157
Cdd:TIGR03719 107 SAKYAEPDADFDKLAAEQAELqeiidaadawdldsqleIAMDALRcppwDADVTKLSGGERRRVALCRLLLSKPDMLLLD 186
|
170 180 190
....*....|....*....|....*....|.
gi 1828880889 158 EPTVGVDPGLRASFWRYFRELtdEGASILIT 188
Cdd:TIGR03719 187 EPTNHLDAESVAWLERHLQEY--PGTVVAVT 215
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
15-209 |
4.48e-11 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 60.99 E-value: 4.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 15 DFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGrkmpDKEVLArvgympQELALYLNLTVEEN 94
Cdd:PRK13546 36 TFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG----EVSVIA------ISAGLSGQLTGIEN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 95 LWFYSRLYGLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLILDEP-TVGVDPGLRASFWR 173
Cdd:PRK13546 106 IEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEAlSVGDQTFAQKCLDK 185
|
170 180 190
....*....|....*....|....*....|....*..
gi 1828880889 174 YFrELTDEGASILITTHYMDEAVN-CDRVAIVIAGRV 209
Cdd:PRK13546 186 IY-EFKEQNKTIFFVSHNLGQVRQfCTKIAWIEGGKL 221
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
18-215 |
9.11e-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: 59.43 E-value: 9.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 18 AVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGR---KMPDKEVLARVGYMPQELALYlNLTVEEN 94
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVdisKIGLHDLRSRISIIPQDPVLF-SGTIRSN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 95 LWFYSR-----LYglpreeferrkeEVLRFVGLEEFrdrlVAELSGGM--------------QRR-ASLACALVHEPEFL 154
Cdd:cd03244 98 LDPFGEysdeeLW------------QALERVGLKEF----VESLPGGLdtvveeggenlsvgQRQlLCLARALLRKSKIL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1828880889 155 ILDEPTVGVDPG----LRASFWRYFRELTdegasILITTHYMDEAVNCDRVAIVIAGRVLVTATP 215
Cdd:cd03244 162 VLDEATASVDPEtdalIQKTIREAFKDCT-----VLTIAHRLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
22-201 |
1.40e-10 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 60.58 E-value: 1.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 22 LSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKMPDkevlarvgympQELALYLNL--TVEENLWFYS 99
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTA-----------DNREAYRQLfsAVFSDFHLFD 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 100 RLYGLPREEFERRKEEVLRFVGLEE---FRDRLVA--ELSGGMQRRASLACALVHEPEFLILDEPTVGVDPGLRASFwrY 174
Cdd:COG4615 420 RLLGLDGEADPARARELLERLELDHkvsVEDGRFSttDLSQGQRKRLALLVALLEDRPILVFDEWAADQDPEFRRVF--Y 497
|
170 180 190
....*....|....*....|....*....|...
gi 1828880889 175 FR---ELTDEGASILITTH---YMDEAvncDRV 201
Cdd:COG4615 498 TEllpELKARGKTVIAISHddrYFDLA---DRV 527
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
12-160 |
1.64e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 60.35 E-value: 1.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 12 SYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIEL--------LGRKMPDKE---VLARVGYMP 80
Cdd:PRK11147 12 SFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYeqdlivarLQQDPPRNVegtVYDFVAEGI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 81 QELALYL-----------------NL----TVEE-----NLW-FYSRLYglpreeferrkeEVLRFVGLEEfrDRLVAEL 133
Cdd:PRK11147 92 EEQAEYLkryhdishlvetdpsekNLnelaKLQEqldhhNLWqLENRIN------------EVLAQLGLDP--DAALSSL 157
|
170 180
....*....|....*....|....*..
gi 1828880889 134 SGGMQRRASLACALVHEPEFLILDEPT 160
Cdd:PRK11147 158 SGGWLRKAALGRALVSNPDVLLLDEPT 184
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
11-212 |
1.81e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 60.19 E-value: 1.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 11 KSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDS--GEIELLG-----RKMPDKEVLARVgYMPQEL 83
Cdd:NF040905 9 KTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGevcrfKDIRDSEALGIV-IIHQEL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 84 ALYLNLTVEENL-------------WfysrlyglprEEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHE 150
Cdd:NF040905 88 ALIPYLSIAENIflgnerakrgvidW----------NETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1828880889 151 PEFLILDEPTVGVDPGLRASFWRYFRELTDEG-ASILItTHYMDE--AVnCDRVAIVIAGRVLVT 212
Cdd:NF040905 158 VKLLILDEPTAALNEEDSAALLDLLLELKAQGiTSIII-SHKLNEirRV-ADSITVLRDGRTIET 220
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
22-223 |
2.91e-10 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 59.47 E-value: 2.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 22 LSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLkPDSGE-----IELLGRKMPD-KEVLARVGYMPQELALylnlTVEENL 95
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSlkingIELRELDPESwRKHLSWVGQNPQLPHG----TLRDNV 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 96 wfysrLYGLPREEFERRKEeVLRFVGLEEFRDRLV-----------AELSGGMQRRASLACALVHEPEFLILDEPTVGVD 164
Cdd:PRK11174 444 -----LLGNPDASDEQLQQ-ALENAWVSEFLPLLPqgldtpigdqaAGLSVGQAQRLALARALLQPCQLLLLDEPTASLD 517
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1828880889 165 pglRASFWRYFRELTD--EGASILITTHYMDEAVNCDRVAIVIAGRVLVTATPEEIMAETG 223
Cdd:PRK11174 518 ---AHSEQLVMQALNAasRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGG 575
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-220 |
3.07e-10 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 59.05 E-value: 3.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 1 MPALVVK----ELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPD---------SGEIELLgrKM 67
Cdd:PRK15093 1 MPLLDIRnltiEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNwrvtadrmrFDDIDLL--RL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 68 PDKEVLARVGY-------MPQElALYLNLTVEENL------WFYSRLYGLPREEFERRKEEVLRFVGLEEFRDRLVA--- 131
Cdd:PRK15093 79 SPRERRKLVGHnvsmifqEPQS-CLDPSERVGRQLmqnipgWTYKGRWWQRFGWRKRRAIELLHRVGIKDHKDAMRSfpy 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 132 ELSGGMQRRASLACALVHEPEFLILDEPTVGVDPGLRASFWRYFRELT-DEGASILITTHYMDEAVN-CDRVAIVIAGRV 209
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNqNNNTTILLISHDLQMLSQwADKINVLYCGQT 237
|
250
....*....|.
gi 1828880889 210 LVTATPEEIMA 220
Cdd:PRK15093 238 VETAPSKELVT 248
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
9-190 |
3.10e-10 |
|
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: 57.58 E-value: 3.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 9 LRKSYGDFEAVRGLSfEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGrkmpdkevlARVGYMPQELalyln 88
Cdd:cd03222 6 CVKRYGVFFLLVELG-VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDG---------ITPVYKPQYI----- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 89 ltveenlwfysrlyglpreeferrkeevlrfvgleefrdrlvaELSGGMQRRASLACALVHEPEFLILDEPTVGVDPGLR 168
Cdd:cd03222 71 -------------------------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQR 107
|
170 180
....*....|....*....|...
gi 1828880889 169 ASFWRYFRELTDEGA-SILITTH 190
Cdd:cd03222 108 LNAARAIRRLSEEGKkTALVVEH 130
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
2-168 |
4.97e-10 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 59.03 E-value: 4.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 2 PALVVKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELlgrkmpDKEVlaRVGYMPQ 81
Cdd:PRK10636 311 PLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL------AKGI--KLGYFAQ 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 82 ELALYLNLTvEENLWFYSRLyglpreeFERRKEEVLR-FVGLEEFRDRLVAE----LSGGMQRRASLACALVHEPEFLIL 156
Cdd:PRK10636 383 HQLEFLRAD-ESPLQHLARL-------APQELEQKLRdYLGGFGFQGDKVTEetrrFSGGEKARLVLALIVWQRPNLLLL 454
|
170
....*....|..
gi 1828880889 157 DEPTVGVDPGLR 168
Cdd:PRK10636 455 DEPTNHLDLDMR 466
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
19-190 |
1.21e-09 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 57.93 E-value: 1.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 19 VRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPD--SGEIELLGrkMPDK-EVLARV-GYMPQELALYLNLTVEEN 94
Cdd:PLN03140 896 LREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGyiEGDIRISG--FPKKqETFARIsGYCEQNDIHSPQVTVRES 973
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 95 LwFYSRLYGLPREEFERRKEE----VLRFVGLEEFRDRLVA-----ELSGGMQRRASLACALVHEPEFLILDEPTVGVDP 165
Cdd:PLN03140 974 L-IYSAFLRLPKEVSKEEKMMfvdeVMELVELDNLKDAIVGlpgvtGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDA 1052
|
170 180
....*....|....*....|....*
gi 1828880889 166 GLRASFWRYFRELTDEGASILITTH 190
Cdd:PLN03140 1053 RAAAIVMRTVRNTVDTGRTVVCTIH 1077
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1-220 |
2.53e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 56.51 E-value: 2.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 1 MPALVVKELRKSY----GDF------EAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKM--P 68
Cdd:PRK11308 3 QPLLQAIDLKKHYpvkrGLFkperlvKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLlkA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 69 DKEVLA---------------------RVGYMPQE-LALYLNLTVEENlwfysrlyglpreefERRKEEVLRFVGLE-EF 125
Cdd:PRK11308 83 DPEAQKllrqkiqivfqnpygslnprkKVGQILEEpLLINTSLSAAER---------------REKALAMMAKVGLRpEH 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 126 RDRLVAELSGGMQRRASLACALVHEPEFLILDEPTVGVDPGLRASFWRYFRELTDE-GASILITTHymDEAVN---CDRV 201
Cdd:PRK11308 148 YDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQElGLSYVFISH--DLSVVehiADEV 225
|
250
....*....|....*....
gi 1828880889 202 AIVIAGRVLVTATPEEIMA 220
Cdd:PRK11308 226 MVMYLGRCVEKGTKEQIFN 244
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
19-219 |
3.79e-09 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 55.60 E-value: 3.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 19 VRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPD--------SGEIELLGRKMP--DKEVLARV-GYMPQELALYL 87
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAaiDAPRLARLrAVLPQAAQPAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 88 NLTVEENLWF----YSRLYGLPREEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVH---------EPEFL 154
Cdd:PRK13547 97 AFSAREIVLLgrypHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAQlwpphdaaqPPRYL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1828880889 155 ILDEPTVGVDPGLRASFWRYFRELTDE-GASILITTHYMDEAV-NCDRVAIVIAGRVLVTATPEEIM 219
Cdd:PRK13547 177 LLDEPTAALDLAHQHRLLDTVRRLARDwNLGVLAIVHDPNLAArHADRIAMLADGAIVAHGAPADVL 243
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
127-226 |
3.86e-09 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 56.38 E-value: 3.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 127 DRLVAELSGGMQRRASLACALVHEPEFL--ILDEPTVGVDPGLRASFWRYFRELTDEGASILITTHymDEAV--NCDRV- 201
Cdd:PRK00635 471 ERALATLSGGEQERTALAKHLGAELIGItyILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEH--DEQMisLADRIi 548
|
90 100 110
....*....|....*....|....*....|
gi 1828880889 202 -----AIVIAGRVLVTATPEEIMAETGSAT 226
Cdd:PRK00635 549 digpgAGIFGGEVLFNGSPREFLAKSDSLT 578
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
4-220 |
3.99e-09 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 55.57 E-value: 3.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 4 LVVKELRKSY----GDF-----EAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKMPDKEVL- 73
Cdd:PRK15112 5 LEVRNLSKTFryrtGWFrrqtvEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSy 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 74 --ARVGYMPQELALYLN--LTVEENLWFYSRL-YGLPREEFERRKEEVLRFVGLeeFRDRLV---AELSGGMQRRASLAC 145
Cdd:PRK15112 85 rsQRIRMIFQDPSTSLNprQRISQILDFPLRLnTDLEPEQREKQIIETLRQVGL--LPDHASyypHMLAPGQKQRLGLAR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1828880889 146 ALVHEPEFLILDEPTVGVDPGLRASFWRYFRELTDEG--ASILITTHY-MDEAVNcDRVAIVIAGRVLVTATPEEIMA 220
Cdd:PRK15112 163 ALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQgiSYIYVTQHLgMMKHIS-DQVLVMHQGEVVERGSTADVLA 239
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
2-209 |
6.41e-09 |
|
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: 54.19 E-value: 6.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 2 PALVVKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPD---SGEIELLGrkMPDKEVLAR--- 75
Cdd:cd03233 6 WRNISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNG--IPYKEFAEKypg 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 76 -VGYMPQELALYLNLTVEENLWFYSRLYGlpreeferrkeevlrfvgleefrDRLVAELSGGMQRRASLACALVHEPEFL 154
Cdd:cd03233 84 eIIYVSEEDVHFPTLTVRETLDFALRCKG-----------------------NEFVRGISGGERKRVSIAEALVSRASVL 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1828880889 155 ILDEPTVGVDPGLRASFWRYFRELTDE-GASILIT-THYMDEAVNC-DRVAIVIAGRV 209
Cdd:cd03233 141 CWDNSTRGLDSSTALEILKCIRTMADVlKTTTFVSlYQASDEIYDLfDKVLVLYEGRQ 198
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
33-160 |
1.75e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 54.35 E-value: 1.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 33 GLIGPNGAGKTTTIKTIVGLLKPDSGEIellgRKMPDkevlARVGYMPQELALYLNLTVEEN-----------LWFY--- 98
Cdd:PRK11819 37 GVLGLNGAGKSTLLRIMAGVDKEFEGEA----RPAPG----IKVGYLPQEPQLDPEKTVRENveegvaevkaaLDRFnei 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 99 SRLYGLPREEFERRKEEVLRfvgLEEFRD------------------RL------VAELSGGMQRRASLACALVHEPEFL 154
Cdd:PRK11819 109 YAAYAEPDADFDALAAEQGE---LQEIIDaadawdldsqleiamdalRCppwdakVTKLSGGERRRVALCRLLLEKPDML 185
|
....*.
gi 1828880889 155 ILDEPT 160
Cdd:PRK11819 186 LLDEPT 191
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
18-208 |
1.91e-08 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 54.21 E-value: 1.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 18 AVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKMPDKEVLArvgympqelalYLNL--TVEENL 95
Cdd:PRK10522 338 SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPED-----------YRKLfsAVFTDF 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 96 WFYSRLYGLPREEFERRKEEV-LRFVGLE---EFRDRLVA--ELSGGMQRRASLACALVHEPEFLILDEPTVGVDPGLRA 169
Cdd:PRK10522 407 HLFDQLLGPEGKPANPALVEKwLERLKMAhklELEDGRISnlKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRR 486
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1828880889 170 SFWR-YFRELTDEGASILITTH---YMDEAvncDRVAIVIAGR 208
Cdd:PRK10522 487 EFYQvLLPLLQEMGKTIFAISHddhYFIHA---DRLLEMRNGQ 526
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
18-210 |
2.16e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 54.09 E-value: 2.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 18 AVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRK---MPDKEVLA---RVGYMPQELALYLN--L 89
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRidtLSPGKLQAlrrDIQFIFQDPYASLDprQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 90 TVEENLWFYSRLYGL-PREEFERRKEEVLRFVGLE-EFRDRLVAELSGGMQRRASLACALVHEPEFLILDEPTVGVDPGL 167
Cdd:PRK10261 419 TVGDSIMEPLRVHGLlPGKAAAARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSI 498
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1828880889 168 RASFWRYFRELTDE-GASILITTHYMD--EAVNcDRVAIVIAGRVL 210
Cdd:PRK10261 499 RGQIINLLLDLQRDfGIAYLFISHDMAvvERIS-HRVAVMYLGQIV 543
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
19-159 |
6.66e-08 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 52.99 E-value: 6.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 19 VRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGrkmpdkevlaRVGYMPQeLALYLNLTVEENLwfy 98
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG----------RISFSPQ-TSWIMPGTIKDNI--- 507
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1828880889 99 srLYGLprEEFERRKEEVLRFVGLEE------FRDRLV-----AELSGGMQRRASLACALVHEPEFLILDEP 159
Cdd:TIGR01271 508 --IFGL--SYDEYRYTSVIKACQLEEdialfpEKDKTVlgeggITLSGGQRARISLARAVYKDADLYLLDSP 575
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
19-159 |
7.80e-08 |
|
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: 51.78 E-value: 7.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 19 VRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGrkmpdkevlaRVGYMPQeLALYLNLTVEENLwfy 98
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG----------RISFSSQ-FSWIMPGTIKENI--- 118
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1828880889 99 srLYGLprEEFERRKEEVLRFVGLEE----FRDR---LVAE----LSGGMQRRASLACALVHEPEFLILDEP 159
Cdd:cd03291 119 --IFGV--SYDEYRYKSVVKACQLEEditkFPEKdntVLGEggitLSGGQRARISLARAVYKDADLYLLDSP 186
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
4-210 |
8.67e-08 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 51.33 E-value: 8.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 4 LVVKELRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGL--LKPDSGEIELLGRKMPDKEVLARVG---Y 78
Cdd:PRK09580 2 LSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELSPEDRAGegiF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 79 M----PQELA-----LYLNLTVEEnLWFYSRLYGLPREEFERRKEEVLRFVGL-EEFRDRLVAE-LSGGMQRRASLACAL 147
Cdd:PRK09580 82 MafqyPVEIPgvsnqFFLQTALNA-VRSYRGQEPLDRFDFQDLMEEKIALLKMpEDLLTRSVNVgFSGGEKKRNDILQMA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1828880889 148 VHEPEFLILDEPTVGVDPGLRASFWRYFRELTDEGASILITTHYMD--EAVNCDRVAIVIAGRVL 210
Cdd:PRK09580 161 VLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYQRilDYIKPDYVHVLYQGRIV 225
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
132-190 |
8.72e-08 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 51.62 E-value: 8.72e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1828880889 132 ELSGGMQRRASLACAL---VHEPEFLILDEPTVGVDPGLRASFWRYFRELTDEGASILITTH 190
Cdd:pfam13304 236 ELSDGTKRLLALLAALlsaLPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTH 297
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
18-223 |
1.31e-07 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 51.64 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 18 AVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKMPDKEV------LARVGYMP--------QEL 83
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLdswrsrLAVVSQTPflfsdtvaNNI 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 84 ALYLNLTVEENLWFYSRLYGLpreeferrKEEVLRfvgLEEFRDRLVAE----LSGGMQRRASLACALVHEPEFLILDEP 159
Cdd:PRK10789 410 ALGRPDATQQEIEHVARLASV--------HDDILR---LPQGYDTEVGErgvmLSGGQKQRISIARALLLNAEILILDDA 478
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1828880889 160 TVGVDPGLRASFWRYFRELTdEGASILITTHYMDEAVNCDRVAIVIAGRVLVTATPEEIMAETG 223
Cdd:PRK10789 479 LSAVDGRTEHQILHNLRQWG-EGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSG 541
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
19-190 |
4.62e-07 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 50.13 E-value: 4.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 19 VRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGL--------LKPDSGEIELLGRK-------------MPD-KEVLARV 76
Cdd:TIGR00954 468 IESLSFEVPSGNNLLICGPNGCGKSSLFRILGELwpvyggrlTKPAKGKLFYVPQRpymtlgtlrdqiiYPDsSEDMKRR 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 77 GYMPQELALYLNLTVEENLwfysrlyglpreeferrkeeVLRFVGLEEFRDrLVAELSGGMQRRASLACALVHEPEFLIL 156
Cdd:TIGR00954 548 GLSDKDLEQILDNVQLTHI--------------------LEREGGWSAVQD-WMDVLSGGEKQRIAMARLFYHKPQFAIL 606
|
170 180 190
....*....|....*....|....*....|....
gi 1828880889 157 DEPTVGVDPGLRAsfwRYFRELTDEGASILITTH 190
Cdd:TIGR00954 607 DECTSAVSVDVEG---YMYRLCREFGITLFSVSH 637
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
20-160 |
6.56e-07 |
|
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: 49.43 E-value: 6.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 20 RGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLG---RKMPDKEVLARVGYMPQELALYlNLTVEENLw 96
Cdd:COG5265 375 KGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGqdiRDVTQASLRAAIGIVPQDTVLF-NDTIAYNI- 452
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1828880889 97 fysrLYGLPREEFERRKEE-----VLRFV-GLEEFRDRLVAE----LSGGMQRRASLACALVHEPEFLILDEPT 160
Cdd:COG5265 453 ----AYGRPDASEEEVEAAaraaqIHDFIeSLPDGYDTRVGErglkLSGGEKQRVAIARTLLKNPPILIFDEAT 522
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
14-164 |
9.48e-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: 49.17 E-value: 9.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 14 GDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRkmpdkevlarVGYMPQElALYLNLTVEE 93
Cdd:TIGR00957 649 DLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS----------VAYVPQQ-AWIQNDSLRE 717
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1828880889 94 NLWFYSRLYGlPREEFERRKEEVLRFVGLEEFRDRL-VAE----LSGGMQRRASLACALVHEPEFLILDEPTVGVD 164
Cdd:TIGR00957 718 NILFGKALNE-KYYQQVLEACALLPDLEILPSGDRTeIGEkgvnLSGGQKQRVSLARAVYSNADIYLFDDPLSAVD 792
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
34-223 |
9.55e-07 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 48.95 E-value: 9.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 34 LIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKMPD------KEVLARVGYMPQELA--LYLNLTV-----EENLWfysr 100
Cdd:PRK10790 372 LVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSlshsvlRQGVAMVQQDPVVLAdtFLANVTLgrdisEEQVW---- 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 101 lyglpreeferrkeEVLRFVGLEEFRDRL-------VAE----LSGGMQRRASLACALVHEPEFLILDEPTVGVDPGLRA 169
Cdd:PRK10790 448 --------------QALETVQLAELARSLpdglytpLGEqgnnLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQ 513
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1828880889 170 SFWRYFRELTDEGASILItTHYMDEAVNCDRVAIVIAGRVLVTATPEEIMAETG 223
Cdd:PRK10790 514 AIQQALAAVREHTTLVVI-AHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQG 566
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
19-223 |
1.09e-06 |
|
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: 49.17 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 19 VRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKMPD---KEVLARVGYMPQELALY-----LNLT 90
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKiglHDLRFKITIIPQDPVLFsgslrMNLD 1381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 91 -----VEENLWFYSRLYGLPReeferrkeevlrFV-GLEEFRDRLVAE----LSGGMQRRASLACALVHEPEFLILDEPT 160
Cdd:TIGR00957 1382 pfsqySDEEVWWALELAHLKT------------FVsALPDKLDHECAEggenLSVGQRQLVCLARALLRKTKILVLDEAT 1449
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1828880889 161 VGVD--------PGLRASFwryfreltdEGASILITTHYMDEAVNCDRVAIVIAGRVLVTATPEEIMAETG 223
Cdd:TIGR00957 1450 AAVDletdnliqSTIRTQF---------EDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRG 1511
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
133-204 |
1.25e-06 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 46.97 E-value: 1.25e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1828880889 133 LSGGMQRRASLACALVHEPE----FLILDEPTVGVDPGLRASFWRYFRELTDEGASILITTHYMDEAVNCDRVAIV 204
Cdd:cd03227 78 LSGGEKELSALALILALASLkprpLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLPELAELADKLIHI 153
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
18-223 |
1.55e-06 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 48.48 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 18 AVRGLSFEVEKGEIFGLIGPNGAGKTTtiktIVGLLKP----DSGEIELLGRKMPDKEVLA---RVGYMPQELALYlNLT 90
Cdd:PRK11176 358 ALRNINFKIPAGKTVALVGRSGSGKST----IANLLTRfydiDEGEILLDGHDLRDYTLASlrnQVALVSQNVHLF-NDT 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 91 VEENLWF-----YSRlyglPREEFERRKEEVLRFV-GLEEFRDRLVAE----LSGGMQRRASLACALVHEPEFLILDEPT 160
Cdd:PRK11176 433 IANNIAYarteqYSR----EQIEEAARMAYAMDFInKMDNGLDTVIGEngvlLSGGQRQRIAIARALLRDSPILILDEAT 508
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1828880889 161 VGVDPGLRASFWRYFRELTDEGASILItTHYMDEAVNCDRVAIVIAGRVLVTATPEEIMAETG 223
Cdd:PRK11176 509 SALDTESERAIQAALDELQKNRTSLVI-AHRLSTIEKADEILVVEDGEIVERGTHAELLAQNG 570
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
4-224 |
1.62e-06 |
|
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: 47.93 E-value: 1.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 4 LVVKELRKSY--GDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDsGEIELLG---RKMPDKEVLARVGY 78
Cdd:cd03289 3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGvswNSVPLQKWRKAFGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 79 MPQELALY-----LNLT-----VEENLWFYSRLYGLPREeferrkeevlrfvgLEEFRDRL--VAE-----LSGGMQRRA 141
Cdd:cd03289 82 IPQKVFIFsgtfrKNLDpygkwSDEEIWKVAEEVGLKSV--------------IEQFPGQLdfVLVdggcvLSHGHKQLM 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 142 SLACALVHEPEFLILDEPTVGVDP--------GLRASFwryfreltdEGASILITTHYMDEAVNCDRVAIVIAGRVLVTA 213
Cdd:cd03289 148 CLARSVLSKAKILLLDEPSAHLDPityqvirkTLKQAF---------ADCTVILSEHRIEAMLECQRFLVIEENKVRQYD 218
|
250
....*....|.
gi 1828880889 214 TPEEIMAETGS 224
Cdd:cd03289 219 SIQKLLNEKSH 229
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
121-221 |
3.34e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 47.32 E-value: 3.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 121 GLEEFRDRLVAELSGGMQRRASLACALVHEPEFLILDEPTVGVDPGLRASFWRYFRELTDEGASILITTHYMDEAVNCDR 200
Cdd:PRK10938 124 GITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQ 203
|
90 100
....*....|....*....|..
gi 1828880889 201 VAIVIAGRVLV-TATPEEIMAE 221
Cdd:PRK10938 204 FAGVLADCTLAeTGEREEILQQ 225
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
22-164 |
3.54e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 47.66 E-value: 3.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 22 LSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPdsgeiellgrkMPDKEVLAR--VGYMPQeLALYLNLTVEENLWFYS 99
Cdd:PLN03232 636 INLEIPVGSLVAIVGGTGEGKTSLISAMLGELSH-----------AETSSVVIRgsVAYVPQ-VSWIFNATVRENILFGS 703
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1828880889 100 RL----YGLPREEFERRKEEVLrFVG--LEEFRDRLVaELSGGMQRRASLACALVHEPEFLILDEPTVGVD 164
Cdd:PLN03232 704 DFeserYWRAIDVTALQHDLDL-LPGrdLTEIGERGV-NISGGQKQRVSMARAVYSNSDIYIFDDPLSALD 772
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
4-165 |
4.14e-06 |
|
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: 47.21 E-value: 4.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 4 LVVKELRKSY--GDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDsGEIELLG---RKMPDKEVLARVGY 78
Cdd:TIGR01271 1218 MDVQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGvswNSVTLQTWRKAFGV 1296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 79 MPQELALYLNlTVEENLWFYSRLyglpreeFERRKEEVLRFVGL----EEFRDRL--VAE-----LSGGMQRRASLACAL 147
Cdd:TIGR01271 1297 IPQKVFIFSG-TFRKNLDPYEQW-------SDEEIWKVAEEVGLksviEQFPDKLdfVLVdggyvLSNGHKQLMCLARSI 1368
|
170
....*....|....*...
gi 1828880889 148 VHEPEFLILDEPTVGVDP 165
Cdd:TIGR01271 1369 LSKAKILLLDEPSAHLDP 1386
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
28-190 |
4.96e-06 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 45.06 E-value: 4.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 28 KGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIellgrkmpdkevlarvgympqelaLYLNLTveenlwfysrlyglpre 107
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGV------------------------IYIDGE----------------- 39
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 108 eferRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACALVHEPEFLILDEPTVGVDPGLRASFWRY------FRELTDE 181
Cdd:smart00382 40 ----DILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrllLLLKSEK 115
|
....*....
gi 1828880889 182 GASILITTH 190
Cdd:smart00382 116 NLTVILTTN 124
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
15-199 |
7.10e-06 |
|
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: 45.40 E-value: 7.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 15 DFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELlGRKMPDKEVLAR--------VGYMPQELALy 86
Cdd:cd03290 13 GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHW-SNKNESEPSFEAtrsrnrysVAYAAQKPWL- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 87 LNLTVEENLWFYS-----RLYGLPREEFERRKEEVLRFVGLEEFRDRLVaELSGGMQRRASLACALVHEPEFLILDEPTV 161
Cdd:cd03290 91 LNATVEENITFGSpfnkqRYKAVTDACSLQPDIDLLPFGDQTEIGERGI-NLSGGQRQRICVARALYQNTNIVFLDDPFS 169
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1828880889 162 GVDPGLRASFWR--YFRELTDEGASILITTHYMDEAVNCD 199
Cdd:cd03290 170 ALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLPHAD 209
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
1-220 |
8.26e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 46.65 E-value: 8.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 1 MPALVVKE---LRKSYGDFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPdsgeiellgrkMPDKEVLAR-- 75
Cdd:PLN03130 612 LPAISIKNgyfSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPP-----------RSDASVVIRgt 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 76 VGYMPQeLALYLNLTVEENLWFYS-----RLYGLPREEFERRKEEVLRFVGLEEFRDRLVaELSGGMQRRASLACALVHE 150
Cdd:PLN03130 681 VAYVPQ-VSWIFNATVRDNILFGSpfdpeRYERAIDVTALQHDLDLLPGGDLTEIGERGV-NISGGQKQRVSMARAVYSN 758
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1828880889 151 PEFLILDEPTVGVDPGL-RASFWRYFRELTDEGASILITT--HYMDEAvncDRVAIVIAGRVLVTATPEEIMA 220
Cdd:PLN03130 759 SDVYIFDDPLSALDAHVgRQVFDKCIKDELRGKTRVLVTNqlHFLSQV---DRIILVHEGMIKEEGTYEELSN 828
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
128-219 |
1.14e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 45.98 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 128 RLVAELSGGMQRRASLACAL---VHEPEFLILDEPTVGVDPGLRASFWRYFRELTDEGASILITTHYMDEAVNCDRVAIV 204
Cdd:PRK00635 805 RPLSSLSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNMHVVKVADYVLEL 884
|
90 100
....*....|....*....|.
gi 1828880889 205 ------IAGRVLVTATPEEIM 219
Cdd:PRK00635 885 gpeggnLGGYLLASCSPEELI 905
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
29-160 |
3.35e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 44.50 E-value: 3.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 29 GEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELlgrkmpdkEVLARVGYMPQELALYLNLTV-------EENLWFY--- 98
Cdd:PRK15064 27 GNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSL--------DPNERLGKLRQDQFAFEEFTVldtvimgHTELWEVkqe 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 99 -SRLYGLPREEFERRKEE---------------------VLRFVGL-EEFRDRLVAELSGGMQRRASLACALVHEPEFLI 155
Cdd:PRK15064 99 rDRIYALPEMSEEDGMKVadlevkfaemdgytaearageLLLGVGIpEEQHYGLMSEVAPGWKLRVLLAQALFSNPDILL 178
|
....*
gi 1828880889 156 LDEPT 160
Cdd:PRK15064 179 LDEPT 183
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
26-192 |
9.87e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 43.17 E-value: 9.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 26 VEKGEIFGLIGPNGAGKTTTIKTI----VGLLKPDSGEIELLGRKMPD--KEVLARVGYMPQELALYLNLTVEENLWFYS 99
Cdd:TIGR00956 84 IKPGELTVVLGRPGSGCSTLLKTIasntDGFHIGVEGVITYDGITPEEikKHYRGDVVYNAETDVHFPHLTVGETLDFAA 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 100 RLYGlP---------REEFERRKEEVLRFVGLEEFRDRLVAE-----LSGGMQRRASLACALVHEPEFLILDEPTVGVDP 165
Cdd:TIGR00956 164 RCKT-PqnrpdgvsrEEYAKHIADVYMATYGLSHTRNTKVGNdfvrgVSGGERKRVSIAEASLGGAKIQCWDNATRGLDS 242
|
170 180
....*....|....*....|....*..
gi 1828880889 166 GLRASFWRYFRELtdegASILITTHYM 192
Cdd:TIGR00956 243 ATALEFIRALKTS----ANILDTTPLV 265
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
56-203 |
2.79e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 41.94 E-value: 2.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 56 DSGEIELLGRKMPD---KEVLARVGYMPQELALYlNLTVEENLWFYSRlyglprEEFERRKEEVLRFVGLEEFRDRLVAE 132
Cdd:PTZ00265 1275 NSGKILLDGVDICDynlKDLRNLFSIVSQEPMLF-NMSIYENIKFGKE------DATREDVKRACKFAAIDEFIESLPNK 1347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 133 -----------LSGGMQRRASLACALVHEPEFLILDEPTVGVDPGLRASFWRYFRELTDEGASILIT-THYMDEAVNCDR 200
Cdd:PTZ00265 1348 ydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITiAHRIASIKRSDK 1427
|
...
gi 1828880889 201 VAI 203
Cdd:PTZ00265 1428 IVV 1430
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
16-190 |
3.85e-04 |
|
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: 40.76 E-value: 3.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 16 FEAVRGLSFEVEKGeIFGLIGPNGAGKTTTIKTIVGLLKPDSG-------------------EIEL--------LGRKMP 68
Cdd:COG3593 11 FRSIKDLSIELSDD-LTVLVGENNSGKSSILEALRLLLGPSSSrkfdeedfylgddpdlpeiEIELtfgsllsrLLRLLL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 69 DKEVLARVGYMPQELALYLNLTVEE-----NLWFYSRLYGL-----PREEFERRKEEVLRfVGLEEFRDRLVAELSGGMQ 138
Cdd:COG3593 90 KEEDKEELEEALEELNEELKEALKAlnellSEYLKELLDGLdleleLSLDELEDLLKSLS-LRIEDGKELPLDRLGSGFQ 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1828880889 139 RRASLACALV-------HEPEFLILDEPTVGVDPGLRASFWRYFRELTDEGASILITTH 190
Cdd:COG3593 169 RLILLALLSAlaelkraPANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTH 227
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
155-226 |
4.65e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 41.17 E-value: 4.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 155 ILDEPTVG-----VDPGLRAsfwryFRELTDEGASILITTHYMDeavncdrvaiVIA----------------GRVLVTA 213
Cdd:COG0178 852 ILDEPTTGlhfhdIRKLLEV-----LHRLVDKGNTVVVIEHNLD----------VIKtadwiidlgpeggdggGEIVAEG 916
|
90
....*....|...
gi 1828880889 214 TPEEIMAETGSAT 226
Cdd:COG0178 917 TPEEVAKVKASYT 929
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
20-164 |
5.39e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 40.61 E-value: 5.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 20 RGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIEllgrkmpdKEVLARVGYMPQELALYLNLTVEEnLWFYS 99
Cdd:PLN03073 526 KNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVF--------RSAKVRMAVFSQHHVDGLDLSSNP-LLYMM 596
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1828880889 100 RLY-GLPREEFERRkeevLRFVGLE-EFRDRLVAELSGGMQRRASLACALVHEPEFLILDEPTVGVD 164
Cdd:PLN03073 597 RCFpGVPEQKLRAH----LGSFGVTgNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD 659
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
19-164 |
5.77e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 40.92 E-value: 5.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 19 VRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEiellgrkmpdkeVLAR--VGYMPQElALYLNLTVEENLW 96
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGR------------VWAErsIAYVPQQ-AWIMNATVRGNIL 742
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1828880889 97 FY-----SRLYGLPREEFERRKEEVLRfVGLE-EFRDRLVaELSGGMQRRASLACALVHEPEFLILDEPTVGVD 164
Cdd:PTZ00243 743 FFdeedaARLADAVRVSQLEADLAQLG-GGLEtEIGEKGV-NLSGGQKARVSLARAVYANRDVYLLDDPLSALD 814
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
19-167 |
8.57e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 40.15 E-value: 8.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 19 VRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIELLGRKMPD---KEVLARVGYMPQELALYlNLTVEENL 95
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAyglRELRRQFSMIPQDPVLF-DGTVRQNV 1404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 96 WFYSRlyglpreEFERRKEEVLRFVGLeefRDRLVAE--------LSGGM-----QRR-ASLACALVHEPE-FLILDEPT 160
Cdd:PTZ00243 1405 DPFLE-------ASSAEVWAALELVGL---RERVASEsegidsrvLEGGSnysvgQRQlMCMARALLKKGSgFILMDEAT 1474
|
....*..
gi 1828880889 161 VGVDPGL 167
Cdd:PTZ00243 1475 ANIDPAL 1481
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
132-199 |
1.70e-03 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 38.75 E-value: 1.70e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1828880889 132 ELSGGMQRRASLACALVHE---PEFLILDEPTVGVDPGLRASFWRYFRELTDEGASILITTHYMDEAVNCD 199
Cdd:cd03271 169 TLSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIKCAD 239
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
15-164 |
1.86e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 39.24 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 15 DFEAVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVGLLKPDSGEIeLLGRKMPDKEV-----LARVGYMPQELALYLNl 89
Cdd:PTZ00265 397 DVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDI-IINDSHNLKDInlkwwRSKIGVVSQDPLLFSN- 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 90 TVEENLWFysRLYGLPREEFERRKEE-----------------------------------------------------V 116
Cdd:PTZ00265 475 SIKNNIKY--SLYSLKDLEALSNYYNedgndsqenknkrnscrakcagdlndmsnttdsneliemrknyqtikdsevvdV 552
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1828880889 117 LRFVGLEEF-------RDRLV----AELSGGMQRRASLACALVHEPEFLILDEPTVGVD 164
Cdd:PTZ00265 553 SKKVLIHDFvsalpdkYETLVgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
124-172 |
1.88e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 39.07 E-value: 1.88e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1828880889 124 EFRDRLVAELSGGMQRRASLACALVHEPEFLILDEPTVGVDpgLRASFW 172
Cdd:PLN03073 336 EMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD--LHAVLW 382
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
11-190 |
2.08e-03 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 38.02 E-value: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 11 KSYGDFEAVRGLSFE-VEKGEIFGLIGPNGAGKTTTIKTIVGLLkpdSGEIELLGRKMPDKEVLArvgymPQELALYLNL 89
Cdd:cd03279 9 KNFGPFREEQVIDFTgLDNNGLFLICGPTGAGKSTILDAITYAL---YGKTPRYGRQENLRSVFA-----PGEDTAEVSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 90 TVEENLWFYS--RLYGLprEEFERRKEEVLRFVGLEEFRDRLVAELSGGMQRRASLACAL-----VHEP-----EFLILD 157
Cdd:cd03279 81 TFQLGGKKYRveRSRGL--DYDQFTRIVLLPQGEFDRFLARPVSTLSGGETFLASLSLALalsevLQNRggarlEALFID 158
|
170 180 190
....*....|....*....|....*....|...
gi 1828880889 158 EPTVGVDPGLRASFWRYFRELTDEGASILITTH 190
Cdd:cd03279 159 EGFGTLDPEALEAVATALELIRTENRMVGVISH 191
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
18-190 |
2.75e-03 |
|
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: 37.30 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 18 AVRGLSFEVEKGEIFGLIGPNGAGKTTTIKTIVgllkPDSGEIELL-GRKMPDKEVLARVGympqELALYLNLTVEenlw 96
Cdd:cd03238 10 NLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGL----YASGKARLIsFLPKFSRNKLIFID----QLQFLIDVGLG---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 97 fYSRLyglpreeferrkeevlrfvgleefrDRLVAELSGGMQRRASLACALVHEPE--FLILDEPTVGVDPGLRASFWRY 174
Cdd:cd03238 78 -YLTL-------------------------GQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEV 131
|
170
....*....|....*.
gi 1828880889 175 FRELTDEGASILITTH 190
Cdd:cd03238 132 IKGLIDLGNTVILIEH 147
|
|
| flhF |
PRK06995 |
flagellar biosynthesis protein FlhF; |
26-46 |
5.64e-03 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 235904 [Multi-domain] Cd Length: 484 Bit Score: 37.64 E-value: 5.64e-03
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
117-226 |
7.67e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 37.30 E-value: 7.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880889 117 LRF---VGLEEFR-DRLVAELSGGMQRRASLACAL------VhepeFLILDEPTVGVDPGLRASFWRYFRELTDEGASIL 186
Cdd:TIGR00630 469 LGFlidVGLDYLSlSRAAGTLSGGEAQRIRLATQIgsgltgV----LYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLI 544
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1828880889 187 ITTHYMDEAVNCDRV------AIVIAGRVLVTATPEEIMAETGSAT 226
Cdd:TIGR00630 545 VVEHDEDTIRAADYVidigpgAGEHGGEVVASGTPEEILANPDSLT 590
|
|
| |
