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Conserved domains on  [gi|1237882582|gb|PAJ76393|]
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hypothetical protein CJF42_00395 [Pseudoalteromonas sp. NBT06-2]

Protein Classification

amidohydrolase family protein( domain architecture ID 10005476)

amidohydrolase family protein is a metallo-dependent hydrolase with a TIM barrel fold and a conserved metal binding site, involving four histidines and one aspartic acid residue; similar to 2-amino-3-carboxymuconate-6-semialdehyde decarboxylase (ACMSD), a metal-dependent enzyme that converts ACMS to alpha-aminomuconate semialdehyde (AMS)

Gene Ontology:  GO:0046872|GO:0016787
PubMed:  9144792
SCOP:  3000428

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
LigW COG2159
5-carboxyvanillate decarboxylase LigW (lignin degradation), amidohydro domain [Carbohydrate ...
98-382 1.74e-37

5-carboxyvanillate decarboxylase LigW (lignin degradation), amidohydro domain [Carbohydrate transport and metabolism];


:

Pssm-ID: 441762 [Multi-domain]  Cd Length: 253  Bit Score: 135.88  E-value: 1.74e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237882582  98 PETMLQDMDDSHIYSASLFPNVANYivnhknisaQASQAYATGYNTWLYEYCSQDPERLHGLGLISRHDPTTMVNQLE-A 176
Cdd:COG2159    13 PEERLADMDEAGIDKAVLSPTPLAD---------PELAALARAANDWLAELVARYPDRFIGFATVDPQDPDAAVEELErA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237882582 177 IEKLGWTCITLRPDIiAGHSLGSPAYETFWQACEDKGISIAFHGGTSLQAPTAGTERYSSRFALHacshyieiqlaflsl 256
Cdd:COG2159    84 VEELGFRGVKLHPAV-GGFPLDDPRLDPLYEAAAELGLPVLVHPGTPPGPPPGLDLYYAAPLILS--------------- 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237882582 257 ldaGVLERYPTLKLGFFEAGASWLPAWLWRLdnicypefpglvknrIKMLPSeyfkrqCWI---AIEMDEPCLAQVIDIV 333
Cdd:COG2159   148 ---GVAERFPDLKFILAHGGGPWLPELLGRL---------------LKRLPN------VYFdtsGVFPRPEALRELLETL 203
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1237882582 334 GHDRLLFGTDFPHPDHLHFdFKHLEQQNsDIKPPDLDCILQHNPKQFFG 382
Cdd:COG2159   204 GADRILFGSDYPHWDPPEA-LEALEELP-GLSEEDREKILGGNAARLLG 250
 
Name Accession Description Interval E-value
LigW COG2159
5-carboxyvanillate decarboxylase LigW (lignin degradation), amidohydro domain [Carbohydrate ...
98-382 1.74e-37

5-carboxyvanillate decarboxylase LigW (lignin degradation), amidohydro domain [Carbohydrate transport and metabolism];


Pssm-ID: 441762 [Multi-domain]  Cd Length: 253  Bit Score: 135.88  E-value: 1.74e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237882582  98 PETMLQDMDDSHIYSASLFPNVANYivnhknisaQASQAYATGYNTWLYEYCSQDPERLHGLGLISRHDPTTMVNQLE-A 176
Cdd:COG2159    13 PEERLADMDEAGIDKAVLSPTPLAD---------PELAALARAANDWLAELVARYPDRFIGFATVDPQDPDAAVEELErA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237882582 177 IEKLGWTCITLRPDIiAGHSLGSPAYETFWQACEDKGISIAFHGGTSLQAPTAGTERYSSRFALHacshyieiqlaflsl 256
Cdd:COG2159    84 VEELGFRGVKLHPAV-GGFPLDDPRLDPLYEAAAELGLPVLVHPGTPPGPPPGLDLYYAAPLILS--------------- 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237882582 257 ldaGVLERYPTLKLGFFEAGASWLPAWLWRLdnicypefpglvknrIKMLPSeyfkrqCWI---AIEMDEPCLAQVIDIV 333
Cdd:COG2159   148 ---GVAERFPDLKFILAHGGGPWLPELLGRL---------------LKRLPN------VYFdtsGVFPRPEALRELLETL 203
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1237882582 334 GHDRLLFGTDFPHPDHLHFdFKHLEQQNsDIKPPDLDCILQHNPKQFFG 382
Cdd:COG2159   204 GADRILFGSDYPHWDPPEA-LEALEELP-GLSEEDREKILGGNAARLLG 250
Amidohydro_2 pfam04909
Amidohydrolase; These proteins are amidohydrolases that are related to pfam01979.
90-382 1.09e-20

Amidohydrolase; These proteins are amidohydrolases that are related to pfam01979.


Pssm-ID: 428190 [Multi-domain]  Cd Length: 283  Bit Score: 91.05  E-value: 1.09e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237882582  90 DKRKQAAFPETMLQDMDDSHIYSASLFPNVANYIVNHKNIS-AQASQAYATGYNTWLYEYCSQDPERLHGLGLISRHDPT 168
Cdd:pfam04909  10 DDERIGFDPGGRLPFMKRRGYDPRDASPEDLLALGAALGVArAVVVAASCRGANNRVAAEALARPGRFLGGVAVVPLDPE 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237882582 169 TMVNQLE-AIEKLGWTCITLRPDIIAGHSLGSPAYETFWQACEDKGISIAFHGGtslqaptagteryssrfalhaCSHYI 247
Cdd:pfam04909  90 DAAAELErAVGEAGFRGVRLNPHPGGDPLLGDRLDRPIYEALEELGLPVDIHTG---------------------FGDRP 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237882582 248 EIQLAFLSLLDAGVLERYPTLKLGFFEAGASWLPAWLWRLDNIcypefpglvkNRIKMLPSEYFKRQCWIAIEMDEPC-- 325
Cdd:pfam04909 149 EDTRAIQPLLLAGVARKFPDLKIVLDHGGGPWIPEGLDDPAAL----------ALLARRPNVYVKLSGLYRDLYFDAPla 218
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1237882582 326 ----LAQVIDIVGHDRLLFGTDFPHPD--HLHFDFKHLEQQNSDIKPPDL-DCILQHNPKQFFG 382
Cdd:pfam04909 219 drpyLARLLEAFGPDRILFGSDWPHPPleISPDDGVLLDLPLLLALSDEErEKILGGNAARLYG 282
 
Name Accession Description Interval E-value
LigW COG2159
5-carboxyvanillate decarboxylase LigW (lignin degradation), amidohydro domain [Carbohydrate ...
98-382 1.74e-37

5-carboxyvanillate decarboxylase LigW (lignin degradation), amidohydro domain [Carbohydrate transport and metabolism];


Pssm-ID: 441762 [Multi-domain]  Cd Length: 253  Bit Score: 135.88  E-value: 1.74e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237882582  98 PETMLQDMDDSHIYSASLFPNVANYivnhknisaQASQAYATGYNTWLYEYCSQDPERLHGLGLISRHDPTTMVNQLE-A 176
Cdd:COG2159    13 PEERLADMDEAGIDKAVLSPTPLAD---------PELAALARAANDWLAELVARYPDRFIGFATVDPQDPDAAVEELErA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237882582 177 IEKLGWTCITLRPDIiAGHSLGSPAYETFWQACEDKGISIAFHGGTSLQAPTAGTERYSSRFALHacshyieiqlaflsl 256
Cdd:COG2159    84 VEELGFRGVKLHPAV-GGFPLDDPRLDPLYEAAAELGLPVLVHPGTPPGPPPGLDLYYAAPLILS--------------- 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237882582 257 ldaGVLERYPTLKLGFFEAGASWLPAWLWRLdnicypefpglvknrIKMLPSeyfkrqCWI---AIEMDEPCLAQVIDIV 333
Cdd:COG2159   148 ---GVAERFPDLKFILAHGGGPWLPELLGRL---------------LKRLPN------VYFdtsGVFPRPEALRELLETL 203
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1237882582 334 GHDRLLFGTDFPHPDHLHFdFKHLEQQNsDIKPPDLDCILQHNPKQFFG 382
Cdd:COG2159   204 GADRILFGSDYPHWDPPEA-LEALEELP-GLSEEDREKILGGNAARLLG 250
Amidohydro_2 pfam04909
Amidohydrolase; These proteins are amidohydrolases that are related to pfam01979.
90-382 1.09e-20

Amidohydrolase; These proteins are amidohydrolases that are related to pfam01979.


Pssm-ID: 428190 [Multi-domain]  Cd Length: 283  Bit Score: 91.05  E-value: 1.09e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237882582  90 DKRKQAAFPETMLQDMDDSHIYSASLFPNVANYIVNHKNIS-AQASQAYATGYNTWLYEYCSQDPERLHGLGLISRHDPT 168
Cdd:pfam04909  10 DDERIGFDPGGRLPFMKRRGYDPRDASPEDLLALGAALGVArAVVVAASCRGANNRVAAEALARPGRFLGGVAVVPLDPE 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237882582 169 TMVNQLE-AIEKLGWTCITLRPDIIAGHSLGSPAYETFWQACEDKGISIAFHGGtslqaptagteryssrfalhaCSHYI 247
Cdd:pfam04909  90 DAAAELErAVGEAGFRGVRLNPHPGGDPLLGDRLDRPIYEALEELGLPVDIHTG---------------------FGDRP 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237882582 248 EIQLAFLSLLDAGVLERYPTLKLGFFEAGASWLPAWLWRLDNIcypefpglvkNRIKMLPSEYFKRQCWIAIEMDEPC-- 325
Cdd:pfam04909 149 EDTRAIQPLLLAGVARKFPDLKIVLDHGGGPWIPEGLDDPAAL----------ALLARRPNVYVKLSGLYRDLYFDAPla 218
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1237882582 326 ----LAQVIDIVGHDRLLFGTDFPHPD--HLHFDFKHLEQQNSDIKPPDL-DCILQHNPKQFFG 382
Cdd:pfam04909 219 drpyLARLLEAFGPDRILFGSDWPHPPleISPDDGVLLDLPLLLALSDEErEKILGGNAARLYG 282
COG3618 COG3618
Predicted metal-dependent hydrolase, TIM-barrel fold [General function prediction only];
324-382 1.55e-03

Predicted metal-dependent hydrolase, TIM-barrel fold [General function prediction only];


Pssm-ID: 442836 [Multi-domain]  Cd Length: 272  Bit Score: 39.81  E-value: 1.55e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1237882582 324 PCLAQVIDIVGHDRLLFGTDFPHPDHLHFD---FKHLEQQNSDIKPPDLDCILQHNPKQFFG 382
Cdd:COG3618   208 PYARALLEAFGPDRLMWGSDWPVTLLAPDYgelLDLLEELLPDLSEAERRAILGDNAARLYG 269
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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