|
Name |
Accession |
Description |
Interval |
E-value |
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-245 |
4.90e-74 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 238.81 E-value: 4.90e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 4 VEVRNGYKYYGSKsnpkIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGAKPGEPGSGVpGSRV 83
Cdd:COG1131 1 IEVRGLTKRYGDK----TALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEV-RRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 84 GFMPQEIALVEEMTVKETIFYFGRIYGLTDERIREKFKLLKELLQLPPAR-QMIKQCSGGQQRRLSFACAMIHDPELLIL 162
Cdd:COG1131 76 GYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAAdRKVGTLSGGMKQRLGLALALLHDPELLIL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 163 DEPTVGLDPMLREKIWDFLVETTRNSKlAVIITTHYIEEAKQ-ANCIGLMRNGVLLAEDTPTNIMikfgTQSIEDAFLIL 241
Cdd:COG1131 156 DEPTSGLDPEARRELWELLRELAAEGK-TVLLSTHYLEEAERlCDRVAIIDKGRIVADGTPDELK----ARLLEDVFLEL 230
|
....
gi 24582012 242 SQRQ 245
Cdd:COG1131 231 TGEE 234
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-222 |
2.22e-56 |
|
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: 191.56 E-value: 2.22e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 4 VEVRNGYKYYGSKSNPkiVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGaKPGEPGSGVPGSRV 83
Cdd:cd03263 1 LQIRNLTKTYKKGTKP--AVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYING-YSIRTDRKAARQSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 84 GFMPQEIALVEEMTVKETIFYFGRIYGLTDERIREKFKLLKELLQLPPAR-QMIKQCSGGQQRRLSFACAMIHDPELLIL 162
Cdd:cd03263 78 GYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKAnKRARTLSGGMKRKLSLAIALIGGPSVLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24582012 163 DEPTVGLDPMLREKIWDFLVETTRNSklAVIITTHYIEEAKQ-ANCIGLMRNGVLLAEDTP 222
Cdd:cd03263 158 DEPTSGLDPASRRAIWDLILEVRKGR--SIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSP 216
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-216 |
6.49e-56 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 188.38 E-value: 6.49e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 4 VEVRNGYKYYGSKsnpkIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGAKPGEPGSGVPGsRV 83
Cdd:cd03230 1 IEVRNLSKRYGKK----TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKR-RI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 84 GFMPQEIALVEEMTVKETIFYfgriygltderirekfkllkellqlpparqmikqcSGGQQRRLSFACAMIHDPELLILD 163
Cdd:cd03230 76 GYLPEEPSLYENLTVRENLKL-----------------------------------SGGMKQRLALAQALLHDPELLILD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 24582012 164 EPTVGLDPMLREKIWDFLVETTRNSKlAVIITTHYIEEAKQ-ANCIGLMRNGVL 216
Cdd:cd03230 121 EPTSGLDPESRREFWELLRELKKEGK-TILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
5-239 |
1.71e-52 |
|
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: 181.59 E-value: 1.71e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 5 EVRNGYKYYGSKsnpkIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGAKPGEPGSGVPgSRVG 84
Cdd:COG4555 3 EVENLSKKYGKV----PALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREAR-RQIG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 85 FMPQEIALVEEMTVKETIFYFGRIYGLTDERIREKFKLLKELLQL-PPARQMIKQCSGGQQRRLSFACAMIHDPELLILD 163
Cdd:COG4555 78 VLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLeEFLDRRVGELSTGMKKKVALARALVHDPKVLLLD 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24582012 164 EPTVGLDPMLREKIWDFLVEtTRNSKLAVIITTHYIEE-AKQANCIGLMRNGVLLAEDTPTNIMIKFGTQSIEDAFL 239
Cdd:COG4555 158 EPTNGLDVMARRLLREILRA-LKKEGKTVLFSSHIMQEvEALCDRVVILHKGKVVAQGSLDELREEIGEENLEDAFV 233
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
11-299 |
1.52e-51 |
|
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: 181.05 E-value: 1.52e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 11 KYYGsksnpKIV-LNQLNMNVMRGSIYGLLGASGCGKTTL---LSCIV----GQRRLNGGEVVVLGAKPGEpgsgvpgsR 82
Cdd:TIGR01188 1 KVYG-----DFKaVDGVNFKVREGEVFGFLGPNGAGKTTTirmLTTLLrptsGTARVAGYDVVREPRKVRR--------S 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 83 VGFMPQEIALVEEMTVKETIFYFGRIYGLTDERIREKFKLLKELLQLPPAR-QMIKQCSGGQQRRLSFACAMIHDPELLI 161
Cdd:TIGR01188 68 IGIVPQYASVDEDLTGRENLEMMGRLYGLPKDEAEERAEELLELFELGEAAdRPVGTYSGGMRRRLDIAASLIHQPDVLF 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 162 LDEPTVGLDPMLREKIWDfLVETTRNSKLAVIITTHYIEEAKQ-ANCIGLMRNGVLLAEDTPTNIMIKFGTQSIEDAFLI 240
Cdd:TIGR01188 148 LDEPTTGLDPRTRRAIWD-YIRALKEEGVTILLTTHYMEEADKlCDRIAIIDHGRIIAEGTPEELKRRLGKDTLESRPRD 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 24582012 241 LSQRQGNEDELAQIMDHNKNQALpAAVLPPEVIDTHEPNMPEKQPIPFEEpLNENRKKI 299
Cdd:TIGR01188 227 IQSLKVEVSMLIAELGETGLGLL-AVTVDSDRIKILVPDGDETVPEIVEA-AIRNGIRI 283
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
4-225 |
4.16e-47 |
|
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: 166.01 E-value: 4.16e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 4 VEVRNGYKYYGSKsnpkIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGAKPGEPGSGVPgSRV 83
Cdd:cd03265 1 IEVENLVKKYGDF----EAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVR-RRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 84 GFMPQEIALVEEMTVKETIFYFGRIYGLTDERIREKFKLLKELLQLPPAR-QMIKQCSGGQQRRLSFACAMIHDPELLIL 162
Cdd:cd03265 76 GIVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAAdRLVKTYSGGMRRRLEIARSLVHRPEVLFL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24582012 163 DEPTVGLDPMLREKIWDFLVETTRNSKLAVIITTHYIEEAKQ-ANCIGLMRNGVLLAEDTPTNI 225
Cdd:cd03265 156 DEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-202 |
1.96e-41 |
|
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: 150.31 E-value: 1.96e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 4 VEVRNGYKYYGSKSNPKIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGAKPGEPGSgvpgsRV 83
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGP-----DR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 84 GFMPQEIALVEEMTVKETIFyFG-RIYGLTDERIREKFKLLKELLQLPP-ARQMIKQCSGGQQRRLSFACAMIHDPELLI 161
Cdd:cd03293 76 GYVFQQDALLPWLTVLDNVA-LGlELQGVPKAEARERAEELLELVGLSGfENAYPHQLSGGMRQRVALARALAVDPDVLL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 24582012 162 LDEPTVGLDPMLREKIWDFLVETTRNSKLAVIITTHYIEEA 202
Cdd:cd03293 155 LDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEA 195
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-218 |
4.14e-41 |
|
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: 149.21 E-value: 4.14e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 4 VEVRNGYKYYGSKsnpkIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVlgakPGEPGSGVPGSR- 82
Cdd:cd03259 1 LELKGLSKTYGSV----RALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILI----DGRDVTGVPPERr 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 83 -VGFMPQEIALVEEMTVKETIFYFGRIYGLTDERIREKFKLLKELLQLPP-ARQMIKQCSGGQQRRLSFACAMIHDPELL 160
Cdd:cd03259 73 nIGMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGlLNRYPHELSGGQQQRVALARALAREPSLL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 24582012 161 ILDEPTVGLDPMLREKIWDFLVETTRNSKLAVIITTHYIEEA-KQANCIGLMRNGVLLA 218
Cdd:cd03259 153 LLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEAlALADRIAVMNEGRIVQ 211
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
4-225 |
5.63e-40 |
|
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: 146.88 E-value: 5.63e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 4 VEVRNGYKYYGSKsnpkIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLG---AKPGEPGSGVPG 80
Cdd:cd03261 1 IELRGLTKSFGGR----TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGediSGLSEAELYRLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 81 SRVGFMPQEIALVEEMTVKETIFYFGRIYG-LTDERIREKFKLLKELLQLPPA-RQMIKQCSGGQQRRLSFACAMIHDPE 158
Cdd:cd03261 77 RRMGMLFQSGALFDSLTVFENVAFPLREHTrLSEEEIREIVLEKLEAVGLRGAeDLYPAELSGGMKKRVALARALALDPE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24582012 159 LLILDEPTVGLDPMLREKIWDFLVETTRNSKLAVIITTHYIEEAKQ-ANCIGLMRNGVLLAEDTPTNI 225
Cdd:cd03261 157 LLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEEL 224
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
2-226 |
7.56e-40 |
|
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: 146.66 E-value: 7.56e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 2 AAVEVRNGYKYYGSKsnpkIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLG---AKPGEPGSGV 78
Cdd:COG1127 4 PMIEVRNLTKSFGDR----VVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGqdiTGLSEKELYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 79 PGSRVGFMPQEIALVEEMTVKETI-FYFGRIYGLTDERIREK--FKLlkELLQLPPAR-QMIKQCSGGQQRRLSFACAMI 154
Cdd:COG1127 80 LRRRIGMLFQGGALFDSLTVFENVaFPLREHTDLSEAEIRELvlEKL--ELVGLPGAAdKMPSELSGGMRKRVALARALA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24582012 155 HDPELLILDEPTVGLDPMLREKIWDFLVETTRNSKLAVIITTHYIEEAKQ-ANCIGLMRNGVLLAEDTPTNIM 226
Cdd:COG1127 158 LDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEELL 230
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-235 |
2.12e-39 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 147.18 E-value: 2.12e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 3 AVEVRNGYKYYGSKsnpkIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGakpgEPGSGVPGSR 82
Cdd:COG4152 1 MLELKGLTKRFGDK----TAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDG----EPLDPEDRRR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 83 VGFMPQEIALVEEMTVKETIFYFGRIYGLTDERIREKFKLLKELLQLPPARQM-IKQCSGGQQRRLSFACAMIHDPELLI 161
Cdd:COG4152 73 IGYLPEERGLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKkVEELSKGNQQKVQLIAALLHDPELLI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24582012 162 LDEPTVGLDPMLREKIWDFLVETTRNSKlAVIITTH---YIEEAkqanC--IGLMRNGVLLAEDTPTNIMIKFGTQSIE 235
Cdd:COG4152 153 LDEPFSGLDPVNVELLKDVIRELAAKGT-TVIFSSHqmeLVEEL----CdrIVIINKGRKVLSGSVDEIRRQFGRNTLR 226
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-202 |
2.51e-39 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 146.00 E-value: 2.51e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 1 MAAVEVRNGYKYYGSKSNPKIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVlgakPGEPGSGvPG 80
Cdd:COG1116 5 APALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLV----DGKPVTG-PG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 81 SRVGFMPQEIALVEEMTVKETIfYFG-RIYGLTDERIREKfklLKELLQL----------PparqmiKQCSGGQQRRLSF 149
Cdd:COG1116 80 PDRGVVFQEPALLPWLTVLDNV-ALGlELRGVPKAERRER---ARELLELvglagfedayP------HQLSGGMRQRVAI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 24582012 150 ACAMIHDPELLILDEPTVGLDPMLREKIWDFLVETTRNSKLAVIITTHYIEEA 202
Cdd:COG1116 150 ARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEA 202
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-219 |
7.39e-39 |
|
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: 142.74 E-value: 7.39e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 4 VEVRNGYKYYGSKSnpkiVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGAKPGEPGSGVpgSRV 83
Cdd:cd03268 1 LKTNDLTKTYGKKR----VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEAL--RRI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 84 GFMPQEIALVEEMTVKETIFYFGRIYGLTDERIREkfkLLKELLQLPPARQMIKQCSGGQQRRLSFACAMIHDPELLILD 163
Cdd:cd03268 75 GALIEAPGFYPNLTARENLRLLARLLGIRKKRIDE---VLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILD 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24582012 164 EPTVGLDPM----LREKIWDFlvettRNSKLAVIITTHYIEEAKQ-ANCIGLMRNGVLLAE 219
Cdd:cd03268 152 EPTNGLDPDgikeLRELILSL-----RDQGITVLISSHLLSEIQKvADRIGIINKGKLIEE 207
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-216 |
7.90e-39 |
|
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: 143.01 E-value: 7.90e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 4 VEVRNGYKYYGSKSNPKIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGakpgEPGSGVPGSR- 82
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDG----TDISKLSEKEl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 83 -------VGFMPQEIALVEEMTVKETIFYFGRIYGLTDERIREKFKLLKELLQLPP-ARQMIKQCSGGQQRRLSFACAMI 154
Cdd:cd03255 77 aafrrrhIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDrLNHYPSELSGGQQQRVAIARALA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24582012 155 HDPELLILDEPTVGLDPMLREKIWDFLVETTRNSKLAVIITTHYIEEAKQANCIGLMRNGVL 216
Cdd:cd03255 157 NDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-215 |
1.24e-38 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 142.42 E-value: 1.24e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 4 VEVRNGYKYYGSKSnpkiVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGakpgEPGSGVPGSRV 83
Cdd:cd03269 1 LEVENVTKRFGRVT----ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDG----KPLDIAARNRI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 84 GFMPQEIALVEEMTVKETIFYFGRIYGLTDERIREKFKLLKELLQLPP-ARQMIKQCSGGQQRRLSFACAMIHDPELLIL 162
Cdd:cd03269 73 GYLPEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEyANKRVEELSKGNQQKVQFIAAVIHDPELLIL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 24582012 163 DEPTVGLDPMLREKIWDFLVETTRNSKlAVIITTHYIEEAkQANC--IGLMRNGV 215
Cdd:cd03269 153 DEPFSGLDPVNVELLKDVIRELARAGK-TVILSTHQMELV-EELCdrVLLLNKGR 205
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-235 |
1.35e-38 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 146.13 E-value: 1.35e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 1 MAAVEVRNGYKYYGSKsnpkIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGAKpgepgsgVPG 80
Cdd:PRK13536 39 TVAIDLAGVSKSYGDK----AVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVP-------VPA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 81 ------SRVGFMPQEIALVEEMTVKETIFYFGRIYGLTDERIREKFKLLKELLQLP-PARQMIKQCSGGQQRRLSFACAM 153
Cdd:PRK13536 108 rarlarARIGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLEsKADARVSDLSGGMKRRLTLARAL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 154 IHDPELLILDEPTVGLDPMLREKIWDFLVETTRNSKlAVIITTHYIEEAKQ-ANCIGLMRNGVLLAEDTPTN-IMIKFGT 231
Cdd:PRK13536 188 INDPQLLILDEPTTGLDPHARHLIWERLRSLLARGK-TILLTTHFMEEAERlCDRLCVLEAGRKIAEGRPHAlIDEHIGC 266
|
....
gi 24582012 232 QSIE 235
Cdd:PRK13536 267 QVIE 270
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-219 |
9.34e-38 |
|
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: 139.64 E-value: 9.34e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 4 VEVRNGYKYYGSKsnpkIVLNQLNMNVMRGsIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGAKPGEPGSGVPgSRV 83
Cdd:cd03264 1 LQLENLTKRYGKK----RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLR-RRI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 84 GFMPQEIALVEEMTVKETIFYFGRIYGLTDERIREKFKLLKELLQLPP-ARQMIKQCSGGQQRRLSFACAMIHDPELLIL 162
Cdd:cd03264 75 GYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDrAKKKIGSLSGGMRRRVGIAQALVGDPSILIV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 24582012 163 DEPTVGLDPMLREKIWDFLVETTRNSklAVIITTHYIEE-AKQANCIGLMRNGVLLAE 219
Cdd:cd03264 155 DEPTAGLDPEERIRFRNLLSELGEDR--IVILSTHIVEDvESLCNQVAVLNKGKLVFE 210
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-222 |
1.45e-37 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 142.25 E-value: 1.45e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 2 AAVEVRNGYKYYGSKsnpkIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGakpgEPgsgVPG- 80
Cdd:PRK13537 6 APIDFRNVEKRYGDK----LVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCG----EP---VPSr 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 81 -----SRVGFMPQEIALVEEMTVKETIFYFGRIYGLTDERIREKFKLLKELLQLP-PARQMIKQCSGGQQRRLSFACAMI 154
Cdd:PRK13537 75 arharQRVGVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLEnKADAKVGELSGGMKRRLTLARALV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24582012 155 HDPELLILDEPTVGLDPMLREKIWDFLVETTRNSKlAVIITTHYIEEAKQ-ANCIGLMRNGVLLAEDTP 222
Cdd:PRK13537 155 NDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGK-TILLTTHFMEEAERlCDRLCVIEEGRKIAEGAP 222
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-214 |
3.15e-37 |
|
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: 137.32 E-value: 3.15e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 4 VEVRNGYKYYGSKsnpkIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGAKPGEPGSGVPGSR- 82
Cdd:cd03229 1 LELKNVSKRYGQK----TVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLRr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 83 -VGFMPQEIALVEEMTVKETIfyfgrIYGLtderirekfkllkellqlpparqmikqcSGGQQRRLSFACAMIHDPELLI 161
Cdd:cd03229 77 rIGMVFQDFALFPHLTVLENI-----ALGL----------------------------SGGQQQRVALARALAMDPDVLL 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 24582012 162 LDEPTVGLDPMLREKIWDFLVETTRNSKLAVIITTHYIEEAKQ-ANCIGLMRNG 214
Cdd:cd03229 124 LDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARlADRVVVLRDG 177
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
32-238 |
3.71e-37 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 149.50 E-value: 3.71e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 32 RGSIYGLLGASGCGKTT-------LLSCIVGQRRLNGGEVvvlgakpgEPGSGVPGSRVGFMPQEIALVEEMTVKETIFY 104
Cdd:NF033858 291 RGEIFGFLGSNGCGKSTtmkmltgLLPASEGEAWLFGQPV--------DAGDIATRRRVGYMSQAFSLYGELTVRQNLEL 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 105 FGRIYGLTDERIR-------EKFKLLKELLQLPPA-----RQmikqcsggqqrRLSFACAMIHDPELLILDEPTVGLDPM 172
Cdd:NF033858 363 HARLFHLPAAEIAarvaemlERFDLADVADALPDSlplgiRQ-----------RLSLAVAVIHKPELLILDEPTSGVDPV 431
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24582012 173 LREKIWDFLVETTRNSKLAVIITTHYIEEAkqANC--IGLMRNGVLLAEDTPTNIMIKFGTQSIEDAF 238
Cdd:NF033858 432 ARDMFWRLLIELSREDGVTIFISTHFMNEA--ERCdrISLMHAGRVLASDTPAALVAARGAATLEEAF 497
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
23-248 |
7.99e-36 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 145.27 E-value: 7.99e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 23 LNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGAKPGEPG--SGVpGSRVGFMPQEIA--LVEEMTV 98
Cdd:NF033858 17 LDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARhrRAV-CPRIAYMPQGLGknLYPTLSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 99 KETIFYFGRIYGLT----DERIREkfkLLKE--LLQLP--PARQMikqcSGGQQRRLSFACAMIHDPELLILDEPTVGLD 170
Cdd:NF033858 96 FENLDFFGRLFGQDaaerRRRIDE---LLRAtgLAPFAdrPAGKL----SGGMKQKLGLCCALIHDPDLLILDEPTTGVD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 171 PMLREKIWDfLVETTR--NSKLAVIITTHYIEEAKQANCIGLMRNGVLLAEDTPTNIMIKFGTQSIEDAFLIL---SQRQ 245
Cdd:NF033858 169 PLSRRQFWE-LIDRIRaeRPGMSVLVATAYMEEAERFDWLVAMDAGRVLATGTPAELLARTGADTLEAAFIALlpeEKRR 247
|
...
gi 24582012 246 GNE 248
Cdd:NF033858 248 GHQ 250
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-225 |
8.71e-36 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 138.69 E-value: 8.71e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 1 MAAVEVRNGYKYYGSKsnpkIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVvLGakpGEPGSGVPG 80
Cdd:COG3842 3 MPALELENVSKRYGDV----TALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRIL-LD---GRDVTGLPP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 81 SR--VGFMPQEIALVEEMTVKETIFYFGRIYGLTDERIREKFKLLKELLQLPP-ARQMIKQCSGGQQRRLSFACAMIHDP 157
Cdd:COG3842 75 EKrnVGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGlADRYPHQLSGGQQQRVALARALAPEP 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24582012 158 ELLILDEPTVGLDPMLREKIWDFLVETTRNSKLAVIITTHYIEEA-----KqancIGLMRNGVLLAEDTPTNI 225
Cdd:COG3842 155 RVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEAlaladR----IAVMNDGRIEQVGTPEEI 223
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-221 |
1.60e-35 |
|
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: 134.55 E-value: 1.60e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 3 AVEVRNGYKYYGSKSNPKIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGAKPGEPGSGVPGSR 82
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 83 VGFMPQEI--ALVEEMTVKETIFYFGRIYGLTD--ERIREkfkLLkELLQLPPA--RQMIKQCSGGQQRRLSFACAMIHD 156
Cdd:COG1124 81 VQMVFQDPyaSLHPRHTVDRILAEPLRIHGLPDreERIAE---LL-EQVGLPPSflDRYPHQLSGGQRQRVAIARALILE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24582012 157 PELLILDEPTVGLDPMLREKIWDFLVETTRNSKLAVIITTHYIEE-AKQANCIGLMRNGVLLAEDT 221
Cdd:COG1124 157 PELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVvAHLCDRVAVMQNGRIVEELT 222
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-219 |
6.78e-35 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 132.09 E-value: 6.78e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 1 MAAV-EVRNGYKYYGSKSNPKIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLG---AKPGEPG- 75
Cdd:COG1136 1 MSPLlELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGqdiSSLSEREl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 76 SGVPGSRVGFMPQEIALVEEMTVKETIFYFGRIYGLTDERIREKFKLLKELLQLPP-ARQMIKQCSGGQQRRLSFACAMI 154
Cdd:COG1136 81 ARLRRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDrLDHRPSQLSGGQQQRVAIARALV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24582012 155 HDPELLILDEPTVGLDPMLREKIWDFLVETTRNSKLAVIITTHYIEEAKQANCIGLMRNGVLLAE 219
Cdd:COG1136 161 NRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAARADRVIRLRDGRIVSD 225
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
5-214 |
4.05e-34 |
|
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: 129.51 E-value: 4.05e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 5 EVRNGYKYYGSKSNPkiVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGAKPGEPGSGVPGSRVG 84
Cdd:cd03225 1 ELKNLSFSYPDGARP--ALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 85 FMPQEialVEEMTVKETIF---YFG-RIYGLTDERIREKFKLLKELLQLPPAR-QMIKQCSGGQQRRLSFACAMIHDPEL 159
Cdd:cd03225 79 LVFQN---PDDQFFGPTVEeevAFGlENLGLPEEEIEERVEEALELVGLEGLRdRSPFTLSGGQKQRVAIAGVLAMDPDI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 24582012 160 LILDEPTVGLDPMLREKIWDFLvETTRNSKLAVIITTHYIEEAKQ-ANCIGLMRNG 214
Cdd:cd03225 156 LLLDEPTAGLDPAGRRELLELL-KKLKAEGKTIIIVTHDLDLLLElADRVIVLEDG 210
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-226 |
6.00e-34 |
|
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: 129.76 E-value: 6.00e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 4 VEVRN-GYKYYGSKSnpkiVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGAKPGEPGSGVPGSR 82
Cdd:COG1122 1 IELENlSFSYPGGTP----ALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 83 VGFMPQ--EIALVEEmTVKETIFyFG-RIYGLTDERIREKFK--L----LKELLQLPPArqmikQCSGGQQRRLSFACAM 153
Cdd:COG1122 77 VGLVFQnpDDQLFAP-TVEEDVA-FGpENLGLPREEIRERVEeaLelvgLEHLADRPPH-----ELSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24582012 154 IHDPELLILDEPTVGLDPMLREKIWDFLvETTRNSKLAVIITTHYIEEA-KQANCIGLMRNGVLLAEDTPTNIM 226
Cdd:COG1122 150 AMEPEVLVLDEPTAGLDPRGRRELLELL-KRLNKEGKTVIIVTHDLDLVaELADRVIVLDDGRIVADGTPREVF 222
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
4-214 |
1.33e-33 |
|
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: 128.78 E-value: 1.33e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 4 VEVRNGYKYYGSKSNPKIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLG---AKPGEPGSGVPG 80
Cdd:cd03257 2 LEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGkdlLKLSRRLRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 81 SRVGFMPQEI--ALVEEMTVK----ETIFYFGRIYGltDERIREKFKLLKELLQLPP--ARQMIKQCSGGQQRRLSFACA 152
Cdd:cd03257 82 KEIQMVFQDPmsSLNPRMTIGeqiaEPLRIHGKLSK--KEARKEAVLLLLVGVGLPEevLNRYPHELSGGQRQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24582012 153 MIHDPELLILDEPTVGLDPMLREKIWDFLVETTRNSKLAVIITTHYIEEAKQ-ANCIGLMRNG 214
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKiADRVAVMYAG 222
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
4-219 |
1.72e-33 |
|
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: 127.87 E-value: 1.72e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 4 VEVRNGYKYYGSKSNPKIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLG----AKPGEPGSgvp 79
Cdd:cd03266 2 ITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfdvvKEPAEARR--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 80 gsRVGFMPQEIALVEEMTVKETIFYFGRIYGLTDERIREKFKLLKELLQLPPARQM-IKQCSGGQQRRLSFACAMIHDPE 158
Cdd:cd03266 79 --RLGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRrVGGFSTGMRQKVAIARALVHDPP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24582012 159 LLILDEPTVGLDPMLREKIWDFLVETTRNSKlAVIITTHYIEEAkQANC--IGLMRNGVLLAE 219
Cdd:cd03266 157 VLLLDEPTTGLDVMATRALREFIRQLRALGK-CILFSTHIMQEV-ERLCdrVVVLHRGRVVYE 217
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
20-199 |
2.47e-33 |
|
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: 128.22 E-value: 2.47e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 20 KIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGAKPGEPGSGVPgSRVGF-MPQEIALVEEMTV 98
Cdd:cd03267 34 VEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFL-RRIGVvFGQKTQLWWDLPV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 99 KETIFYFGRIYGLTDERIREKFKLLKELLQLPPA-RQMIKQCSGGQQRRLSFACAMIHDPELLILDEPTVGLDPMLREKI 177
Cdd:cd03267 113 IDSFYLLAAIYDLPPARFKKRLDELSELLDLEELlDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENI 192
|
170 180
....*....|....*....|..
gi 24582012 178 WDFLVETTRNSKLAVIITTHYI 199
Cdd:cd03267 193 RNFLKEYNRERGTTVLLTSHYM 214
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
20-197 |
3.26e-33 |
|
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: 126.82 E-value: 3.26e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 20 KIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGAKPGEPGSGVPgSRVGFMPQEIALVEEMTVK 99
Cdd:COG4133 15 RLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYR-RRLAYLGHADGLKPELTVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 100 ETIFYFGRIYGL--TDERIREkfkLLkELLQLPPAR-QMIKQCSGGQQRRLSFACAMIHDPELLILDEPTVGLDPMLREK 176
Cdd:COG4133 94 ENLRFWAALYGLraDREAIDE---AL-EAVGLAGLAdLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVAL 169
|
170 180
....*....|....*....|.
gi 24582012 177 IWDfLVETTRNSKLAVIITTH 197
Cdd:COG4133 170 LAE-LIAAHLARGGAVLLTTH 189
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-226 |
3.89e-33 |
|
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: 128.24 E-value: 3.89e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 3 AVEVRNGYKYYGSKsnpkIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLG-----------AKp 71
Cdd:COG1120 1 MLEAENLSVGYGGR----PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGrdlaslsrrelAR- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 72 gepgsgvpgsRVGFMPQEIALVEEMTVKETIF-----YFGRIYGLTDE---RIREKFKLLkELLQLppARQMIKQCSGGQ 143
Cdd:COG1120 76 ----------RIAYVPQEPPAPFGLTVRELVAlgrypHLGLFGRPSAEdreAVEEALERT-GLEHL--ADRPVDELSGGE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 144 QRRLSFACAMIHDPELLILDEPTVGLDPMLREKIWDFLVETTRNSKLAVIITTHYIEEAKQ-ANCIGLMRNGVLLAEDTP 222
Cdd:COG1120 143 RQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARyADRLVLLKDGRIVAQGPP 222
|
....
gi 24582012 223 TNIM 226
Cdd:COG1120 223 EEVL 226
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-214 |
4.77e-33 |
|
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: 124.66 E-value: 4.77e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 5 EVRNGYKYYGSKsnpkIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGakpgepgsgvpgsrvg 84
Cdd:cd00267 1 EIENLSFRYGGR----TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDG---------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 85 fmpQEIALVEEMTVKETIFYfgriygltderirekfkllkellqlpparqmIKQCSGGQQRRLSFACAMIHDPELLILDE 164
Cdd:cd00267 61 ---KDIAKLPLEELRRRIGY-------------------------------VPQLSGGQRQRVALARALLLNPDLLLLDE 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 24582012 165 PTVGLDPMLREKIWDFLVEtTRNSKLAVIITTHYIEEAKQA-NCIGLMRNG 214
Cdd:cd00267 107 PTSGLDPASRERLLELLRE-LAEEGRTVIIVTHDPELAELAaDRVIVLKDG 156
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-197 |
8.55e-33 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 126.74 E-value: 8.55e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 1 MAAVEVRNGYKYYGSKsnpkIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGAKPGEPGSgvpg 80
Cdd:COG1121 4 MPAIELENLTVSYGGR----PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARR---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 81 sRVGFMPQEIALVEE--MTVKETI---FY----FGRIYGLTD-ERIREKFKLLkELLQLppARQMIKQCSGGQQRRLSFA 150
Cdd:COG1121 76 -RIGYVPQRAEVDWDfpITVRDVVlmgRYgrrgLFRRPSRADrEAVDEALERV-GLEDL--ADRPIGELSGGQQQRVLLA 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 24582012 151 CAMIHDPELLILDEPTVGLDPMLREKIWDfLVETTRNSKLAVIITTH 197
Cdd:COG1121 152 RALAQDPDLLLLDEPFAGVDAATEEALYE-LLRELRREGKTILVVTH 197
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
4-236 |
1.68e-32 |
|
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: 125.88 E-value: 1.68e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 4 VEVRNGYKYYGsksNPKIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIvgqRRL---NGGEVVVlgakPGEPGSGVPG 80
Cdd:cd03295 1 IEFENVTKRYG---GGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMI---NRLiepTSGEIFI----DGEDIREQDP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 81 S----RVGFMPQEIALVEEMTVKETIFYFGRIYGLTDERIREKFKLLKELLQLPPARQMIK---QCSGGQQRRLSFACAM 153
Cdd:cd03295 71 VelrrKIGYVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPAEFADRyphELSGGQQQRVGVARAL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 154 IHDPELLILDEPTVGLDPMLREKIWDFLVETTRNSKLAVIITTHYIEEA-KQANCIGLMRNGVLLAEDTPTNIMIKFGTQ 232
Cdd:cd03295 151 AADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAfRLADRIAIMKNGEIVQVGTPDEILRSPAND 230
|
....
gi 24582012 233 SIED 236
Cdd:cd03295 231 FVAE 234
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
23-167 |
3.80e-32 |
|
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: 121.60 E-value: 3.80e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 23 LNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGAKPGEPGSGVPGSRVGFMPQEIALVEEMTVKETI 102
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 103 FYFGRIYGLTDERIREKFKLLKELLQLP-----PARQMIKQCSGGQQRRLSFACAMIHDPELLILDEPTV 167
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGdladrPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-226 |
1.16e-31 |
|
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: 129.64 E-value: 1.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 4 VEVRNGYKYYGSKSNPKI-VLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGakpgEPGSGVPGSR 82
Cdd:COG1123 261 LEVRNLSKRYPVRGKGGVrAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDG----KDLTKLSRRS 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 83 VGFMPQEIALV---------EEMTVKETIFYFGRIYGLTD-----ERIREkfkLLkELLQLPP--ARQMIKQCSGGQQRR 146
Cdd:COG1123 337 LRELRRRVQMVfqdpysslnPRMTVGDIIAEPLRLHGLLSraerrERVAE---LL-ERVGLPPdlADRYPHELSGGQRQR 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 147 LSFACAMIHDPELLILDEPTVGLDPMLREKIWDFLVETTRNSKLAVIITTHYIEEAKQ-ANCIGLMRNGVLLAEDTPTNI 225
Cdd:COG1123 413 VAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPTEEV 492
|
.
gi 24582012 226 M 226
Cdd:COG1123 493 F 493
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
16-197 |
1.59e-31 |
|
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: 122.76 E-value: 1.59e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 16 KSNPKIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGqRRLNG----GEVVVLGaKPGEPGSgVPgSRVGFMPQEIA 91
Cdd:cd03234 16 WNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISG-RVEGGgttsGQILFNG-QPRKPDQ-FQ-KCVAYVRQDDI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 92 LVEEMTVKETIFYFGRIYG--LTDERIREK---FKLLKELLQLPPARQMIKQCSGGQQRRLSFACAMIHDPELLILDEPT 166
Cdd:cd03234 92 LLPGLTVRETLTYTAILRLprKSSDAIRKKrveDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPT 171
|
170 180 190
....*....|....*....|....*....|.
gi 24582012 167 VGLDPMLREKIWDFLVETTRNSKLaVIITTH 197
Cdd:cd03234 172 SGLDSFTALNLVSTLSQLARRNRI-VILTIH 201
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
4-225 |
9.34e-31 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 123.72 E-value: 9.34e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 4 VEVRNGYKYYGSKSnpkiVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVG-------QRRLNGgEVVVLGAKPGEpgs 76
Cdd:COG1118 3 IEVRNISKRFGSFT----LLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGletpdsgRIVLNG-RDLFTNLPPRE--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 77 gvpgSRVGFMPQEIALVEEMTVKETIfYFG-RIYGLTDERIREK-FKLLkELLQLP-PARQMIKQCSGGQQRRLSFACAM 153
Cdd:COG1118 75 ----RRVGFVFQHYALFPHMTVAENI-AFGlRVRPPSKAEIRARvEELL-ELVQLEgLADRYPSQLSGGQRQRVALARAL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24582012 154 IHDPELLILDEPTVGLDPMLREKIWDFLVETTRNSKLAVIITTHYIEEAKQ-ANCIGLMRNGVLLAEDTPTNI 225
Cdd:COG1118 149 AVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALElADRVVVMNQGRIEQVGTPDEV 221
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-225 |
1.01e-30 |
|
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: 120.42 E-value: 1.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 4 VEVRNGYKYYGSKsnpkIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVlgakPGEPGSGVPGSR- 82
Cdd:cd03300 1 IELENVSKFYGGF----VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILL----DGKDITNLPPHKr 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 83 -VGFMPQEIALVEEMTVKETIFYFGRIYGLTDERIREKFKLLKELLQLPP-ARQMIKQCSGGQQRRLSFACAMIHDPELL 160
Cdd:cd03300 73 pVNTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGyANRKPSQLSGGQQQRVAIARALVNEPKVL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24582012 161 ILDEPTVGLDPMLREKIWDFLVETTRNSKLAVIITTHYIEEA-KQANCIGLMRNGVLLAEDTPTNI 225
Cdd:cd03300 153 LLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEAlTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
33-218 |
1.30e-30 |
|
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: 119.71 E-value: 1.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 33 GSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGA--KPGEPGSGVPGS--RVGFMPQEIALVEEMTVKETIfyfgrI 108
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlFDSRKKINLPPQqrKIGLVFQQYALFPHLNVRENL-----A 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 109 YGLTDERIREKFKLLKELLQL----PPARQMIKQCSGGQQRRLSFACAMIHDPELLILDEPTVGLDPMLREKIWDFLVET 184
Cdd:cd03297 98 FGLKRKRNREDRISVDELLDLlgldHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQI 177
|
170 180 190
....*....|....*....|....*....|....*
gi 24582012 185 TRNSKLAVIITTHYIEEA-KQANCIGLMRNGVLLA 218
Cdd:cd03297 178 KKNLNIPVIFVTHDLSEAeYLADRIVVMEDGRLQY 212
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-224 |
4.23e-30 |
|
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: 118.44 E-value: 4.23e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 4 VEVRNGYKYYGSKSnpkiVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIvgqRRLN--------GGEVVVLGAKPGEPG 75
Cdd:cd03260 1 IELRDLNVYYGDKH----ALKDISLDIPKGEITALIGPSGCGKSTLLRLL---NRLNdlipgapdEGEVLLDGKDIYDLD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 76 SGVPGSR--VGFMPQEIALVEeMTVKETIFYFGRIYGLTDERIREKfkLLKELLQ---LPPA---RQMIKQCSGGQQRRL 147
Cdd:cd03260 74 VDVLELRrrVGMVFQKPNPFP-GSIYDNVAYGLRLHGIKLKEELDE--RVEEALRkaaLWDEvkdRLHALGLSGGQQQRL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24582012 148 SFACAMIHDPELLILDEPTVGLDPMLREKIWDFLVETtrNSKLAVIITTHYIEEAKQ-ANCIGLMRNGVLLaEDTPTN 224
Cdd:cd03260 151 CLARALANEPEVLLLDEPTSALDPISTAKIEELIAEL--KKEYTIVIVTHNMQQAARvADRTAFLLNGRLV-EFGPTE 225
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
5-214 |
5.00e-30 |
|
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: 118.82 E-value: 5.00e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 5 EVRNGYKYYGsksNPKIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGAK-PGEPGSGVPGSR- 82
Cdd:cd03256 2 EVENLSKTYP---NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDiNKLKGKALRQLRr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 83 -VGFMPQEIALVEEMTVKETIFyFGR---------IYGL-TDERIREKFKLLKELLQLPPARQMIKQCSGGQQRRLSFAC 151
Cdd:cd03256 79 qIGMIFQQFNLIERLSVLENVL-SGRlgrrstwrsLFGLfPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24582012 152 AMIHDPELLILDEPTVGLDPMLREKIWDFLVETTRNSKLAVIITTHYIEEAKQ-ANCIGLMRNG 214
Cdd:cd03256 158 ALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREyADRIVGLKDG 221
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
14-204 |
8.29e-30 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 117.22 E-value: 8.29e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 14 GSKSNPKIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGakpgEPGSGVPG----SRVGFMPQE 89
Cdd:COG4619 7 SFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDG----KPLSAMPPpewrRQVAYVPQE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 90 IALVEEmTVKEtifYFGRIYGLTDERI-REKFKLLKELLQLPPA--RQMIKQCSGGQQRRLSFACAMIHDPELLILDEPT 166
Cdd:COG4619 83 PALWGG-TVRD---NLPFPFQLRERKFdRERALELLERLGLPPDilDKPVERLSGGERQRLALIRALLLQPDVLLLDEPT 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 24582012 167 VGLDPMLREKIWDFLVETTRNSKLAVIITTHYIEEAKQ 204
Cdd:COG4619 159 SALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIER 196
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-226 |
8.51e-30 |
|
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: 124.25 E-value: 8.51e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 1 MAAV-EVRNGYKYYGSKSNPkiVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNG---GEVVVLGAKPGEPGS 76
Cdd:COG1123 1 MTPLlEVRDLSVRYPGGDVP--AVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 77 GVPGSRVGFMPQE--IALVEeMTVKETIFYFGRIYGLTDERIREKFKLLKELLQLPP-ARQMIKQCSGGQQRRLSFACAM 153
Cdd:COG1123 79 ALRGRRIGMVFQDpmTQLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERrLDRYPHQLSGGQRQRVAIAMAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24582012 154 IHDPELLILDEPTVGLDPMLREKIWDFLVETTRNSKLAVIITTHYIEEAKQ-ANCIGLMRNGVLLAEDTPTNIM 226
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEIL 231
|
|
| YadH |
COG0842 |
ABC-type multidrug transport system, permease component [Defense mechanisms]; |
513-710 |
2.44e-29 |
|
ABC-type multidrug transport system, permease component [Defense mechanisms];
Pssm-ID: 440604 [Multi-domain] Cd Length: 200 Bit Score: 115.68 E-value: 2.44e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 513 FQQYCAPGVVMTMVFFLATLMTAAVFISERMDGIWDRTLLAGVSATEMLWAHLLTQLIIMALQSFEVIMYIGLVFD-TYN 591
Cdd:COG0842 1 YLAFLVPGLLAMSLLFTALMLTALSIAREREQGTLERLLVTPVSRLEILLGKVLAYLLRGLLQALLVLLVALLFFGvPLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 592 NGDTTTLIGLLTLTAFCGMLFGLFISVFCKSHTEANFVATGAFYPMIILCGLLWPLESMPQFLQDLVMVLPFTIPSISAR 671
Cdd:COG0842 81 GLSLLLLLLVLLLFALAFSGLGLLISTLARSQEQASAISNLVILPLTFLSGAFFPIESLPGWLQAIAYLNPLTYFVEALR 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 24582012 672 NVIEKGWSITHekVYNGFLVMAGWTIIFFVLCLIGIRRK 710
Cdd:COG0842 161 ALFLGGAGLAD--VWPSLLVLLAFAVVLLALALRLFRRR 197
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-202 |
1.58e-28 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 114.96 E-value: 1.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 1 MAAVEVRNGYKYYGSKSNPKIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVlgakPGEPGSGvPG 80
Cdd:COG4525 1 MSMLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITL----DGVPVTG-PG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 81 SRVGFMPQEIALVEEMTVKETIfYFG-RIYGLT----DERIREKFKLLKeLLQLppARQMIKQCSGGQQRRLSFACAMIH 155
Cdd:COG4525 76 ADRGVVFQKDALLPWLNVLDNV-AFGlRLRGVPkaerRARAEELLALVG-LADF--ARRRIWQLSGGMRQRVGIARALAA 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 24582012 156 DPELLILDEPTVGLDPMLREKIWDFLVETTRNSKLAVIITTHYIEEA 202
Cdd:COG4525 152 DPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEA 198
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
1-225 |
2.17e-28 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 117.06 E-value: 2.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 1 MAAVEVRNGYKYYGSKSnpkiVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLG----AKPgepgs 76
Cdd:TIGR03265 2 SPYLSIDNIRKRFGAFT----ALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGrditRLP----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 77 gvPGSR-VGFMPQEIALVEEMTVKETIfyfgrIYGLTD-----ERIREKFKLLKELLQLPPA-RQMIKQCSGGQQRRLSF 149
Cdd:TIGR03265 73 --PQKRdYGIVFQSYALFPNLTVADNI-----AYGLKNrgmgrAEVAERVAELLDLVGLPGSeRKYPGQLSGGQQQRVAL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24582012 150 ACAMIHDPELLILDEPTVGLDPMLREKIWDFLVETTRNSKLAVIITTHYIEEA-KQANCIGLMRNGVLLAEDTPTNI 225
Cdd:TIGR03265 146 ARALATSPGLLLLDEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEAlSMADRIVVMNHGVIEQVGTPQEI 222
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-218 |
3.80e-28 |
|
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: 113.64 E-value: 3.80e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 1 MAAVEVRNGYKYYGSKsnpkIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRR-LNGGEVVVLGAKPGepGSGVP 79
Cdd:COG1119 1 DPLLELRNVTVRRGGK----TILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPpTYGNDVRLFGERRG--GEDVW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 80 G--SRVGFMPQEIA--LVEEMTVKETI---FY--FGRIYGLTDERIREKFKLLKEL--LQLppARQMIKQCSGGQQRRLS 148
Cdd:COG1119 75 ElrKRIGLVSPALQlrFPRDETVLDVVlsgFFdsIGLYREPTDEQRERARELLELLglAHL--ADRPFGTLSQGEQRRVL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24582012 149 FACAMIHDPELLILDEPTVGLDPMLREKIWDFLVETTRNSKLAVIITTHYIEEAkqANCIG---LMRNGVLLA 218
Cdd:COG1119 153 IARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEI--PPGIThvlLLKDGRVVA 223
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-225 |
5.11e-28 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 115.94 E-value: 5.11e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 1 MAAVEVRNGYKYYGSKsnpkIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEV-----VVLGAKPGEPG 75
Cdd:COG3839 1 MASLELENVSKSYGGV----EALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEIliggrDVTDLPPKDRN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 76 sgvpgsrVGFMPQEIALVEEMTVKETIfYFG-RIYGLTDERIREKFKLLKELLQLPP-----ARQMikqcSGGQQRRLSF 149
Cdd:COG3839 77 -------IAMVFQSYALYPHMTVYENI-AFPlKLRKVPKAEIDRRVREAAELLGLEDlldrkPKQL----SGGQRQRVAL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24582012 150 ACAMIHDPELLILDEPTVGLDPMLREKIWDFLVETTRNSKLAVIITTHYIEEAKQ-ANCIGLMRNGVLLAEDTPTNI 225
Cdd:COG3839 145 GRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTlADRIAVMNDGRIQQVGTPEEL 221
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-226 |
6.83e-28 |
|
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: 112.25 E-value: 6.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 4 VEVRNGYKYYGSKSnpkiVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVlgakPGEPGSGVPGSR- 82
Cdd:cd03218 1 LRAENLSKRYGKRK----VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILL----DGQDITKLPMHKr 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 83 ----VGFMPQEIALVEEMTVKETIFYFGRIYGLTDERIREKFKLLKELLQLPPAR-QMIKQCSGGQQRRLSFACAMIHDP 157
Cdd:cd03218 73 arlgIGYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRkSKASSLSGGERRRVEIARALATNP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 158 ELLILDEPTVGLDPMLREKIwDFLVETTRNSKLAVIITTHYIEEAKQ-ANCIGLMRNGVLLAEDTPTNIM 226
Cdd:cd03218 153 KFLLLDEPFAGVDPIAVQDI-QKIIKILKDRGIGVLITDHNVRETLSiTDRAYIIYEGKVLAEGTPEEIA 221
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
38-225 |
9.36e-28 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 114.51 E-value: 9.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 38 LLGASGCGKTTLLSCIVGQRRLNGGEVVVlgakPGEPGSGVPGSR--VGFMPQEIALVEEMTVKETIFYFGRIYGLTDER 115
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIML----DGEDVTNVPPHLrhINMVFQSYALFPHMTVEENVAFGLKMRKVPRAE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 116 IREKFKLLKELLQLPP-ARQMIKQCSGGQQRRLSFACAMIHDPELLILDEPTVGLDPMLREKIWDFLVETTRNSKLAVII 194
Cdd:TIGR01187 77 IKPRVLEALRLVQLEEfADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVF 156
|
170 180 190
....*....|....*....|....*....|..
gi 24582012 195 TTHYIEEA-KQANCIGLMRNGVLLAEDTPTNI 225
Cdd:TIGR01187 157 VTHDQEEAmTMSDRIAIMRKGKIAQIGTPEEI 188
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-216 |
1.02e-27 |
|
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: 111.19 E-value: 1.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 4 VEVRNGYKYYGSKsnpkIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLG-----AKPGEPGsgv 78
Cdd:cd03301 1 VELENVTKRFGNV----TALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGrdvtdLPPKDRD--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 79 pgsrVGFMPQEIALVEEMTVKETIFYFGRIYGLT----DERIREKFKLLK--ELLQLPParqmiKQCSGGQQRRLSFACA 152
Cdd:cd03301 74 ----IAMVFQNYALYPHMTVYDNIAFGLKLRKVPkdeiDERVREVAELLQieHLLDRKP-----KQLSGGQRQRVALGRA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24582012 153 MIHDPELLILDEPTVGLDPMLREKIWDFLVETTRNSKLAVIITTH-YIEEAKQANCIGLMRNGVL 216
Cdd:cd03301 145 IVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHdQVEAMTMADRIAVMNDGQI 209
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
4-200 |
1.17e-27 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 111.30 E-value: 1.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 4 VEVRNGYKYYGsksNPKIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGAKPGE-PGSGVPGSR 82
Cdd:COG2884 2 IRFENVSKRYP---GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRlKRREIPYLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 83 --VGFMPQEIALVEEMTVKETIFYFGRIYGLTDERIREK-FKLLKE--LLQLppARQMIKQCSGGQQRRLSFACAMIHDP 157
Cdd:COG2884 79 rrIGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRvREVLDLvgLSDK--AKALPHELSGGEQQRVAIARALVNRP 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 24582012 158 ELLILDEPTVGLDPMLREKIWDFLVETTRNSKlAVIITTHYIE 200
Cdd:COG2884 157 ELLLADEPTGNLDPETSWEIMELLEEINRRGT-TVLIATHDLE 198
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
5-220 |
1.37e-27 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 111.34 E-value: 1.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 5 EVRNGYKYYGSKSnpkiVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVlgakPGEPGSGVPGSRVG 84
Cdd:TIGR03740 2 ETKNLSKRFGKQT----AVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIF----DGHPWTRKDLHKIG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 85 FMPQEIALVEEMTVKETIFYFGRIYGLTDERIREkfkLLKELLQLPPARQMIKQCSGGQQRRLSFACAMIHDPELLILDE 164
Cdd:TIGR03740 74 SLIESPPLYENLTARENLKVHTTLLGLPDSRIDE---VLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDE 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24582012 165 PTVGLDPM----LREkiwdfLVETTRNSKLAVIITTHYIEEAKQ-ANCIGLMRNGVLLAED 220
Cdd:TIGR03740 151 PTNGLDPIgiqeLRE-----LIRSFPEQGITVILSSHILSEVQQlADHIGIISEGVLGYQG 206
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
2-204 |
1.60e-27 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 111.69 E-value: 1.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 2 AAVEVRNGYKYYGSKsnpKIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGAKPGE-PGSGVPG 80
Cdd:COG3638 1 PMLELRNLSKRYPGG---TPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTAlRGRALRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 81 --SRVGFMPQEIALVEEMTVKE-----------TIFYFGRIYGlTDERIR-----EKFKLLKELLQlpPARQMikqcSGG 142
Cdd:COG3638 78 lrRRIGMIFQQFNLVPRLSVLTnvlagrlgrtsTWRSLLGLFP-PEDRERalealERVGLADKAYQ--RADQL----SGG 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24582012 143 QQRRLSFACAMIHDPELLILDEPTVGLDPMLREKIWDFLVETTRNSKLAVIITTHYIEEAKQ 204
Cdd:COG3638 151 QQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARR 212
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
3-225 |
1.98e-27 |
|
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: 111.28 E-value: 1.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 3 AVEVRNGYKYYGSKsnpkIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVlgakPGEPGSGVPGSR 82
Cdd:cd03296 2 SIEVRNVSKRFGDF----VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILF----GGEDATDVPVQE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 83 --VGFMPQEIALVEEMTVKETIfYFG-----RIYGLTDERIREKFKLLKELLQLPP-ARQMIKQCSGGQQRRLSFACAMI 154
Cdd:cd03296 74 rnVGFVFQHYALFRHMTVFDNV-AFGlrvkpRSERPPEAEIRAKVHELLKLVQLDWlADRYPAQLSGGQRQRVALARALA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24582012 155 HDPELLILDEPTVGLDPMLREKIWDFLVETTRNSKLAVIITTHYIEEAKQ-ANCIGLMRNGVLLAEDTPTNI 225
Cdd:cd03296 153 VEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEvADRVVVMNKGRIEQVGTPDEV 224
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
22-228 |
2.35e-27 |
|
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: 110.89 E-value: 2.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 22 VLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGA-----KPGEpgsgvpgSRVGFMPQEIALVEEM 96
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKditnlPPEK-------RDISYVPQNYALFPHM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 97 TVKETIFYFGRIYGLT----DERIREKFKLLK--ELLQLPPARqmikqCSGGQQRRLSFACAMIHDPELLILDEPTVGLD 170
Cdd:cd03299 87 TVYKNIAYGLKKRKVDkkeiERKVLEIAEMLGidHLLNRKPET-----LSGGEQQRVAIARALVVNPKILLLDEPFSALD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 24582012 171 PMLREKIWDFLVETTRNSKLAVIITTHYIEEAKQ-ANCIGLMRNGVLLAEDTPTNIMIK 228
Cdd:cd03299 162 VRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFKK 220
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-219 |
4.53e-27 |
|
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: 108.29 E-value: 4.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 5 EVRNGYKYYGSKSnpkiVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGAKPGEPGSGVPGSRVG 84
Cdd:cd03214 1 EVENLSVGYGGRT----VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 85 FMPQEIALVEemtvketifyfgrIYGLTDERIREkfkLlkellqlpparqmikqcSGGQQRRLSFACAMIHDPELLILDE 164
Cdd:cd03214 77 YVPQALELLG-------------LAHLADRPFNE---L-----------------SGGERQRVLLARALAQEPPILLLDE 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 24582012 165 PTVGLDPMLREKIWDFLVETTRNSKLAVIITTHYIEEAKQ-ANCIGLMRNGVLLAE 219
Cdd:cd03214 124 PTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARyADRVILLKDGRIVAQ 179
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
4-221 |
1.26e-26 |
|
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: 108.82 E-value: 1.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 4 VEVRNGYKYYGSKSNPKIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGAKPGE-PGSGVPGSR 82
Cdd:cd03258 2 IELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLlSGKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 83 --VGFMPQEIALVEEMTVKETIFYFGRIYGLTDERIREKFKLLKELLQLP-PARQMIKQCSGGQQRRLSFACAMIHDPEL 159
Cdd:cd03258 82 rrIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEdKADAYPAQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24582012 160 LILDEPTVGLDPMLREKIWDFLVETTRNSKLAVIITTHYIEEAKQ-ANCIGLMRNGVLLAEDT 221
Cdd:cd03258 162 LLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGT 224
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
20-197 |
1.52e-26 |
|
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: 108.00 E-value: 1.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 20 KIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGAKPGEPGSgvpgsRVGFMPQeIALVEE---M 96
Cdd:cd03235 12 HPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERK-----RIGYVPQ-RRSIDRdfpI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 97 TVKET--------IFYFGRIYGLTDERIREKFKLLkELLQLppARQMIKQCSGGQQRRLSFACAMIHDPELLILDEPTVG 168
Cdd:cd03235 86 SVRDVvlmglyghKGLFRRLSKADKAKVDEALERV-GLSEL--ADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAG 162
|
170 180
....*....|....*....|....*....
gi 24582012 169 LDPMLREKIWDfLVETTRNSKLAVIITTH 197
Cdd:cd03235 163 VDPKTQEDIYE-LLRELRREGMTILVVTH 190
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-222 |
1.80e-26 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 109.46 E-value: 1.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 4 VEVRN-GYKYYGSKSNPKIVLNQLNMNVMRGSIYGLLGASGCGKTTLLscivgqRRLNG------GEVVVLG----AKPG 72
Cdd:TIGR04521 1 IKLKNvSYIYQPGTPFEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLI------QHLNGllkptsGTVTIDGrditAKKK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 73 EPGSGVPgSRVGFMPQ--EIALVEEmTVKETIFYFGRIYGLTDERIREKFKLLKELLQLPPArqmIK-----QCSGGQQR 145
Cdd:TIGR04521 75 KKLKDLR-KKVGLVFQfpEHQLFEE-TVYKDIAFGPKNLGLSEEEAEERVKEALELVGLDEE---YLerspfELSGGQMR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24582012 146 RLSFACAMIHDPELLILDEPTVGLDPMLREKIWDFLVETTRNSKLAVIITTHYIEE-AKQANCIGLMRNGVLLAEDTP 222
Cdd:TIGR04521 150 RVAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDvAEYADRVIVMHKGKIVLDGTP 227
|
|
| GldA_ABC_ATP |
TIGR03522 |
gliding motility-associated ABC transporter ATP-binding subunit GldA; Members of this protein ... |
3-238 |
1.92e-26 |
|
gliding motility-associated ABC transporter ATP-binding subunit GldA; Members of this protein family are exclusive to the Bacteroidetes phylum (previously Cytophaga-Flavobacteria-Bacteroides). GldA is an ABC transporter ATP-binding protein (pfam00005) linked to a type of rapid surface gliding motility found in certain Bacteroidetes, such as Flavobacterium johnsoniae and Cytophaga hutchinsonii. Knockouts of GldA abolish the gliding phenotype. Gliding motility appears closely linked to chitin utilization in the model species Flavobacterium johnsoniae. Bacteroidetes with members of this protein family appear to have all of the genes associated with gliding motility.
Pssm-ID: 132561 [Multi-domain] Cd Length: 301 Bit Score: 110.25 E-value: 1.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 3 AVEVRNGYKYYGSKSnpkiVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGAKPGEPGSGVPGSr 82
Cdd:TIGR03522 2 SIRVSSLTKLYGTQN----ALDEVSFEAQKGRIVGFLGPNGAGKSTTMKIITGYLPPDSGSVQVCGEDVLQNPKEVQRN- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 83 VGFMPQEIALVEEMTVKETIFYFGRIYGLTDERIREKFKLLKELLQL-PPARQMIKQCSGGQQRRLSFACAMIHDPELLI 161
Cdd:TIGR03522 77 IGYLPEHNPLYLDMYVREYLQFIAGIYGMKGQLLKQRVEEMIELVGLrPEQHKKIGQLSKGYRQRVGLAQALIHDPKVLI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 162 LDEPTVGLDP----MLREKIWDFLVETTrnsklaVIITTHYIEEAkQANC--IGLMRNGVLLAEDTPTNIMIKFGTQSIE 235
Cdd:TIGR03522 157 LDEPTTGLDPnqlvEIRNVIKNIGKDKT------IILSTHIMQEV-EAICdrVIIINKGKIVADKKLDELSAANKKQVIE 229
|
...
gi 24582012 236 DAF 238
Cdd:TIGR03522 230 VEF 232
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
5-226 |
2.42e-26 |
|
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: 107.52 E-value: 2.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 5 EVRNGYKYYGsKSNpkiVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGakpgEPGSGVPGSR-- 82
Cdd:cd03224 2 EVENLNAGYG-KSQ---ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDG----RDITGLPPHEra 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 83 ---VGFMPQEIALVEEMTVKETI---FYFGRIYGLTD--ERIREKFKLLKELLqlppaRQMIKQCSGGQQRRLSFACAMI 154
Cdd:cd03224 74 ragIGYVPEGRRIFPELTVEENLllgAYARRRAKRKArlERVYELFPRLKERR-----KQLAGTLSGGEQQMLAIARALM 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24582012 155 HDPELLILDEPTVGLDPMLREKIWDfLVETTRNSKLAVIITTHYIEEAKQancIG----LMRNGVLLAEDTPTNIM 226
Cdd:cd03224 149 SRPKLLLLDEPSEGLAPKIVEEIFE-AIRELRDEGVTILLVEQNARFALE---IAdrayVLERGRVVLEGTAAELL 220
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-214 |
7.88e-26 |
|
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: 104.39 E-value: 7.88e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 4 VEVRNGYKYYGSKSNPkiVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGAKPGEPGSGVPGSRV 83
Cdd:cd03228 1 IEFKNVSFSYPGRPKP--VLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 84 GFMPQEIALVEeMTVKETIFyfgriygltderirekfkllkellqlpparqmikqcSGGQQRRLSFACAMIHDPELLILD 163
Cdd:cd03228 79 AYVPQDPFLFS-GTIRENIL------------------------------------SGGQRQRIAIARALLRDPPILILD 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 24582012 164 EPTVGLDPMLREKIWDFLVETTRNSklAVIITTHYIEEAKQANCIGLMRNG 214
Cdd:cd03228 122 EATSALDPETEALILEALRALAKGK--TVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
23-201 |
1.09e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 108.25 E-value: 1.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 23 LNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGAKPGEpgsgvpgSRVGFMpQEIALV--------E 94
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFK-------RRKEFA-RRIGVVfgqrsqlwW 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 95 EMTVKETIFYFGRIYGLTDERIREKFKLLKELLQLP-----PARQMikqcSGGQQRRLSFACAMIHDPELLILDEPTVGL 169
Cdd:COG4586 110 DLPAIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGelldtPVRQL----SLGQRMRCELAAALLHRPKILFLDEPTIGL 185
|
170 180 190
....*....|....*....|....*....|....*
gi 24582012 170 DPMLREKIWDFLVETTRNSKLAVIITTHY---IEE 201
Cdd:COG4586 186 DVVSKEAIREFLKEYNRERGTTILLTSHDmddIEA 220
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-226 |
2.41e-25 |
|
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: 111.01 E-value: 2.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 2 AAVEVRN-GYKYYGSksnPKIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVvLGakpGEPGSGVPG 80
Cdd:COG4987 332 PSLELEDvSFRYPGA---GRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSIT-LG---GVDLRDLDE 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 81 ----SRVGFMPQEIALVEeMTVKETIfYFGRIyGLTDERIR---EKFKLLKELLQLPP---------ARQMikqcSGGQQ 144
Cdd:COG4987 405 ddlrRRIAVVPQRPHLFD-TTLRENL-RLARP-DATDEELWaalERVGLGDWLAALPDgldtwlgegGRRL----SGGER 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 145 RRLSFACAMIHDPELLILDEPTVGLDPMLREKIWDFLVETTRNSklAVIITTHYIEEAKQANCIGLMRNGVLLAEDTPTN 224
Cdd:COG4987 478 RRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGR--TVLLITHRLAGLERMDRILVLEDGRIVEQGTHEE 555
|
..
gi 24582012 225 IM 226
Cdd:COG4987 556 LL 557
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-183 |
3.57e-25 |
|
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: 104.68 E-value: 3.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 1 MAAVEVRNGYKYYGsksnPKIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGakpgEPGSGVPG 80
Cdd:COG0410 1 MPMLEVENLHAGYG----GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDG----EDITGLPP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 81 SR-----VGFMPQEIALVEEMTVKETI---FYFGRIYGLTDERIREKFKL---LKELLqlppaRQMIKQCSGGQQRRLSF 149
Cdd:COG0410 73 HRiarlgIGYVPEGRRIFPSLTVEENLllgAYARRDRAEVRADLERVYELfprLKERR-----RQRAGTLSGGEQQMLAI 147
|
170 180 190
....*....|....*....|....*....|....
gi 24582012 150 ACAMIHDPELLILDEPTVGLDPMLREKIWDFLVE 183
Cdd:COG0410 148 GRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRR 181
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-197 |
5.63e-25 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 109.38 E-value: 5.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 4 VEVRNGYKYYGSKsnpkIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVlgakpgepGSGVpgsRV 83
Cdd:COG0488 316 LELEGLSKSYGDK----TLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL--------GETV---KI 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 84 GFMPQE-IALVEEMTVKETIFYFGRiyGLTDERIRekfKLLKELLqLPPARQM--IKQCSGGQQRRLSFACAMIHDPELL 160
Cdd:COG0488 381 GYFDQHqEELDPDKTVLDELRDGAP--GGTEQEVR---GYLGRFL-FSGDDAFkpVGVLSGGEKARLALAKLLLSPPNVL 454
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 24582012 161 ILDEPTVGLDPMLREKIWDFLVE---TtrnsklaVIITTH 197
Cdd:COG0488 455 LLDEPTNHLDIETLEALEEALDDfpgT-------VLLVSH 487
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
3-225 |
6.56e-25 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 106.71 E-value: 6.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 3 AVEVRNGYKYYGSKSnpkiVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVG-------QRRLNGGEVVVLGAKpgepg 75
Cdd:PRK10851 2 SIEIANIKKSFGRTQ----VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGlehqtsgHIRFHGTDVSRLHAR----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 76 sgvpGSRVGFMPQEIALVEEMTVKETIfyfgrIYGLT----DER-----IREKFKLLKELLQLPP-ARQMIKQCSGGQQR 145
Cdd:PRK10851 73 ----DRKVGFVFQHYALFRHMTVFDNI-----AFGLTvlprRERpnaaaIKAKVTQLLEMVQLAHlADRYPAQLSGGQKQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 146 RLSFACAMIHDPELLILDEPTVGLDPMLREKIWDFLVETTRNSKLAVIITTHYIEEAKQ-ANCIGLMRNGVLLAEDTPTN 224
Cdd:PRK10851 144 RVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEvADRVVVMSQGNIEQAGTPDQ 223
|
.
gi 24582012 225 I 225
Cdd:PRK10851 224 V 224
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
4-225 |
8.80e-25 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 103.53 E-value: 8.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 4 VEVRNGYKYYGsksNPKIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLG---AKPGEPGSGVPG 80
Cdd:TIGR02315 2 LEVENLSKVYP---NGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGtdiTKLRGKKLRKLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 81 SRVGFMPQEIALVEEMTVKETIFYfGR---------IYGL-TDERIREKFKLLKELLQLPPARQMIKQCSGGQQRRLSFA 150
Cdd:TIGR02315 79 RRIGMIFQHYNLIERLTVLENVLH-GRlgykptwrsLLGRfSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24582012 151 CAMIHDPELLILDEPTVGLDPMLREKIWDFLVETTRNSKLAVIITTHYIEEAKQ-ANCIGLMRNGVLLAEDTPTNI 225
Cdd:TIGR02315 158 RALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKyADRIVGLKAGEIVFDGAPSEL 233
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
3-248 |
1.09e-24 |
|
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: 110.87 E-value: 1.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 3 AVEVRNGYKYYGSKSNPKIvlNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVlGAKPGEPGSGVPGSR 82
Cdd:TIGR01257 928 GVCVKNLVKIFEPSGRPAV--DRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLV-GGKDIETNLDAVRQS 1004
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 83 VGFMPQEIALVEEMTVKETIFYFGRIYGLTDERIREKFKLLKELLQLPPAR-QMIKQCSGGQQRRLSFACAMIHDPELLI 161
Cdd:TIGR01257 1005 LGMCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRnEEAQDLSGGMQRKLSVAIAFVGDAKVVV 1084
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 162 LDEPTVGLDPMLREKIWDFLVETtrNSKLAVIITTHYIEEAK-QANCIGLMRNGVLLAEDTPTNIMIKFGT----QSIED 236
Cdd:TIGR01257 1085 LDEPTSGVDPYSRRSIWDLLLKY--RSGRTIIMSTHHMDEADlLGDRIAIISQGRLYCSGTPLFLKNCFGTgfylTLVRK 1162
|
250
....*....|..
gi 24582012 237 AFLILSQRQGNE 248
Cdd:TIGR01257 1163 MKNIQSQRGGCE 1174
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
20-197 |
1.71e-24 |
|
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: 101.47 E-value: 1.71e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 20 KIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNG--GEVVVLGaKPGEPGSgvPGSRVGFMPQEIALVEEMT 97
Cdd:cd03213 22 KQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLING-RPLDKRS--FRKIIGYVPQDDILHPTLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 98 VKETIFYFGRIYGLtderirekfkllkellqlpparqmikqcSGGQQRRLSFACAMIHDPELLILDEPTVGLDP------ 171
Cdd:cd03213 99 VRETLMFAAKLRGL----------------------------SGGERKRVSIALELVSNPSLLFLDEPTSGLDSssalqv 150
|
170 180
....*....|....*....|....*...
gi 24582012 172 --MLREkiwdfLVETTRNsklaVIITTH 197
Cdd:cd03213 151 msLLRR-----LADTGRT----IICSIH 169
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-216 |
2.51e-24 |
|
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: 101.45 E-value: 2.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 4 VEVRNGYKYYGSKSnpkiVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGAKPGEPGSGVPG--S 81
Cdd:cd03262 1 IEIKNLHKSFGDFH----VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINElrQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 82 RVGFMPQEIALVEEMTVKETIfyfgrIYGLT-------DERIREKFKLLKELLQLPPARQMIKQCSGGQQRRLSFACAMI 154
Cdd:cd03262 77 KVGMVFQQFNLFPHLTVLENI-----TLAPIkvkgmskAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24582012 155 HDPELLILDEPTVGLDPMLREKIWDFLVETTRnSKLAVIITTHYIEEAKQ-ANCIGLMRNGVL 216
Cdd:cd03262 152 MNPKVMLFDEPTSALDPELVGEVLDVMKDLAE-EGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
11-251 |
2.52e-24 |
|
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: 109.72 E-value: 2.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 11 KYYGSKSNPKIvlNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGAKPGEPGSGVPGSrVGFMPQEI 90
Cdd:TIGR01257 1945 KVYSGTSSPAV--DRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQN-MGYCPQFD 2021
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 91 ALVEEMTVKETIFYFGRIYGLTDERIREKFKLLKELLQLPP-ARQMIKQCSGGQQRRLSFACAMIHDPELLILDEPTVGL 169
Cdd:TIGR01257 2022 AIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLyADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGM 2101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 170 DPMLREKIWDFLVETTRNSKlAVIITTHYIEEAkQANC--IGLMRNGVLLAEDTPTNIMIKFGtqsieDAFLILSQRQGN 247
Cdd:TIGR01257 2102 DPQARRMLWNTIVSIIREGR-AVVLTSHSMEEC-EALCtrLAIMVKGAFQCLGTIQHLKSKFG-----DGYIVTMKIKSP 2174
|
....
gi 24582012 248 EDEL 251
Cdd:TIGR01257 2175 KDDL 2178
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
4-226 |
7.37e-24 |
|
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: 101.57 E-value: 7.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 4 VEVRNGYKYYGS--------------------KSNPKIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGE 63
Cdd:cd03294 1 IKIKGLYKIFGKnpqkafkllakgkskeeilkKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 64 VVVlgakPGEPGSGVPGS--------RVGFMPQEIALVEEMTVKETIFYFGRIYGLtDERIREKFKLlkELLQL----PP 131
Cdd:cd03294 81 VLI----DGQDIAAMSRKelrelrrkKISMVFQSFALLPHRTVLENVAFGLEVQGV-PRAEREERAA--EALELvgleGW 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 132 ARQMIKQCSGGQQRRLSFACAMIHDPELLILDEPTVGLDPMLREKIWDFLVETTRNSKLAVIITTHYIEEA-KQANCIGL 210
Cdd:cd03294 154 EHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEAlRLGDRIAI 233
|
250
....*....|....*.
gi 24582012 211 MRNGVLLAEDTPTNIM 226
Cdd:cd03294 234 MKDGRLVQVGTPEEIL 249
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-197 |
1.08e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 105.53 E-value: 1.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 6 VRNGYKYYGSKsnpkIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLgakpgepgsgvPGSRVGF 85
Cdd:COG0488 1 LENLSKSFGGR----PLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP-----------KGLRIGY 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 86 MPQEIALVEEMTVKETIFY-FGRIYGLTDE-------------------RIREKF-------------KLLKEL-LQLPP 131
Cdd:COG0488 66 LPQEPPLDDDLTVLDTVLDgDAELRALEAEleeleaklaepdedlerlaELQEEFealggweaearaeEILSGLgFPEED 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24582012 132 ARQMIKQCSGGQQRRLSFACAMIHDPELLILDEPTVGLDpmLREKIW--DFLvettRNSKLAVIITTH 197
Cdd:COG0488 146 LDRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLD--LESIEWleEFL----KNYPGTVLVVSH 207
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
5-226 |
1.21e-23 |
|
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: 100.20 E-value: 1.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 5 EVRNGYKYYGSKSnpkiVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGakpgEPGSGVPgsrvg 84
Cdd:cd03219 2 EVRGLTKRFGGLV----ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDG----EDITGLP----- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 85 fmPQEIA------------LVEEMTVKETI----------FYFGRIYGLTDERIREK-FKLLkELLQLPP-ARQMIKQCS 140
Cdd:cd03219 69 --PHEIArlgigrtfqiprLFPELTVLENVmvaaqartgsGLLLARARREEREARERaEELL-ERVGLADlADRPAGELS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 141 GGQQRRLSFACAMIHDPELLILDEPTVGLDPMLREKIWDfLVETTRNSKLAVIITTHYIEEAKQ-ANCIGLMRNGVLLAE 219
Cdd:cd03219 146 YGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAE-LIRELRERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAE 224
|
....*..
gi 24582012 220 DTPTNIM 226
Cdd:cd03219 225 GTPDEVR 231
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
22-226 |
2.08e-23 |
|
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: 104.84 E-value: 2.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 22 VLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGAKPGEPGSGVPGSRVGFMPQEIALVEeMTVKET 101
Cdd:COG4988 352 ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFA-GTIREN 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 102 IfyfgRIY--GLTDERIR---EKFKLLKELLQLPP---------ARQMikqcSGGQQRRLSFACAMIHDPELLILDEPTV 167
Cdd:COG4988 431 L----RLGrpDASDEELEaalEAAGLDEFVAALPDgldtplgegGRGL----SGGQAQRLALARALLRDAPLLLLDEPTA 502
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 24582012 168 GLDPMLREKIWDFLVETTRNSklAVIITTHYIEEAKQANCIGLMRNGVLLAEDTPTNIM 226
Cdd:COG4988 503 HLDAETEAEILQALRRLAKGR--TVILITHRLALLAQADRILVLDDGRIVEQGTHEELL 559
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-225 |
2.10e-23 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 99.72 E-value: 2.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 1 MAAVEVRNGYKYYGSKsnpkIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLG-----------A 69
Cdd:COG1137 1 MMTLEAENLVKSYGKR----TVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGedithlpmhkrA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 70 KPGepgsgvpgsrVGFMPQEIALVEEMTVKETIFYFGRIYGLTDERIREKF-KLLKELLQLPPARQMIKQCSGGQQRRLS 148
Cdd:COG1137 77 RLG----------IGYLPQEASIFRKLTVEDNILAVLELRKLSKKEREERLeELLEEFGITHLRKSKAYSLSGGERRRVE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 149 FACAMIHDPELLILDEPTVGLDPMLREKIWDfLVETTRNSKLAVIITTH------------YIeeakqanciglMRNGVL 216
Cdd:COG1137 147 IARALATNPKFILLDEPFAGVDPIAVADIQK-IIRHLKERGIGVLITDHnvretlgicdraYI-----------ISEGKV 214
|
....*....
gi 24582012 217 LAEDTPTNI 225
Cdd:COG1137 215 LAEGTPEEI 223
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
22-202 |
3.32e-23 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 97.49 E-value: 3.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 22 VLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGAKPGEPGSGVPGSRvgfmpQEIALVEE------ 95
Cdd:TIGR01166 7 VLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDYSRKGLLERR-----QRVGLVFQdpddql 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 96 --MTVKETIFYFGRIYGLTDERIREKFKLLKELLQLPP-ARQMIKQCSGGQQRRLSFACAMIHDPELLILDEPTVGLDPM 172
Cdd:TIGR01166 82 faADVDQDVAFGPLNLGLSEAEVERRVREALTAVGASGlRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPA 161
|
170 180 190
....*....|....*....|....*....|
gi 24582012 173 LREKIWDfLVETTRNSKLAVIITTHYIEEA 202
Cdd:TIGR01166 162 GREQMLA-ILRRLRAEGMTVVISTHDVDLA 190
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-219 |
4.27e-23 |
|
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: 96.34 E-value: 4.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 4 VEVRNGYKYYGSKsnpkIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGaKPGEPGSgvpgsrv 83
Cdd:cd03216 1 LELRGITKRFGGV----KALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG-KEVSFAS------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 84 gfmPQEialveemtvketifyfgriygltderirekfkllkellqlppARQ----MIKQCSGGQQRRLSFACAMIHDPEL 159
Cdd:cd03216 69 ---PRD------------------------------------------ARRagiaMVYQLSVGERQMVEIARALARNARL 103
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24582012 160 LILDEPTVGLDPMLREKIWDFlVETTRNSKLAVIITTHYIEEAKQ-ANCIGLMRNGVLLAE 219
Cdd:cd03216 104 LILDEPTAALTPAEVERLFKV-IRRLRAQGVAVIFISHRLDEVFEiADRVTVLRDGRVVGT 163
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
4-220 |
4.82e-23 |
|
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: 97.99 E-value: 4.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 4 VEVRNGYKYYGSKSNP------------------KIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVV 65
Cdd:cd03220 1 IELENVSKSYPTYKGGssslkklgilgrkgevgeFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 66 VLGaKPgepgSGVPGSRVGFMPqeialveEMTVKETIFYFGRIYGLTDERIREKFKLLKELLQLPPARQM-IKQCSGGQQ 144
Cdd:cd03220 81 VRG-RV----SSLLGLGGGFNP-------ELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLpVKTYSSGMK 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24582012 145 RRLSFACAMIHDPELLILDEPT-VGlDPMLREKIWDFLVETTRNSKlAVIITTHYIEEAKQ-ANCIGLMRNGVLLAED 220
Cdd:cd03220 149 ARLAFAIATALEPDILLIDEVLaVG-DAAFQEKCQRRLRELLKQGK-TVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
4-225 |
8.27e-23 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 100.79 E-value: 8.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 4 VEVRNGYKYYGSKSnpkiVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVlgakPGEPGSGVPGSR- 82
Cdd:PRK09452 15 VELRGISKSFDGKE----VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIML----DGQDITHVPAENr 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 83 -VGFMPQEIALVEEMTVKETIFYFGRIYGLTDERIREKFKLLKELLQLPP-ARQMIKQCSGGQQRRLSFACAMIHDPELL 160
Cdd:PRK09452 87 hVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEfAQRKPHQLSGGQQQRVAIARAVVNKPKVL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24582012 161 ILDEPTVGLDPMLREKIWDFLVETTRNSKLAVIITTHYIEEA-KQANCIGLMRNGVLLAEDTPTNI 225
Cdd:PRK09452 167 LLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEAlTMSDRIVVMRDGRIEQDGTPREI 232
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-228 |
2.51e-22 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 100.86 E-value: 2.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 1 MAAVEVRNGYKYYGsksnPKIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGaKPGEPGSgvPG 80
Cdd:COG1129 2 EPLLEMRGISKSFG----GVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDG-EPVRFRS--PR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 81 ----SRVGFMPQEIALVEEMTVKETIFyFGR---IYGLTDER-IREKF-KLLKEL-LQLPPaRQMIKQCSGGQQRRLSFA 150
Cdd:COG1129 75 daqaAGIAIIHQELNLVPNLSVAENIF-LGReprRGGLIDWRaMRRRArELLARLgLDIDP-DTPVGDLSVAQQQLVEIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 151 CAMIHDPELLILDEPTVGLDPMLREKIWDfLVETTRNSKLAVIITTHYIEEAKQ-ANCIGLMRNG----VLLAEDTPTNI 225
Cdd:COG1129 153 RALSRDARVLILDEPTASLTEREVERLFR-IIRRLKAQGVAIIYISHRLDEVFEiADRVTVLRDGrlvgTGPVAELTEDE 231
|
...
gi 24582012 226 MIK 228
Cdd:COG1129 232 LVR 234
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
10-214 |
2.79e-22 |
|
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: 95.40 E-value: 2.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 10 YKYYGSKSnpkiVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGAKPGepgSGVPGSRVGFMPQE 89
Cdd:cd03226 7 FSYKKGTE----ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIK---AKERRKSIGYVMQD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 90 I--ALVEEmTVKETIFYFGRIYGLTDERIRE---KFKLLKELLQLPPArqmikqCSGGQQRRLSFACAMIHDPELLILDE 164
Cdd:cd03226 80 VdyQLFTD-SVREELLLGLKELDAGNEQAETvlkDLDLYALKERHPLS------LSGGQKQRLAIAAALLSGKDLLIFDE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 24582012 165 PTVGLDPMLREKIWDfLVETTRNSKLAVIITTHYIE-EAKQANCIGLMRNG 214
Cdd:cd03226 153 PTSGLDYKNMERVGE-LIRELAAQGKAVIVITHDYEfLAKVCDRVLLLANG 202
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-226 |
3.79e-22 |
|
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: 96.26 E-value: 3.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 1 MAAVEVRNGYKYYGSksnpkIV-LNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGakpgEPGSGVP 79
Cdd:COG0411 2 DPLLEVRGLTKRFGG-----LVaVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDG----RDITGLP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 80 GSRV---G----FmpQEIALVEEMTVKE----------------TIFYFGRiYGLTDERIREK-FKLLkELLQLPP-ARQ 134
Cdd:COG0411 73 PHRIarlGiartF--QNPRLFPELTVLEnvlvaaharlgrgllaALLRLPR-ARREEREARERaEELL-ERVGLADrADE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 135 MIKQCSGGQQRRLSFACAMIHDPELLILDEPTVGLDPMLREKIWDFLVETTRNSKLAVIITTHYIEEakqancigLMR-- 212
Cdd:COG0411 149 PAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDL--------VMGla 220
|
250 260
....*....|....*....|.
gi 24582012 213 -------NGVLLAEDTPTNIM 226
Cdd:COG0411 221 drivvldFGRVIAEGTPAEVR 241
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-197 |
7.13e-22 |
|
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: 97.05 E-value: 7.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 4 VEVRNGYKYYGSKSNPKIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVG---QRRLNGGEVVVLG----AKPGEPGS 76
Cdd:COG0444 2 LEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGllpPPGITSGEILFDGedllKLSEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 77 GVPGSRVGFMPQE--IAL--VeeMTVKETIFYFGRIYGLTDERirEKFKLLKELLQ---LPPARQMIK----QCSGGQQR 145
Cdd:COG0444 82 KIRGREIQMIFQDpmTSLnpV--MTVGDQIAEPLRIHGGLSKA--EARERAIELLErvgLPDPERRLDryphELSGGMRQ 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 24582012 146 RLSFACAMIHDPELLILDEPTVGLDPMLREKIWDFLVETTRNSKLAVIITTH 197
Cdd:COG0444 158 RVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITH 209
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
35-244 |
9.35e-22 |
|
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: 97.49 E-value: 9.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 35 IYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGAKPGEPGSGVPGS----RVGFMPQEIALVEEMTVKETIfyfgrIYG 110
Cdd:TIGR02142 25 VTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFLPpekrRIGYVFQEARLFPHLSVRGNL-----RYG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 111 LTDERIREK---FKLLKELLQLPP-ARQMIKQCSGGQQRRLSFACAMIHDPELLILDEPTVGLDPMLREKIWDFLVETTR 186
Cdd:TIGR02142 100 MKRARPSERrisFERVIELLGIGHlLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLERLHA 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24582012 187 NSKLAVIITTHYIEE-AKQANCIGLMRNGVLLAEDTPTNIMIK--FGTQSIEDAFLILSQR 244
Cdd:TIGR02142 180 EFGIPILYVSHSLQEvLRLADRVVVLEDGRVAAAGPIAEVWASpdLPWLAREDQGSLIEGV 240
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
322-702 |
1.17e-21 |
|
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter family pfam01061.
Pssm-ID: 463674 [Multi-domain] Cd Length: 345 Bit Score: 97.08 E-value: 1.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 322 PSGIIFMLLFPIIQLTCFYLAIG---KTPTNLEIGVYSGEVENYGEcfdeNLVTVYKDSDnesclfnklscryirvlgdD 398
Cdd:pfam12698 1 KSFLIITLLLPILLILLLGLIFSnavNDPEELPVAVVDEDNSSLSR----QLVRALEASP-------------------T 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 399 VATRKYYASEADALNDAKRATTVGYLHFAQNFSDSILSVMEdgihssdgavdhAELSIHIDMTDQQVAYFMQRKLrDKFS 478
Cdd:pfam12698 58 VNLVQYVDSEEEAKEALKNGKIDGLLVIPKGFSKDLLKGES------------ATVTVYINSSNLLVSKLILNAL-QSLL 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 479 TFMRSVVKDCNVSTAIVDLPVQFQEPIFGSTDIEFQQYCAPGVVMTMVFFLAtLMTAAVFISERMDGIWDRTLLAGVSAT 558
Cdd:pfam12698 125 QQLNASALVLLLEALSTSAPIPVESTPLFNPQSGYAYYLVGLILMIIILIGA-AIIAVSIVEEKESRIKERLLVSGVSPL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 559 EMLWAHLLTQLIIMALQsfeVIMYIGLVFDT-YNNGDTTTLIGLLTLTAFCGMLFGLFISVFCKSHTEANFVATGAFYPM 637
Cdd:pfam12698 204 QYWLGKILGDFLVGLLQ---LLIILLLLFGIgIPFGNLGLLLLLFLLYGLAYIALGYLLGSLFKNSEDAQSIIGIVILLL 280
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24582012 638 IILCGLLWPLESMPQFLQDLVMVLPFTIPSISARNVIEKGWSIThekVYNGFLVMAGWTIIFFVL 702
Cdd:pfam12698 281 SGFFGGLFPLEDPPSFLQWIFSIIPFFSPIDGLLRLIYGDSLWE---IAPSLIILLLFAVVLLLL 342
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
13-216 |
1.58e-21 |
|
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: 92.28 E-value: 1.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 13 YGSKSNPkiVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGAKPGEPGSGVPGSRVGFMPQEIAL 92
Cdd:cd03246 10 YPGAEPP--VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLPQDDEL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 93 VEEmTVKETIFyfgriygltderirekfkllkellqlpparqmikqcSGGQQRRLSFACAMIHDPELLILDEPTVGLDPM 172
Cdd:cd03246 88 FSG-SIAENIL------------------------------------SGGQRQRLGLARALYGNPRILVLDEPNSHLDVE 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 24582012 173 LREKIWDfLVETTRNSKLAVIITTHYIEEAKQANCIGLMRNGVL 216
Cdd:cd03246 131 GERALNQ-AIAALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
13-219 |
1.73e-21 |
|
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: 92.38 E-value: 1.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 13 YGSKSNPKIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGAKPGEPGSGVpGSRVGFMPQeial 92
Cdd:cd03247 8 FSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKAL-SSLISVLNQ---- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 93 veemtvketifyfgRIYgLTDERIREKFKllkellqlpparqmiKQCSGGQQRRLSFACAMIHDPELLILDEPTVGLDPM 172
Cdd:cd03247 83 --------------RPY-LFDTTLRNNLG---------------RRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPI 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 24582012 173 LREKIWDFLVETTRNSklAVIITTHYIEEAKQANCIGLMRNGVLLAE 219
Cdd:cd03247 133 TERQLLSLIFEVLKDK--TLIWITHHLTGIEHMDKILFLENGKIIMQ 177
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
4-227 |
2.89e-21 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 93.62 E-value: 2.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 4 VEVRNGYKYYGsksnPKIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGAKPGEPGSGVPGSR- 82
Cdd:PRK09493 2 IEFKNVSKHFG----PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIRq 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 83 -VGFMPQEIALVEEMTVKETIFyFG--RIYGLTDERIRekfKLLKELLQ----LPPARQMIKQCSGGQQRRLSFACAMIH 155
Cdd:PRK09493 78 eAGMVFQQFYLFPHLTALENVM-FGplRVRGASKEEAE---KQARELLAkvglAERAHHYPSELSGGQQQRVAIARALAV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24582012 156 DPELLILDEPTVGLDPMLREKIWDfLVETTRNSKLAVIITTHYIEEAKQ-ANCIGLMRNGvLLAEDTPTNIMI 227
Cdd:PRK09493 154 KPKLMLFDEPTSALDPELRHEVLK-VMQDLAEEGMTMVIVTHEIGFAEKvASRLIFIDKG-RIAEDGDPQVLI 224
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
4-214 |
4.14e-21 |
|
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: 91.76 E-value: 4.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 4 VEVRNGYKYYGSKSN-PKIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVlgakpgepgsgvpGSR 82
Cdd:cd03250 1 ISVEDASFTWDSGEQeTSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSV-------------PGS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 83 VGFMPQEiALVEEMTVKETIFyFGRIYgltDErirEKFK-------LLKELLQLPPARQ-MIKQ----CSGGQQRRLSFA 150
Cdd:cd03250 68 IAYVSQE-PWIQNGTIRENIL-FGKPF---DE---ERYEkvikacaLEPDLEILPDGDLtEIGEkginLSGGQKQRISLA 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24582012 151 CAMIHDPELLILDEPTVGLDPMLREKIWDFLV-ETTRNSKlAVIITTHYIEEAKQANCIGLMRNG 214
Cdd:cd03250 140 RAVYSDADIYLLDDPLSAVDAHVGRHIFENCIlGLLLNNK-TRILVTHQLQLLPHADQIVVLDNG 203
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
23-202 |
4.26e-21 |
|
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: 92.53 E-value: 4.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 23 LNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGAKPGEPGsgvPGSRVGFmpQEIALVEEMTVKETI 102
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPG---PDRMVVF--QNYSLLPWLTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 103 fYFGRIYGLTDERIREKFKLLKELLQL----PPARQMIKQCSGGQQRRLSFACAMIHDPELLILDEPTVGLDPMLREKIW 178
Cdd:TIGR01184 76 -ALAVDRVLPDLSKSERRAIVEEHIALvgltEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQ 154
|
170 180
....*....|....*....|....
gi 24582012 179 DFLVETTRNSKLAVIITTHYIEEA 202
Cdd:TIGR01184 155 EELMQIWEEHRVTVLMVTHDVDEA 178
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
4-225 |
5.95e-21 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 95.29 E-value: 5.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 4 VEVRNGYKYYGSKSnpkiVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVlgakPGEPGSGVPGSR- 82
Cdd:PRK11607 20 LEIRNLTKSFDGQH----AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIML----DGVDLSHVPPYQr 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 83 -VGFMPQEIALVEEMTVKETIfyfgrIYGLTDERI--REKFKLLKELLQLPPARQMIK----QCSGGQQRRLSFACAMIH 155
Cdd:PRK11607 92 pINMMFQSYALFPHMTVEQNI-----AFGLKQDKLpkAEIASRVNEMLGLVHMQEFAKrkphQLSGGQRQRVALARSLAK 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24582012 156 DPELLILDEPTVGLDPMLREKIWDFLVETTRNSKLAVIITTHYIEEA-KQANCIGLMRNGVLLAEDTPTNI 225
Cdd:PRK11607 167 RPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAmTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
10-225 |
6.97e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 93.36 E-value: 6.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 10 YKYYGSKSNPKIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLG----AKPGEPGSGVPGSRVGF 85
Cdd:PRK13641 10 YIYSPGTPMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitPETGNKNLKKLRKKVSL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 86 MPQ--EIALVEEmTVKETIFYFGRIYGLTDERIREKfkLLKELLQLPPARQMIKQC----SGGQQRRLSFACAMIHDPEL 159
Cdd:PRK13641 90 VFQfpEAQLFEN-TVLKDVEFGPKNFGFSEDEAKEK--ALKWLKKVGLSEDLISKSpfelSGGQMRRVAIAGVMAYEPEI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24582012 160 LILDEPTVGLDPMLREKIWDFLVETTRNSKlAVIITTHYIEE-AKQANCIGLMRNGVLLAEDTPTNI 225
Cdd:PRK13641 167 LCLDEPAAGLDPEGRKEMMQLFKDYQKAGH-TVILVTHNMDDvAEYADDVLVLEHGKLIKHASPKEI 232
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
4-221 |
1.66e-20 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 93.22 E-value: 1.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 4 VEVRNGYKYYGSKSNPKIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLgakpGEPGSGVPGS-- 81
Cdd:COG1135 2 IELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVD----GVDLTALSERel 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 82 -----RVGFMPQEIALVEEMTVKETIFYFGRIYGLTDERIREKfklLKELLQL---------PPArqmikQCSGGQQRRL 147
Cdd:COG1135 78 raarrKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKR---VAELLELvglsdkadaYPS-----QLSGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 148 SFACAMIHDPELLILDEPTVGLDPmlrekiwdflvETTR---------NSKL--AVIITTHYIEEAKQ-ANCIGLMRNGV 215
Cdd:COG1135 150 GIARALANNPKVLLCDEATSALDP-----------ETTRsildllkdiNRELglTIVLITHEMDVVRRiCDRVAVLENGR 218
|
....*.
gi 24582012 216 LLAEDT 221
Cdd:COG1135 219 IVEQGP 224
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
3-230 |
1.68e-20 |
|
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: 96.44 E-value: 1.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 3 AVEVRNGYKYYGSKSNPkiVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVlgakpgepgSGVP--- 79
Cdd:COG2274 473 DIELENVSFRYPGDSPP--VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILI---------DGIDlrq 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 80 ------GSRVGFMPQEIALVEeMTVKETIFYFGRiyGLTDERIREKFK---LLKELLQLPPARQMI-----KQCSGGQQR 145
Cdd:COG2274 542 idpaslRRQIGVVLQDVFLFS-GTIRENITLGDP--DATDEEIIEAARlagLHDFIEALPMGYDTVvgeggSNLSGGQRQ 618
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 146 RLSFACAMIHDPELLILDEPTVGLDPMLREKIWDFLVETTRNSklAVIITTHYIEEAKQANCIGLMRNGVLLAEDTPTNI 225
Cdd:COG2274 619 RLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGR--TVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEEL 696
|
....*
gi 24582012 226 MIKFG 230
Cdd:COG2274 697 LARKG 701
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
4-197 |
2.52e-20 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 90.16 E-value: 2.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 4 VEVRNGYKYYGsksNPKIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLG-AKPGEPGSGVPGSR 82
Cdd:cd03292 1 IEFINVTKTYP---NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGqDVSDLRGRAIPYLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 83 --VGFMPQEIALVEEMTVKETIFYFGRIYGLTDERIREKFKLLKELLQLP-PARQMIKQCSGGQQRRLSFACAMIHDPEL 159
Cdd:cd03292 78 rkIGVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLShKHRALPAELSGGEQQRVAIARAIVNSPTI 157
|
170 180 190
....*....|....*....|....*....|....*...
gi 24582012 160 LILDEPTVGLDPMLREKIWDfLVETTRNSKLAVIITTH 197
Cdd:cd03292 158 LIADEPTGNLDPDTTWEIMN-LLKKINKAGTTVVVATH 194
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-222 |
4.39e-20 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 90.14 E-value: 4.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 1 MA-AVEVRNGYKYY------------------GSKSNPKIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNG 61
Cdd:COG1134 1 MSsMIEVENVSKSYrlyhepsrslkelllrrrRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 62 GEVVVLG--AKPGEPGsgvpgsrVGFMPqeialveEMTVKETIFYFGRIYGLTDERIREKFKL------LKELLQLPpar 133
Cdd:COG1134 81 GRVEVNGrvSALLELG-------AGFHP-------ELTGRENIYLNGRLLGLSRKEIDEKFDEivefaeLGDFIDQP--- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 134 qmIKQCSGGQQRRLSFACAMIHDPELLILDEPT-VGlDPMLREKIWDFLVETTRNSKlAVIITTHYIEEAKQ-ANCIGLM 211
Cdd:COG1134 144 --VKTYSSGMRARLAFAVATAVDPDILLVDEVLaVG-DAAFQKKCLARIRELRESGR-TVIFVSHSMGAVRRlCDRAIWL 219
|
250
....*....|.
gi 24582012 212 RNGVLLAEDTP 222
Cdd:COG1134 220 EKGRLVMDGDP 230
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
22-211 |
4.43e-20 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 88.44 E-value: 4.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 22 VLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVlgakpgepgsgVPGSRVGFMPQEIALVEEM--TVK 99
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRR-----------AGGARVAYVPQRSEVPDSLplTVR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 100 E--TIFYFGRIyGLTDERIREKFKLLKELLQ------LppARQMIKQCSGGQQRRLSFACAMIHDPELLILDEPTVGLDP 171
Cdd:NF040873 76 DlvAMGRWARR-GLWRRLTRDDRAAVDDALErvgladL--AGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 24582012 172 MLREKIWDFLVETTRNsKLAVIITTHYIEEAKQANCIGLM 211
Cdd:NF040873 153 ESRERIIALLAEEHAR-GATVVVVTHDLELVRRADPCVLL 191
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-226 |
5.32e-20 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 90.57 E-value: 5.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 4 VEVRN-GYKYYGSKsnpKIVLNQLNMNVMRGSIYGLLGASGCGKTTLlscivgQRRLNG------GEVVVLGAKPGEPgs 76
Cdd:TIGR04520 1 IEVENvSFSYPESE---KPALKNVSLSIEKGEFVAIIGHNGSGKSTL------AKLLNGlllptsGKVTVDGLDTLDE-- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 77 gvpgSRVGFMPQEIALVEE--------MTVKETI-FyfgriyGL------TDE---RIREKFKL--LKELLQLPPARqmi 136
Cdd:TIGR04520 70 ----ENLWEIRKKVGMVFQnpdnqfvgATVEDDVaF------GLenlgvpREEmrkRVDEALKLvgMEDFRDREPHL--- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 137 kqCSGGQQRRLSFACAMIHDPELLILDEPTVGLDPMLREKIWDFLVETTRNSKLAVIITTHYIEEAKQANCIGLMRNGVL 216
Cdd:TIGR04520 137 --LSGGQKQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVLADRVIVMNKGKI 214
|
250
....*....|
gi 24582012 217 LAEDTPTNIM 226
Cdd:TIGR04520 215 VAEGTPREIF 224
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
20-222 |
1.60e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 89.34 E-value: 1.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 20 KIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGAKPGEPGSGVPGSR--VGFMPQ--EIALVEE 95
Cdd:PRK13637 20 KKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSDIRkkVGLVFQypEYQLFEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 96 mTVKETIFYFGRIYGLTDERIREKFKLLKELLQLPpaRQMIK-----QCSGGQQRRLSFACAMIHDPELLILDEPTVGLD 170
Cdd:PRK13637 100 -TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLD--YEDYKdkspfELSGGQKRRVAIAGVVAMEPKILILDEPTAGLD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 24582012 171 PMLREKIWDFLVETTRNSKLAVIITTHYIEE-AKQANCIGLMRNGVLLAEDTP 222
Cdd:PRK13637 177 PKGRDEILNKIKELHKEYNMTIILVSHSMEDvAKLADRIIVMNKGKCELQGTP 229
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
22-197 |
1.67e-19 |
|
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: 92.35 E-value: 1.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 22 VLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGAKPGEPGSGVPGSRVGFMPQEIALVEEmTVKET 101
Cdd:TIGR02857 337 ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAG-TIAEN 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 102 IfYFGRIYGlTDERIREKFKL--LKELLQ-LPparQMIKQ--------CSGGQQRRLSFACAMIHDPELLILDEPTVGLD 170
Cdd:TIGR02857 416 I-RLARPDA-SDAEIREALERagLDEFVAaLP---QGLDTpigeggagLSGGQAQRLALARAFLRDAPLLLLDEPTAHLD 490
|
170 180
....*....|....*....|....*..
gi 24582012 171 PMLREKIWDFLVETTRNSklAVIITTH 197
Cdd:TIGR02857 491 AETEAEVLEALRALAQGR--TVLLVTH 515
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
20-225 |
1.98e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 89.31 E-value: 1.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 20 KIVLNQLNMNVMRGSIYGLLGASGCGKTTLLscivgqRRLNG------GeVVVLGAKPGEPGSG-----VPGSRVGFMPQ 88
Cdd:PRK13634 20 RRALYDVNVSIPSGSYVAIIGHTGSGKSTLL------QHLNGllqptsG-TVTIGERVITAGKKnkklkPLRKKVGIVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 89 --EIALVEEmTVKETIfYFGRI-YGLTDERIREKFKLLKELLQLPPA--RQMIKQCSGGQQRRLSFACAMIHDPELLILD 163
Cdd:PRK13634 93 fpEHQLFEE-TVEKDI-CFGPMnFGVSEEDAKQKAREMIELVGLPEEllARSPFELSGGQMRRVAIAGVLAMEPEVLVLD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24582012 164 EPTVGLDPMLREKIWDFLVETTRNSKLAVIITTHYIEEAKQ-ANCIGLMRNGVLLAEDTPTNI 225
Cdd:PRK13634 171 EPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREI 233
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
5-221 |
2.61e-19 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 87.58 E-value: 2.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 5 EVRNGYKYYGSKSnpkiVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVlgakPGEPGSGVPGSR-- 82
Cdd:TIGR03410 2 EVSNLNVYYGQSH----ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRL----DGEDITKLPPHEra 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 83 ---VGFMPQEIALVEEMTVKETIfyfgrIYGLTDERIREKfKLLKELLQLPPA-RQMIKQ----CSGGQQRRLSFACAMI 154
Cdd:TIGR03410 74 ragIAYVPQGREIFPRLTVEENL-----LTGLAALPRRSR-KIPDEIYELFPVlKEMLGRrggdLSGGQQQQLAIARALV 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24582012 155 HDPELLILDEPTVGLDPMLREKIWDFLVETTRNSKLAVIITTHYIEEAKQ-ANCIGLMRNGVLLAEDT 221
Cdd:TIGR03410 148 TRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARElADRYYVMERGRVVASGA 215
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-226 |
2.96e-19 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 87.64 E-value: 2.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 1 MAAVEVRNGYKYYGSKSnpkiVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVlgakPGEPGSGVP- 79
Cdd:PRK10895 1 MATLTAKNLAKAYKGRR----VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIII----DDEDISLLPl 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 80 ---GSR-VGFMPQEIALVEEMTVKETIFYFGRI-YGLTDERIREKFKLLKELLQLPPARQMIKQC-SGGQQRRLSFACAM 153
Cdd:PRK10895 73 harARRgIGYLPQEASIFRRLSVYDNLMAVLQIrDDLSAEQREDRANELMEEFHIEHLRDSMGQSlSGGERRRVEIARAL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24582012 154 IHDPELLILDEPTVGLDPMlreKIWDF--LVETTRNSKLAVIITTHYIEEAKQAnC--IGLMRNGVLLAEDTPTNIM 226
Cdd:PRK10895 153 AANPKFILLDEPFAGVDPI---SVIDIkrIIEHLRDSGLGVLITDHNVRETLAV-CerAYIVSQGHLIAHGTPTEIL 225
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-221 |
3.18e-19 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 87.24 E-value: 3.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 1 MAAVEVRNGYKYYGsksnpKI-VLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGakpgEPGSGVP 79
Cdd:PRK11614 3 KVMLSFDKVSAHYG-----KIqALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDG----KDITDWQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 80 GSRVgfMPQEIALVEE-------MTVKETI----FYFGRiyGLTDERIREKFKLLKELLQLPPARQmiKQCSGGQQRRLS 148
Cdd:PRK11614 74 TAKI--MREAVAIVPEgrrvfsrMTVEENLamggFFAER--DQFQERIKWVYELFPRLHERRIQRA--GTMSGGEQQMLA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24582012 149 FACAMIHDPELLILDEPTVGLDPMLREKIWDfLVETTRNSKLAVIITTHYIEEA-KQANCIGLMRNGVLLAEDT 221
Cdd:PRK11614 148 IGRALMSQPRLLLLDEPSLGLAPIIIQQIFD-TIEQLREQGMTIFLVEQNANQAlKLADRGYVLENGHVVLEDT 220
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
4-177 |
6.43e-19 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 89.01 E-value: 6.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 4 VEVRNGYKYYGSKSnpkiVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGAKPGEpgSGVPGSRV 83
Cdd:PRK11432 7 VVLKNITKRFGSNT----VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTH--RSIQQRDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 84 GFMPQEIALVEEMTVKETIFYFGRIYGLTDERIREKFKLLKELLQLPP-ARQMIKQCSGGQQRRLSFACAMIHDPELLIL 162
Cdd:PRK11432 81 CMVFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGfEDRYVDQISGGQQQRVALARALILKPKVLLF 160
|
170
....*....|....*....
gi 24582012 163 DEPTVGLDPML----REKI 177
Cdd:PRK11432 161 DEPLSNLDANLrrsmREKI 179
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
20-202 |
7.86e-19 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 86.68 E-value: 7.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 20 KIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVlgakPGEPGSGvPGSRVGFMPQEIALVEEMTVK 99
Cdd:PRK11248 14 KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITL----DGKPVEG-PGAERGVVFQNEGLLPWRNVQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 100 ETIFYFGRIYGLTDERIREKFKLLKELLQLPPARQ-MIKQCSGGQQRRLSFACAMIHDPELLILDEPTVGLDPMLREKIW 178
Cdd:PRK11248 89 DNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKrYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQ 168
|
170 180
....*....|....*....|....
gi 24582012 179 DFLVETTRNSKLAVIITTHYIEEA 202
Cdd:PRK11248 169 TLLLKLWQETGKQVLLITHDIEEA 192
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-223 |
8.44e-19 |
|
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: 85.95 E-value: 8.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 2 AAVEVRNGYKYYGSKSNPKIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGAKPG----EPGSG 77
Cdd:COG4181 7 PIIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFaldeDARAR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 78 VPGSRVGFMPQEIALVEEMTVKETIfyfgriyGLTDE--RIREKFKLLKELLQ----------LPpaRQMikqcSGGQQR 145
Cdd:COG4181 87 LRARHVGFVFQSFQLLPTLTALENV-------MLPLElaGRRDARARARALLErvglghrldhYP--AQL----SGGEQQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24582012 146 RLSFACAMIHDPELLILDEPTVGLDPMLREKIWDFLVETTRNSKLAVIITTHYIEEAKQANCIGLMRNGVLLAEDTPT 223
Cdd:COG4181 154 RVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAARCDRVLRLRAGRLVEDTAAT 231
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
4-222 |
1.18e-18 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 85.82 E-value: 1.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 4 VEVRNGYKYYGSKsnpkIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGAKPGEPGSGVPG--S 81
Cdd:COG1126 2 IEIENLHKSFGDL----EVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDINKlrR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 82 RVGFMPQEIALVEEMTVKETIfyfgrIYGLT-------DERIREKFKLLkELLQLPP-ARQMIKQCSGGQQRRLSFACAM 153
Cdd:COG1126 78 KVGMVFQQFNLFPHLTVLENV-----TLAPIkvkkmskAEAEERAMELL-ERVGLADkADAYPAQLSGGQQQRVAIARAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24582012 154 IHDPELLILDEPTVGLDP-MLREkiwdflVETT----RNSKLAVIITTHYIEEAKQ-ANCIGLMRNGVLLAEDTP 222
Cdd:COG1126 152 AMEPKVMLFDEPTSALDPeLVGE------VLDVmrdlAKEGMTMVVVTHEMGFAREvADRVVFMDGGRIVEEGPP 220
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
21-197 |
1.58e-18 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 89.34 E-value: 1.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 21 IVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGAKPGEPGSGVPGSRVGFMPQEiALVEEMTVKE 100
Cdd:TIGR02868 349 PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQD-AHLFDTTVRE 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 101 TIFyFGRiYGLTDERIR---EKFKLLKELLQLPPARQMI-----KQCSGGQQRRLSFACAMIHDPELLILDEPTVGLDPM 172
Cdd:TIGR02868 428 NLR-LAR-PDATDEELWaalERVGLADWLRALPDGLDTVlgeggARLSGGERQRLALARALLADAPILLLDEPTEHLDAE 505
|
170 180
....*....|....*....|....*
gi 24582012 173 LREKIWDFLVETTrnSKLAVIITTH 197
Cdd:TIGR02868 506 TADELLEDLLAAL--SGRTVVLITH 528
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
23-200 |
1.63e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 86.44 E-value: 1.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 23 LNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVvLGAKPgepgsgVPGSRVGFMP--QEIALVEE----- 95
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRIL-FDGKP------IDYSRKGLMKlrESVGMVFQdpdnq 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 96 ---MTVKETIFYFGRIYGLTDERIREKFKLLKELLQLPPARQMIKQC-SGGQQRRLSFACAMIHDPELLILDEPTVGLDP 171
Cdd:PRK13636 95 lfsASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHClSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDP 174
|
170 180
....*....|....*....|....*....
gi 24582012 172 MLREKIWDFLVETTRNSKLAVIITTHYIE 200
Cdd:PRK13636 175 MGVSEIMKLLVEMQKELGLTIIIATHDID 203
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
26-214 |
2.90e-18 |
|
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: 82.87 E-value: 2.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 26 LNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGaKPGEPGSgvPGSR----VGFMP---QEIALVEEMTV 98
Cdd:cd03215 19 VSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDG-KPVTRRS--PRDAiragIAYVPedrKREGLVLDLSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 99 KETIfyfgriygltderirekfkLLKELLqlpparqmikqcSGGQQRRLSFACAMIHDPELLILDEPTVGLDPMLREKIW 178
Cdd:cd03215 96 AENI-------------------ALSSLL------------SGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIY 144
|
170 180 190
....*....|....*....|....*....|....*..
gi 24582012 179 DFLVETTRNSKlAVIITTHYIEEAKQ-ANCIGLMRNG 214
Cdd:cd03215 145 RLIRELADAGK-AVLLISSELDELLGlCDRILVMYEG 180
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-197 |
4.87e-18 |
|
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: 81.34 E-value: 4.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 4 VEVRNGYKYYGSKsnpkIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLgakpgepgsgvPGSRV 83
Cdd:cd03221 1 IELENLSKTYGGK----LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG-----------STVKI 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 84 GFMPQeialveemtvketifyfgriygltderirekfkllkellqLpparqmikqcSGGQQRRLSFACAMIHDPELLILD 163
Cdd:cd03221 66 GYFEQ----------------------------------------L----------SGGEKMRLALAKLLLENPNLLLLD 95
|
170 180 190
....*....|....*....|....*....|....
gi 24582012 164 EPTVGLDPMLREKIWDFLVETTRnsklAVIITTH 197
Cdd:cd03221 96 EPTNHLDLESIEALEEALKEYPG----TVILVSH 125
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-197 |
8.97e-18 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 83.55 E-value: 8.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 2 AAVEVRNGYKYYGSKSnpkiVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIvgqRRLN--------GGEVVVLGAKPGE 73
Cdd:COG1117 10 PKIEVRNLNVYYGDKQ----ALKDINLDIPENKVTALIGPSGCGKSTLLRCL---NRMNdlipgarvEGEILLDGEDIYD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 74 PGSGVPG--SRVGfM--------PqeialveeMTVKETIFYFGRIYGLT-----DERIREKFK---LLKEL---LQLPPA 132
Cdd:COG1117 83 PDVDVVElrRRVG-MvfqkpnpfP--------KSIYDNVAYGLRLHGIKskselDEIVEESLRkaaLWDEVkdrLKKSAL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24582012 133 RqmikqCSGGQQRRLSFACAMIHDPELLILDEPTVGLDPMLREKIWDFLVETtrNSKLAVIITTH 197
Cdd:COG1117 154 G-----LSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILEL--KKDYTIVIVTH 211
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
3-235 |
1.30e-17 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 85.17 E-value: 1.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 3 AVEVRNGYKYYGSKSnpkiVLNQLNMNVMRGSIYGLLGASGCG--KTTLLSCIVGQRRlnggevvvlGAKPGEPGSGVPG 80
Cdd:NF000106 13 AVEVRGLVKHFGEVK----AVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GPDA---------GRRPWRF*TWCAN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 81 SRV------GFMPQEIALVEEMTVKETIFYFGRIYGLTDERIREKFKLLKELLQLPPAR-QMIKQCSGGQQRRLSFACAM 153
Cdd:NF000106 80 RRAlrrtig*HRPVR*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAgRAAAKYSGGMRRRLDLAASM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 154 IHDPELLILDEPTVGLDPMLREKIWDFLVETTRNSKlAVIITTHYIEEAKQ-ANCIGLMRNGVLLAEDTPTNIMIKFGTQ 232
Cdd:NF000106 160 IGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGA-TVLLTTQYMEEAEQlAHELTVIDRGRVIADGKVDELKTKVGGR 238
|
...
gi 24582012 233 SIE 235
Cdd:NF000106 239 TLQ 241
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
10-225 |
2.65e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 82.86 E-value: 2.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 10 YKYYGSKSNPKIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVG-----QRRLNGGEVVVLGAKPGEPGSGVPgSRVG 84
Cdd:PRK13643 9 YTYQPNSPFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGllqptEGKVTVGDIVVSSTSKQKEIKPVR-KKVG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 85 FMPQ--EIALVEEMTVKETIFYfGRIYGLTDERIR----EKFKLL---KELLQLPPArqmikQCSGGQQRRLSFACAMIH 155
Cdd:PRK13643 88 VVFQfpESQLFEETVLKDVAFG-PQNFGIPKEKAEkiaaEKLEMVglaDEFWEKSPF-----ELSGGQMRRVAIAGILAM 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24582012 156 DPELLILDEPTVGLDPMLREKIWDfLVETTRNSKLAVIITTHYIEE-AKQANCIGLMRNGVLLAEDTPTNI 225
Cdd:PRK13643 162 EPEVLVLDEPTAGLDPKARIEMMQ-LFESIHQSGQTVVLVTHLMDDvADYADYVYLLEKGHIISCGTPSDV 231
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
3-228 |
4.68e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 82.16 E-value: 4.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 3 AVEVRN-GYKYygsKSNPKIVLNQLNMNVMRGSIYGLLGASGCGKTT---LLSCIVGQRRLNGGEVVVLGAKPGEPGSGV 78
Cdd:PRK13640 5 IVEFKHvSFTY---PDSKKPALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDNPNSKITVDGITLTAKTVWD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 79 PGSRVGFMPQ--EIALVEEmTVKETIfyfgrIYGLTDERI-REKF-----KLLKELLQLPPARQMIKQCSGGQQRRLSFA 150
Cdd:PRK13640 82 IREKVGIVFQnpDNQFVGA-TVGDDV-----AFGLENRAVpRPEMikivrDVLADVGMLDYIDSEPANLSGGQKQRVAIA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24582012 151 CAMIHDPELLILDEPTVGLDPMLREKIWDFLVETTRNSKLAVIITTHYIEEAKQANCIGLMRNGVLLAEDTPTNIMIK 228
Cdd:PRK13640 156 GILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSK 233
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
4-219 |
5.01e-17 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 80.59 E-value: 5.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 4 VEVRNGYKYYGSKSNPKIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLG----AKPGEPGSGVP 79
Cdd:PRK10584 7 VEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGqplhQMDEEARAKLR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 80 GSRVGFMPQEIALVEEMTVKETIFYFGRIYGLTDERIREKFKLLKELLQLPPA-RQMIKQCSGGQQRRLSFACAMIHDPE 158
Cdd:PRK10584 87 AKHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRlDHLPAQLSGGEQQRVALARAFNGRPD 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24582012 159 LLILDEPTVGLDPMLREKIWDFLVETTRNSKLAVIITTHYIEEAKQANCIGLMRNGVLLAE 219
Cdd:PRK10584 167 VLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNGQLQEE 227
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
3-214 |
5.42e-17 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 80.83 E-value: 5.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 3 AVEVRNGYKYYGSKSnpkiVLNQLNMNVMRGSIYGLLGASGCGKTTLLscivgqRRLN------GGEVVV------LGAK 70
Cdd:PRK11124 2 SIQLNGINCFYGAHQ----ALFDITLDCPQGETLVLLGPSGAGKSSLL------RVLNllemprSGTLNIagnhfdFSKT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 71 PGEPGSGVPGSRVGFMPQEIALVEEMTVKET-IFYFGRIYGLTDERIREKFKLLKELLQLPP-ARQMIKQCSGGQQRRLS 148
Cdd:PRK11124 72 PSDKAIRELRRNVGMVFQQYNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPyADRFPLHLSGGQQQRVA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24582012 149 FACAMIHDPELLILDEPTVGLDPMLREKIWDFLVEtTRNSKLAVIITTHYIEEAKQ-ANCIGLMRNG 214
Cdd:PRK11124 152 IARALMMEPQVLLFDEPTAALDPEITAQIVSIIRE-LAETGITQVIVTHEVEVARKtASRVVYMENG 217
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
13-226 |
6.99e-17 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 80.83 E-value: 6.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 13 YGSKSnpkiVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVgqrRLN---GGEVVVLGAKPGEPGSGVPGSRVGFMPQE 89
Cdd:PRK11231 12 YGTKR----ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFA---RLLtpqSGTVFLGDKPISMLSSRQLARRLALLPQH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 90 IALVEEMTVKETIFY--------FGRIyGLTDERIREKFKLLKELLQLppARQMIKQCSGGQQRRLSFACAMIHDPELLI 161
Cdd:PRK11231 85 HLTPEGITVRELVAYgrspwlslWGRL-SAEDNARVNQAMEQTRINHL--ADRRLTDLSGGQRQRAFLAMVLAQDTPVVL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24582012 162 LDEPTVGLDPMLREKIWDFLVETTRNSKlAVIITTHYIEEA-KQANCIGLMRNGVLLAEDTPTNIM 226
Cdd:PRK11231 162 LDEPTTYLDINHQVELMRLMRELNTQGK-TVVTVLHDLNQAsRYCDHLVVLANGHVMAQGTPEEVM 226
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
24-197 |
7.04e-17 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 80.80 E-value: 7.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 24 NQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVlgakPGEPGSGVPGSRVGFMP-----QEIALVEEMTV 98
Cdd:PRK11300 22 NNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILL----RGQHIEGLPGHQIARMGvvrtfQHVRLFREMTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 99 KETIfyfgriygLTDERIREKFKLLKELLQLPPARQMIKQC------------------------SGGQQRRLSFACAMI 154
Cdd:PRK11300 98 IENL--------LVAQHQQLKTGLFSGLLKTPAFRRAESEAldraatwlervgllehanrqagnlAYGQQRRLEIARCMV 169
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 24582012 155 HDPELLILDEPTVGLDPMLREKIWDFLVETTRNSKLAVIITTH 197
Cdd:PRK11300 170 TQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEH 212
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
4-230 |
7.13e-17 |
|
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: 80.35 E-value: 7.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 4 VEVRNGYKYYGSKsnpKIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVlgakPGEPGSGVP---- 79
Cdd:cd03254 3 IEFENVNFSYDEK---KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILI----DGIDIRDISrksl 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 80 GSRVGFMPQEIALVEEmTVKETIFYFGRIygLTDERIREKFKLLK---ELLQLPPARQMI-----KQCSGGQQRRLSFAC 151
Cdd:cd03254 76 RSMIGVVLQDTFLFSG-TIMENIRLGRPN--ATDEEVIEAAKEAGahdFIMKLPNGYDTVlgengGNLSQGERQLLAIAR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24582012 152 AMIHDPELLILDEPTVGLDPMLREKIWDFLvETTRNSKLAVIItTHYIEEAKQANCIGLMRNGVLLAEDTPTNIMIKFG 230
Cdd:cd03254 153 AMLRDPKILILDEATSNIDTETEKLIQEAL-EKLMKGRTSIII-AHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
20-218 |
1.29e-16 |
|
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: 83.55 E-value: 1.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 20 KIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGAKPGEPGSGVPGSRVGFMPQEIALVEEmTVK 99
Cdd:TIGR01842 331 KPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPG-TVA 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 100 ETIFYFGRiyGLTDERIREKFKL--LKEL-LQLP--------PARQMIkqcSGGQQRRLSFACAMIHDPELLILDEPTVG 168
Cdd:TIGR01842 410 ENIARFGE--NADPEKIIEAAKLagVHELiLRLPdgydtvigPGGATL---SGGQRQRIALARALYGDPKLVVLDEPNSN 484
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 24582012 169 LDP----MLREKIWDFlvettRNSKLAVIITTHYIEEAKQANCIGLMRNGVLLA 218
Cdd:TIGR01842 485 LDEegeqALANAIKAL-----KARGITVVVITHRPSLLGCVDKILVLQDGRIAR 533
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
26-203 |
1.73e-16 |
|
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: 78.69 E-value: 1.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 26 LNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGAkpgEPGSGVPGSR-VGFMPQEIALVEEMTVKETIfY 104
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGV---DVTAAPPADRpVSMLFQENNLFAHLTVEQNV-G 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 105 FGRIYGLT-DERIREKFK-------LLKELLQLPparqmiKQCSGGQQRRLSFACAMIHDPELLILDEPTVGLDPMLREK 176
Cdd:cd03298 93 LGLSPGLKlTAEDRQAIEvalarvgLAGLEKRLP------GELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAE 166
|
170 180
....*....|....*....|....*..
gi 24582012 177 IWDFLVETTRNSKLAVIITTHYIEEAK 203
Cdd:cd03298 167 MLDLVLDLHAETKMTVLMVTHQPEDAK 193
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
22-239 |
1.87e-16 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 80.05 E-value: 1.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 22 VLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGAKPGEPGSGVPGSRvgfmpQEIALVEEmTVKET 101
Cdd:PRK13638 16 VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLLALR-----QQVATVFQ-DPEQQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 102 IFYFG---------RIYGLTDERIREKFKLLKELLQLPPARQMIKQC-SGGQQRRLSFACAMIHDPELLILDEPTVGLDP 171
Cdd:PRK13638 90 IFYTDidsdiafslRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQClSHGQKKRVAIAGALVLQARYLLLDEPTAGLDP 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24582012 172 MLREKIWDFLVETTRNSKlAVIITTHYIEEAKQ-ANCIGLMRNGVLLAEDTPTNIMIKfgTQSIEDAFL 239
Cdd:PRK13638 170 AGRTQMIAIIRRIVAQGN-HVIISSHDIDLIYEiSDAVYVLRQGQILTHGAPGEVFAC--TEAMEQAGL 235
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
37-226 |
2.44e-16 |
|
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: 81.30 E-value: 2.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 37 GLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGaKP---GEPGSGVP--GSRVGFMPQEIALVEEMTVKETIFYfGRIYGL 111
Cdd:COG4148 29 ALFGPSGSGKTTLLRAIAGLERPDSGRIRLGG-EVlqdSARGIFLPphRRRIGYVFQEARLFPHLSVRGNLLY-GRKRAP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 112 TDERiREKF----KLLK--ELLQLPPArqmikQCSGGQQRRLSFACAMIHDPELLILDEPTVGLDPMLREKIWDFLVETT 185
Cdd:COG4148 107 RAER-RISFdevvELLGigHLLDRRPA-----TLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILPYLERLR 180
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 24582012 186 RNSKLAVIITTHYIEEAKQ-ANCIGLMRNGVLLAEDTPTNIM 226
Cdd:COG4148 181 DELDIPILYVSHSLDEVARlADHVVLLEQGRVVASGPLAEVL 222
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
10-225 |
2.95e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 79.75 E-value: 2.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 10 YKYY-GSKSNPKIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGAKPGEPGSGVP-GSRVGFMP 87
Cdd:PRK13633 12 YKYEsNEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWDiRNKAGMVF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 88 QE------IALVEEMTVketifyFG-RIYGLTDERIREKF-KLLKELLQLPPARQMIKQCSGGQQRRLSFACAMIHDPEL 159
Cdd:PRK13633 92 QNpdnqivATIVEEDVA------FGpENLGIPPEEIRERVdESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPEC 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24582012 160 LILDEPTVGLDPMLREKIWDFLVETTRNSKLAVIITTHYIEEAKQANCIGLMRNGVLLAEDTPTNI 225
Cdd:PRK13633 166 IIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEI 231
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-226 |
3.14e-16 |
|
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: 82.16 E-value: 3.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 4 VEVRNGYKYYGSKSNPKI-VLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEV-VVLG------AKPGEPG 75
Cdd:TIGR03269 280 IKVRNVSKRYISVDRGVVkAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnVRVGdewvdmTKPGPDG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 76 SGVPGSRVGFMPQEIALVEEMTVKETI---------FYFGR---IYGLTDERIREKFKllKELLQlpparQMIKQCSGGQ 143
Cdd:TIGR03269 360 RGRAKRYIGILHQEYDLYPHRTVLDNLteaiglelpDELARmkaVITLKMVGFDEEKA--EEILD-----KYPDELSEGE 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 144 QRRLSFACAMIHDPELLILDEPTVGLDPMLREKIWDFLVETTRNSKLAVIITTHYIEEAKQAnC--IGLMRNGVLLAEDT 221
Cdd:TIGR03269 433 RHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDV-CdrAALMRDGKIVKIGD 511
|
....*
gi 24582012 222 PTNIM 226
Cdd:TIGR03269 512 PEEIV 516
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
4-225 |
4.35e-16 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 80.23 E-value: 4.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 4 VEVRNGYKYYGSKSNPKIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLG---AKPGEPGSGVPG 80
Cdd:PRK11153 2 IELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGqdlTALSEKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 81 SRVGFMPQEIALVEEMTVKETIFYFGRIYGLTDERIREKfklLKELLQLP---------PArqmikQCSGGQQRRLSFAC 151
Cdd:PRK11153 82 RQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKAR---VTELLELVglsdkadryPA-----QLSGGQKQRVAIAR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24582012 152 AMIHDPELLILDEPTVGLDPMLREKIWDFLVETTRNSKLAVIITTHYIEEAKQ-ANCIGLMRNGVLLAEDTPTNI 225
Cdd:PRK11153 154 ALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRiCDRVAVIDAGRLVEQGTVSEV 228
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-214 |
7.74e-16 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 80.84 E-value: 7.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 3 AVEVRNGYKYYGSKsnpkIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGaKPGEPGSgvPG-- 80
Cdd:COG3845 5 ALELRGITKRFGGV----VANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDG-KPVRIRS--PRda 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 81 --SRVGFMPQEIALVEEMTVKETIF--YFGRIYGLTD-----ERIREkfkLLKEL-LQLPPARqMIKQCSGGQQRRLSFA 150
Cdd:COG3845 78 iaLGIGMVHQHFMLVPNLTVAENIVlgLEPTKGGRLDrkaarARIRE---LSERYgLDVDPDA-KVEDLSVGEQQRVEIL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24582012 151 CAMIHDPELLILDEPTVGLDPMLREKIWDFLVETTRNSKlAVIITTHYIEEAKQ-ANCIGLMRNG 214
Cdd:COG3845 154 KALYRGARILILDEPTAVLTPQEADELFEILRRLAAEGK-SIIFITHKLREVMAiADRVTVLRRG 217
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
27-204 |
8.79e-16 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 77.10 E-value: 8.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 27 NMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLG----AKPgepgsgvPGSR-VGFMPQEIALVEEMTVKET 101
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGqdltALP-------PAERpVSMLFQENNLFPHLTVAQN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 102 IfYFGRIYGL---TDERIR-----EKFKLlKELLQLPPArqmikQCSGGQQRRLSFACAMIHDPELLILDEPTVGLDPML 173
Cdd:COG3840 92 I-GLGLRPGLkltAEQRAQveqalERVGL-AGLLDRLPG-----QLSGGQRQRVALARCLVRKRPILLLDEPFSALDPAL 164
|
170 180 190
....*....|....*....|....*....|.
gi 24582012 174 REKIWDFLVETTRNSKLAVIITTHYIEEAKQ 204
Cdd:COG3840 165 RQEMLDLVDELCRERGLTVLMVTHDPEDAAR 195
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
23-202 |
9.15e-16 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 77.75 E-value: 9.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 23 LNQLNMNVMRGSIYGLLGASGCGKTTLL---SCIVGQRRLNGGEVVVLG---AKPGEPGSGVPGSR--VGFMPQEIALVE 94
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLrhlSGLITGDKSAGSHIELLGrtvQREGRLARDIRKSRanTGYIFQQFNLVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 95 EMTVKETI---------FYFGRIYGLTDERIREKFKLLKELLQLPPARQMIKQCSGGQQRRLSFACAMIHDPELLILDEP 165
Cdd:PRK09984 100 RLSVLENVligalgstpFWRTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEP 179
|
170 180 190
....*....|....*....|....*....|....*..
gi 24582012 166 TVGLDPMLREKIWDFLVETTRNSKLAVIITTHYIEEA 202
Cdd:PRK09984 180 IASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYA 216
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
4-219 |
1.32e-15 |
|
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: 77.54 E-value: 1.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 4 VEVRNGYKYYGS-----KSNPKIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVlgakPGEPGSGV 78
Cdd:TIGR02769 3 LEVRDVTHTYRTgglfgAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSF----RGQDLYQL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 79 PGSRVGFMPQEIALV---------EEMTVKETIFYFGRIYGLTDERIRE-KFKLLKELLQLPP--ARQMIKQCSGGQQRR 146
Cdd:TIGR02769 79 DRKQRRAFRRDVQLVfqdspsavnPRMTVRQIIGEPLRHLTSLDESEQKaRIAELLDMVGLRSedADKLPRQLSGGQLQR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24582012 147 LSFACAMIHDPELLILDEPTVGLDPMLREKIWDFLVETTRNSKLAVIITTHYIEEAKQ-ANCIGLMRNGVLLAE 219
Cdd:TIGR02769 159 INIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSfCQRVAVMDKGQIVEE 232
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
2-214 |
1.63e-15 |
|
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: 80.18 E-value: 1.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 2 AAVEVRN-GYKYYGSKsnpKIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGAKPGEPGSGVPG 80
Cdd:COG4618 329 GRLSVENlTVVPPGSK---RPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELG 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 81 SRVGFMPQEIALVEEmTVKETIFYFGRIyglTDERIREKFKL--LKEL-LQLP--------PARQMIkqcSGGQQRRLSF 149
Cdd:COG4618 406 RHIGYLPQDVELFDG-TIAENIARFGDA---DPEKVVAAAKLagVHEMiLRLPdgydtrigEGGARL---SGGQRQRIGL 478
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24582012 150 ACAMIHDPELLILDEPTVGLDP----MLREKIWDFlvettRNSKLAVIITTHYIEEAKQANCIGLMRNG 214
Cdd:COG4618 479 ARALYGDPRLVVLDEPNSNLDDegeaALAAAIRAL-----KARGATVVVITHRPSLLAAVDKLLVLRDG 542
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
4-225 |
1.92e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 77.04 E-value: 1.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 4 VEVRN-GYKYygskSNPKIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGAKPGEPGSGVPGSR 82
Cdd:PRK13639 2 LETRDlKYSY----PDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLEVR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 83 --VG----------FMPqeialveemTVKETIfYFGRI-YGLTDERIREKFK-LLKELLQLPPARQMIKQCSGGQQRRLS 148
Cdd:PRK13639 78 ktVGivfqnpddqlFAP---------TVEEDV-AFGPLnLGLSKEEVEKRVKeALKAVGMEGFENKPPHHLSGGQKKRVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24582012 149 FACAMIHDPELLILDEPTVGLDPMLREKIWDFLVETTRNSkLAVIITTHYIEEA-KQANCIGLMRNGVLLAEDTPTNI 225
Cdd:PRK13639 148 IAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEG-ITIIISTHDVDLVpVYADKVYVMSDGKIIKEGTPKEV 224
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
12-236 |
1.96e-15 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 76.74 E-value: 1.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 12 YYGSKSnpkiVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGgEVVVLGAKPGEpGSGVPGSRVGF--MPQE 89
Cdd:PRK14239 14 YYNKKK----ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNP-EVTITGSIVYN-GHNIYSPRTDTvdLRKE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 90 IALVEE------MTVKETIFYFGRIYGLTDERIREKfkLLKELLQLPPARQMIKQ--------CSGGQQRRLSFACAMIH 155
Cdd:PRK14239 88 IGMVFQqpnpfpMSIYENVVYGLRLKGIKDKQVLDE--AVEKSLKGASIWDEVKDrlhdsalgLSGGQQQRVCIARVLAT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 156 DPELLILDEPTVGLDPMLREKIWDFLVETtrNSKLAVIITTHYIEEAKQ-ANCIGLMRNGVLLAEDTPTNIMIKFGTQSI 234
Cdd:PRK14239 166 SPKIILLDEPTSALDPISAGKIEETLLGL--KDDYTMLLVTRSMQQASRiSDRTGFFLDGDLIEYNDTKQMFMNPKHKET 243
|
..
gi 24582012 235 ED 236
Cdd:PRK14239 244 ED 245
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-228 |
2.21e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 77.15 E-value: 2.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 1 MAAVEVRN-GYKYYGSKSnpkiVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGAKPGEPGSGVP 79
Cdd:PRK13652 1 MHLIETRDlCYSYSGSKE----ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 80 GSRVGFMPQEIA-LVEEMTVKETIfYFGRI-YGLTDERIREKFKLLKELLQLPPARQMI-KQCSGGQQRRLSFACAMIHD 156
Cdd:PRK13652 77 RKFVGLVFQNPDdQIFSPTVEQDI-AFGPInLGLDEETVAHRVSSALHMLGLEELRDRVpHHLSGGEKKRVAIAGVIAME 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24582012 157 PELLILDEPTVGLDPMLREKIWDFLVETTRNSKLAVIITTHYIE-EAKQANCIGLMRNGVLLAEDTPTNIMIK 228
Cdd:PRK13652 156 PQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDlVPEMADYIYVMDKGRIVAYGTVEEIFLQ 228
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-281 |
2.23e-15 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 76.65 E-value: 2.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 1 MAAVEVRNGYKYYGS-----KSNPKIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGakpgEPG 75
Cdd:PRK10419 1 MTLLNVSGLSHHYAHgglsgKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRG----EPL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 76 SGVPGSRVGFMPQEIALVEE-----MTVKETIfyfGRIYG-----LTDERIREKFKLLKELLQ---LPP--ARQMIKQCS 140
Cdd:PRK10419 77 AKLNRAQRKAFRRDIQMVFQdsisaVNPRKTV---REIIReplrhLLSLDKAERLARASEMLRavdLDDsvLDKRPPQLS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 141 GGQQRRLSFACAMIHDPELLILDEPTVGLDPMLREKIWDFLVETTRNSKLAVIITTHyieeakqanciglmrnGVLLAED 220
Cdd:PRK10419 154 GGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITH----------------DLRLVER 217
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24582012 221 TPTNIMIKFGTQSIEDAFLILSQRqgnedelaqiMDHNKNQALPAAVLPPEVIDTHEPNMP 281
Cdd:PRK10419 218 FCQRVMVMDNGQIVETQPVGDKLT----------FSSPAGRVLQNAVLPAFPVRRRTTEKV 268
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
23-226 |
2.29e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 76.95 E-value: 2.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 23 LNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGAKPGEPgSGVPGSR--VG--FMPQEIALVEEmTV 98
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDF-SKLQGIRklVGivFQNPETQFVGR-TV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 99 KETIFYFGRIYGLTDERIREKFKLLKELLQLPPAR-QMIKQCSGGQQRRLSFACAMIHDPELLILDEPTVGLDPMLREKI 177
Cdd:PRK13644 96 EEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRhRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAV 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 24582012 178 WDFLVETTRNSKlAVIITTHYIEEAKQANCIGLMRNGVLLAEDTPTNIM 226
Cdd:PRK13644 176 LERIKKLHEKGK-TIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVL 223
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
10-235 |
2.43e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 76.98 E-value: 2.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 10 YKYygsKSNPKIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGAKPGEPGSGVPGSRVGFMPQ- 88
Cdd:PRK13635 13 FRY---PDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGMVFQn 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 89 -EIALVEEmTVKETIfyfgrIYGLTD---------ERIREKFKL--LKELLQLPPARqmikqCSGGQQRRLSFACAMIHD 156
Cdd:PRK13635 90 pDNQFVGA-TVQDDV-----AFGLENigvpreemvERVDQALRQvgMEDFLNREPHR-----LSGGQKQRVAIAGVLALQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24582012 157 PELLILDEPTVGLDPMLREKIWDFLVETTRNSKLAVIITTHYIEEAKQANCIGLMRNGVLLAEDTPTNIMiKFGTQSIE 235
Cdd:PRK13635 159 PDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIF-KSGHMLQE 236
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
26-205 |
3.72e-15 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 74.83 E-value: 3.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 26 LNMNVMRGSIYGLLGASGCGKTTLLSCIVG----------QRRLNGGEvvvLGAKPGEPgsgvpgSRVGFMPQEIALVEE 95
Cdd:COG4136 20 LSLTVAPGEILTLMGPSGSGKSTLLAAIAGtlspafsasgEVLLNGRR---LTALPAEQ------RRIGILFQDDLLFPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 96 MTVKETIfyfgrIYGLTDERIR-EKFKLLKELLQ---LPP-ARQMIKQCSGGQQRRLSFACAMIHDPELLILDEPTVGLD 170
Cdd:COG4136 91 LSVGENL-----AFALPPTIGRaQRRARVEQALEeagLAGfADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLD 165
|
170 180 190
....*....|....*....|....*....|....*
gi 24582012 171 PMLREKIWDFLVETTRNSKLAVIITTHYIEEAKQA 205
Cdd:COG4136 166 AALRAQFREFVFEQIRQRGIPALLVTHDEEDAPAA 200
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
4-172 |
4.42e-15 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 75.96 E-value: 4.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 4 VEVRNGYKYYGSKSnpkiVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGAK-PGEPGSGVPGSR 82
Cdd:PRK11831 8 VDMRGVSFTRGNRC----IFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENiPAMSRSRLYTVR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 83 --VGFMPQEIALVEEMTVKETIFYFGRIYG-LTDERIREKFKLLKELLQLPPARQ-MIKQCSGGQQRRLSFACAMIHDPE 158
Cdd:PRK11831 84 krMSMLFQSGALFTDMNVFDNVAYPLREHTqLPAPLLHSTVMMKLEAVGLRGAAKlMPSELSGGMARRAALARAIALEPD 163
|
170
....*....|....
gi 24582012 159 LLILDEPTVGLDPM 172
Cdd:PRK11831 164 LIMFDEPFVGQDPI 177
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
23-263 |
4.54e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 76.20 E-value: 4.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 23 LNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGAKPgePGSGVPGSRVGFMPQEIALV----EEMTV 98
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAI--PANLKKIKEVKRLRKEIGLVfqfpEYQLF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 99 KETI---FYFGRIY-GLTDERIREKFKLLKELLQLPpaRQMIK----QCSGGQQRRLSFACAMIHDPELLILDEPTVGLD 170
Cdd:PRK13645 105 QETIekdIAFGPVNlGENKQEAYKKVPELLKLVQLP--EDYVKrspfELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLD 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 171 PMLREKIWDFLVETTRNSKLAVIITTHYIEEA-KQANCIGLMRNGVLLAEDTPTNImikFGTQSiedaflILSQRQGNED 249
Cdd:PRK13645 183 PKGEEDFINLFERLNKEYKKRIIMVTHNMDQVlRIADEVIVMHEGKVISIGSPFEI---FSNQE------LLTKIEIDPP 253
|
250
....*....|....
gi 24582012 250 ELAQIMDHNKNQAL 263
Cdd:PRK13645 254 KLYQLMYKLKNKGI 267
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
16-170 |
4.77e-15 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 78.94 E-value: 4.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 16 KSNPKIVLNQLNMNVMRGSIYGLLGASGCGKTTLLScIVGQRRLNG----GEVVVLGAKPGEPGSGVpgsRVGFMPQEIA 91
Cdd:TIGR00955 34 ERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMN-ALAFRSPKGvkgsGSVLLNGMPIDAKEMRA---ISAYVQQDDL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 92 LVEEMTVKETIFYFGRIYGLTDERIREKFKLLKELLQ---LPPARQMI-------KQCSGGQQRRLSFACAMIHDPELLI 161
Cdd:TIGR00955 110 FIPTLTVREHLMFQAHLRMPRRVTKKEKRERVDEVLQalgLRKCANTRigvpgrvKGLSGGERKRLAFASELLTDPPLLF 189
|
....*....
gi 24582012 162 LDEPTVGLD 170
Cdd:TIGR00955 190 CDEPTSGLD 198
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-197 |
4.79e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 75.84 E-value: 4.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 1 MAAVEVRNGYKYYGSKSnpkiVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGgEVVVLGaKPGEPGSGVPG 80
Cdd:PRK14258 5 IPAIKVNNLSFYYDTQK----ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELES-EVRVEG-RVEFFNQNIYE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 81 SRVGF--MPQEIALVEE------MTVKETIFYFGRIYG---------LTDERIRE-------KFKLLKELLQLpparqmi 136
Cdd:PRK14258 79 RRVNLnrLRRQVSMVHPkpnlfpMSVYDNVAYGVKIVGwrpkleiddIVESALKDadlwdeiKHKIHKSALDL------- 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24582012 137 kqcSGGQQRRLSFACAMIHDPELLILDEPTVGLDPMLREKIWDFLVETTRNSKLAVIITTH 197
Cdd:PRK14258 152 ---SGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSH 209
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-174 |
4.87e-15 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 77.38 E-value: 4.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 1 MAAVEVRNGYKYYGSKsnpkIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGAKPGEpgsgVPG 80
Cdd:PRK11000 1 MASVTLRNVTKAYGDV----VISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMND----VPP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 81 SR--VGFMPQEIALVEEMTVKETIFYFGRIYGLTDERIREKFKLLKELLQLPP--ARQMiKQCSGGQQRRLSFACAMIHD 156
Cdd:PRK11000 73 AErgVGMVFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHllDRKP-KALSGGQRQRVAIGRTLVAE 151
|
170
....*....|....*...
gi 24582012 157 PELLILDEPTVGLDPMLR 174
Cdd:PRK11000 152 PSVFLLDEPLSNLDAALR 169
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
3-222 |
5.04e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 75.93 E-value: 5.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 3 AVEVRNGYKYY--GSKSnpkivLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGAKPGEPGSGVPG 80
Cdd:PRK13647 4 IIEVEDLHFRYkdGTKA-----LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 81 SRVGFMPQEIA-LVEEMTVKETIFYFGRIYGLT----DERIREKFKL--LKELLQLPParqmiKQCSGGQQRRLSFACAM 153
Cdd:PRK13647 79 SKVGLVFQDPDdQVFSSTVWDDVAFGPVNMGLDkdevERRVEEALKAvrMWDFRDKPP-----YHLSYGQKKRVAIAGVL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 154 IHDPELLILDEPTVGLDPMLREKIWDFLVETTRNSKlAVIITTHYIEEAKQ-ANCIGLMRNGVLLAEDTP 222
Cdd:PRK13647 154 AMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGK-TVIVATHDVDLAAEwADQVIVLKEGRVLAEGDK 222
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
4-214 |
5.59e-15 |
|
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: 74.96 E-value: 5.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 4 VEVRN-GYKYYGSKSNpkiVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCI-------VGQRRLNGGEVVVLGAKPGEpg 75
Cdd:cd03251 1 VEFKNvTFRYPGDGPP---VLRDISLDIPAGETVALVGPSGSGKSTLVNLIprfydvdSGRILIDGHDVRDYTLASLR-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 76 sgvpgSRVGFMPQEIALVEEmTVKETIFYfGRiYGLTDERIREKFKL--LKELL-QLPPARQMI-----KQCSGGQQRRL 147
Cdd:cd03251 76 -----RQIGLVSQDVFLFND-TVAENIAY-GR-PGATREEVEEAARAanAHEFImELPEGYDTVigergVKLSGGQRQRI 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24582012 148 SFACAMIHDPELLILDEPTVGLDPMLREKIWDFLVETTRNSklAVIITTHYIEEAKQANCIGLMRNG 214
Cdd:cd03251 148 AIARALLKDPPILILDEATSALDTESERLVQAALERLMKNR--TTFVIAHRLSTIENADRIVVLEDG 212
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
20-226 |
6.97e-15 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 75.21 E-value: 6.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 20 KIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGAKPGEPGSGVPGSRVGFMPQEIALVEEMTVK 99
Cdd:PRK10575 24 RTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQLPAAEGMTVR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 100 ETIFY--------FGRiYGLTDeriREKFKLLKELLQLPP-ARQMIKQCSGGQQRRLSFACAMIHDPELLILDEPTVGLD 170
Cdd:PRK10575 104 ELVAIgrypwhgaLGR-FGAAD---REKVEEAISLVGLKPlAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALD 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 24582012 171 PMLREKIWDFLVETTRNSKLAVIITTHYIE-EAKQANCIGLMRNGVLLAEDTPTNIM 226
Cdd:PRK10575 180 IAHQVDVLALVHRLSQERGLTVIAVLHDINmAARYCDYLVALRGGEMIAQGTPAELM 236
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
3-204 |
7.81e-15 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 74.66 E-value: 7.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 3 AVEVRNGYKYYGSKSnpkiVLNQLNMNVMRGSIYGLLGASGCGKTTLLscivgqRRLN------GGEVVVLG------AK 70
Cdd:COG4161 2 SIQLKNINCFYGSHQ----ALFDINLECPSGETLVLLGPSGAGKSSLL------RVLNlletpdSGQLNIAGhqfdfsQK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 71 PGEPGSGVPGSRVGFMPQEIALVEEMTVKET-IFYFGRIYGLTDERIREKFKLLKELLQLPP-ARQMIKQCSGGQQRRLS 148
Cdd:COG4161 72 PSEKAIRLLRQKVGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDkADRFPLHLSGGQQQRVA 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 24582012 149 FACAMIHDPELLILDEPTVGLDPMLREKIWDFLVETTRNSKLAVIItTHYIEEAKQ 204
Cdd:COG4161 152 IARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIV-THEVEFARK 206
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
23-225 |
1.40e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 74.82 E-value: 1.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 23 LNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVV----LGAKPGEPGSGVPGSRVGFMPQ--EIALVEEm 96
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVdditITHKTKDKYIRPVRKRIGMVFQfpESQLFED- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 97 TVKETIFYFGRIYGLTDERIREK-FKLLKEL------LQLPPArqmikQCSGGQQRRLSFACAMIHDPELLILDEPTVGL 169
Cdd:PRK13646 102 TVEREIIFGPKNFKMNLDEVKNYaHRLLMDLgfsrdvMSQSPF-----QMSGGQMRKIAIVSILAMNPDIIVLDEPTAGL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 24582012 170 DPMLREKIWDFLVETTRNSKLAVIITTHYIEE-AKQANCIGLMRNGVLLAEDTPTNI 225
Cdd:PRK13646 177 DPQSKRQVMRLLKSLQTDENKTIILVSHDMNEvARYADEVIVMKEGSIVSQTSPKEL 233
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
18-214 |
1.84e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 76.79 E-value: 1.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 18 NPKIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVlgakpgepgSGVPGSRVGfmpqEIALVEEMT 97
Cdd:PRK11160 351 QPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILL---------NGQPIADYS----EAALRQAIS 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 98 VKETifyfgRIY---------------GLTDERIREKFKL--LKELLQLPPA---------RQMikqcSGGQQRRLSFAC 151
Cdd:PRK11160 418 VVSQ-----RVHlfsatlrdnlllaapNASDEALIEVLQQvgLEKLLEDDKGlnawlgeggRQL----SGGEQRRLGIAR 488
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24582012 152 AMIHDPELLILDEPTVGLDPMLREKIWDFLVETTRNSklAVIITTHYIEEAKQANCIGLMRNG 214
Cdd:PRK11160 489 ALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNK--TVLMITHRLTGLEQFDRICVMDNG 549
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
25-202 |
2.07e-14 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 72.97 E-value: 2.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 25 QLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVlgakPGEPGSGVPGSR--VGFMPQEIALVEEMTVKETI 102
Cdd:TIGR01277 16 EFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKV----NDQSHTGLAPYQrpVSMLFQENNLFAHLTVRQNI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 103 fYFGRIYGLtderireKFKLLKELLQLPPARQM---------IKQCSGGQQRRLSFACAMIHDPELLILDEPTVGLDPML 173
Cdd:TIGR01277 92 -GLGLHPGL-------KLNAEQQEKVVDAAQQVgiadyldrlPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLL 163
|
170 180
....*....|....*....|....*....
gi 24582012 174 REKIWDFLVETTRNSKLAVIITTHYIEEA 202
Cdd:TIGR01277 164 REEMLALVKQLCSERQRTLLMVTHHLSDA 192
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
4-225 |
2.39e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 74.50 E-value: 2.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 4 VEVRNGYKYYGSK-SNPKIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEV----VVLGAK-PGEPGSG 77
Cdd:PRK13631 22 LRVKNLYCVFDEKqENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdIYIGDKkNNHELIT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 78 VPGSR-----------VGFMPQ--EIALVEEmTVKETIFyFGRI-YGLTDERIRE--KFKLLKELLQLPPARQMIKQCSG 141
Cdd:PRK13631 102 NPYSKkiknfkelrrrVSMVFQfpEYQLFKD-TIEKDIM-FGPVaLGVKKSEAKKlaKFYLNKMGLDDSYLERSPFGLSG 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 142 GQQRRLSFACAMIHDPELLILDEPTVGLDPMLREKIWDFLVETTRNSKlAVIITTHYIEEAKQ-ANCIGLMRNGVLLAED 220
Cdd:PRK13631 180 GQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNK-TVFVITHTMEHVLEvADEVIVMDKGKILKTG 258
|
....*
gi 24582012 221 TPTNI 225
Cdd:PRK13631 259 TPYEI 263
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
3-197 |
2.45e-14 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 72.62 E-value: 2.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 3 AVEVRN-GYKYYGSksnPKIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGAKPGEPGSGVPGS 81
Cdd:cd03245 2 RIEFRNvSFSYPNQ---EIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 82 RVGFMPQEIALVEEmTVKETIFYFGRIygLTDERIREKFKL--LKELLQLPP---ARQMIKQ---CSGGQQRRLSFACAM 153
Cdd:cd03245 79 NIGYVPQDVTLFYG-TLRDNITLGAPL--ADDERILRAAELagVTDFVNKHPnglDLQIGERgrgLSGGQRQAVALARAL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 24582012 154 IHDPELLILDEPTVGLDPMLREKIWDFLVETTRNSklAVIITTH 197
Cdd:cd03245 156 LNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDK--TLIIITH 197
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
3-222 |
3.12e-14 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 75.97 E-value: 3.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 3 AVEVRN-GYKYYGSKsnpkIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVlgakpgepgSGVP-- 79
Cdd:COG1132 339 EIEFENvSFSYPGDR----PVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILI---------DGVDir 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 80 -------GSRVGFMPQEIALVEeMTVKETIFYfGRIyGLTDERIREKFKL--LKE-LLQLPPARQMI-----KQCSGGQQ 144
Cdd:COG1132 406 dltleslRRQIGVVPQDTFLFS-GTIRENIRY-GRP-DATDEEVEEAAKAaqAHEfIEALPDGYDTVvgergVNLSGGQR 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 145 RRLSFACAMIHDPELLILDEPTVGLDP----MLREKIWDFLVETTrnsklaVIITTHYIEEAKQANCIGLMRNGVLLAED 220
Cdd:COG1132 483 QRIAIARALLKDPPILILDEATSALDTeteaLIQEALERLMKGRT------TIVIAHRLSTIRNADRILVLDDGRIVEQG 556
|
..
gi 24582012 221 TP 222
Cdd:COG1132 557 TH 558
|
|
| ABC2_membrane |
pfam01061 |
ABC-2 type transporter; |
505-664 |
3.43e-14 |
|
ABC-2 type transporter;
Pssm-ID: 426023 [Multi-domain] Cd Length: 204 Bit Score: 71.92 E-value: 3.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 505 IFGSTDIEFQQYCAPGVVMTMVFFLA-TLMTAAVFISERMDGIWDRTLLAGV-SATEMLWAHLLTQLIIMALQS--FEVI 580
Cdd:pfam01061 33 LFGNLGNQQGGLNRPGLLFFSILFNAfSALSGISPVFEKERGVLYRELASPLySPSAYVLAKILSELPLSLLQSliFLLI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 581 MY--IGLvfdTYNNGDTTTLIGLLTLTAFCGMLFGLFISVFCKSHTEANFVATGAFYPMIILCGLLWPLESMPQFLQDLV 658
Cdd:pfam01061 113 VYfmVGL---PPSAGRFFLFLLVLLLTALAASSLGLFISALAPSFEDASQLGPLVLLPLLLLSGFFIPIDSMPVWWQWIY 189
|
....*.
gi 24582012 659 MVLPFT 664
Cdd:pfam01061 190 YLNPLT 195
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
22-238 |
5.31e-14 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 74.49 E-value: 5.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 22 VLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGAKPGEPGSGVPGSRVGFMPQEIALVEEMTVkET 101
Cdd:PRK09536 18 VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLSFEFDV-RQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 102 IFYFGRI--------YGLTDERIREKFKLLKELLQLppARQMIKQCSGGQQRRLSFACAMIHDPELLILDEPTVGLD--- 170
Cdd:PRK09536 97 VVEMGRTphrsrfdtWTETDRAAVERAMERTGVAQF--ADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDinh 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24582012 171 -----PMLREkiwdfLVETTRnsklAVIITTHYIE-EAKQANCIGLMRNGVLLAEDTPTNIMIkfgTQSIEDAF 238
Cdd:PRK09536 175 qvrtlELVRR-----LVDDGK----TAVAAIHDLDlAARYCDELVLLADGRVRAAGPPADVLT---ADTLRAAF 236
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
4-226 |
5.96e-14 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 74.30 E-value: 5.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 4 VEVRNGYKYYGS--------------------KSNPKIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGE 63
Cdd:PRK10070 5 LEIKNLYKIFGEhpqrafkyieqglskeqileKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 64 VVVLGAKPGEPGSG----VPGSRVGFMPQEIALVEEMTVKETIFYFGRIYGLTDERIREK-FKLLKELLQLPPARQMIKQ 138
Cdd:PRK10070 85 VLIDGVDIAKISDAelreVRRKKIAMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKaLDALRQVGLENYAHSYPDE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 139 CSGGQQRRLSFACAMIHDPELLILDEPTVGLDPMLREKIWDFLVETTRNSKLAVIITTHYIEEAKQ-ANCIGLMRNGVLL 217
Cdd:PRK10070 165 LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRiGDRIAIMQNGEVV 244
|
....*....
gi 24582012 218 AEDTPTNIM 226
Cdd:PRK10070 245 QVGTPDEIL 253
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-226 |
7.68e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 72.33 E-value: 7.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 2 AAVEVRNGYKYYGSKSNPkiVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGAKpgepgsgVPGS 81
Cdd:PRK13632 6 VMIKVENVSFSYPNSENN--ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGIT-------ISKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 82 RVGFMPQEIALVEE--------MTVKETIfyfgrIYGLTDERI-REKFKllKELLQLPPARQMIKQC-------SGGQQR 145
Cdd:PRK13632 77 NLKEIRKKIGIIFQnpdnqfigATVEDDI-----AFGLENKKVpPKKMK--DIIDDLAKKVGMEDYLdkepqnlSGGQKQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 146 RLSFACAMIHDPELLILDEPTVGLDPMLREKIWDFLVETTRNSKLAVIITTHYIEEAKQANCIGLMRNGVLLAEDTPTNI 225
Cdd:PRK13632 150 RVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEI 229
|
.
gi 24582012 226 M 226
Cdd:PRK13632 230 L 230
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-174 |
1.07e-13 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 72.95 E-value: 1.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 1 MAAVEVRNGYKYYGSKSNpkiVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEV-----VVLGAKPGEPG 75
Cdd:PRK11650 1 MAGLKLQAVRKSYDGKTQ---VIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIwiggrVVNELEPADRD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 76 sgvpgsrVGFMPQEIALVEEMTVKETIFYFGRIYGLT----DERIREKFKLLK--ELLQLPPArqmikQCSGGQQRRLSF 149
Cdd:PRK11650 78 -------IAMVFQNYALYPHMSVRENMAYGLKIRGMPkaeiEERVAEAARILElePLLDRKPR-----ELSGGQRQRVAM 145
|
170 180
....*....|....*....|....*
gi 24582012 150 ACAMIHDPELLILDEPTVGLDPMLR 174
Cdd:PRK11650 146 GRAIVREPAVFLFDEPLSNLDAKLR 170
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-197 |
1.08e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 71.41 E-value: 1.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 1 MAAVEVRNGYKYYGSKSnpkiVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNG-----GEVVVLGAKPGEPG 75
Cdd:PRK14267 2 KFAIETVNLRVYYGSNH----VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEearveGEVRLFGRNIYSPD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 76 SGVPGSR--VGFMPQEIALVEEMTVKETIFYFGRIYGLT------DERIREKFKL------LKELLQLPPArqmikQCSG 141
Cdd:PRK14267 78 VDPIEVRreVGMVFQYPNPFPHLTIYDNVAIGVKLNGLVkskkelDERVEWALKKaalwdeVKDRLNDYPS-----NLSG 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 24582012 142 GQQRRLSFACAMIHDPELLILDEPTVGLDPMLREKIWDFLVETTRNskLAVIITTH 197
Cdd:PRK14267 153 GQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE--YTIVLVTH 206
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-217 |
1.33e-13 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 71.32 E-value: 1.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 1 MAAVEVRNGYKyygsKSNPKIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCI-------VGQRRLngGEVVVLGAKP-G 72
Cdd:PRK11264 1 MSAIEVKNLVK----KFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCInlleqpeAGTIRV--GDITIDTARSlS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 73 EPGSGVPGSR--VGFMPQEIALVEEMTVKETIfyfgrIYG---LTDERIREKFKLLKELLqlppARQMI--------KQC 139
Cdd:PRK11264 75 QQKGLIRQLRqhVGFVFQNFNLFPHRTVLENI-----IEGpviVKGEPKEEATARARELL----AKVGLagketsypRRL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 140 SGGQQRRLSFACAMIHDPELLILDEPTVGLDPMLREKIwdflVETTR---NSKLAVIITTHYIEEAKQ-ANCIGLMRNGV 215
Cdd:PRK11264 146 SGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEV----LNTIRqlaQEKRTMVIVTHEMSFARDvADRAIFMDQGR 221
|
..
gi 24582012 216 LL 217
Cdd:PRK11264 222 IV 223
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
4-214 |
1.55e-13 |
|
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: 70.44 E-value: 1.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 4 VEVRNGYKYYGSKSNpkiVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGAKPGEPGSGVPGSR- 82
Cdd:cd03290 1 VQVTNGYFSWGSGLA---TLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRn 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 83 ---VGFMPQEIALVEEmTVKETIFyFGRIYGltderiREKFKLLKELLQLPPARQMIK------------QCSGGQQRRL 147
Cdd:cd03290 78 rysVAYAAQKPWLLNA-TVEENIT-FGSPFN------KQRYKAVTDACSLQPDIDLLPfgdqteigergiNLSGGQRQRI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24582012 148 SFACAMIHDPELLILDEPTVGL-----DPMLREKIWDFLvettRNSKLAVIITTHYIEEAKQANCIGLMRNG 214
Cdd:cd03290 150 CVARALYQNTNIVFLDDPFSALdihlsDHLMQEGILKFL----QDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
22-221 |
1.58e-13 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 70.61 E-value: 1.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 22 VLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGAKPGEPGSG----VPGSRVGFMPQEIALVEEMT 97
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAakaeLRNQKLGFIYQFHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 98 VKETIFYFGRIYGLTDERIREK-FKLLKELLQLPPARQMIKQCSGGQQRRLSFACAMIHDPELLILDEPTVGLDPMLREK 176
Cdd:PRK11629 104 ALENVAMPLLIGKKKPAEINSRaLEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADS 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 24582012 177 IWDFLVETTRNSKLAVIITTHYIEEAKQANCIGLMRNGVLLAEDT 221
Cdd:PRK11629 184 IFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAELS 228
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
20-170 |
2.12e-13 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 73.76 E-value: 2.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 20 KIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNG--GEVVVLGAKPGEPGSgvpgSRVGFMPQEIALVEEMT 97
Cdd:PLN03211 81 RTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTKQIL----KRTGFVTQDDILYPHLT 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 98 VKETIFYFGRIY---GLT-DERIREKFKLLKEL-----LQLPPARQMIKQCSGGQQRRLSFACAMIHDPELLILDEPTVG 168
Cdd:PLN03211 157 VRETLVFCSLLRlpkSLTkQEKILVAESVISELgltkcENTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSG 236
|
..
gi 24582012 169 LD 170
Cdd:PLN03211 237 LD 238
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-202 |
2.59e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 70.33 E-value: 2.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 1 MAAVEVRNGYKYYGSKSnpkiVLNQLNMNVMRGSIYGLLGASGCGKTTLLscivgqRRLN-----------GGEVVVLGA 69
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVE----VLDGVNLEIPDNTITALMGPSGSGKSTLL------RVFNrlielypearvSGEVYLDGQ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 70 KPGEPGSGVPGSRVGFMPQEIALVEEMTVKETIFYFGRIYGLTD------ERIR---EKFKLLKEL---LQLPPARqmik 137
Cdd:PRK14247 71 DIFKMDVIELRRRVQMVFQIPNPIPNLSIFENVALGLKLNRLVKskkelqERVRwalEKAQLWDEVkdrLDAPAGK---- 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24582012 138 qCSGGQQRRLSFACAMIHDPELLILDEPTVGLDPMLREKIWDFLVETTRNskLAVIITTHYIEEA 202
Cdd:PRK14247 147 -LSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQA 208
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
18-197 |
2.67e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 69.52 E-value: 2.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 18 NPKIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVvlgAKPGEPGSGVPGSRVGFMPQEIALVEEMT 97
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIK---LDGGDIDDPDVAEACHYLGHRNAMKPALT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 98 VKETIFYFGRIYGLTDERIRE--KFKLLKELLQLPparqmIKQCSGGQQRRLSFACAMIHDPELLILDEPTVGLDP---- 171
Cdd:PRK13539 90 VAENLEFWAAFLGGEELDIAAalEAVGLAPLAHLP-----FGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAaava 164
|
170 180
....*....|....*....|....*.
gi 24582012 172 MLREkiwdfLVETTRNSKLAVIITTH 197
Cdd:PRK13539 165 LFAE-----LIRAHLAQGGIVIAATH 185
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
10-226 |
2.98e-13 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 70.38 E-value: 2.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 10 YKYYGSKSnpkiVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCI-------VGQRRLNGGEVVVLGAKPGEPGSG----- 77
Cdd:PRK10619 12 HKRYGEHE----VLKGVSLQANAGDVISIIGSSGSGKSTFLRCInflekpsEGSIVVNGQTINLVRDKDGQLKVAdknql 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 78 -VPGSRVGFMPQEIALVEEMTVKETIFYFG-RIYGLTDERIREK--FKLLKELLQLPPARQMIKQCSGGQQRRLSFACAM 153
Cdd:PRK10619 88 rLLRTRLTMVFQHFNLWSHMTVLENVMEAPiQVLGLSKQEARERavKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARAL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24582012 154 IHDPELLILDEPTVGLDPMLREKIWDFLVETTRNSKLAVIItTHYIEEAKQ-ANCIGLMRNGVLLAEDTPTNIM 226
Cdd:PRK10619 168 AMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVV-THEMGFARHvSSHVIFLHQGKIEEEGAPEQLF 240
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
12-214 |
4.47e-13 |
|
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: 69.44 E-value: 4.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 12 YYGSKSNPKIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGAKPGEPGSGVPGSRVGFMPQEIA 91
Cdd:cd03252 7 RFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGVVLQENV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 92 LVEEmTVKETIfyfgriyGLTD-----ERIREKFKLLKE---LLQLPPARQMI-----KQCSGGQQRRLSFACAMIHDPE 158
Cdd:cd03252 87 LFNR-SIRDNI-------ALADpgmsmERVIEAAKLAGAhdfISELPEGYDTIvgeqgAGLSGGQRQRIAIARALIHNPR 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 24582012 159 LLILDEPTVGLDPMLREKIWDFLVETTRNSklAVIITTHYIEEAKQANCIGLMRNG 214
Cdd:cd03252 159 ILIFDEATSALDYESEHAIMRNMHDICAGR--TVIIIAHRLSTVKNADRIIVMEKG 212
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
6-197 |
4.91e-13 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 69.57 E-value: 4.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 6 VRNGYKYYGsksnPKIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGaKPGEP----GSGVPGS 81
Cdd:PRK11701 9 VRGLTKLYG----PRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRM-RDGQLrdlyALSEAER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 82 RV------GFMPQEIALVEEMTVK------ETIFYFG-RIYGltdeRIREKFKLLKELLQLPPAR--QMIKQCSGGQQRR 146
Cdd:PRK11701 84 RRllrtewGFVHQHPRDGLRMQVSaggnigERLMAVGaRHYG----DIRATAGDWLERVEIDAARidDLPTTFSGGMQQR 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 24582012 147 LSFACAMIHDPELLILDEPTVGLDPMLREKIWDFLVETTRNSKLAVIITTH 197
Cdd:PRK11701 160 LQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTH 210
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
5-197 |
5.83e-13 |
|
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: 72.02 E-value: 5.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 5 EVRNGYKYYGSKSNPKIVLNQLNMNVMRGSIYGLLGASGCGKT-TLLS----------CIVGQRRLNGGEVvvLGAKPGE 73
Cdd:COG4172 8 SVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSilrllpdpaaHPSGSILFDGQDL--LGLSERE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 74 PgSGVPGSRVGFMPQE--IALVEEMTV----KETIfyfgRIY-GLTDERIREKFKLLKELLQLPPARQMIK----QCSGG 142
Cdd:COG4172 86 L-RRIRGNRIAMIFQEpmTSLNPLHTIgkqiAEVL----RLHrGLSGAAARARALELLERVGIPDPERRLDayphQLSGG 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 24582012 143 QQRRLSFACAMIHDPELLILDEPTVGLDPMLREKIWDFLVETTRNSKLAVIITTH 197
Cdd:COG4172 161 QRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITH 215
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
18-217 |
6.43e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 69.31 E-value: 6.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 18 NPKIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSC------IVGQRRLNGGEVVVLGAKPGEPGSGVPGSRVGFMPQEIA 91
Cdd:PRK14246 21 NDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVlnrlieIYDSKIKVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 92 LVEEMTVKETIFYFGRIYGLTDERirEKFKLLKELLQL------------PPARQMikqcSGGQQRRLSFACAMIHDPEL 159
Cdd:PRK14246 101 PFPHLSIYDNIAYPLKSHGIKEKR--EIKKIVEECLRKvglwkevydrlnSPASQL----SGGQQQRLTIARALALKPKV 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 24582012 160 LILDEPTVGLDPMLREKIWDFLVETTRnsKLAVIITTHYIEE-AKQANCIGLMRNGVLL 217
Cdd:PRK14246 175 LLMDEPTSMIDIVNSQAIEKLITELKN--EIAIVIVSHNPQQvARVADYVAFLYNGELV 231
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
22-205 |
6.59e-13 |
|
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: 68.61 E-value: 6.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 22 VLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGAkpgepgsgvpGSRVgfmpqEIALVEEMTV--- 98
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHD----------GGWV-----DLAQASPREIlal 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 99 -KETIFY---FGRI----------------YGLTDERIREK-------FKLLKELLQLPPArqmikQCSGGQQRRLSFAC 151
Cdd:COG4778 91 rRRTIGYvsqFLRViprvsaldvvaeplleRGVDREEARARarellarLNLPERLWDLPPA-----TFSGGEQQRVNIAR 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 24582012 152 AMIHDPELLILDEPTVGLDPmlrekiwdflvettrNSKLAVIittHYIEEAKQA 205
Cdd:COG4778 166 GFIADPPLLLLDEPTASLDA---------------ANRAVVV---ELIEEAKAR 201
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
22-219 |
6.67e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 71.59 E-value: 6.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 22 VLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGA--KPGEPGSGVpGSRVGFMP---QEIALVEEM 96
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKpvRIRSPRDAI-RAGIAYVPedrKGEGLVLDL 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 97 TVKE--TIFYFGRI--YGLTDER-IREKFKLLKELLQL--PPARQMIKQCSGGQQRRLSFACAMIHDPELLILDEPTVGL 169
Cdd:COG1129 346 SIREniTLASLDRLsrGGLLDRRrERALAEEYIKRLRIktPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGI 425
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 24582012 170 DPMLREKIWDFLVETTRNSKlAVIITTHYIEEAkqancIGL------MRNGVLLAE 219
Cdd:COG1129 426 DVGAKAEIYRLIRELAAEGK-AVIVISSELPEL-----LGLsdrilvMREGRIVGE 475
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
22-197 |
6.69e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 68.99 E-value: 6.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 22 VLNQLNMNVMRGSIYGLLGASGCGKTTLLScivgqrrlnggevVVLGAKpgEPGSGV----PGSRVGFMPQEIALveEMT 97
Cdd:PRK09544 19 VLSDVSLELKPGKILTLLGPNGAGKSTLVR-------------VVLGLV--APDEGVikrnGKLRIGYVPQKLYL--DTT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 98 VKETIFYFGRIY-GLTDERIREKFKLLK--ELLQLPparqmIKQCSGGQQRRLSFACAMIHDPELLILDEPTVGLDPMLR 174
Cdd:PRK09544 82 LPLTVNRFLRLRpGTKKEDILPALKRVQagHLIDAP-----MQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQ 156
|
170 180
....*....|....*....|...
gi 24582012 175 EKIWDFLVETTRNSKLAVIITTH 197
Cdd:PRK09544 157 VALYDLIDQLRRELDCAVLMVSH 179
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
22-197 |
6.85e-13 |
|
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: 68.15 E-value: 6.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 22 VLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVvLGAKPGEPGSGVPGSRVGFMPQEIALVEEMTVKET 101
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVR-WNGTPLAEQRDEPHENILYLGHLPGLKPELSALEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 102 IFYFGRIYGLTDERIREKFKL--LKELLQLPPArqmikQCSGGQQRRLSFACAMIHDPELLILDEPTVGLDPMLREKIWD 179
Cdd:TIGR01189 94 LHFWAAIHGGAQRTIEDALAAvgLTGFEDLPAA-----QLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAG 168
|
170
....*....|....*...
gi 24582012 180 FLVETTRNSKlAVIITTH 197
Cdd:TIGR01189 169 LLRAHLARGG-IVLLTTH 185
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-202 |
9.42e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 68.96 E-value: 9.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 4 VEVRNGYKYYGSKS-NPKIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGAKpgepgsgvpgsr 82
Cdd:COG1101 2 LELKNLSKTFNPGTvNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKD------------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 83 VGFMPQE-----IALV---------EEMTVKE--TIFY-----FGRIYGLTDERiREKFK-LLKEL-------LQLPpar 133
Cdd:COG1101 70 VTKLPEYkrakyIGRVfqdpmmgtaPSMTIEEnlALAYrrgkrRGLRRGLTKKR-RELFReLLATLglglenrLDTK--- 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24582012 134 qmIKQCSGGQQRRLSFACAMIHDPELLILDEPTVGLDPmlreKIWDFLVETTRN----SKLAVIITTHYIEEA 202
Cdd:COG1101 146 --VGLLSGGQRQALSLLMATLTKPKLLLLDEHTAALDP----KTAALVLELTEKiveeNNLTTLMVTHNMEQA 212
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
3-228 |
1.08e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 71.93 E-value: 1.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 3 AVEVRNGYKYYGSK-SNPkiVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQrrlnggevvvlgAKPGEPGSGVPGS 81
Cdd:PLN03232 614 AISIKNGYFSWDSKtSKP--TLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGE------------LSHAETSSVVIRG 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 82 RVGFMPQeIALVEEMTVKETIFyFGRIYglTDERIREKFKL--LKELLQLPPARQMIK------QCSGGQQRRLSFACAM 153
Cdd:PLN03232 680 SVAYVPQ-VSWIFNATVRENIL-FGSDF--ESERYWRAIDVtaLQHDLDLLPGRDLTEigergvNISGGQKQRVSMARAV 755
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24582012 154 IHDPELLILDEPTVGLDPMLREKIWDFLVETTRNSKLAVIITThyieeakQANCIGLMRNGVLLAEDtptniMIK 228
Cdd:PLN03232 756 YSNSDIYIFDDPLSALDAHVAHQVFDSCMKDELKGKTRVLVTN-------QLHFLPLMDRIILVSEG-----MIK 818
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
20-226 |
1.22e-12 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 68.70 E-value: 1.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 20 KIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQ----RRLNGGEVVVLGAKPGEPGSGVPGSRV----GFMPQEIA 91
Cdd:PRK13547 14 RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDltggGAPRGARVTGDVTLNGEPLAAIDAPRLarlrAVLPQAAQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 92 LVEEMTVKETI----FYFGRIYGLTDERIREkfkLLKELLQL----PPARQMIKQCSGGQQRRLSFA--CAMIH------ 155
Cdd:PRK13547 94 PAFAFSAREIVllgrYPHARRAGALTHRDGE---IAWQALALagatALVGRDVTTLSGGELARVQFArvLAQLWpphdaa 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24582012 156 -DPELLILDEPTVGLDPMLREKIWDFLVETTRNSKLAVIITTHYIE-EAKQANCIGLMRNGVLLAEDTPTNIM 226
Cdd:PRK13547 171 qPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNlAARHADRIAMLADGAIVAHGAPADVL 243
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
23-197 |
1.39e-12 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 67.59 E-value: 1.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 23 LNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGAKPGE-PGSGVPGSR--VGFMPQEIALVEEMTVK 99
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRlKNREVPFLRrqIGMIFQDHHLLMDRTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 100 ETIFYFGRIYGLTDERIREKFKL-LKELLQLPPARQMIKQCSGGQQRRLSFACAMIHDPELLILDEPTVGLDPMLREKIW 178
Cdd:PRK10908 98 DNVAIPLIIAGASGDDIRRRVSAaLDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGIL 177
|
170
....*....|....*....
gi 24582012 179 DFLVETTRnSKLAVIITTH 197
Cdd:PRK10908 178 RLFEEFNR-VGVTVLMATH 195
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
21-231 |
1.64e-12 |
|
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: 67.56 E-value: 1.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 21 IVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIvgQR--RLNGGEVVVLGAKPGEPGSGVPGSRVGFMPQEIALVEeMTV 98
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLL--ERfyDPTSGEILLDGVDIRDLNLRWLRSQIGLVSQEPVLFD-GTI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 99 KETIFYfGRiYGLTDERIREKFKL---LKELLQLP-----PARQMIKQCSGGQQRRLSFACAMIHDPELLILDEPTVGLD 170
Cdd:cd03249 94 AENIRY-GK-PDATDEEVEEAAKKaniHDFIMSLPdgydtLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALD 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24582012 171 P----MLREKIWDFLVETTrnsklaVIITTHYIEEAKQANCIGLMRNGVLLAEDTPTNIMIKFGT 231
Cdd:cd03249 172 AesekLVQEALDRAMKGRT------TIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGV 230
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
2-173 |
2.10e-12 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 67.90 E-value: 2.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 2 AAVEVRNGYKYYGSKSnpkiVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVV----LGAKPGEPGSG 77
Cdd:COG4598 7 PALEVRDLHKSFGDLE----VLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVggeeIRLKPDRDGEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 78 VPG---------SRVGFMPQEIALVEEMTVKETIFyFGRIY--GLTDERIREKFKLLKELLQLPPARQMI-KQCSGGQQR 145
Cdd:COG4598 83 VPAdrrqlqrirTRLGMVFQSFNLWSHMTVLENVI-EAPVHvlGRPKAEAIERAEALLAKVGLADKRDAYpAHLSGGQQQ 161
|
170 180
....*....|....*....|....*...
gi 24582012 146 RLSFACAMIHDPELLILDEPTVGLDPML 173
Cdd:COG4598 162 RAAIARALAMEPEVMLFDEPTSALDPEL 189
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
11-220 |
2.71e-12 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 67.40 E-value: 2.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 11 KYYGSKSnpkiVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVlGAKPgePGSGVPGSRVGFmpQEI 90
Cdd:PRK11247 20 KRYGERT----VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLA-GTAP--LAEAREDTRLMF--QDA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 91 ALveeMTVKETIFYFGriYGLTDERIREKFKLLKELLQLPPARQMIKQCSGGQQRRLSFACAMIHDPELLILDEPTVGLD 170
Cdd:PRK11247 91 RL---LPWKKVIDNVG--LGLKGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 24582012 171 PMLREKIWDFLVETTRNSKLAVIITTHYIEEAKQanciglMRNGVLLAED 220
Cdd:PRK11247 166 ALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVA------MADRVLLIEE 209
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
3-197 |
4.21e-12 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 69.51 E-value: 4.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 3 AVEVRN-GYKYYGSKSNpkiVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGAKPGEPGSGVPGS 81
Cdd:TIGR03375 463 EIEFRNvSFAYPGQETP---ALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADLRR 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 82 RVGFMPQEIALVEEmTVKETIFYFGRiyGLTDERIREKFKL--LKELLQLPPA--RQMI----KQCSGGQQRRLSFACAM 153
Cdd:TIGR03375 540 NIGYVPQDPRLFYG-TLRDNIALGAP--YADDEEILRAAELagVTEFVRRHPDglDMQIgergRSLSGGQRQAVALARAL 616
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 24582012 154 IHDPELLILDEPTVGLD----PMLREKIWDFLVETTrnsklaVIITTH 197
Cdd:TIGR03375 617 LRDPPILLLDEPTSAMDnrseERFKDRLKRWLAGKT------LVLVTH 658
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
18-238 |
5.60e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 66.83 E-value: 5.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 18 NPKIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGAKPGEpgsGVPGSRVGFMPQ--EI----- 90
Cdd:PRK15056 18 NGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ---ALQKNLVAYVPQseEVdwsfp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 91 ALVEEMTVKETIFYFG--RIYGLTDERIREkfKLLKELLQLPPARQMIKQCSGGQQRRLSFACAMIHDPELLILDEPTVG 168
Cdd:PRK15056 95 VLVEDVVMMGRYGHMGwlRRAKKRDRQIVT--AALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTG 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 169 LDPMLREKIWDFLVEtTRNSKLAVIITTHYIEEAKQANCIGLMRNGVLLAEDtPTNimIKFGTQSIEDAF 238
Cdd:PRK15056 173 VDVKTEARIISLLRE-LRDEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASG-PTE--TTFTAENLELAF 238
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
4-208 |
5.91e-12 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 68.50 E-value: 5.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 4 VEVRNGYKYYgsksNPKIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVG---QRRLNggEVVVLGAKPGEpgsgvpG 80
Cdd:PRK10938 261 IVLNNGVVSY----NDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGdhpQGYSN--DLTLFGRRRGS------G 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 81 SRVGFMPQEIALVE---------EMTVKETIF--YFGRI--YGLTDERIREKFKLLKELLQLPP--ARQMIKQCSGGQQR 145
Cdd:PRK10938 329 ETIWDIKKHIGYVSsslhldyrvSTSVRNVILsgFFDSIgiYQAVSDRQQKLAQQWLDILGIDKrtADAPFHSLSWGQQR 408
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24582012 146 RLSFACAMIHDPELLILDEPTVGLDPMLREKIWDFLVETTRNSKLAVIITTHYIEEAkqANCI 208
Cdd:PRK10938 409 LALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSHHAEDA--PACI 469
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
25-204 |
6.90e-12 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 65.76 E-value: 6.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 25 QLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVlgakPGEPGSGVPGSR--VGFMPQEIALVEEMTVKETI 102
Cdd:PRK10771 17 RFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTL----NGQDHTTTPPSRrpVSMLFQENNLFSHLTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 103 fYFGRIYGL--------TDERIREKFKLLKELLQLPparqmiKQCSGGQQRRLSFACAMIHDPELLILDEPTVGLDPMLR 174
Cdd:PRK10771 93 -GLGLNPGLklnaaqreKLHAIARQMGIEDLLARLP------GQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALR 165
|
170 180 190
....*....|....*....|....*....|
gi 24582012 175 EKIWDFLVETTRNSKLAVIITTHYIEEAKQ 204
Cdd:PRK10771 166 QEMLTLVSQVCQERQLTLLMVSHSLEDAAR 195
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
11-170 |
7.16e-12 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 68.61 E-value: 7.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 11 KYYGSKsnpKIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLgakpgepgsgvPGSRVGFMPQEI 90
Cdd:PRK11819 14 KVVPPK---KQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPA-----------PGIKVGYLPQEP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 91 ALVEEMTVKETIFY-FGRIYGLTDE--RIREKF--------KLLKEL-------------------------LQLPPARQ 134
Cdd:PRK11819 80 QLDPEKTVRENVEEgVAEVKAALDRfnEIYAAYaepdadfdALAAEQgelqeiidaadawdldsqleiamdaLRCPPWDA 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 24582012 135 MIKQCSGGQQRRLSFACAMIHDPELLILDEPTVGLD 170
Cdd:PRK11819 160 KVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD 195
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
4-170 |
7.22e-12 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 67.06 E-value: 7.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 4 VEVRNGYKYYGSKS-----NPKIV--LNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGakpgEPGS 76
Cdd:COG4608 8 LEVRDLKKHFPVRGglfgrTVGVVkaVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDG----QDIT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 77 GVPGSRVGFMPQEIALV---------EEMTVKETIfyfG---RIYGLTD-----ERIREkfkLLkELLQLPP--ARQMIK 137
Cdd:COG4608 84 GLSGRELRPLRRRMQMVfqdpyaslnPRMTVGDII---AeplRIHGLASkaerrERVAE---LL-ELVGLRPehADRYPH 156
|
170 180 190
....*....|....*....|....*....|...
gi 24582012 138 QCSGGQQRRLSFACAMIHDPELLILDEPTVGLD 170
Cdd:COG4608 157 EFSGGQRQRIGIARALALNPKLIVCDEPVSALD 189
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
4-197 |
7.48e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 67.03 E-value: 7.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 4 VEVRNGYKYYGSKSNPKI-VLNQLNMNVMRGSIYGLLGASGCGKTTLLscivgqRRLNG------GEVV------VLGAK 70
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTELkALDNVSVEINQGEFIAIIGQTGSGKTTFI------EHLNAlllpdtGTIEwifkdeKNKKK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 71 PGEPGSGVPG------------------SRVGFMPQ--EIALVEEmTVKETIFYFGRIYGLTDERIREKFKLLKELLQLP 130
Cdd:PRK13651 77 TKEKEKVLEKlviqktrfkkikkikeirRRVGVVFQfaEYQLFEQ-TIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLD 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24582012 131 paRQMIKQC----SGGQQRRLSFACAMIHDPELLILDEPTVGLDPMLREKIWDFLVETTRNSKlAVIITTH 197
Cdd:PRK13651 156 --ESYLQRSpfelSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGK-TIILVTH 223
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
20-197 |
7.55e-12 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 68.30 E-value: 7.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 20 KIVLNQLNMNVMRGSiyGLL--GASGCGKTTLLscivgqRRLNG------GEVVVlgakpgePgsgvPGSRVGFMPQEIA 91
Cdd:COG4178 376 RPLLEDLSLSLKPGE--RLLitGPSGSGKSTLL------RAIAGlwpygsGRIAR-------P----AGARVLFLPQRPY 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 92 LVEEmTVKETIFYFGRIYGLTDERIREkfkLLkELLQLPPARQMI-------KQCSGGQQRRLSFACAMIHDPELLILDE 164
Cdd:COG4178 437 LPLG-TLREALLYPATAEAFSDAELRE---AL-EAVGLGHLAERLdeeadwdQVLSLGEQQRLAFARLLLHKPDWLFLDE 511
|
170 180 190
....*....|....*....|....*....|...
gi 24582012 165 PTVGLDPMLREKIWDFLVETTRNSklAVIITTH 197
Cdd:COG4178 512 ATSALDEENEAALYQLLREELPGT--TVISVGH 542
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
17-194 |
7.94e-12 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 68.13 E-value: 7.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 17 SNPKIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGAKPGEPGsgvPGSR----VGFMPQE--- 89
Cdd:COG3845 268 DRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLS---PRERrrlgVAYIPEDrlg 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 90 IALVEEMTVKE----TIFY-----------FGRIYGLTDERIrEKFKllkelLQLPPARQMIKQCSGGQQRRLSFACAMI 154
Cdd:COG3845 345 RGLVPDMSVAEnlilGRYRrppfsrggfldRKAIRAFAEELI-EEFD-----VRTPGPDTPARSLSGGNQQKVILARELS 418
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 24582012 155 HDPELLILDEPTVGLDPMLREKIWDFLVEtTRNSKLAVII 194
Cdd:COG3845 419 RDPKLLIAAQPTRGLDVGAIEFIHQRLLE-LRDAGAAVLL 457
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
26-226 |
8.40e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 65.72 E-value: 8.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 26 LNMNVMRGSIYGLLGASGCGKTTLLSCIVGQrrLNG-GEVVVLGAkpgePGSGVPGS----RVGFMPQEIALVEEMTVke 100
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGL--LPGsGSIQFAGQ----PLEAWSAAelarHRAYLSQQQTPPFAMPV-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 101 tiFYFGRIYGLTDERIREKFKLLKEL---LQLPP--ARqMIKQCSGGQ-QR-RLSFACAMIH---DPE--LLILDEPTVG 168
Cdd:PRK03695 87 --FQYLTLHQPDKTRTEAVASALNEVaeaLGLDDklGR-SVNQLSGGEwQRvRLAAVVLQVWpdiNPAgqLLLLDEPMNS 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 24582012 169 LDpMLREKIWDFLVETTRNSKLAVIITTHYIEE-AKQANCIGLMRNGVLLAEDTPTNIM 226
Cdd:PRK03695 164 LD-VAQQAALDRLLSELCQQGIAVVMSSHDLNHtLRHADRVWLLKQGKLLASGRRDEVL 221
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
23-225 |
1.16e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 65.92 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 23 LNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGA--KPGEPGSGVPGSR--VGFMPQ--EIALVEEM 96
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTliTSTSKNKDIKQIRkkVGLVFQfpESQLFEET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 97 TVKETIF---YFGRIYGLTDERIREKFKLL---KELLQLPPArqmikQCSGGQQRRLSFACAMIHDPELLILDEPTVGLD 170
Cdd:PRK13649 103 VLKDVAFgpqNFGVSQEEAEALAREKLALVgisESLFEKNPF-----ELSGGQMRRVAIAGILAMEPKILVLDEPTAGLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 24582012 171 PMLREKIWDfLVETTRNSKLAVIITTHYIEE-AKQANCIGLMRNGVLLAEDTPTNI 225
Cdd:PRK13649 178 PKGRKELMT-LFKKLHQSGMTIVLVTHLMDDvANYADFVYVLEKGKLVLSGKPKDI 232
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-229 |
1.31e-11 |
|
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: 67.52 E-value: 1.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 4 VEVRNGYKYYGSKSnpkiVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVG--QRRLNGGEV------------VVLGA 69
Cdd:TIGR03269 1 IEVKNLTKKFDGKE----VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIiyhvalcekcgyVERPS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 70 KPGEPGSGVPGS---------------------RVGFMPQE-IALVEEMTVKETIF-------YFGriygltDERIREKF 120
Cdd:TIGR03269 77 KVGEPCPVCGGTlepeevdfwnlsdklrrrirkRIAIMLQRtFALYGDDTVLDNVLealeeigYEG------KEAVGRAV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 121 KLLKELLQLPPARQMIKQCSGGQQRRLSFACAMIHDPELLILDEPTVGLDPMLREKIWDFLVETTRNSKLAVIITTHYIE 200
Cdd:TIGR03269 151 DLIEMVQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPE 230
|
250 260 270
....*....|....*....|....*....|
gi 24582012 201 E-AKQANCIGLMRNGVLLAEDTPTNIMIKF 229
Cdd:TIGR03269 231 ViEDLSDKAIWLENGEIKEEGTPDEVVAVF 260
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
22-214 |
1.38e-11 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 65.65 E-value: 1.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 22 VLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRrlnggevvvlgakpgEPGSGV--PGSRVGFMPQeIALVEEMTVK 99
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGEL---------------EPSEGKikHSGRISFSSQ-FSWIMPGTIK 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 100 ETIfyfgrIYGLTDERIREKF-----KLLKELLQLPPARQMIK-----QCSGGQQRRLSFACAMIHDPELLILDEPTVGL 169
Cdd:cd03291 116 ENI-----IFGVSYDEYRYKSvvkacQLEEDITKFPEKDNTVLgeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYL 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 24582012 170 DPMLREKIWDFLVETTRNSKLAVIITTHyIEEAKQANCIGLMRNG 214
Cdd:cd03291 191 DVFTEKEIFESCVCKLMANKTRILVTSK-MEHLKKADKILILHEG 234
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
20-195 |
1.60e-11 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 63.33 E-value: 1.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 20 KIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVvlgaKPgepgsgvPGSRVGFMPQEialveemtvk 99
Cdd:cd03223 14 RVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIG----MP-------EGEDLLFLPQR---------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 100 eTIFYFGRiygltderirekfklLKELLQLPPARQMikqcSGGQQRRLSFACAMIHDPELLILDEPTVGLDPMLREKIWD 179
Cdd:cd03223 73 -PYLPLGT---------------LREQLIYPWDDVL----SGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQ 132
|
170
....*....|....*.
gi 24582012 180 FLVEttrnsKLAVIIT 195
Cdd:cd03223 133 LLKE-----LGITVIS 143
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
23-214 |
2.40e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 66.49 E-value: 2.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 23 LNQLNMNVMRGSIYGLLGASGCGKTTL---LSCIV------GQRRLNGGEVVVLGAKPGEpgsgvpgsRVG--FMPQEIA 91
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLmkvLSGVYphgtyeGEIIFEGEELQASNIRDTE--------RAGiaIIHQELA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 92 LVEEMTVKETIF------YFGRI-YgltDERIREKFKLLKEL-LQLPPArQMIKQCSGGQQRRLSFACAMIHDPELLILD 163
Cdd:PRK13549 93 LVKELSVLENIFlgneitPGGIMdY---DAMYLRAQKLLAQLkLDINPA-TPVGNLGLGQQQLVEIAKALNKQARLLILD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 24582012 164 EPTVGLDPMLREKIWDfLVETTRNSKLAVIITTHYIEEAKQ-ANCIGLMRNG 214
Cdd:PRK13549 169 EPTASLTESETAVLLD-IIRDLKAHGIACIYISHKLNEVKAiSDTICVIRDG 219
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
4-226 |
2.53e-11 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 66.66 E-value: 2.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 4 VEVRNGYKYYGSKSNPkiVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGAKPGEPGSGVPGSRV 83
Cdd:TIGR02203 331 VEFRNVTFRYPGRDRP--ALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQV 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 84 GFMPQEIALVEEmTVKETIFYfGRIYGLTDERIREKFKL--LKELL-QLP-----PARQMIKQCSGGQQRRLSFACAMIH 155
Cdd:TIGR02203 409 ALVSQDVVLFND-TIANNIAY-GRTEQADRAEIERALAAayAQDFVdKLPlgldtPIGENGVLLSGGQRQRLAIARALLK 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24582012 156 DPELLILDEPTVGLDPMLREKIWDFLVETTRNSKLAVIitTHYIEEAKQANCIGLMRNGVLLAEDTPTNIM 226
Cdd:TIGR02203 487 DAPILILDEATSALDNESERLVQAALERLMQGRTTLVI--AHRLSTIEKADRIVVMDDGRIVERGTHNELL 555
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
13-226 |
2.62e-11 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 64.62 E-value: 2.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 13 YGSKsnpkIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGAKPGEPGSGVPGSRVGFMPQEIAL 92
Cdd:PRK10253 17 YGKY----TVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 93 VEEMTVKETIF--------YFGRiYGLTDERIREKFKLLKELLQLppARQMIKQCSGGQQRRLSFACAMIHDPELLILDE 164
Cdd:PRK10253 93 PGDITVQELVArgryphqpLFTR-WRKEDEEAVTKAMQATGITHL--ADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24582012 165 PTVGLDPMLREKIWDFLVETTRNSKLAVIITTHYIEEA-KQANCIGLMRNGVLLAEDTPTNIM 226
Cdd:PRK10253 170 PTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQAcRYASHLIALREGKIVAQGAPKEIV 232
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
3-214 |
3.03e-11 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 67.28 E-value: 3.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 3 AVEVRNGyKYYGSKSNPKiVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGAkpgepgsgvpgsr 82
Cdd:TIGR00957 636 SITVHNA-TFTWARDLPP-TLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS------------- 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 83 VGFMPQEiALVEEMTVKETIFyFGRiyGLTDERIR---EKFKLLKELLQLPPA-RQMIKQ----CSGGQQRRLSFACAMI 154
Cdd:TIGR00957 701 VAYVPQQ-AWIQNDSLRENIL-FGK--ALNEKYYQqvlEACALLPDLEILPSGdRTEIGEkgvnLSGGQKQRVSLARAVY 776
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24582012 155 HDPELLILDEPTVGLDPMLREKIWD-------FLVETTRnsklavIITTHYIEEAKQANCIGLMRNG 214
Cdd:TIGR00957 777 SNADIYLFDDPLSAVDAHVGKHIFEhvigpegVLKNKTR------ILVTHGISYLPQVDVIIVMSGG 837
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
16-197 |
3.27e-11 |
|
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: 63.03 E-value: 3.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 16 KSNPKIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIvGQRRLNG---GEVVVLGAKPGEPGSgvpgSRVGFMPQEIAL 92
Cdd:cd03232 16 KGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVL-AGRKTAGvitGEILINGRPLDKNFQ----RSTGYVEQQDVH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 93 VEEMTVKETIFYFGRIYGLTDErirekfkllkellqlpparqmikqcsggQQRRLSFACAMIHDPELLILDEPTVGLDPM 172
Cdd:cd03232 91 SPNLTVREALRFSALLRGLSVE----------------------------QRKRLTIGVELAAKPSILFLDEPTSGLDSQ 142
|
170 180
....*....|....*....|....*
gi 24582012 173 LREKIWDFLvETTRNSKLAVIITTH 197
Cdd:cd03232 143 AAYNIVRFL-KKLADSGQAILCTIH 166
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
4-221 |
3.37e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 66.23 E-value: 3.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 4 VEVRNGYKYYGSKSnpkiVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGaKPGEPGSGVPGSRV 83
Cdd:PRK15439 12 LCARSISKQYSGVE----VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGG-NPCARLTPAKAHQL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 84 G--FMPQEIALVEEMTVKETIfyfgrIYGLTDERIREK--FKLLKEL-LQLPPA----------RQMIKQCSGgqqrrls 148
Cdd:PRK15439 87 GiyLVPQEPLLFPNLSVKENI-----LFGLPKRQASMQkmKQLLAALgCQLDLDssagslevadRQIVEILRG------- 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24582012 149 facaMIHDPELLILDEPTVGLDPMLREKIWDFLVEtTRNSKLAVIITTHYIEEAKQ-ANCIGLMRNG-VLLAEDT 221
Cdd:PRK15439 155 ----LMRDSRILILDEPTASLTPAETERLFSRIRE-LLAQGVGIVFISHKLPEIRQlADRISVMRDGtIALSGKT 224
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
11-197 |
3.45e-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: 66.11 E-value: 3.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 11 KYYGSKsnpKIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEvvvlgAKPGepgsgvPGSRVGFMPQEI 90
Cdd:TIGR03719 12 KVVPPK---KEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGE-----ARPQ------PGIKVGYLPQEP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 91 ALVEEMTVKETIFY-FGRIYGLTDE--RIREKF--------KLLKEL-------------------------LQLPPARQ 134
Cdd:TIGR03719 78 QLDPTKTVRENVEEgVAEIKDALDRfnEISAKYaepdadfdKLAAEQaelqeiidaadawdldsqleiamdaLRCPPWDA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24582012 135 MIKQCSGGQQRRLSFACAMIHDPELLILDEPTVGLDPmlrEKIwDFLVETTRNSKLAVIITTH 197
Cdd:TIGR03719 158 DVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDA---ESV-AWLERHLQEYPGTVVAVTH 216
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-223 |
4.00e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 64.35 E-value: 4.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 1 MAAVEVRNGYKyygsksnPKIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCI------VGQRRLNGGevVVLGAKPGEP 74
Cdd:PRK14271 22 MAAVNLTLGFA-------GKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLnrmndkVSGYRYSGD--VLLGGRSIFN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 75 GSGVPG--SRVGFMPQEIALVEeMTVKETIFYFGRIY---------GLTDERIREK--FKLLKELLQLPPARqmikqCSG 141
Cdd:PRK14271 93 YRDVLEfrRRVGMLFQRPNPFP-MSIMDNVLAGVRAHklvprkefrGVAQARLTEVglWDAVKDRLSDSPFR-----LSG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 142 GQQRRLSFACAMIHDPELLILDEPTVGLDPMLREKIWDFLveTTRNSKLAVIITTHYIEEAKQ-ANCIGLMRNGVLLaED 220
Cdd:PRK14271 167 GQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFI--RSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLV-EE 243
|
...
gi 24582012 221 TPT 223
Cdd:PRK14271 244 GPT 246
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
3-170 |
4.13e-11 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 66.07 E-value: 4.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 3 AVEVRNGYKYYGSKSnpkiVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVvvlgaKPGEpgsgvpGSR 82
Cdd:PRK15064 319 ALEVENLTKGFDNGP----LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV-----KWSE------NAN 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 83 VGFMPQEIA--LVEEMTVKETIFYFgRIYGLTDERIREkfKLLKELLQLPPARQMIKQCSGGQQRRLSFACAMIHDPELL 160
Cdd:PRK15064 384 IGYYAQDHAydFENDLTLFDWMSQW-RQEGDDEQAVRG--TLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVL 460
|
170
....*....|
gi 24582012 161 ILDEPTVGLD 170
Cdd:PRK15064 461 VMDEPTNHMD 470
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
12-202 |
6.74e-11 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 63.26 E-value: 6.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 12 YYGSKsnpkIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIvgqRRLNG--------GEVVVLGAKPGEPG---SGVPg 80
Cdd:PRK14243 19 YYGSF----LAVKNVWLDIPKNQITAFIGPSGCGKSTILRCF---NRLNDlipgfrveGKVTFHGKNLYAPDvdpVEVR- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 81 SRVGFMPQEIALVEEmTVKETIFYFGRIYGLT---DERIRekfKLLKELLQLPPARQMIKQC----SGGQQRRLSFACAM 153
Cdd:PRK14243 91 RRIGMVFQKPNPFPK-SIYDNIAYGARINGYKgdmDELVE---RSLRQAALWDEVKDKLKQSglslSGGQQQRLCIARAI 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 24582012 154 IHDPELLILDEPTVGLDPMLREKIWDFLVETTRnsKLAVIITTHYIEEA 202
Cdd:PRK14243 167 AVQPEVILMDEPCSALDPISTLRIEELMHELKE--QYTIIIVTHNMQQA 213
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4-214 |
7.91e-11 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 64.85 E-value: 7.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 4 VEVRNGYKYYGSKSnpkiVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIV---------GQRRLNGGEVVVLGAKPGEP 74
Cdd:TIGR02633 2 LEMKGIVKTFGGVK----ALDGIDLEVRPGECVGLCGENGAGKSTLMKILSgvyphgtwdGEIYWSGSPLKASNIRDTER 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 75 GSgvpgsrVGFMPQEIALVEEMTVKETIFYFGRIY---GLTD--ERIREKFKLLKEL-LQLPPARQMIKQCSGGQQRRLS 148
Cdd:TIGR02633 78 AG------IVIIHQELTLVPELSVAENIFLGNEITlpgGRMAynAMYLRAKNLLRELqLDADNVTRPVGDYGGGQQQLVE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24582012 149 FACAMIHDPELLILDEPTVGLDPMLREKIWDfLVETTRNSKLAVIITTHYIEEAKQ-ANCIGLMRNG 214
Cdd:TIGR02633 152 IAKALNKQARLLILDEPSSSLTEKETEILLD-IIRDLKAHGVACVYISHKLNEVKAvCDTICVIRDG 217
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
20-230 |
8.88e-11 |
|
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: 62.63 E-value: 8.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 20 KIVLNQLNMNVMRGSIYGLLGASGCGKTTLLscivgqrRL-------NGGEVVVlgakPGEPGSGVP----GSRVGFMPQ 88
Cdd:cd03253 14 RPVLKDVSFTIPAGKKVAIVGPSGSGKSTIL-------RLlfrfydvSSGSILI----DGQDIREVTldslRRAIGVVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 89 EIALVEEmtvkeTIFY---FGRIyGLTDERIREKFKLLK---ELLQLPPARQMI-----KQCSGGQQRRLSFACAMIHDP 157
Cdd:cd03253 83 DTVLFND-----TIGYnirYGRP-DATDEEVIEAAKAAQihdKIMRFPDGYDTIvgergLKLSGGEKQRVAIARAILKNP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24582012 158 ELLILDEPTVGLDPMLREKIWDFLVETTRNSKLAVIitTHYIEEAKQANCIGLMRNGVLLAEDTPTNIMIKFG 230
Cdd:cd03253 157 PILLLDEATSALDTHTEREIQAALRDVSKGRTTIVI--AHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGG 227
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-222 |
1.17e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 62.83 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 1 MAAVEVRN-GYKYYGSKSNPkiVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGAKPGEpgsgvp 79
Cdd:PRK13650 2 SNIIEVKNlTFKYKEDQEKY--TLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTE------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 80 gSRVGFMPQEIALVEE--------MTVKETIFYFGRIYGLTDERIREKfklLKELLQL---------PPARqmikqCSGG 142
Cdd:PRK13650 74 -ENVWDIRHKIGMVFQnpdnqfvgATVEDDVAFGLENKGIPHEEMKER---VNEALELvgmqdfkerEPAR-----LSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 143 QQRRLSFACAMIHDPELLILDEPTVGLDPMLREKiwdfLVETTRNSK----LAVIITTHYIEEAKQANCIGLMRNGVLLA 218
Cdd:PRK13650 145 QKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLE----LIKTIKGIRddyqMTVISITHDLDEVALSDRVLVMKNGQVES 220
|
....
gi 24582012 219 EDTP 222
Cdd:PRK13650 221 TSTP 224
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
4-255 |
1.69e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 62.42 E-value: 1.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 4 VEVRNGYKYYGSKSNpkivLNQLN---MNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGAKpgepgsgVPG 80
Cdd:PRK13642 5 LEVENLVFKYEKESD----VNQLNgvsFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGEL-------LTA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 81 SRVGFMPQEIALVEE--------MTVKETIFYFGRIYGLT-DERIREKFKLLKELLQLPPARQMIKQCSGGQQRRLSFAC 151
Cdd:PRK13642 74 ENVWNLRRKIGMVFQnpdnqfvgATVEDDVAFGMENQGIPrEEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 152 AMIHDPELLILDEPTVGLDPMLREKIWDFLVETTRNSKLAVIITTHYIEEAKQANCIGLMRNGVLLAEDTPTNI------ 225
Cdd:PRK13642 154 IIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELfatsed 233
|
250 260 270
....*....|....*....|....*....|....*....
gi 24582012 226 MIKFGTQSIEDAFLI---------LSQRQGNEDELAQIM 255
Cdd:PRK13642 234 MVEIGLDVPFSSNLMkdlrkngfdLPEKYLSEDELVELL 272
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
22-215 |
1.73e-10 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 64.55 E-value: 1.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 22 VLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGakpgepgsgvpgsRVGFMPQeIALVEEMTVKET 101
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------RISFSPQ-TSWIMPGTIKDN 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 102 IfyfgrIYGLT-DE-RIREKFKL--LKELLQLPPARQMIK------QCSGGQQRRLSFACAMIHDPELLILDEPTVGLDP 171
Cdd:TIGR01271 507 I-----IFGLSyDEyRYTSVIKAcqLEEDIALFPEKDKTVlgeggiTLSGGQRARISLARAVYKDADLYLLDSPFTHLDV 581
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 24582012 172 MLREKIWDFLVETTRNSKLAVIITTHyIEEAKQANCIGLMRNGV 215
Cdd:TIGR01271 582 VTEKEIFESCLCKLMSNKTRILVTSK-LEHLKKADKILLLHEGV 624
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
5-226 |
2.12e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 63.65 E-value: 2.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 5 EVRNgykyYGSKSNPKIvlNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGA--KPGEP------GS 76
Cdd:PRK09700 267 EVRN----VTSRDRKKV--RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKdiSPRSPldavkkGM 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 77 G-VPGSR--VGFMPQeIALVEEMTVKETIFY--FGRIYGLTDERIREKF-KLLKELLQLPPA--RQMIKQCSGGQQRRLS 148
Cdd:PRK09700 341 AyITESRrdNGFFPN-FSIAQNMAISRSLKDggYKGAMGLFHEVDEQRTaENQRELLALKCHsvNQNITELSGGNQQKVL 419
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24582012 149 FACAMIHDPELLILDEPTVGLDPMLREKIWDFLVETTRNSKLAVIITTHYIEEAKQANCIGLMRNGVLLAEDTPTNIM 226
Cdd:PRK09700 420 ISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRDDM 497
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
33-197 |
2.41e-10 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 62.42 E-value: 2.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 33 GSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGaKPGEPGSGVPGSRVGFMPQEI------ALVEEMTVKETIFYFG 106
Cdd:PRK15079 47 GETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLG-KDLLGMKDDEWRAVRSDIQMIfqdplaSLNPRMTIGEIIAEPL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 107 RIY--GLTDERIREKFKLLKELLQLPParQMIK----QCSGGQQRRLSFACAMIHDPELLILDEPTVGLDPMLREKIWDF 180
Cdd:PRK15079 126 RTYhpKLSRQEVKDRVKAMMLKVGLLP--NLINryphEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNL 203
|
170
....*....|....*..
gi 24582012 181 LVETTRNSKLAVIITTH 197
Cdd:PRK15079 204 LQQLQREMGLSLIFIAH 220
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
16-225 |
3.44e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 61.31 E-value: 3.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 16 KSNPKIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVlgakpgePGSGVPGSRVGFMPQEIALV-- 93
Cdd:PRK13648 18 QSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFY-------NNQAITDDNFEKLRKHIGIVfq 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 94 --EEMTVKETIFYfGRIYGL------TDERIREKFKLLKELLQLPPARQMIKQCSGGQQRRLSFACAMIHDPELLILDEP 165
Cdd:PRK13648 91 npDNQFVGSIVKY-DVAFGLenhavpYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 166 TVGLDPMLREKIWDFLVETTRNSKLAVIITTHYIEEAKQANCIGLMRNGVLLAEDTPTNI 225
Cdd:PRK13648 170 TSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEI 229
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
22-216 |
3.81e-10 |
|
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: 60.56 E-value: 3.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 22 VLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGaKPgepgsgVPGSRVGFMPQEIALVEEmtvkET 101
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDG-KP------ISQYEHKYLHSKVSLVGQ----EP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 102 IFYFGRI-----YGLTDErireKFKLLKELLQLPPARQMIK---------------QCSGGQQRRLSFACAMIHDPELLI 161
Cdd:cd03248 98 VLFARSLqdniaYGLQSC----SFECVKEAAQKAHAHSFISelasgydtevgekgsQLSGGQKQRVAIARALIRNPQVLI 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 24582012 162 LDEPTVGLDPMLREKIWDFLVETTRNSKLAVIitTHYIEEAKQANCIGLMRNGVL 216
Cdd:cd03248 174 LDEATSALDAESEQQVQQALYDWPERRTVLVI--AHRLSTVERADQILVLDGGRI 226
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
20-219 |
7.72e-10 |
|
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: 59.08 E-value: 7.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 20 KIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQrrlnggevvvlgakpgePGSGVPGSRVGFMPQEIAlveEMTVk 99
Cdd:cd03217 13 KEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGH-----------------PKYEVTEGEILFKGEDIT---DLPP- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 100 etifyfgriygltDERIREKFKLLkelLQLPPARQMIKQC----------SGGQQRRLSFACAMIHDPELLILDEPTVGL 169
Cdd:cd03217 72 -------------EERARLGIFLA---FQYPPEIPGVKNAdflryvnegfSGGEKKRNEILQLLLLEPDLAILDEPDSGL 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 24582012 170 DPMLREKIWDfLVETTRNSKLAVIITTHY--IEEAKQANCIGLMRNGVLLAE 219
Cdd:cd03217 136 DIDALRLVAE-VINKLREEGKSVLIITHYqrLLDYIKPDRVHVLYDGRIVKS 186
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
20-170 |
8.99e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 61.89 E-value: 8.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 20 KIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVlGAKpgepgsgvpgSRVGFMPQ-EIALVEEMTV 98
Cdd:PRK11147 332 KQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-GTK----------LEVAYFDQhRAELDPEKTV 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 99 -------KETIFYFGriygltdeRIREKFKLLKELLqLPPARQM--IKQCSGGQQRRLSFACAMIHDPELLILDEPTVGL 169
Cdd:PRK11147 401 mdnlaegKQEVMVNG--------RPRHVLGYLQDFL-FHPKRAMtpVKALSGGERNRLLLARLFLKPSNLLILDEPTNDL 471
|
.
gi 24582012 170 D 170
Cdd:PRK11147 472 D 472
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
20-226 |
1.07e-09 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 59.79 E-value: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 20 KIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGA-----KPGEPGSgvpgsRVGFMPQEIALVE 94
Cdd:PRK13548 15 RTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRpladwSPAELAR-----RRAVLPQHSSLSF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 95 EMTVKETIfYFGRiYGLTDERIREKfKLLKELLQL----PPARQMIKQCSGGQQRRLSFACAMI------HDPELLILDE 164
Cdd:PRK13548 90 PFTVEEVV-AMGR-APHGLSRAEDD-ALVAAALAQvdlaHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPPRWLLLDE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24582012 165 PTVGLDPMLREKIWDFLVETTRNSKLAVIITTHYIEEAKQ-ANCIGLMRNGVLLAEDTPTNIM 226
Cdd:PRK13548 167 PTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARyADRIVLLHQGRLVADGTPAEVL 229
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
7-170 |
1.09e-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: 58.81 E-value: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 7 RNGYKYYGSKSNPKIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNG---GEVVVLGAKPGEPGSGVPGSRV 83
Cdd:cd03233 7 RNISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsveGDIHYNGIPYKEFAEKYPGEII 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 84 gFMPQEIALVEEMTVKETIFYFGRIYGltderirekfkllkellqlppaRQMIKQCSGGQQRRLSFACAMIHDPELLILD 163
Cdd:cd03233 87 -YVSEEDVHFPTLTVRETLDFALRCKG----------------------NEFVRGISGGERKRVSIAEALVSRASVLCWD 143
|
....*..
gi 24582012 164 EPTVGLD 170
Cdd:cd03233 144 NSTRGLD 150
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
23-170 |
1.10e-09 |
|
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: 61.62 E-value: 1.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 23 LNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVgqrRLN--GGEVVVLGakpgEPGSGVPGSRVGFMPQEIALVEE----- 95
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALL---RLIpsEGEIRFDG----QDLDGLSRRALRPLRRRMQVVFQdpfgs 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 96 ----MTVKETI---FYFGRIyGLT----DERIREkfkLLKELlQLPPArqMIK----QCSGGQQRRLSFACAMIHDPELL 160
Cdd:COG4172 375 lsprMTVGQIIaegLRVHGP-GLSaaerRARVAE---ALEEV-GLDPA--ARHryphEFSGGQRQRIAIARALILEPKLL 447
|
170
....*....|
gi 24582012 161 ILDEPTVGLD 170
Cdd:COG4172 448 VLDEPTSALD 457
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
26-216 |
1.37e-09 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 59.33 E-value: 1.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 26 LNMNVMRGSIYGLLGASGCGKTtlLSCIV-------GQRRLNGGevVVLGAKPGEPGSgVPGS---------RVGFMPqe 89
Cdd:PRK10418 22 VSLTLQRGRVLALVGGSGSGKS--LTCAAalgilpaGVRQTAGR--VLLDGKPVAPCA-LRGRkiatimqnpRSAFNP-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 90 ialVEEMT--VKETIFYFGRIYglTDERIREKFkllkELLQLPPARQMIK----QCSGGQQRRLSFACAMIHDPELLILD 163
Cdd:PRK10418 95 ---LHTMHthARETCLALGKPA--DDATLTAAL----EAVGLENAARVLKlypfEMSGGMLQRMMIALALLCEAPFIIAD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 24582012 164 EPTVGLDPMLREKIWDFLVETTRNSKLAVIITTHYIE-EAKQANCIGLMRNGVL 216
Cdd:PRK10418 166 EPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGvVARLADDVAVMSHGRI 219
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
20-198 |
1.71e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 59.03 E-value: 1.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 20 KIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQR--RLNGGEVV-----VLGAKPGE-PGSGVpgsrvgFM----P 87
Cdd:PRK09580 14 KAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEfkgkdLLELSPEDrAGEGI------FMafqyP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 88 QEIALVEEMTVKETIFYFGRIYGLTDERIREKFKLLKE----LLQLPP---ARQMIKQCSGGQQRRLSFACAMIHDPELL 160
Cdd:PRK09580 88 VEIPGVSNQFFLQTALNAVRSYRGQEPLDRFDFQDLMEekiaLLKMPEdllTRSVNVGFSGGEKKRNDILQMAVLEPELC 167
|
170 180 190
....*....|....*....|....*....|....*...
gi 24582012 161 ILDEPTVGLDpMLREKIWDFLVETTRNSKLAVIITTHY 198
Cdd:PRK09580 168 ILDESDSGLD-IDALKIVADGVNSLRDGKRSFIIVTHY 204
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
3-221 |
2.05e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 61.29 E-value: 2.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 3 AVEVRNGYKYYGSKsNPKIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQ-RRLNGGEVVVLGakpgepgsgvpgs 81
Cdd:PLN03130 614 AISIKNGYFSWDSK-AERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGElPPRSDASVVIRG------------- 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 82 RVGFMPQeIALVEEMTVKETIfyfgrIYGLTDERIR-EK---FKLLKELLQLPPARQMIK------QCSGGQQRRLSFAC 151
Cdd:PLN03130 680 TVAYVPQ-VSWIFNATVRDNI-----LFGSPFDPERyERaidVTALQHDLDLLPGGDLTEigergvNISGGQKQRVSMAR 753
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24582012 152 AMIHDPELLILDEPTVGLDPMLREKIWDFLVETTRNSKLAVIITT--HYIeeaKQANCIGLMRNGVLLAEDT 221
Cdd:PLN03130 754 AVYSNSDVYIFDDPLSALDAHVGRQVFDKCIKDELRGKTRVLVTNqlHFL---SQVDRIILVHEGMIKEEGT 822
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-218 |
2.61e-09 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 60.51 E-value: 2.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 1 MAA-VEVRNGYKYYGSKSNPKIVLNQLNMNVMRGSIYGLLGASGCGKTTL---LSCI----VGQRRLNGGEVVVLGakpG 72
Cdd:PRK10535 1 MTAlLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLmniLGCLdkptSGTYRVAGQDVATLD---A 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 73 EPGSGVPGSRVGFMPQEIALVEEMTVKETIFYFGRIYGLTDERIREKFKLLKELLQL------PPArqmikQCSGGQQRR 146
Cdd:PRK10535 78 DALAQLRREHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLedrveyQPS-----QLSGGQQQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24582012 147 LSFACAMIHDPELLILDEPTVGLDPMLREKIWDFLvETTRNSKLAVIITTHYIEEAKQANCIGLMRNGVLLA 218
Cdd:PRK10535 153 VSIARALMNGGQVILADEPTGALDSHSGEEVMAIL-HQLRDRGHTVIIVTHDPQVAAQAERVIEIRDGEIVR 223
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
16-170 |
3.02e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 60.51 E-value: 3.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 16 KSNPKIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGqrRLNGGeVVVLGAK--PGEPGSGVPGSRVGFMPQEIALV 93
Cdd:TIGR00956 772 KKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAE--RVTTG-VITGGDRlvNGRPLDSSFQRSIGYVQQQDLHL 848
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 94 EEMTVKETIFYFGRIYGLTDERIREKFKLLKELLQLPPARQMIKQCSG--------GQQRRLSFACAMIHDPELLI-LDE 164
Cdd:TIGR00956 849 PTSTVRESLRFSAYLRQPKSVSKSEKMEYVEEVIKLLEMESYADAVVGvpgeglnvEQRKRLTIGVELVAKPKLLLfLDE 928
|
....*.
gi 24582012 165 PTVGLD 170
Cdd:TIGR00956 929 PTSGLD 934
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
24-197 |
3.09e-09 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 58.97 E-value: 3.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 24 NQLNMNVMRGSIYGLLGASGCGKTT-------LLSC---IVGQRRLNGGEVVVLGAKP-------------GEPGSGV-P 79
Cdd:PRK09473 33 NDLNFSLRAGETLGIVGESGSGKSQtafalmgLLAAngrIGGSATFNGREILNLPEKElnklraeqismifQDPMTSLnP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 80 GSRVGFMPQEIALVEEMTVKETIFyfgriygltDERIRekfklLKELLQLPPARQMIK----QCSGGQQRRLSFACAMIH 155
Cdd:PRK09473 113 YMRVGEQLMEVLMLHKGMSKAEAF---------EESVR-----MLDAVKMPEARKRMKmyphEFSGGMRQRVMIAMALLC 178
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 24582012 156 DPELLILDEPTVGLDPMLREKIWDFLVETTRNSKLAVIITTH 197
Cdd:PRK09473 179 RPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITH 220
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
14-206 |
4.81e-09 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 57.42 E-value: 4.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 14 GSKSNPKIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVlgakPGEPGSGVPGSR----VGFMPQE 89
Cdd:PRK10247 14 GYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLF----EGEDISTLKPEIyrqqVSYCAQT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 90 IALVEEmTVKETIFYFGRIYGLTDERIR-----EKFKLLKELLQlpparQMIKQCSGGQQRRLSFACAMIHDPELLILDE 164
Cdd:PRK10247 90 PTLFGD-TVYDNLIFPWQIRNQQPDPAIflddlERFALPDTILT-----KNIAELSGGEKQRISLIRNLQFMPKVLLLDE 163
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 24582012 165 PTVGLDPMLREKIWDFLVETTRNSKLAVIITTHYIEEAKQAN 206
Cdd:PRK10247 164 ITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINHAD 205
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
23-201 |
5.00e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 59.15 E-value: 5.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 23 LNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEvVVLGAKPGEPGSGVP--GSRVGFMPQEIALVEEMTVKE 100
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGS-ILIDGQEMRFASTTAalAAGVAIIYQELHLVPEMTVAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 101 TIfYFGRI---YGLTDER--IREKFKLLKEL-LQLPPARQmIKQCSGGQQRRLSFACAMIHDPELLILDEPTVGLDPmlR 174
Cdd:PRK11288 99 NL-YLGQLphkGGIVNRRllNYEAREQLEHLgVDIDPDTP-LKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSA--R 174
|
170 180
....*....|....*....|....*...
gi 24582012 175 EKIWDF-LVETTRNSKLAVIITTHYIEE 201
Cdd:PRK11288 175 EIEQLFrVIRELRAEGRVILYVSHRMEE 202
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
16-193 |
5.73e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 59.25 E-value: 5.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 16 KSNPKI-VLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGaKP----GEPGSGVPGsrVGFMPQEI 90
Cdd:PRK10762 12 KAFPGVkALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLG-KEvtfnGPKSSQEAG--IGIIHQEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 91 ALVEEMTVKETIFY-------FGRIygLTDERIREKFKLLKELLQLPPARQMIKQCSGGQQRRLSFACAMIHDPELLILD 163
Cdd:PRK10762 89 NLIPQLTIAENIFLgrefvnrFGRI--DWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMD 166
|
170 180 190
....*....|....*....|....*....|
gi 24582012 164 EPTvgldpmlrekiwDFLVETTRNSKLAVI 193
Cdd:PRK10762 167 EPT------------DALTDTETESLFRVI 184
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
15-214 |
9.81e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 58.20 E-value: 9.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 15 SKSNPKI-VLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGaKPGEPGSGVPG--SRVGFMPQEIA 91
Cdd:PRK10982 5 SKSFPGVkALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQG-KEIDFKSSKEAleNGISMVHQELN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 92 LVEEMTVKETIfYFGR-----IYGLTDERIREKFKLLKEL-LQLPPaRQMIKQCSGGQQRRLSFACAMIHDPELLILDEP 165
Cdd:PRK10982 84 LVLQRSVMDNM-WLGRyptkgMFVDQDKMYRDTKAIFDELdIDIDP-RAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 24582012 166 TVGLDpmlrEKIWDFL---VETTRNSKLAVIITTHYIEEAKQ-ANCIGLMRNG 214
Cdd:PRK10982 162 TSSLT----EKEVNHLftiIRKLKERGCGIVYISHKMEEIFQlCDEITILRDG 210
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-197 |
1.25e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 57.06 E-value: 1.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 1 MAAVEVRNGYKYYGSKSNPKIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVG------------------------- 55
Cdd:PRK11022 1 MALLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGlidypgrvmaeklefngqdlqrise 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 56 --QRRLNGGEVVVLGAKPGEpgSGVPGSRVGFMPQEIALVEEMTVKETifyfgriygltdeRIREKFKLLKeLLQLP-PA 132
Cdd:PRK11022 81 keRRNLVGAEVAMIFQDPMT--SLNPCYTVGFQIMEAIKVHQGGNKKT-------------RRQRAIDLLN-QVGIPdPA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24582012 133 RQM---IKQCSGGQQRRLSFACAMIHDPELLILDEPTVGLDPMLREKIWDFLVETTRNSKLAVIITTH 197
Cdd:PRK11022 145 SRLdvyPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITH 212
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
19-197 |
1.44e-08 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 57.79 E-value: 1.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 19 PKIVLNQLNMNVMRGSIYGLLGASGCGKTT----LLSCIVGQrrlngGEVVVLGaKPGE---PGSGVPGSR---VGFMPQ 88
Cdd:PRK15134 298 HNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINSQ-----GEIWFDG-QPLHnlnRRQLLPVRHriqVVFQDP 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 89 EIALVEEMTVKETIFYFGRIY--GLTDERIREKFKLLKELLQLPPA-RQMI-KQCSGGQQRRLSFACAMIHDPELLILDE 164
Cdd:PRK15134 372 NSSLNPRLNVLQIIEEGLRVHqpTLSAAQREQQVIAVMEEVGLDPEtRHRYpAEFSGGQRQRIAIARALILKPSLIILDE 451
|
170 180 190
....*....|....*....|....*....|...
gi 24582012 165 PTVGLDPMLREKIWDFLVETTRNSKLAVIITTH 197
Cdd:PRK15134 452 PTSSLDKTVQAQILALLKSLQQKHQLAYLFISH 484
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
20-197 |
1.51e-08 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 55.19 E-value: 1.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 20 KIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVvLGAKPGEPGSGVPGSRVGFMPQEIALVEEMTVK 99
Cdd:cd03231 13 RALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVL-LNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 100 ETIFYFGRIYGltDERIREKFKL--LKELLQLPPArqmikQCSGGQQRRLSFACAMIHDPELLILDEPTVGLDPMLREKI 177
Cdd:cd03231 92 ENLRFWHADHS--DEQVEEALARvgLNGFEDRPVA-----QLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARF 164
|
170 180
....*....|....*....|
gi 24582012 178 WDFLVETTRNSKlAVIITTH 197
Cdd:cd03231 165 AEAMAGHCARGG-MVVLTTH 183
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-186 |
1.59e-08 |
|
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: 57.64 E-value: 1.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 4 VEVRNGYKYYGSKsnpkIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVlgakpgepGSGVpgsRV 83
Cdd:TIGR03719 323 IEAENLTKAFGDK----LLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI--------GETV---KL 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 84 GFMPQE-IALVEEMTVKETifyfgrIYGLTDERIREKFKLlkellqlpPAR--------------QMIKQCSGGQQRRLS 148
Cdd:TIGR03719 388 AYVDQSrDALDPNKTVWEE------ISGGLDIIKLGKREI--------PSRayvgrfnfkgsdqqKKVGQLSGGERNRVH 453
|
170 180 190
....*....|....*....|....*....|....*...
gi 24582012 149 FACAMIHDPELLILDEPTVGLDpmlrekiwdflVETTR 186
Cdd:TIGR03719 454 LAKTLKSGGNVLLLDEPTNDLD-----------VETLR 480
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
22-198 |
1.61e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 55.73 E-value: 1.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 22 VLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIvgqrrlnggevvvLGAKPGEPGSGVPGSRVGFMPQEIALVE----EMT 97
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLL-------------AGALKGTPVAGCVDVPDNQFGREASLIDaigrKGD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 98 VKETIFYFGRIyGLTDERI-REKFKLLkellqlpparqmikqcSGGQQRRLSFACAMIHDPELLILDEPTVGLDPML-RE 175
Cdd:COG2401 112 FKDAVELLNAV-GLSDAVLwLRRFKEL----------------STGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTaKR 174
|
170 180
....*....|....*....|...
gi 24582012 176 KIWDFLVETTRNSKLAVIITTHY 198
Cdd:COG2401 175 VARNLQKLARRAGITLVVATHHY 197
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
10-214 |
2.71e-08 |
|
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: 57.06 E-value: 2.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 10 YKY-YGSKsnpkiVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGAKPGEPGSGVPGSRVGFMPQ 88
Cdd:TIGR01193 481 YSYgYGSN-----ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQ 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 89 EiALVEEMTVKETIFyFGRIYGLTDERIREKFKLL---KELLQLPPARQM-----IKQCSGGQQRRLSFACAMIHDPELL 160
Cdd:TIGR01193 556 E-PYIFSGSILENLL-LGAKENVSQDEIWAACEIAeikDDIENMPLGYQTelseeGSSISGGQKQRIALARALLTDSKVL 633
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 24582012 161 ILDEPTVGLDPMLREKIWDFLVETTRNSklaVIITTHYIEEAKQANCIGLMRNG 214
Cdd:TIGR01193 634 ILDESTSNLDTITEKKIVNNLLNLQDKT---IIFVAHRLSVAKQSDKIIVLDHG 684
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
20-216 |
3.30e-08 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 56.78 E-value: 3.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 20 KIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVG------QRRLNGGEVVVLgakpgEPGSGVpgSRVGFMPQEIALV 93
Cdd:PRK11174 363 KTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGflpyqgSLKINGIELREL-----DPESWR--KHLSWVGQNPQLP 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 94 EEmTVKETIFyFGRIyGLTDERIR---------EKFKLLKELLQLPPARQMIKqCSGGQQRRLSFACAMIHDPELLILDE 164
Cdd:PRK11174 436 HG-TLRDNVL-LGNP-DASDEQLQqalenawvsEFLPLLPQGLDTPIGDQAAG-LSVGQAQRLALARALLQPCQLLLLDE 511
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 24582012 165 PTVGLDPMLREKIWDFLVETTRNSklAVIITTHYIEEAKQANCIGLMRNGVL 216
Cdd:PRK11174 512 PTASLDAHSEQLVMQALNAASRRQ--TTLMVTHQLEDLAQWDQIWVMQDGQI 561
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
138-214 |
5.49e-08 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 55.87 E-value: 5.49e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24582012 138 QCSGGQQRRLSFACAMIHDPELLILDEPTVGLDPMLREKIWDFLVETTRNSKLAVIITTHYIEEAKQ-ANCIGLMRNG 214
Cdd:PRK15134 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKlADRVAVMQNG 233
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
19-214 |
8.58e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 55.94 E-value: 8.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 19 PKIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEvvVLGAKpgepgsgvpgsRVGFMPQEiALVEEMTV 98
Cdd:PTZ00243 672 PKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGR--VWAER-----------SIAYVPQQ-AWIMNATV 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 99 KETIFYFgriygltDERIREKF-------KLLKELLQLPPAR-----QMIKQCSGGQQRRLSFACAMIHDPELLILDEPT 166
Cdd:PTZ00243 738 RGNILFF-------DEEDAARLadavrvsQLEADLAQLGGGLeteigEKGVNLSGGQKARVSLARAVYANRDVYLLDDPL 810
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 24582012 167 VGLDPMLREKIwdflVETTRNSKLA---VIITTHYIEEAKQANCIGLMRNG 214
Cdd:PTZ00243 811 SALDAHVGERV----VEECFLGALAgktRVLATHQVHVVPRADYVVALGDG 857
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
4-226 |
1.10e-07 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 55.11 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 4 VEVRNGYKYYGSKSNpKIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVlgakpgepgSGVPGSRV 83
Cdd:TIGR00958 479 IEFQDVSFSYPNRPD-VPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLL---------DGVPLVQY 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 84 G--FMPQEIALVEEM------TVKETIfyfgrIYGLT---DERIREKFKL------LKELLQL------PPARQMikqcS 140
Cdd:TIGR00958 549 DhhYLHRQVALVGQEpvlfsgSVRENI-----AYGLTdtpDEEIMAAAKAanahdfIMEFPNGydtevgEKGSQL----S 619
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 141 GGQQRRLSFACAMIHDPELLILDEPTVGLDPMLrekiwDFLVETTRNSK-LAVIITTHYIEEAKQANCIGLMRNGVLLAE 219
Cdd:TIGR00958 620 GGQKQRIAIARALVRKPRVLILDEATSALDAEC-----EQLLQESRSRAsRTVLLIAHRLSTVERADQILVLKKGSVVEM 694
|
....*..
gi 24582012 220 DTPTNIM 226
Cdd:TIGR00958 695 GTHKQLM 701
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
17-170 |
1.16e-07 |
|
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: 53.57 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 17 SNPKIV--LNQLNMNVMRGSIY-----GLLGASGCGKTTLLscivgqrRLNGGEVvvlgaKPGEPGSGVPGSRVGFMPQE 89
Cdd:cd03237 2 TYPTMKktLGEFTLEVEGGSISeseviGILGPNGIGKTTFI-------KMLAGVL-----KPDEGDIEIELDTVSYKPQY 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 90 IALVEEMTVKETIFYFGRIYGLTDERIREKFKLLKeLLQLppARQMIKQCSGGQQRRLSFACAMIHDPELLILDEPTVGL 169
Cdd:cd03237 70 IKADYEGTVRDLLSSITKDFYTHPYFKTEIAKPLQ-IEQI--LDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYL 146
|
.
gi 24582012 170 D 170
Cdd:cd03237 147 D 147
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
23-203 |
1.28e-07 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 54.90 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 23 LNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLG-AKPGEPGSGVPGSRVGfmpqeialVEEMTVKet 101
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGsAALIAISSGLNGQLTG--------IENIELK-- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 102 ifyfGRIYGLTDERIREKFKLLKELLQLPP-ARQMIKQCSGGQQRRLSFACAMIHDPELLILDEP-TVGlDPMLREKIWD 179
Cdd:PRK13545 110 ----GLMMGLTKEKIKEIIPEIIEFADIGKfIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEAlSVG-DQTFTKKCLD 184
|
170 180
....*....|....*....|....
gi 24582012 180 FLVETTRNSKLAVIItTHYIEEAK 203
Cdd:PRK13545 185 KMNEFKEQGKTIFFI-SHSLSQVK 207
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
20-197 |
1.41e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 52.64 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 20 KIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGAKPGEPGSGVPgSRVGFMPQEIALVEEMTVK 99
Cdd:PRK13540 14 QPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQ-KQLCFVGHRSGINPYLTLR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 100 ETIfYFGRIYGLTDERIREKFKL--LKELLQLPparqmikqC---SGGQQRRLSFACAMIHDPELLILDEPTVGLDPMLR 174
Cdd:PRK13540 93 ENC-LYDIHFSPGAVGITELCRLfsLEHLIDYP--------CgllSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSL 163
|
170 180
....*....|....*....|...
gi 24582012 175 EKIWDfLVETTRNSKLAVIITTH 197
Cdd:PRK13540 164 LTIIT-KIQEHRAKGGAVLLTSH 185
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
26-237 |
1.45e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 54.67 E-value: 1.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 26 LNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGAkpgEPGSGVPGSRVG----FMP---QEIAL------ 92
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGK---EINALSTAQRLArglvYLPedrQSSGLyldapl 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 93 ---VEEMTVKETIFYFGRIYgltDERIREKFKllKEL-LQLPPARQMIKQCSGGQQRRLSFACAMIHDPELLILDEPTVG 168
Cdd:PRK15439 359 awnVCALTHNRRGFWIKPAR---ENAVLERYR--RALnIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRG 433
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24582012 169 LDPMLREKIWDfLVETTRNSKLAVIITTHYIEEAKQ-ANCIGLMR----NGVLLAEDTPT-NIM-IKFGTQSIEDA 237
Cdd:PRK15439 434 VDVSARNDIYQ-LIRSIAAQNVAVLFISSDLEEIEQmADRVLVMHqgeiSGALTGAAINVdTIMrLAFGEHQAQEA 508
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
25-197 |
2.06e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 54.48 E-value: 2.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 25 QLNMNVMRGSIYGLLGASGCGKTT-------LLSCIVGQ--------RRLNGgEVVVLGAKPGEPGSGVPGSRVGFMPQE 89
Cdd:PRK10261 34 NLSFSLQRGETLAIVGESGSGKSVtalalmrLLEQAGGLvqcdkmllRRRSR-QVIELSEQSAAQMRHVRGADMAMIFQE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 90 --IALVEEMTVKETIFYFGRIY-GLTDERIREKFKLLKELLQLPPARQMIK----QCSGGQQRRLSFACAMIHDPELLIL 162
Cdd:PRK10261 113 pmTSLNPVFTVGEQIAESIRLHqGASREEAMVEAKRMLDQVRIPEAQTILSryphQLSGGMRQRVMIAMALSCRPAVLIA 192
|
170 180 190
....*....|....*....|....*....|....*
gi 24582012 163 DEPTVGLDPMLREKIWDFLVETTRNSKLAVIITTH 197
Cdd:PRK10261 193 DEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITH 227
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-204 |
2.30e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 54.02 E-value: 2.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 4 VEVRNGYKYYGsksnPKIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLG-----------AKPG 72
Cdd:PRK09700 6 ISMAGIGKSFG----PVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNinynkldhklaAQLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 73 epgsgvpgsrVGFMPQEIALVEEMTVKETIfYFGR-----IYGL-----TDERIREKFKLLKELLQLPPaRQMIKQCSGG 142
Cdd:PRK09700 82 ----------IGIIYQELSVIDELTVLENL-YIGRhltkkVCGVniidwREMRVRAAMMLLRVGLKVDL-DEKVANLSIS 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24582012 143 QQRRLSFACAMIHDPELLILDEPTVGLDPMLREKIWdFLVETTRNSKLAVIITTHYIEEAKQ 204
Cdd:PRK09700 150 HKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLF-LIMNQLRKEGTAIVYISHKLAEIRR 210
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
4-222 |
2.31e-07 |
|
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: 52.11 E-value: 2.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 4 VEVRNGYKYYGSKSNPkiVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVlgakPGEPGSGVP---- 79
Cdd:cd03244 3 IEFKNVSLRYRPNLPP--VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILI----DGVDISKIGlhdl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 80 GSRVGFMPQEiALVEEMTVKETIFYFGRiygLTDERIR---EKFKLLKELLQLPPARQMI-----KQCSGGQQRRLSFAC 151
Cdd:cd03244 77 RSRISIIPQD-PVLFSGTIRSNLDPFGE---YSDEELWqalERVGLKEFVESLPGGLDTVveeggENLSVGQRQLLCLAR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24582012 152 AMIHDPELLILDEPTVGLDP----MLREKIWDFLVETTrnsklaVIITTHYIEEAKQANCIGLMRNGVLLAEDTP 222
Cdd:cd03244 153 ALLRKSKILVLDEATASVDPetdaLIQKTIREAFKDCT------VLTIAHRLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
5-170 |
2.80e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 53.78 E-value: 2.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 5 EVRNGYKYYGSKSNPKIVlNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVG--QRRlNGGEVVVLGaKPGEPGSGVPGSR 82
Cdd:PRK13549 261 EVRNLTAWDPVNPHIKRV-DDVSFSLRRGEILGIAGLVGAGRTELVQCLFGayPGR-WEGEIFIDG-KPVKIRNPQQAIA 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 83 VGfmpqeIALVEE----------MTVKETI-------FYFGRIYGLTDER--IREKFKLLKelLQLPPARQMIKQCSGGQ 143
Cdd:PRK13549 338 QG-----IAMVPEdrkrdgivpvMGVGKNItlaaldrFTGGSRIDDAAELktILESIQRLK--VKTASPELAIARLSGGN 410
|
170 180
....*....|....*....|....*..
gi 24582012 144 QRRLSFACAMIHDPELLILDEPTVGLD 170
Cdd:PRK13549 411 QQKAVLAKCLLLNPKILILDEPTRGID 437
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
30-170 |
5.11e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.89 E-value: 5.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 30 VMRGSIYGLLGASGCGKTTLLscivgqrRLNGGEVvvlgaKPGEpGSGVPGSRVGFMPQEIALVEEMTVKETIFYFGRIY 109
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFA-------KLLAGVL-----KPDE-GEVDPELKISYKPQYIKPDYDGTVEDLLRSITDDL 428
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24582012 110 GLT--DERIREKFKLlKELLQlpparQMIKQCSGGQQRRLSFACAMIHDPELLILDEPTVGLD 170
Cdd:PRK13409 429 GSSyyKSEIIKPLQL-ERLLD-----KNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 485
|
|
| TagG |
COG1682 |
ABC-type polysaccharide/teichoic acid/polyol phosphate export permease [Carbohydrate transport ... |
507-709 |
5.79e-07 |
|
ABC-type polysaccharide/teichoic acid/polyol phosphate export permease [Carbohydrate transport and metabolism];
Pssm-ID: 441288 [Multi-domain] Cd Length: 258 Bit Score: 51.34 E-value: 5.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 507 GSTDIEFQQYCAPGVVMTMVFFLATLMTAAVFISermdgiwDRTLLA--GVSATEMLWAHLLTQLIIMALQSFeVIMYIG 584
Cdd:COG1682 57 PSGGVPYALFLLAGLLPWNFFSEALNRGSGSIVA-------NAGLIKkvYFPREILPLARVLSALVNFLISLV-VLLVVL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 585 LVFDTYNNGDTTTLIGLLTLTAFCGMLFGLFISVFCKSHTEANFVATGAFYPMIILCGLLWPLESMPQFLQDLVMVLPFT 664
Cdd:COG1682 129 LLFGVPPSWTLLLLPLALLLLLLFGLGLGLLLAALNVFFRDVQQIVGLLLQLLFFLSPVFYPLSTLPEPLRWLLLLNPLT 208
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 24582012 665 IPSISARNVIEKGWSIThekvYNGFLVMAGWTIIFFVLCLIGIRR 709
Cdd:COG1682 209 HIIELFRAALLGGYLPD----WLSLLYALLVSLVLLLLGLLLFRR 249
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
20-183 |
6.58e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 52.86 E-value: 6.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 20 KIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVlgAKpgepgsgvpGSRVGFMPQEiaLVEEMTVK 99
Cdd:PRK10636 325 RIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL--AK---------GIKLGYFAQH--QLEFLRAD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 100 ET-IFYFGRIYGltderiREKFKLLKELL-----QLPPARQMIKQCSGGQQRRLSFACAMIHDPELLILDEPTVGLDPML 173
Cdd:PRK10636 392 ESpLQHLARLAP------QELEQKLRDYLggfgfQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDM 465
|
170
....*....|
gi 24582012 174 REKIWDFLVE 183
Cdd:PRK10636 466 RQALTEALID 475
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
33-197 |
6.93e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 52.55 E-value: 6.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 33 GSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGAKPGE-PGSGVPGSR--VGFMPQE--IALVEEMTVKETIFYFGR 107
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTlSPGKLQALRrdIQFIFQDpyASLDPRQTVGDSIMEPLR 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 108 IYGLTD-ERIREKFKLLKELLQLPP--ARQMIKQCSGGQQRRLSFACAMIHDPELLILDEPTVGLDPMLREKIWDFLVET 184
Cdd:PRK10261 430 VHGLLPgKAAAARVAWLLERVGLLPehAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDL 509
|
170
....*....|...
gi 24582012 185 TRNSKLAVIITTH 197
Cdd:PRK10261 510 QRDFGIAYLFISH 522
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
20-198 |
7.55e-07 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 50.84 E-value: 7.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 20 KIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVG--QRRLNGGEVV-----VLGAKPGEPgsgvpgSRVG-FM----P 87
Cdd:COG0396 13 KEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGhpKYEVTSGSILldgedILELSPDER------ARAGiFLafqyP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 88 QEIALVeemtvkeTIFYFGRI----YGLTDERIREKFKLLKE---LLQLPPArqMIKQC-----SGGQQRRLSFACAMIH 155
Cdd:COG0396 87 VEIPGV-------SVSNFLRTalnaRRGEELSAREFLKLLKEkmkELGLDED--FLDRYvnegfSGGEKKRNEILQMLLL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 24582012 156 DPELLILDEPTVGLDpmlrekIWDF-----LVETTRNSKLAVIITTHY 198
Cdd:COG0396 158 EPKLAILDETDSGLD------IDALrivaeGVNKLRSPDRGILIITHY 199
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
32-170 |
1.06e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 51.93 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 32 RGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGaKPGEPGSgvpgsrvgfmPQE-----IA----------LVEEM 96
Cdd:PRK10762 277 KGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDG-HEVVTRS----------PQDglangIVyisedrkrdgLVLGM 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 97 TVKE-----TIFYFGRIYGL---TDERIR-EKFKLLKELlQLPPARQMIKQCSGGQQRRLSFACAMIHDPELLILDEPTV 167
Cdd:PRK10762 346 SVKEnmsltALRYFSRAGGSlkhADEQQAvSDFIRLFNI-KTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTR 424
|
...
gi 24582012 168 GLD 170
Cdd:PRK10762 425 GVD 427
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
100-197 |
1.25e-06 |
|
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: 50.85 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 100 ETIFYFGRIYGLTDERIREK--FKLLKELLQLPPARQMikqcSGGQQRRLSFACAMIHDPE---LLILDEPTVGLDPMLR 174
Cdd:pfam13304 200 SDLGEGIEKSLLVDDRLRERglILLENGGGGELPAFEL----SDGTKRLLALLAALLSALPkggLLLIDEPESGLHPKLL 275
|
90 100
....*....|....*....|...
gi 24582012 175 EKIWDFLVETTRNsKLAVIITTH 197
Cdd:pfam13304 276 RRLLELLKELSRN-GAQLILTTH 297
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
23-214 |
1.44e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 51.33 E-value: 1.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 23 LNQLNMNVMRGSIYGLLGASGCGKTTL---LSCIV------GQRRLNGGEVVVLGAKPGEpgsgvpgsRVGF--MPQEIA 91
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLmkvLSGVYphgsyeGEILFDGEVCRFKDIRDSE--------ALGIviIHQELA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 92 LVEEMTVKETIFYFGRI--YGLTD--ERIREKFKLLKEL-LQLPPARQmIKQCSGGQQRRLSFACAMIHDPELLILDEPT 166
Cdd:NF040905 89 LIPYLSIAENIFLGNERakRGVIDwnETNRRARELLAKVgLDESPDTL-VTDIGVGKQQLVEIAKALSKDVKLLILDEPT 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 24582012 167 VGLDPMLREKIWDFLVEtTRNSKLAVIITTHYIEE-AKQANCIGLMRNG 214
Cdd:NF040905 168 AALNEEDSAALLDLLLE-LKAQGITSIIISHKLNEiRRVADSITVLRDG 215
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
30-199 |
1.47e-06 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 51.32 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 30 VMRGSIYGLLGASGCGKTTLLSCIVGqrrlnggevvVLgaKPGEpGSGVPGSRVGFMPQEIALVEEMTVKETIF-YFGRI 108
Cdd:COG1245 363 IREGEVLGIVGPNGIGKTTFAKILAG----------VL--KPDE-GEVDEDLKISYKPQYISPDYDGTVEEFLRsANTDD 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 109 YGLT--DERIREKFKLlKELLQlpparQMIKQCSGGQQRRLSFACAMIHDPELLILDEPTVGLDPMLREKIWDFLVETTR 186
Cdd:COG1245 430 FGSSyyKTEIIKPLGL-EKLLD-----KNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAE 503
|
170
....*....|...
gi 24582012 187 NSKLAVIITTHYI 199
Cdd:COG1245 504 NRGKTAMVVDHDI 516
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
40-205 |
1.69e-06 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 49.14 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 40 GASGCGKTTLLSCIvgqrrlnggEVVVLGAKPgepgsgvPGSRVGF-MPQEIALVEEMTVKETIF--YFGRIYgltdeRI 116
Cdd:cd03240 29 GQNGAGKTTIIEAL---------KYALTGELP-------PNSKGGAhDPKLIREGEVRAQVKLAFenANGKKY-----TI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 117 REKFKLLKELLQLP------PARQMIKQCSGGQQR------RLSFACAMIHDPELLILDEPTVGLDP-MLREKIWDFLVE 183
Cdd:cd03240 88 TRSLAILENVIFCHqgesnwPLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEeNIEESLAEIIEE 167
|
170 180
....*....|....*....|..
gi 24582012 184 TTRNSKLAVIITTHYiEEAKQA 205
Cdd:cd03240 168 RKSQKNFQLIVITHD-EELVDA 188
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
4-193 |
3.06e-06 |
|
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: 48.56 E-value: 3.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 4 VEVRNGYKYYGSKSNPkiVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGAKPGEPGSGVPGSRV 83
Cdd:cd03369 7 IEVENLSVRYAPDLPP--VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 84 GFMPQEIALVEEmTVKETIFYFGRiygLTDERIREKFKLLKELLQLpparqmikqcSGGQQRRLSFACAMIHDPELLILD 163
Cdd:cd03369 85 TIIPQDPTLFSG-TIRSNLDPFDE---YSDEEIYGALRVSEGGLNL----------SQGQRQLLCLARALLKRPRVLVLD 150
|
170 180 190
....*....|....*....|....*....|
gi 24582012 164 EPTVGLDPMLREKIWDFLVETTRNSKLAVI 193
Cdd:cd03369 151 EATASIDYATDALIQKTIREEFTNSTILTI 180
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
4-197 |
3.08e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 49.96 E-value: 3.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 4 VEVRNGYKYY----GSKSNPKIV--LNQLNMNVMRGSIYGLLGASGCGKTTL---LSCI----VGQRRLNGGEVvvLGAK 70
Cdd:PRK11308 6 LQAIDLKKHYpvkrGLFKPERLVkaLDGVSFTLERGKTLAVVGESGCGKSTLarlLTMIetptGGELYYQGQDL--LKAD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 71 PGE--------------P-GSGVPGSRVGfmpqeiALVEEMTVKETifyfgriyGLTDERIREKfkllkellqlppARQM 135
Cdd:PRK11308 84 PEAqkllrqkiqivfqnPyGSLNPRKKVG------QILEEPLLINT--------SLSAAERREK------------ALAM 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24582012 136 IKQC--------------SGGQQRRLSFACAMIHDPELLILDEPTVGLDPMLREKIWDFLVETTRNSKLAVIITTH 197
Cdd:PRK11308 138 MAKVglrpehydryphmfSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISH 213
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
32-206 |
7.48e-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: 46.21 E-value: 7.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 32 RGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGakpgepgsgvpgsrvgfmPQEIALVEEMTVKETIFYFGRIYGL 111
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYID------------------GEDILEEVLDQLLLIIVGGKKASGS 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 112 TDERIREKFKLLKEllqlpparqmikqcsggqqrrlsfacamiHDPELLILDEPTVGLDPMLREKIWD-----FLVETTR 186
Cdd:smart00382 63 GELRLRLALALARK-----------------------------LKPDVLILDEITSLLDAEQEALLLLleelrLLLLLKS 113
|
170 180
....*....|....*....|
gi 24582012 187 NSKLAVIITTHYIEEAKQAN 206
Cdd:smart00382 114 EKNLTVILTTNDEKDLGPAL 133
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
18-171 |
7.68e-06 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 47.54 E-value: 7.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 18 NPKIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVlgakPGEPGSGVPGSR-VGFMPQEIALVEEM 96
Cdd:PRK13543 22 NEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQI----DGKTATRGDRSRfMAYLGHLPGLKADL 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24582012 97 TVKETIFYFGRIYGLTDERIREKFKLLKELLQLppARQMIKQCSGGQQRRLSFACAMIHDPELLILDEPTVGLDP 171
Cdd:PRK13543 98 STLENLHFLCGLHGRRAKQMPGSALAIVGLAGY--EDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL 170
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
4-286 |
8.50e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 49.26 E-value: 8.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 4 VEVRNGYKYYGSKSNPKIvLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGAKP-GEPGSGVPGSR 82
Cdd:PTZ00265 383 IQFKNVRFHYDTRKDVEI-YKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNlKDINLKWWRSK 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 83 VGFMPQEIALVEEmTVKETIFYfgRIYGLTD--------------------------ERIREKFKLL------KELLQLP 130
Cdd:PTZ00265 462 IGVVSQDPLLFSN-SIKNNIKY--SLYSLKDlealsnyynedgndsqenknkrnscrAKCAGDLNDMsnttdsNELIEMR 538
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 131 PARQMIK---------------------------------QCSGGQQRRLSFACAMIHDPELLILDEPTVGLDpmlreKI 177
Cdd:PTZ00265 539 KNYQTIKdsevvdvskkvlihdfvsalpdkyetlvgsnasKLSGGQKQRISIARAIIRNPKILILDEATSSLD-----NK 613
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 178 WDFLVETTRNS-----KLAVIITTHYIEEAKQANCIGLMRNgvllAEDTPTNIMIKFGTQSIEDAfliLSQRQGNEDELA 252
Cdd:PTZ00265 614 SEYLVQKTINNlkgneNRITIIIAHRLSTIRYANTIFVLSN----RERGSTVDVDIIGEDPTKDN---KENNNKNNKDDN 686
|
330 340 350
....*....|....*....|....*....|....*.
gi 24582012 253 QIMDHNKNQALPAAvlPPEVID--THEPNMPEKQPI 286
Cdd:PTZ00265 687 NNNNNNNNNKINNA--GSYIIEqgTHDALMKNKNGI 720
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
4-186 |
1.11e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 48.58 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 4 VEVRNGYKYYGSKsnpkIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVlgakpgepGSGVpgsRV 83
Cdd:PRK11819 325 IEAENLSKSFGDR----LLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI--------GETV---KL 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 84 GFMPQE-IALVEEMTVKETifyfgrIYGLTDERIREKFKLlkellqlpPAR--------------QMIKQCSGGQQRRLS 148
Cdd:PRK11819 390 AYVDQSrDALDPNKTVWEE------ISGGLDIIKVGNREI--------PSRayvgrfnfkggdqqKKVGVLSGGERNRLH 455
|
170 180 190
....*....|....*....|....*....|....*...
gi 24582012 149 FACAMIHDPELLILDEPTVGLDpmlrekiwdflVETTR 186
Cdd:PRK11819 456 LAKTLKQGGNVLLLDEPTNDLD-----------VETLR 482
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
134-198 |
1.19e-05 |
|
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: 46.20 E-value: 1.19e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 134 QMIKQCSGGQQRRLSFACAMIH-----DPeLLILDEPTVGLDPMLREKIWDFLVEtTRNSKLAVIITTHY 198
Cdd:cd03227 73 FTRLQLSGGEKELSALALILALaslkpRP-LYILDEIDRGLDPRDGQALAEAILE-HLVKGAQVIVITHL 140
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
96-213 |
1.71e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 48.49 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 96 MTVKETIfYFGRiYGLTDERIRE--KFKLLKELLQLPPARQMI------KQCSGGQQRRLSFACAMIHDPELLILDEPTV 167
Cdd:PTZ00265 1310 MSIYENI-KFGK-EDATREDVKRacKFAAIDEFIESLPNKYDTnvgpygKSLSGGQKQRIAIARALLREPKILLLDEATS 1387
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 24582012 168 GLDPMLREKIWDFLVETTRNSKLAVIITTHYIEEAKQANCIGLMRN 213
Cdd:PTZ00265 1388 SLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKRSDKIVVFNN 1433
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
4-214 |
1.95e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 47.80 E-value: 1.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 4 VEVRNgykyYGSKSNPKIvlNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGaKPGEPGSGVPGSRV 83
Cdd:PRK10982 251 LEVRN----LTSLRQPSI--RDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHG-KKINNHNANEAINH 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 84 GFmpqeiALVEEMTVKETIF----------------YFGRIYGLTDERIREKFKLLKELLQL--PPARQMIKQCSGGQQR 145
Cdd:PRK10982 324 GF-----ALVTEERRSTGIYayldigfnslisnirnYKNKVGLLDNSRMKSDTQWVIDSMRVktPGHRTQIGSLSGGNQQ 398
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24582012 146 RLSFACAMIHDPELLILDEPTVGLDPMLREKIWDFLVETTRNSKLAVIITTHYIEEAKQANCIGLMRNG 214
Cdd:PRK10982 399 KVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNG 467
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
33-170 |
2.11e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 48.30 E-value: 2.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 33 GSIYGLLGASGCGKTTLLSCIVGqRRLNG---GEVVVlgakpgepgSGVPG-----SRV-GFMPQEIALVEEMTVKETIF 103
Cdd:PLN03140 906 GVLTALMGVSGAGKTTLMDVLAG-RKTGGyieGDIRI---------SGFPKkqetfARIsGYCEQNDIHSPQVTVRESLI 975
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24582012 104 YFGRIYGLTDERIREKFKLLKELLQLPPARQM---------IKQCSGGQQRRLSFACAMIHDPELLILDEPTVGLD 170
Cdd:PLN03140 976 YSAFLRLPKEVSKEEKMMFVDEVMELVELDNLkdaivglpgVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLD 1051
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
4-214 |
2.27e-05 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 47.71 E-value: 2.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 4 VEVRNGYKYYGSKSNPkiVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVlgakpgePGSGVPGSRV 83
Cdd:PRK11176 342 IEFRNVTFTYPGKEVP--ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILL-------DGHDLRDYTL 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 84 GFMPQEIALVEEM------TVKETIFY-FGRIYglTDERIREKFKLLKellqlppARQMIKQ---------------CSG 141
Cdd:PRK11176 413 ASLRNQVALVSQNvhlfndTIANNIAYaRTEQY--SREQIEEAARMAY-------AMDFINKmdngldtvigengvlLSG 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24582012 142 GQQRRLSFACAMIHDPELLILDEPTVGLDPMLREKIWDFLVETTRNSKLAVIitTHYIEEAKQANCIGLMRNG 214
Cdd:PRK11176 484 GQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVI--AHRLSTIEKADEILVVEDG 554
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
23-201 |
3.02e-05 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 46.79 E-value: 3.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 23 LNQLNMNV-----MRGsIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGAKPGEPGSGV---PGSR-VGFMPQEIALV 93
Cdd:PRK11144 10 LGDLCLTVnltlpAQG-ITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGIclpPEKRrIGYVFQDARLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 94 EEMTVKetifyfGRI-YGLTDERiREKFKLLKELLQLPP--ARQMIKqCSGGQQRRLSFACAMIHDPELLILDEPTVGLD 170
Cdd:PRK11144 89 PHYKVR------GNLrYGMAKSM-VAQFDKIVALLGIEPllDRYPGS-LSGGEKQRVAIGRALLTAPELLLMDEPLASLD 160
|
170 180 190
....*....|....*....|....*....|..
gi 24582012 171 -PMLREkIWDFLVETTRNSKLAVIITTHYIEE 201
Cdd:PRK11144 161 lPRKRE-LLPYLERLAREINIPILYVSHSLDE 191
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
38-170 |
6.36e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 46.10 E-value: 6.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 38 LLGASGCGKTTLLSCIVGQRRLNGGEV-----VVLGAKPGEPGSGVPGS------------------------RVGFMPQ 88
Cdd:PRK11147 34 LVGRNGAGKSTLMKILNGEVLLDDGRIiyeqdLIVARLQQDPPRNVEGTvydfvaegieeqaeylkryhdishLVETDPS 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 89 EIALVEEMTVKETIFYFGrIYGLtDERIREKFKLLKellqLPPARQMiKQCSGGQQRRLSFACAMIHDPELLILDEPTVG 168
Cdd:PRK11147 114 EKNLNELAKLQEQLDHHN-LWQL-ENRINEVLAQLG----LDPDAAL-SSLSGGWLRKAALGRALVSNPDVLLLDEPTNH 186
|
..
gi 24582012 169 LD 170
Cdd:PRK11147 187 LD 188
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
18-200 |
6.50e-05 |
|
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: 45.97 E-value: 6.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 18 NPKIV-LNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGAKPGEPGSGVPGSRVGfmpqeIALVEE- 95
Cdd:TIGR02633 270 NPHRKrVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKFEGNVFINGKPVDIRNPAQAIRAG-----IAMVPEd 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 96 ---------MTVKETI-------FYF-GRIYGLTDER-IREKFKLLKelLQLPPARQMIKQCSGGQQRRLSFACAMIHDP 157
Cdd:TIGR02633 345 rkrhgivpiLGVGKNItlsvlksFCFkMRIDAAAELQiIGSAIQRLK--VKTASPFLPIGRLSGGNQQKAVLAKMLLTNP 422
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 24582012 158 ELLILDEPTVGLDPMLREKIWDFLVETTRNSKLAVIITTHYIE 200
Cdd:TIGR02633 423 RVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAE 465
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
22-211 |
6.85e-05 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 45.67 E-value: 6.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 22 VLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVG-----------QRRLNGGEVVVLGakpgepgsgvPGSRVGFMPQEI 90
Cdd:COG4170 22 AVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGitkdnwhvtadRFRWNGIDLLKLS----------PRERRKIIGREI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 91 ALV--EEMT-----------VKETI---FYFGRIYgltdERIREKFKLLKELLQlppaRQMIK-----------QCSGGQ 143
Cdd:COG4170 92 AMIfqEPSScldpsakigdqLIEAIpswTFKGKWW----QRFKWRKKRAIELLH----RVGIKdhkdimnsyphELTEGE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24582012 144 QRRLSFACAMIHDPELLILDEPTVGLDPMLREKIWDFLVETTRNSKLAVIITTHYIEE-AKQANCIGLM 211
Cdd:COG4170 164 CQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESiSQWADTITVL 232
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
17-228 |
7.18e-05 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 44.90 E-value: 7.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 17 SNPKIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGAKPGEPGSGVPGSRVGFMPQEialveem 96
Cdd:cd03288 31 NNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQD------- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 97 tvkeTIFYFGRIYGLTDERIREKFKLLKELLQLPPARQMIKQCSGG---------------QQRRLSFACAMIHDPELLI 161
Cdd:cd03288 104 ----PILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGldavvteggenfsvgQRQLFCLARAFVRKSSILI 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24582012 162 LDEPTVGLDpMLREKIWDFLVETTRNSKLAVIItTHYIEEAKQANCIGLMRNGVLLAEDTPTNIMIK 228
Cdd:cd03288 180 MDEATASID-MATENILQKVVMTAFADRTVVTI-AHRVSTILDADLVLVLSRGILVECDTPENLLAQ 244
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
20-193 |
7.84e-05 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 45.86 E-value: 7.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 20 KIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVlgakPGEPGSGVPGSrvgFMPQEIALVEEMTV- 98
Cdd:PRK10790 354 NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRL----DGRPLSSLSHS---VLRQGVAMVQQDPVv 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 99 -KETIF---YFGRiyGLTDERIREKFkllkELLQLPP-ARQMIK-----------QCSGGQQRRLSFACAMIHDPELLIL 162
Cdd:PRK10790 427 lADTFLanvTLGR--DISEEQVWQAL----ETVQLAElARSLPDglytplgeqgnNLSVGQKQLLALARVLVQTPQILIL 500
|
170 180 190
....*....|....*....|....*....|.
gi 24582012 163 DEPTVGLDPMLREKIWDFLVETTRNSKLAVI 193
Cdd:PRK10790 501 DEATANIDSGTEQAIQQALAAVREHTTLVVI 531
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
21-170 |
1.09e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 45.62 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 21 IVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRrlnggevvvlgakpgEPGSGV----PGSRVGFMPQEiaLVEEM 96
Cdd:PLN03073 523 LLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGEL---------------QPSSGTvfrsAKVRMAVFSQH--HVDGL 585
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24582012 97 TVKET-IFYFGRIY-GLTDERIRE---KFKLLKELlqlppARQMIKQCSGGQQRRLSFACAMIHDPELLILDEPTVGLD 170
Cdd:PLN03073 586 DLSSNpLLYMMRCFpGVPEQKLRAhlgSFGVTGNL-----ALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD 659
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
33-170 |
2.60e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 44.11 E-value: 2.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 33 GSIYGLLGASGCGKTTLLscivgqrRLNGGEVvvlgakpgEPGSGV----PGSRVGFMPQEIALVEEMTVKETIFyFG-- 106
Cdd:PRK15064 27 GNRYGLIGANGCGKSTFM-------KILGGDL--------EPSAGNvsldPNERLGKLRQDQFAFEEFTVLDTVI-MGht 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 107 ----------RIYGL---TDE---RIRE---KFKLLK---------ELLqLP---PARQ---MIKQCSGGQQRRLSFACA 152
Cdd:PRK15064 91 elwevkqerdRIYALpemSEEdgmKVADlevKFAEMDgytaearagELL-LGvgiPEEQhygLMSEVAPGWKLRVLLAQA 169
|
170
....*....|....*...
gi 24582012 153 MIHDPELLILDEPTVGLD 170
Cdd:PRK15064 170 LFSNPDILLLDEPTNNLD 187
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
14-204 |
2.76e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 43.27 E-value: 2.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 14 GSKSNPKIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVvvlgAKPGEPG-----SGVPGSRVGfmpq 88
Cdd:PRK13546 31 KHKNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV----DRNGEVSviaisAGLSGQLTG---- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 89 eialVEEMTVKETIFYFGR--IYGLTDERIreKFKLLKELLQLPparqmIKQCSGGQQRRLSFACAMIHDPELLILDEP- 165
Cdd:PRK13546 103 ----IENIEFKMLCMGFKRkeIKAMTPKII--EFSELGEFIYQP-----VKKYSSGMRAKLGFSINITVNPDILVIDEAl 171
|
170 180 190
....*....|....*....|....*....|....*....
gi 24582012 166 TVGlDPMLREKIWDFLVETTRNSKlAVIITTHYIEEAKQ 204
Cdd:PRK13546 172 SVG-DQTFAQKCLDKIYEFKEQNK-TIFFVSHNLGQVRQ 208
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
4-170 |
3.11e-04 |
|
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: 44.17 E-value: 3.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 4 VEVRNGYKYYgsKSNPKIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGAKPGEPGSGVPGSRV 83
Cdd:TIGR00957 1285 VEFRNYCLRY--REDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKI 1362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 84 GFMPQEIALVEEmTVKETIFYFGRiygLTDERIREKFKL--LKELLQLPPARqMIKQCS-GGQ-----QRRL-SFACAMI 154
Cdd:TIGR00957 1363 TIIPQDPVLFSG-SLRMNLDPFSQ---YSDEEVWWALELahLKTFVSALPDK-LDHECAeGGEnlsvgQRQLvCLARALL 1437
|
170
....*....|....*.
gi 24582012 155 HDPELLILDEPTVGLD 170
Cdd:TIGR00957 1438 RKTKILVLDEATAAVD 1453
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
90-169 |
6.38e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 43.28 E-value: 6.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 90 IALVEEMTVKETIFYFgriygLTDERIREKFKLLKEL-LQLPPARQMIKQCSGGQQRRLSFACAMIH---DPELLILDEP 165
Cdd:PRK00635 765 IADILEMTAYEAEKFF-----LDEPSIHEKIHALCSLgLDYLPLGRPLSSLSGGEIQRLKLAYELLApskKPTLYVLDEP 839
|
....
gi 24582012 166 TVGL 169
Cdd:PRK00635 840 TTGL 843
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
138-214 |
6.66e-04 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 43.03 E-value: 6.66e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24582012 138 QCSGGQQRRLSFACAMIHDPELLILDEPTVGLDPMLREKIWDFLVETTRNSKLAVIitTHYIEEAKQANCIGLMRNG 214
Cdd:PRK13657 471 QLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFII--AHRLSTVRNADRILVFDNG 545
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
18-197 |
9.44e-04 |
|
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: 42.43 E-value: 9.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 18 NPKIVLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVvvlgAKPGEpgsgvpgSRVGFMPQEiALVEEMT 97
Cdd:TIGR00954 463 NGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRL----TKPAK-------GKLFYVPQR-PYMTLGT 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 98 VKETIFYFGRIYGLTDERIREkfKLLKELLQLPPARQMIKQ-------------CSGGQQRRLSFACAMIHDPELLILDE 164
Cdd:TIGR00954 531 LRDQIIYPDSSEDMKRRGLSD--KDLEQILDNVQLTHILEReggwsavqdwmdvLSGGEKQRIAMARLFYHKPQFAILDE 608
|
170 180 190
....*....|....*....|....*....|...
gi 24582012 165 PTVGLDPMLREKIWdflvETTRNSKLAVIITTH 197
Cdd:TIGR00954 609 CTSAVSVDVEGYMY----RLCREFGITLFSVSH 637
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
90-222 |
1.08e-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: 41.45 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 90 IALVEEMTVKETIFYFGRIygltdERIREKFKLLKEL-LQLPPARQMIKQCSGGQQRRLSFACAMIH---DPELLILDEP 165
Cdd:cd03271 125 IADVLDMTVEEALEFFENI-----PKIARKLQTLCDVgLGYIKLGQPATTLSGGEAQRIKLAKELSKrstGKTLYILDEP 199
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24582012 166 TVGLDPMLREKIWDFLVETTRNSKLAVIItTHYIEEAKQANCI------GLMRNGVLLAEDTP 222
Cdd:cd03271 200 TTGLHFHDVKKLLEVLQRLVDKGNTVVVI-EHNLDVIKCADWIidlgpeGGDGGGQVVASGTP 261
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
90-222 |
1.25e-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: 42.31 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 90 IALVEEMTVKETIFYFGRIygltdERIREKFKLLKEL-LQLPPARQMIKQCSGGQQRRLSFA---CAMIHDPELLILDEP 165
Cdd:TIGR00630 785 IADVLDMTVEEAYEFFEAV-----PSISRKLQTLCDVgLGYIRLGQPATTLSGGEAQRIKLAkelSKRSTGRTLYILDEP 859
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24582012 166 TVGLDPMLREKIWDFLVETTRNSKLAVIItTHYIEEAKQANCI------GLMRNGVLLAEDTP 222
Cdd:TIGR00630 860 TTGLHFDDIKKLLEVLQRLVDKGNTVVVI-EHNLDVIKTADYIidlgpeGGDGGGTVVASGTP 921
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
22-210 |
1.88e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 40.24 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 22 VLNQLNMNVMRGSIYGLLGASGCGKTTLLSCIVGQRRLNGGEVVVLGAKPgepgSGVPGSRVGFMPQEIALVEEMTVKET 101
Cdd:PRK13541 15 NLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNI----NNIAKPYCTYIGHNLGLKLEMTVFEN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 102 IFYFGRIYGlTDERIREK---FKlLKELLQlpparqmiKQC---SGGQQRRLSFACAMIHDPELLILDEPTVGLDPMLRE 175
Cdd:PRK13541 91 LKFWSEIYN-SAETLYAAihyFK-LHDLLD--------EKCyslSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRD 160
|
170 180 190
....*....|....*....|....*....|....*
gi 24582012 176 KIWDFLVETTrNSKLAVIITTHYIEEAKQANCIGL 210
Cdd:PRK13541 161 LLNNLIVMKA-NSGGIVLLSSHLESSIKSAQILQL 194
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
22-170 |
3.42e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 40.54 E-value: 3.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 22 VLNQLNMNVMRGSIYGLLGASGCGKTTL-LSC--------IVGQRRLNGGEVVVlgakpgepgSGVPGSrvgfMPQEIAL 92
Cdd:NF040905 275 VVDDVSLNVRRGEIVGIAGLMGAGRTELaMSVfgrsygrnISGTVFKDGKEVDV---------STVSDA----IDAGLAY 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582012 93 VEE----------MTVKE--TIFYFGRI--YGLTDE----RIREKFKllKEL-LQLPPARQMIKQCSGGQQRRLSFACAM 153
Cdd:NF040905 342 VTEdrkgyglnliDDIKRniTLANLGKVsrRGVIDEneeiKVAEEYR--KKMnIKTPSVFQKVGNLSGGNQQKVVLSKWL 419
|
170
....*....|....*..
gi 24582012 154 IHDPELLILDEPTVGLD 170
Cdd:NF040905 420 FTDPDVLILDEPTRGID 436
|
|
| |
