|
Name |
Accession |
Description |
Interval |
E-value |
| PHA_synth_I |
TIGR01838 |
poly(R)-hydroxyalkanoic acid synthase, class I; This model represents the class I subfamily of ... |
141-675 |
0e+00 |
|
poly(R)-hydroxyalkanoic acid synthase, class I; This model represents the class I subfamily of poly(R)-hydroxyalkanoate synthases, which polymerizes hydroxyacyl-CoAs with three to five carbons in the hydroxyacyl backbone into aliphatic esters termed poly(R)-hydroxyalkanoic acids. These polymers accumulate as carbon and energy storage inclusions in many species and can amount to 90 percent of the dry weight of cell. [Fatty acid and phospholipid metabolism, Biosynthesis]
Pssm-ID: 213656 [Multi-domain] Cd Length: 532 Bit Score: 754.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503245622 141 LAQNPEKVIEAQTDLMTGYMSLWAEMTRRSLG--VETPEDTTPKDKRFSDPRWQQNLVFDMMRKSYLLSSTWLNNLVSSV 218
Cdd:TIGR01838 1 LSAQPARLFEAQASYWQQQMQLWQKALLRSAGedVEPFADPEPGDRRFASPAWSSHPFFDFLKQSYLLNSSWLLELVDAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503245622 219 EDVDPLHKRRAEFFTKLVTDAFSPSNFLMSNPAALDTLLSSKGESLVKGMQKFADDLARGDGKLKISQADYAHFKVGENV 298
Cdd:TIGR01838 81 EGLDPKTRRRLEFFTRQLINAMAPSNFLATNPEALRLTVETQGESLVRGMENLAEDLERGGGDLKIRQTDSSAFEVGRNL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503245622 299 ATTPGKVVWRGPLFELLQYNPTTDEVHETPLLIFPPWINKYYILDLQSKNSLIKWLTDQGFSVFVVSWVNPDADLKDVTF 378
Cdd:TIGR01838 161 ATTPGAVVFENELFQLIQYEPTTETVHKTPLLIVPPWINKYYILDLRPQNSLVRWLVEQGHTVFVISWRNPDASQADKTF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503245622 379 EDYMFGGVYKAMSLVREQTGSPKVNTVGYCIGGTLLGVALAHMAAKGDD-SVSSATFFTAQHDFSEAGDLLLFTNEAWLK 457
Cdd:TIGR01838 241 DDYIRDGVIAALEVVEAITGEKQVNCVGYCIGGTLLSTALAYLAARGDDkRIKSATFFTTLLDFSDPGELGVFVDEEIVA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503245622 458 ELERQMDaAGGVLPGAAMADTFNALRANDLVWSFFVNNYLMGKDLTAFDLLCWNADQTRMPKALHMYYLRKFYHENALSQ 537
Cdd:TIGR01838 321 GIERQNG-GGGYLDGRQMAVTFSLLRENDLIWNYYVDNYLKGKSPVPFDLLFWNSDSTNLPGKMHNFYLRNLYLQNALTT 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503245622 538 GKLTIAGVPIDLKNVRIPVFEQSGREDHIAPPGSVFKSARLFGGPVTFVMAGSGHIAGVVNPPAAQKYQHWINElsnakG 617
Cdd:TIGR01838 400 GGLEVCGVRLDLSKVKVPVYIIATREDHIAPWQSAYRGAALLGGPKTFVLGESGHIAGVVNPPSKNKYGHWTNA-----A 474
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 503245622 618 LPETLEAWQKDAVEHKGSWWDYWAQWLHDKSGPMVPARDPSKGKFKPDMDAPGSYVLV 675
Cdd:TIGR01838 475 LPADPEVWLAGATEHPGSWWPDWAAWLAGHSGKQVPARNPGNAKYPPLEPAPGRYVKV 532
|
|
| PhaC |
COG3243 |
Poly-beta-hydroxybutyrate synthase [Lipid transport and metabolism]; |
122-675 |
0e+00 |
|
Poly-beta-hydroxybutyrate synthase [Lipid transport and metabolism];
Pssm-ID: 442475 [Multi-domain] Cd Length: 545 Bit Score: 738.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503245622 122 TPNGDPFQVAPAMTSVMTSLAQNPEKVIEAQTDLMTGYMSLWAEMTRRSLG--VETPEDTTPKDKRFSDPRWQQNLVFDM 199
Cdd:COG3243 1 AAAGDSLAAAAAAAAAAAALLAAPARLLLAQAALAQRLLALWQAAAARLAGggAAPPPIPPPPDDRRFDPDWWWNPPFDF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503245622 200 MRKSYLLSSTWLNNLVSSVEDVDPLHKRRAEFFTKLVTDAFSPSNFLMSNPAALDTLLSSKGESLVKGMQKFADDLARGd 279
Cdd:COG3243 81 IKQAYLLLAQWWLDAVADVEGLDPKTRRRVRFYTRQILDAMSPSNFLATNPEALKETLETGGESLVRGLENLLEDLERG- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503245622 280 gklKISQADYAHFKVGENVATTPGKVVWRGPLFELLQYNPTTDEVHETPLLIFPPWINKYYILDLQSKNSLIKWLTDQGF 359
Cdd:COG3243 160 ---AISQTDESAFEVGENVATTPGKVVYRNDLMELIQYAPTTEKVHKTPLLIVPPWINKYYILDLQPGNSLVRYLVDQGF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503245622 360 SVFVVSWVNPDADLKDVTFEDYMFGGVYKAMSLVREQTGSPKVNTVGYCIGGTLLGVALAHMAAKGDDSVSSATFFTAQH 439
Cdd:COG3243 237 TVFLISWGNPDAEDRDLGLDDYVEDGILAAVDAVREITGEDKVNLLGYCLGGTLLAIYAALLAARGPDRVASLTLLATPL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503245622 440 DFSEAGDLLLFTNEAWLKELERQMDaAGGVLPGAAMADTFNALRANDLVWSFFVNNYLMGKDLTAFDLLCWNADQTRMPK 519
Cdd:COG3243 317 DFSEPGELGVFIDESQLADLEALMA-AKGYLPGRLMAGAFSLLRPNDLIWSYYVNNYLLGENPPPFDLLYWNADSTRLPG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503245622 520 ALHMYYLRKFYHENALSQGKLTIAGVPIDLKNVRIPVFEQSGREDHIAPPGSVFKSARLFGG-PVTFVMAGSGHIAGVVN 598
Cdd:COG3243 396 RMHSQYLRDLYLENRLAKGELELGGRPVDLSDITVPVLVVAGEEDHIAPWRSVYALAQLVGGkDVTFVLAPGGHIGGIVN 475
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503245622 599 PPAAQKYQHWINElsnakGLPETLEAWQKDAVEHKGSWWDYWAQWLHDKSGPMVPARDPskGKFKPDMDAPGSYVLV 675
Cdd:COG3243 476 PPGKPKRSYWTND-----RLPGDPDEWLAGAEEHPGSWWPDWADWLAERSGKKVPARAP--GSGPPLEDAPGTYVKE 545
|
|
| PhaC_N |
pfam07167 |
Poly-beta-hydroxybutyrate polymerase (PhaC) N-terminus; This family represents the N-terminal ... |
182-354 |
1.10e-92 |
|
Poly-beta-hydroxybutyrate polymerase (PhaC) N-terminus; This family represents the N-terminal region of the bacterial poly-beta-hydroxybutyrate polymerase (PhaC). Polyhydroxyalkanoic acids (PHAs) are carbon and energy reserve polymers produced in some bacteria when carbon sources are plentiful and another nutrient, such as nitrogen, phosphate, oxygen, or sulfur, becomes limiting. PHAs composed of monomeric units ranging from 3 to 14 carbons exist in nature. When the carbon source is exhausted, PHA is utilized by the bacterium. PhaC links D-(-)-3-hydroxybutyrl-CoA to an existing PHA molecule by the formation of an ester bond. This family appears to be a partial segment of an alpha/beta hydrolase domain.
Pssm-ID: 462110 [Multi-domain] Cd Length: 173 Bit Score: 284.54 E-value: 1.10e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503245622 182 KDKRFSDPRWQQNLVFDMMRKSYLLSSTWLNNLVSSVEDVDPLHKRRAEFFTKLVTDAFSPSNFLMSNPAALDTLLSSKG 261
Cdd:pfam07167 1 RDRRFADPAWQTNPFFDFLKQAYLLTSKWLMDWVDEVEGLDPKTRARAEFFTRQLIDALAPSNFLATNPEALKETFESGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503245622 262 ESLVKGMQKFADDLARGDGKLKISQADYAHFKVGENVATTPGKVVWRGPLFELLQYNPTTDEVHETPLLIFPPWINKYYI 341
Cdd:pfam07167 81 ESLVRGLENLLEDLERGGGDLKISQTDESAFEVGKNLATTPGKVVFRNELMELIQYKPTTEKVHKRPLLIVPPWINKFYI 160
|
170
....*....|...
gi 503245622 342 LDLQSKNSLIKWL 354
Cdd:pfam07167 161 LDLSPQNSLVRWA 173
|
|
| PHA02682 |
PHA02682 |
ORF080 virion core protein; Provisional |
30-180 |
2.31e-06 |
|
ORF080 virion core protein; Provisional
Pssm-ID: 177464 [Multi-domain] Cd Length: 280 Bit Score: 49.86 E-value: 2.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503245622 30 TPAMAPAPVAKATRKTAPKPKAASVEAPVAPKPAAQSAPSPTPPQSEPSPESTFDSEQMKAledlsinlAKAAITAQTAL 109
Cdd:PHA02682 95 CPACAPAAPAPAVTCPAPAPACPPATAPTCPPPAVCPAPARPAPACPPSTRQCPPAPPLPT--------PKPAPAAKPIF 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503245622 110 ASAVLKQPDFNGTpNGDPFQVAPAMTSVMTSlaQNPEKVIEAQT-----------DLMTGYMSLWAEMTRRSLGVETPED 178
Cdd:PHA02682 167 LHNQLPPPDYPAA-SCPTIETAPAASPVLEP--RIPDKIIDADNddkdlikkelaDIADSVRDLNAESLSLTRDIENAKS 243
|
..
gi 503245622 179 TT 180
Cdd:PHA02682 244 TT 245
|
|
| DedD |
COG3147 |
Cell division protein DedD (periplasmic protein involved in septation) [Cell cycle control, ... |
30-79 |
5.25e-04 |
|
Cell division protein DedD (periplasmic protein involved in septation) [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442381 [Multi-domain] Cd Length: 140 Bit Score: 40.91 E-value: 5.25e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 503245622 30 TPAMAPAPV-AKATRKTAPKPkaasVEAPVAPKPAAQSAPSPTPPQSEPSP 79
Cdd:COG3147 17 APAAAAAPApAAAAAAAAPKP----AAKPAAPKPAAAAAAAPAAKAAAPAG 63
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PHA_synth_I |
TIGR01838 |
poly(R)-hydroxyalkanoic acid synthase, class I; This model represents the class I subfamily of ... |
141-675 |
0e+00 |
|
poly(R)-hydroxyalkanoic acid synthase, class I; This model represents the class I subfamily of poly(R)-hydroxyalkanoate synthases, which polymerizes hydroxyacyl-CoAs with three to five carbons in the hydroxyacyl backbone into aliphatic esters termed poly(R)-hydroxyalkanoic acids. These polymers accumulate as carbon and energy storage inclusions in many species and can amount to 90 percent of the dry weight of cell. [Fatty acid and phospholipid metabolism, Biosynthesis]
Pssm-ID: 213656 [Multi-domain] Cd Length: 532 Bit Score: 754.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503245622 141 LAQNPEKVIEAQTDLMTGYMSLWAEMTRRSLG--VETPEDTTPKDKRFSDPRWQQNLVFDMMRKSYLLSSTWLNNLVSSV 218
Cdd:TIGR01838 1 LSAQPARLFEAQASYWQQQMQLWQKALLRSAGedVEPFADPEPGDRRFASPAWSSHPFFDFLKQSYLLNSSWLLELVDAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503245622 219 EDVDPLHKRRAEFFTKLVTDAFSPSNFLMSNPAALDTLLSSKGESLVKGMQKFADDLARGDGKLKISQADYAHFKVGENV 298
Cdd:TIGR01838 81 EGLDPKTRRRLEFFTRQLINAMAPSNFLATNPEALRLTVETQGESLVRGMENLAEDLERGGGDLKIRQTDSSAFEVGRNL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503245622 299 ATTPGKVVWRGPLFELLQYNPTTDEVHETPLLIFPPWINKYYILDLQSKNSLIKWLTDQGFSVFVVSWVNPDADLKDVTF 378
Cdd:TIGR01838 161 ATTPGAVVFENELFQLIQYEPTTETVHKTPLLIVPPWINKYYILDLRPQNSLVRWLVEQGHTVFVISWRNPDASQADKTF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503245622 379 EDYMFGGVYKAMSLVREQTGSPKVNTVGYCIGGTLLGVALAHMAAKGDD-SVSSATFFTAQHDFSEAGDLLLFTNEAWLK 457
Cdd:TIGR01838 241 DDYIRDGVIAALEVVEAITGEKQVNCVGYCIGGTLLSTALAYLAARGDDkRIKSATFFTTLLDFSDPGELGVFVDEEIVA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503245622 458 ELERQMDaAGGVLPGAAMADTFNALRANDLVWSFFVNNYLMGKDLTAFDLLCWNADQTRMPKALHMYYLRKFYHENALSQ 537
Cdd:TIGR01838 321 GIERQNG-GGGYLDGRQMAVTFSLLRENDLIWNYYVDNYLKGKSPVPFDLLFWNSDSTNLPGKMHNFYLRNLYLQNALTT 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503245622 538 GKLTIAGVPIDLKNVRIPVFEQSGREDHIAPPGSVFKSARLFGGPVTFVMAGSGHIAGVVNPPAAQKYQHWINElsnakG 617
Cdd:TIGR01838 400 GGLEVCGVRLDLSKVKVPVYIIATREDHIAPWQSAYRGAALLGGPKTFVLGESGHIAGVVNPPSKNKYGHWTNA-----A 474
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 503245622 618 LPETLEAWQKDAVEHKGSWWDYWAQWLHDKSGPMVPARDPSKGKFKPDMDAPGSYVLV 675
Cdd:TIGR01838 475 LPADPEVWLAGATEHPGSWWPDWAAWLAGHSGKQVPARNPGNAKYPPLEPAPGRYVKV 532
|
|
| PhaC |
COG3243 |
Poly-beta-hydroxybutyrate synthase [Lipid transport and metabolism]; |
122-675 |
0e+00 |
|
Poly-beta-hydroxybutyrate synthase [Lipid transport and metabolism];
Pssm-ID: 442475 [Multi-domain] Cd Length: 545 Bit Score: 738.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503245622 122 TPNGDPFQVAPAMTSVMTSLAQNPEKVIEAQTDLMTGYMSLWAEMTRRSLG--VETPEDTTPKDKRFSDPRWQQNLVFDM 199
Cdd:COG3243 1 AAAGDSLAAAAAAAAAAAALLAAPARLLLAQAALAQRLLALWQAAAARLAGggAAPPPIPPPPDDRRFDPDWWWNPPFDF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503245622 200 MRKSYLLSSTWLNNLVSSVEDVDPLHKRRAEFFTKLVTDAFSPSNFLMSNPAALDTLLSSKGESLVKGMQKFADDLARGd 279
Cdd:COG3243 81 IKQAYLLLAQWWLDAVADVEGLDPKTRRRVRFYTRQILDAMSPSNFLATNPEALKETLETGGESLVRGLENLLEDLERG- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503245622 280 gklKISQADYAHFKVGENVATTPGKVVWRGPLFELLQYNPTTDEVHETPLLIFPPWINKYYILDLQSKNSLIKWLTDQGF 359
Cdd:COG3243 160 ---AISQTDESAFEVGENVATTPGKVVYRNDLMELIQYAPTTEKVHKTPLLIVPPWINKYYILDLQPGNSLVRYLVDQGF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503245622 360 SVFVVSWVNPDADLKDVTFEDYMFGGVYKAMSLVREQTGSPKVNTVGYCIGGTLLGVALAHMAAKGDDSVSSATFFTAQH 439
Cdd:COG3243 237 TVFLISWGNPDAEDRDLGLDDYVEDGILAAVDAVREITGEDKVNLLGYCLGGTLLAIYAALLAARGPDRVASLTLLATPL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503245622 440 DFSEAGDLLLFTNEAWLKELERQMDaAGGVLPGAAMADTFNALRANDLVWSFFVNNYLMGKDLTAFDLLCWNADQTRMPK 519
Cdd:COG3243 317 DFSEPGELGVFIDESQLADLEALMA-AKGYLPGRLMAGAFSLLRPNDLIWSYYVNNYLLGENPPPFDLLYWNADSTRLPG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503245622 520 ALHMYYLRKFYHENALSQGKLTIAGVPIDLKNVRIPVFEQSGREDHIAPPGSVFKSARLFGG-PVTFVMAGSGHIAGVVN 598
Cdd:COG3243 396 RMHSQYLRDLYLENRLAKGELELGGRPVDLSDITVPVLVVAGEEDHIAPWRSVYALAQLVGGkDVTFVLAPGGHIGGIVN 475
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503245622 599 PPAAQKYQHWINElsnakGLPETLEAWQKDAVEHKGSWWDYWAQWLHDKSGPMVPARDPskGKFKPDMDAPGSYVLV 675
Cdd:COG3243 476 PPGKPKRSYWTND-----RLPGDPDEWLAGAEEHPGSWWPDWADWLAERSGKKVPARAP--GSGPPLEDAPGTYVKE 545
|
|
| PhaC_N |
pfam07167 |
Poly-beta-hydroxybutyrate polymerase (PhaC) N-terminus; This family represents the N-terminal ... |
182-354 |
1.10e-92 |
|
Poly-beta-hydroxybutyrate polymerase (PhaC) N-terminus; This family represents the N-terminal region of the bacterial poly-beta-hydroxybutyrate polymerase (PhaC). Polyhydroxyalkanoic acids (PHAs) are carbon and energy reserve polymers produced in some bacteria when carbon sources are plentiful and another nutrient, such as nitrogen, phosphate, oxygen, or sulfur, becomes limiting. PHAs composed of monomeric units ranging from 3 to 14 carbons exist in nature. When the carbon source is exhausted, PHA is utilized by the bacterium. PhaC links D-(-)-3-hydroxybutyrl-CoA to an existing PHA molecule by the formation of an ester bond. This family appears to be a partial segment of an alpha/beta hydrolase domain.
Pssm-ID: 462110 [Multi-domain] Cd Length: 173 Bit Score: 284.54 E-value: 1.10e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503245622 182 KDKRFSDPRWQQNLVFDMMRKSYLLSSTWLNNLVSSVEDVDPLHKRRAEFFTKLVTDAFSPSNFLMSNPAALDTLLSSKG 261
Cdd:pfam07167 1 RDRRFADPAWQTNPFFDFLKQAYLLTSKWLMDWVDEVEGLDPKTRARAEFFTRQLIDALAPSNFLATNPEALKETFESGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503245622 262 ESLVKGMQKFADDLARGDGKLKISQADYAHFKVGENVATTPGKVVWRGPLFELLQYNPTTDEVHETPLLIFPPWINKYYI 341
Cdd:pfam07167 81 ESLVRGLENLLEDLERGGGDLKISQTDESAFEVGKNLATTPGKVVFRNELMELIQYKPTTEKVHKRPLLIVPPWINKFYI 160
|
170
....*....|...
gi 503245622 342 LDLQSKNSLIKWL 354
Cdd:pfam07167 161 LDLSPQNSLVRWA 173
|
|
| PHA_synth_III_C |
TIGR01836 |
poly(R)-hydroxyalkanoic acid synthase, class III, PhaC subunit; This model represents the PhaC ... |
262-611 |
8.77e-41 |
|
poly(R)-hydroxyalkanoic acid synthase, class III, PhaC subunit; This model represents the PhaC subunit of a heterodimeric form of polyhydroxyalkanoic acid (PHA) synthase. Excepting the PhaC of Bacillus megaterium (which needs PhaR), all members require PhaE (TIGR01834) for activity and are designated class III. This enzyme builds ester polymers for carbon and energy storage that accumulate in inclusions, and both this enzyme and the depolymerase associate with the inclusions. Class III enzymes polymerize short-chain-length hydroxyalkanoates. [Fatty acid and phospholipid metabolism, Biosynthesis]
Pssm-ID: 130895 Cd Length: 350 Bit Score: 152.58 E-value: 8.77e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503245622 262 ESLVKGMQKFADDLARGDGKLkisqADYAHFKVGenvaTTPGKVVWRGPLFELLQYNPTTDEVHETPLLIFPPWINKYYI 341
Cdd:TIGR01836 6 ESLAQEYLDFTRKLKEGYENL----TNEEDIEVG----VTPKEVVYREDKVVLYRYTPVKDNTHKTPLLIVYALVNRPYM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503245622 342 LDLQSKNSLIKWLTDQGFSVFVVSWVNPDADLKDVTFEDYMFGGVYKAMSLVREQTGSPKVNTVGYCIGGTLlgvALAHm 421
Cdd:TIGR01836 78 LDLQEDRSLVRGLLERGQDVYLIDWGYPDRADRYLTLDDYINGYIDKCVDYICRTSKLDQISLLGICQGGTF---SLCY- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503245622 422 AAKGDDSVSSATFFTAQHDFSEAGDLLLFTNEAWlkELERQMDAAGGVlPGAAMADTFNALRAndlvwsfFVNNYlmGKD 501
Cdd:TIGR01836 154 AALYPDKIKNLVTMVTPVDFETPGNMLSNWARHV--DIDLAVDTMGNI-PGELLNLTFLMLKP-------FSLGY--QKY 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503245622 502 LTAFDLLcwnADQT------RM--------PKALHMY--YLRKFYHENALSQGKLTIAGVPIDLKNVRIPVFEQSGREDH 565
Cdd:TIGR01836 222 VNLVDIL---EDERkvenflRMekwifdspDQAGEAFrqFVKDFYQQNGLINGEVEIGGRKVDLKNIKMPILNIYAERDH 298
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 503245622 566 IAPPGSVFKSARLFGGPVTFVMA-GSGHIaGVVNPPAAQK-----YQHWINE 611
Cdd:TIGR01836 299 LVPPDASKALNDLVSSEDYTELSfPGGHI-GIYVSGKAQKevppaIGKWLQA 349
|
|
| Abhydrolase_1 |
pfam00561 |
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes. |
349-599 |
5.53e-14 |
|
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
Pssm-ID: 395444 [Multi-domain] Cd Length: 245 Bit Score: 72.15 E-value: 5.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503245622 349 SLIKWLTDQGFSVFVVSWVNPDADLKDVTFEDYMFGGVYKAMSLVREQTGSPKVNTVGYCIGGTLLgvalAHMAAKGDDS 428
Cdd:pfam00561 18 KLAPALARDGFRVIALDLRGFGKSSRPKAQDDYRTDDLAEDLEYILEALGLEKVNLVGHSMGGLIA----LAYAAKYPDR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503245622 429 VSSATFFTAQHDFSEAGDLLLFTNEAWLKELERQMDAA----GGVLPGAAMADTFNALRA----NDLVWSFFVNNYLMGK 500
Cdd:pfam00561 94 VKALVLLGALDPPHELDEADRFILALFPGFFDGFVADFapnpLGRLVAKLLALLLLRLRLlkalPLLNKRFPSGDYALAK 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503245622 501 DLTAFDLLCWNADQTRmpkalhmyYLRKFYHenalsqgkltiagvpidlkNVRIPVFEQSGREDHIAPPGSVFKSARLFG 580
Cdd:pfam00561 174 SLVTGALLFIETWSTE--------LRAKFLG-------------------RLDEPTLIIWGDQDPLVPPQALEKLAQLFP 226
|
250
....*....|....*....
gi 503245622 581 GPVTFVMAGSGHIAGVVNP 599
Cdd:pfam00561 227 NARLVVIPDAGHFAFLEGP 245
|
|
| PHA02682 |
PHA02682 |
ORF080 virion core protein; Provisional |
30-180 |
2.31e-06 |
|
ORF080 virion core protein; Provisional
Pssm-ID: 177464 [Multi-domain] Cd Length: 280 Bit Score: 49.86 E-value: 2.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503245622 30 TPAMAPAPVAKATRKTAPKPKAASVEAPVAPKPAAQSAPSPTPPQSEPSPESTFDSEQMKAledlsinlAKAAITAQTAL 109
Cdd:PHA02682 95 CPACAPAAPAPAVTCPAPAPACPPATAPTCPPPAVCPAPARPAPACPPSTRQCPPAPPLPT--------PKPAPAAKPIF 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503245622 110 ASAVLKQPDFNGTpNGDPFQVAPAMTSVMTSlaQNPEKVIEAQT-----------DLMTGYMSLWAEMTRRSLGVETPED 178
Cdd:PHA02682 167 LHNQLPPPDYPAA-SCPTIETAPAASPVLEP--RIPDKIIDADNddkdlikkelaDIADSVRDLNAESLSLTRDIENAKS 243
|
..
gi 503245622 179 TT 180
Cdd:PHA02682 244 TT 245
|
|
| PRK14951 |
PRK14951 |
DNA polymerase III subunits gamma and tau; Provisional |
31-137 |
2.07e-05 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237865 [Multi-domain] Cd Length: 618 Bit Score: 47.79 E-value: 2.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503245622 31 PAMAPAPVAKATRKTAPK-PKAASVEAPVAPKPAAQSAPSPTPPQSEPSPestfdsEQMKALEDLSINLAKAAITAQTAL 109
Cdd:PRK14951 387 AAPAAAPVAQAAAAPAPAaAPAAAASAPAAPPAAAPPAPVAAPAAAAPAA------APAAAPAAVALAPAPPAQAAPETV 460
|
90 100
....*....|....*....|....*...
gi 503245622 110 ASAVLKQPDFNGTPNGDPFQVAPAMTSV 137
Cdd:PRK14951 461 AIPVRVAPEPAVASAAPAPAAAPAAARL 488
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
31-133 |
5.06e-05 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 46.77 E-value: 5.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503245622 31 PAMAPAPVAKATRKTAPKPKAASVEAPVAPKPAAQSAPS-PTPPQSEPSPESTFDSEQMKALEDLSINLAKAAITAQTAL 109
Cdd:PRK07003 383 PGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATrAEAPPAAPAPPATADRGDDAADGDAPVPAKANARASADSR 462
|
90 100
....*....|....*....|....
gi 503245622 110 ASAVLKQPDFNGTPNGDPFQVAPA 133
Cdd:PRK07003 463 CDERDAQPPADSGSASAPASDAPP 486
|
|
| DedD |
COG3147 |
Cell division protein DedD (periplasmic protein involved in septation) [Cell cycle control, ... |
30-79 |
5.25e-04 |
|
Cell division protein DedD (periplasmic protein involved in septation) [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442381 [Multi-domain] Cd Length: 140 Bit Score: 40.91 E-value: 5.25e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 503245622 30 TPAMAPAPV-AKATRKTAPKPkaasVEAPVAPKPAAQSAPSPTPPQSEPSP 79
Cdd:COG3147 17 APAAAAAPApAAAAAAAAPKP----AAKPAAPKPAAAAAAAPAAKAAAPAG 63
|
|
| PRK04654 |
PRK04654 |
sec-independent translocase; Provisional |
30-79 |
6.69e-04 |
|
sec-independent translocase; Provisional
Pssm-ID: 135173 [Multi-domain] Cd Length: 214 Bit Score: 41.72 E-value: 6.69e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 503245622 30 TPAMAPAPVAKATRKTAPKPKAASVEAP---VAPKPAAQSAPSPTPPQSEPSP 79
Cdd:PRK04654 140 TPVPAPAPVIAQAQPIAPAPHQTLVPAPhdtIVPAPHAAHLPSAPATPVSVAP 192
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
30-146 |
1.15e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 42.14 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503245622 30 TPAMAPAPVAKATRKT--APKPKAASVEAPVAPKPAAQSAPSPTPPQSEPSPESTfdseqmkALEDLSINLAKAAITAQT 107
Cdd:PRK07003 425 APPAAPAPPATADRGDdaADGDAPVPAKANARASADSRCDERDAQPPADSGSASA-------PASDAPPDAAFEPAPRAA 497
|
90 100 110
....*....|....*....|....*....|....*....
gi 503245622 108 ALASAVLKQPDFNGTPNGDPFQVAPAMTSVMTSLAQNPE 146
Cdd:PRK07003 498 APSAATPAAVPDARAPAAASREDAPAAAAPPAPEARPPT 536
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
35-145 |
1.46e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 42.23 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503245622 35 PAPVAKATRKTAPkPKAASVEAPVAPK--PAAQSAPSPTPPQ--------SEPSPESTFDSEQMKALEDLSINLAKAAIT 104
Cdd:PHA03247 2580 PAVTSRARRPDAP-PQSARPRAPVDDRgdPRGPAPPSPLPPDthapdpppPSPSPAANEPDPHPPPTVPPPERPRDDPAP 2658
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 503245622 105 AQTAL---ASAVLKQPDFNGTPNGDPFQVAPAMTSVMTSLAQNP 145
Cdd:PHA03247 2659 GRVSRprrARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPP 2702
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
30-91 |
1.56e-03 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 41.80 E-value: 1.56e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503245622 30 TPAMAPAPVAKATRKTAPKPKAASVEAPVAPKPAAQSAPSPTPPQSEPSPESTFDSEQMKAL 91
Cdd:PRK12270 59 AAAPAAKAPAAPAPAPPAAAAPAAPPKPAAAAAAAAAPAAPPAAAAAAAPAAAAVEDEVTPL 120
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
30-80 |
1.75e-03 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 41.21 E-value: 1.75e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 503245622 30 TPAMAPAPVAKATRKTAPKPKAASVEAPvAPKPAAQSAPSPTPPQSEPSPE 80
Cdd:PTZ00144 121 GGAPPAAAPAAAAAAKAEKTTPEKPKAA-APTPEPPAASKPTPPAAAKPPE 170
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
30-80 |
2.93e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 41.01 E-value: 2.93e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 503245622 30 TPAMAPAPVAKATRKTAPKPKAASVEAPVAPKPAAQSAPSP--TPPQSEPSPE 80
Cdd:PRK12323 453 APAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADddPPPWEELPPE 505
|
|
| motB |
PRK05996 |
MotB family protein; |
1-102 |
3.60e-03 |
|
MotB family protein;
Pssm-ID: 235665 [Multi-domain] Cd Length: 423 Bit Score: 40.45 E-value: 3.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503245622 1 MTEKSTEKPASKAKTRKAAAPKKAVAAEATPAMAPAPVAKATRKTAPKPKAASVEAPVAPKPAAQSAPSPTPPQSEPSPE 80
Cdd:PRK05996 192 VTTAGDLLPPGQAREQAQGAKSATAAPATVPQAAPLPQAQPKKAATEEELIADAKKAATGEPAANAAKAAKPEPMPDDQQ 271
|
90 100
....*....|....*....|..
gi 503245622 81 STFDSEQMKALEDLSINLAKAA 102
Cdd:PRK05996 272 KEAEQLQAAIAQAIGGVAGKLA 293
|
|
| EstA |
COG1075 |
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ... |
348-434 |
4.08e-03 |
|
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and metabolism];
Pssm-ID: 440693 [Multi-domain] Cd Length: 106 Bit Score: 37.50 E-value: 4.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503245622 348 NSLIKWLTDQGFSVFVVSWVNPDADLKDVTFEdymfggVYKAMSLVREQTGSPKVNTVGYCIGGTLLGVALAHMAakGDD 427
Cdd:COG1075 22 APLAPRLRAAGYPVYALNYPSTNGSIEDSAEQ------LAAFVDAVLAATGAEKVDLVGHSMGGLVARYYLKRLG--GAA 93
|
....*..
gi 503245622 428 SVSSATF 434
Cdd:COG1075 94 KVARVVT 100
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
30-151 |
4.86e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 40.24 E-value: 4.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503245622 30 TPAMAPAPVAKATRK------TAPKPKAASVEAPVAPKPAAQSAPSP-----TPPQSEPSPESTFDSEQMKALEDLSINL 98
Cdd:PRK12323 427 SPAPEALAAARQASArgpggaPAPAPAPAAAPAAAARPAAAGPRPVAaaaaaAPARAAPAAAPAPADDDPPPWEELPPEF 506
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 503245622 99 AKAAITAQTALASAVLKQ--PDFNGTPNGDPF--QVAPAMTSVMTSLAQNPEKVIEA 151
Cdd:PRK12323 507 ASPAPAQPDAAPAGWVAEsiPDPATADPDDAFetLAPAPAAAPAPRAAAATEPVVAP 563
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
31-82 |
5.32e-03 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 40.26 E-value: 5.32e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 503245622 31 PAMAPAPVAKATRKTAPKPKAASVEAPVAPKPAAQSAPSPTPPQSEPSPEST 82
Cdd:PRK12270 38 PGSTAAPTAAAAAAAAAASAPAAAPAAKAPAAPAPAPPAAAAPAAPPKPAAA 89
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
30-80 |
6.83e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 39.58 E-value: 6.83e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 503245622 30 TPAMAPAPVAKATRKTAPKPKAASVEAPVAPKPAAQSAPSPTPPQSEPSPE 80
Cdd:PRK07764 399 PSAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAP 449
|
|
| PRK11633 |
PRK11633 |
cell division protein DedD; Provisional |
30-79 |
8.59e-03 |
|
cell division protein DedD; Provisional
Pssm-ID: 236940 [Multi-domain] Cd Length: 226 Bit Score: 38.45 E-value: 8.59e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 503245622 30 TPAMAPAPVAKATRKTAPKPKAASVEAPvAPKPAAQSAPSPTPPQSEPSP 79
Cdd:PRK11633 96 PVEPEPAPVEPPKPKPVEKPKPKPKPQQ-KVEAPPAPKPEPKPVVEEKAA 144
|
|
|