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Conserved domains on  [gi|1481164567|ref|WP_119679700|]
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metallopeptidase family protein [Indioceanicola profundi]

Protein Classification

metallopeptidase family protein( domain architecture ID 10790413)

metallopeptidase family protein containing a minimal metalloprotease (MMP)-like domain; belongs to a family of zinc-dependent metalloproteases characterized by a conserved HExxHxxGxxD active site motif, called zincins

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG3824 COG3824
Predicted Zn-dependent protease, minimal metalloprotease (MMP)-like domain [Posttranslational ...
 10-131 1.26e-58

Predicted Zn-dependent protease, minimal metalloprotease (MMP)-like domain [Posttranslational modification, protein turnover, chaperones];


:

Pssm-ID: 443036  Cd Length: 122  Bit Score: 177.24  E-value: 1.26e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481164567  10 APTIEEFEAIAARAFDTIPEELRRHVGNVVIQVEEFPDEETEQEMKLESPFDILGLYRGIGLPFQSMTQPHPEPEMIYLY 89
Cdd:COG3824     1 APSLEEFEALVAEALDALPEEFRALLDNVVILVEDFPDDEVLEELGLEDPPDLLGLYEGVPLTERSVSYSGELPDRITLY 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1481164567  90 RRPILDYWCETgEELTDVIRHVLIHEIGHHFGFSDDDMEALE 131
Cdd:COG3824    81 RRPILDYWAER-EELVEEVRHTLVHEIGHHFGLSDEDLHELG 121
 
Name Accession Description Interval E-value
COG3824 COG3824
Predicted Zn-dependent protease, minimal metalloprotease (MMP)-like domain [Posttranslational ...
 10-131 1.26e-58

Predicted Zn-dependent protease, minimal metalloprotease (MMP)-like domain [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443036  Cd Length: 122  Bit Score: 177.24  E-value: 1.26e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481164567  10 APTIEEFEAIAARAFDTIPEELRRHVGNVVIQVEEFPDEETEQEMKLESPFDILGLYRGIGLPFQSMTQPHPEPEMIYLY 89
Cdd:COG3824     1 APSLEEFEALVAEALDALPEEFRALLDNVVILVEDFPDDEVLEELGLEDPPDLLGLYEGVPLTERSVSYSGELPDRITLY 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1481164567  90 RRPILDYWCETgEELTDVIRHVLIHEIGHHFGFSDDDMEALE 131
Cdd:COG3824    81 RRPILDYWAER-EELVEEVRHTLVHEIGHHFGLSDEDLHELG 121
MMP_ACEL2062 cd12952
Minimal MMP-like domain found in Acidothermus cellulolyticus hypothetical protein ACEL2062 and ...
 12-129 5.60e-51

Minimal MMP-like domain found in Acidothermus cellulolyticus hypothetical protein ACEL2062 and similar protein; The subfamily includes an uncharacterized protein from Acidothermus cellulolyticus (ACEL2062) and its homologs from bacteria. Although its biological role remains unclear, ACEL2062 contains a minimal metalloprotease (MMP)-like domain consisting of 3-stranded mixed 2-beta sheets and a HExxHxxGxxD/S (x could be any amino acid) motif. It may belong to a superfamily of bacterial zinc metallo-peptidases, which is characterized by a conserved HExxHxxGxxD motif.


Pssm-ID: 240572  Cd Length: 117  Bit Score: 157.67  E-value: 5.60e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481164567  12 TIEEFEAIAARAFDTIPEELRRHVGNVVIQVEEFPDEETEQEMKLESPFDILGLYRGIGLPFQSMTQPHPEPEMIYLYRR 91
Cdd:cd12952     1 SLEEFEALVEEALDSLPEEFRAALDNVVILVEDFPDDETLEALGIPDPPELLGLYEGVPLTERSVSDSGVLPDRITLFRR 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1481164567  92 PILDYWcETGEELTDVIRHVLIHEIGHHFGFSDDDMEA 129
Cdd:cd12952    81 PLLRYC-RTREELREEVRHTVLHEIGHHFGLSDDDLHE 117
Zincin_1 pfam06262
Zincin-like metallopeptidase; This family of proteins has a conserved HEXXH motif, suggesting ...
 37-131 7.52e-42

Zincin-like metallopeptidase; This family of proteins has a conserved HEXXH motif, suggesting they are putative peptidases of zincin fold. The structure of this family is a minimal version of the metalloprotease fold (PDB:3E11).


Pssm-ID: 428855  Cd Length: 95  Bit Score: 133.82  E-value: 7.52e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481164567  37 NVVIQVEEFPDEETEQEMKLESPFDILGLYRGIGLPFQSMTQPHPEPEMIYLYRRPILDyWCETGEELTDVIRHVLIHEI 116
Cdd:pfam06262   2 NVVVLVEDFPDPEVLAELGLPDPPELLGLYEGVPLTERSVGYTGALPDRITLYRRPLLD-WAETGEELGELVRHTVVHEI 80

                          90
                  ....*....|....*
gi 1481164567 117 GHHFGFSDDDMEALE 131
Cdd:pfam06262  81 GHHFGLSDEDLHALE 95
 
Name Accession Description Interval E-value
COG3824 COG3824
Predicted Zn-dependent protease, minimal metalloprotease (MMP)-like domain [Posttranslational ...
 10-131 1.26e-58

Predicted Zn-dependent protease, minimal metalloprotease (MMP)-like domain [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443036  Cd Length: 122  Bit Score: 177.24  E-value: 1.26e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481164567  10 APTIEEFEAIAARAFDTIPEELRRHVGNVVIQVEEFPDEETEQEMKLESPFDILGLYRGIGLPFQSMTQPHPEPEMIYLY 89
Cdd:COG3824     1 APSLEEFEALVAEALDALPEEFRALLDNVVILVEDFPDDEVLEELGLEDPPDLLGLYEGVPLTERSVSYSGELPDRITLY 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1481164567  90 RRPILDYWCETgEELTDVIRHVLIHEIGHHFGFSDDDMEALE 131
Cdd:COG3824    81 RRPILDYWAER-EELVEEVRHTLVHEIGHHFGLSDEDLHELG 121
MMP_ACEL2062 cd12952
Minimal MMP-like domain found in Acidothermus cellulolyticus hypothetical protein ACEL2062 and ...
 12-129 5.60e-51

Minimal MMP-like domain found in Acidothermus cellulolyticus hypothetical protein ACEL2062 and similar protein; The subfamily includes an uncharacterized protein from Acidothermus cellulolyticus (ACEL2062) and its homologs from bacteria. Although its biological role remains unclear, ACEL2062 contains a minimal metalloprotease (MMP)-like domain consisting of 3-stranded mixed 2-beta sheets and a HExxHxxGxxD/S (x could be any amino acid) motif. It may belong to a superfamily of bacterial zinc metallo-peptidases, which is characterized by a conserved HExxHxxGxxD motif.


Pssm-ID: 240572  Cd Length: 117  Bit Score: 157.67  E-value: 5.60e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481164567  12 TIEEFEAIAARAFDTIPEELRRHVGNVVIQVEEFPDEETEQEMKLESPFDILGLYRGIGLPFQSMTQPHPEPEMIYLYRR 91
Cdd:cd12952     1 SLEEFEALVEEALDSLPEEFRAALDNVVILVEDFPDDETLEALGIPDPPELLGLYEGVPLTERSVSDSGVLPDRITLFRR 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1481164567  92 PILDYWcETGEELTDVIRHVLIHEIGHHFGFSDDDMEA 129
Cdd:cd12952    81 PLLRYC-RTREELREEVRHTVLHEIGHHFGLSDDDLHE 117
Zincin_1 pfam06262
Zincin-like metallopeptidase; This family of proteins has a conserved HEXXH motif, suggesting ...
 37-131 7.52e-42

Zincin-like metallopeptidase; This family of proteins has a conserved HEXXH motif, suggesting they are putative peptidases of zincin fold. The structure of this family is a minimal version of the metalloprotease fold (PDB:3E11).


Pssm-ID: 428855  Cd Length: 95  Bit Score: 133.82  E-value: 7.52e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481164567  37 NVVIQVEEFPDEETEQEMKLESPFDILGLYRGIGLPFQSMTQPHPEPEMIYLYRRPILDyWCETGEELTDVIRHVLIHEI 116
Cdd:pfam06262   2 NVVVLVEDFPDPEVLAELGLPDPPELLGLYEGVPLTERSVGYTGALPDRITLYRRPLLD-WAETGEELGELVRHTVVHEI 80

                          90
                  ....*....|....*
gi 1481164567 117 GHHFGFSDDDMEALE 131
Cdd:pfam06262  81 GHHFGLSDEDLHALE 95
MMP_TTHA0227_like cd12927
Minimal MMP-like domain found in Thermus thermophilus TTHA0227, Acidothermus cellulolyticus ...
 13-120 4.12e-28

Minimal MMP-like domain found in Thermus thermophilus TTHA0227, Acidothermus cellulolyticus ACEL2062 and similar proteins; The family includes hypothetical proteins from bacteria that contain a minimal metalloprotease (MMP)-like domain consisting of 3-stranded mixed 2-beta sheets.These proteins may belong to a superfamily of bacterial zinc metallo-peptidases, which is characterized by a conserved HExxHxxGxxD (x could be any amino acid) motif. However, some family members carry a shorter HExxHxxG motif or HExxH motif. Some others do not have such a motif, but still share very high sequence similarity.


Pssm-ID: 240571  Cd Length: 97  Bit Score: 99.21  E-value: 4.12e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481164567  13 IEEFEAIAARAFDTIPEELRRHVGNVVIQVEEFPDEETEQemkLESPFDILGLYRGIGLpfqsmtqPHPEPEMIYLYRRP 92
Cdd:cd12927     1 AEEFDDLVEEALDRLPERFPDELDNVGIAVEDVPPEDPLG---WEDDPVLLGLYEGAPL-------TGGLPDRIVLYRRP 70

                          90       100
                  ....*....|....*....|....*...
gi 1481164567  93 ILDYWCETgEELTDVIRHVLIHEIGHHF 120
Cdd:cd12927    71 IERRARDE-EELRELVRETVVHELAHHL 97
MMP_TTHA0227_like_1 cd12954
Minimal MMP-like domain found in a group of hypothetical proteins from alphaproteobacteria and ...
 14-121 7.85e-04

Minimal MMP-like domain found in a group of hypothetical proteins from alphaproteobacteria and actinobacteria; The subfamily includes some uncharacterized bacterial proteins which show high sequence similarity with Thermus thermophilus hypothetical protein TTHA0227. However, they do not contain the conserved HExxH (x could be any amino acid) motif. They may not have any zinc metallo-peptidase activity.


Pssm-ID: 240574  Cd Length: 99  Bit Score: 36.47  E-value: 7.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481164567  14 EEFEAIAARAFDTIPEELRRHVGNVVIQVEEFPDeeteqeMKLESPFDilglyRGIGLPfQSMTQPHPEPEMIYLYRRPI 93
Cdd:cd12954     4 ERFDDLVAEAVARLAARWPDELAGVEFAVEDVPP------SDPAPWED-----EPVPLA-RAFPAGRGTPARIVLYRRPI 71

                          90       100
                  ....*....|....*....|....*...
gi 1481164567  94 lDYWCETGEELTDVIRHVLIHEIGHHFG 121
Cdd:cd12954    72 -ERRASSEAELRALVHDVVVEQVAELLG 98
MMP_TTHA0227 cd12953
Minimal MMP-like domain found in Thermus thermophilus hypothetical protein TTHA0227 and ...
 12-119 2.25e-03

Minimal MMP-like domain found in Thermus thermophilus hypothetical protein TTHA0227 and similar proteins; The subfamily includes an uncharacterized protein from Thermus thermophilus (TTHA0227) and its homologs from bacteria. Although its biological role remains unclear, TTHA0227 contains a minimal metalloprotease (MMP)-like domain consisting of 3-stranded mixed 2-beta sheets and a HExxH (x could be any amino acid) motif. It may belong to a superfamily of bacterial zinc metallo-peptidases, which is characterized by a conserved HExxHxxGxxD motif.


Pssm-ID: 240573  Cd Length: 112  Bit Score: 35.28  E-value: 2.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481164567  12 TIEEFEAIAARAFDTIPEELRRHvGNVVIQVEEfpdeeteqEMKLESPFDILGLYRgIGLPFQSMTQPHpepemIYLYRR 91
Cdd:cd12953     1 DIDEFEELLEEIADEIPEAFFRE-LNGGIILLP--------EAKYHPESPNGDLYI-LGEYVRDILGRQ-----IVIYYG 65

                          90       100
                  ....*....|....*....|....*....
gi 1481164567  92 PIL-DYWCETGEELTDVIRHVLIHEIGHH 119
Cdd:cd12953    66 SFAaVYGDESREDWKEELRETLLHELRHH 94
Peptidase_M57 pfam12388
Dual-action HEIGH metallo-peptidase; The catalytic triad for this family of proteases is ...
 105-126 6.90e-03

Dual-action HEIGH metallo-peptidase; The catalytic triad for this family of proteases is HE-H-H, which in many members is in the sequence motif HEIGH.


Pssm-ID: 432518  Cd Length: 212  Bit Score: 35.18  E-value: 6.90e-03
                          10        20
                  ....*....|....*....|..
gi 1481164567 105 TDVIRHVLIHEIGHHFGFSDDD 126
Cdd:pfam12388 130 TDVNEHVITHELGHSIGFRHSD 151
 
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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