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Conserved domains on  [gi|1125100809|gb|OLA62814|]
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hypothetical protein BHW37_00140 [Firmicutes bacterium CAG:272_52_7]

Protein Classification

transglutaminase domain-containing protein( domain architecture ID 10261298)

transglutaminase domain-containing protein similar to mammalian dynein regulatory complex subunit 7 and Drosophila melanogaster lost boys protein (lobo), which are components of the nexin-dynein regulatory complex (N-DRC) and essential for N-DRC integrity

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Transglut_core pfam01841
Transglutaminase-like superfamily; This family includes animal transglutaminases and other ...
 346-445 2.39e-09

Transglutaminase-like superfamily; This family includes animal transglutaminases and other bacterial proteins of unknown function. Sequence conservation in this superfamily primarily involves three motifs that centre around conserved cysteine, histidine, and aspartate residues that form the catalytic triad in the structurally characterized transglutaminase, the human blood clotting factor XIIIa'. On the basis of the experimentally demonstrated activity of the Methanobacterium phage pseudomurein endoisopeptidase, it is proposed that many, if not all, microbial homologs of the transglutaminases are proteases and that the eukaryotic transglutaminases have evolved from an ancestral protease.


:

Pssm-ID: 376628 [Multi-domain]  Cd Length: 108  Bit Score: 54.72  E-value: 2.39e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125100809 346 DLAKKIVNDGMTNDEKIKKIWNYTRLKIKYTgRSTKSDVYTAAYEGMTTGGGDCYTYYAINTLLFRHLGIE-------NT 418
Cdd:pfam01841   2 ALADRITGGATDPLEKARAIYDYVRKNITYD-LPGRSPGDGDAEEFLFTGKGDCEDFASLFVALLRALGIParyvtgyLR 80

                          90       100
                  ....*....|....*....|....*..
gi 1125100809 419 EVRRVEGKSRHWWSLVLFDDGKWYFVD 445
Cdd:pfam01841  81 GPDTVRGGDAHAWVEVYLPGYGWVPVD 107
DUF5011 super family cl47259
Domain of unknown function (DUF5011); This entry represents a bacterial immunoglobulin-like ...
 268-332 5.82e-08

Domain of unknown function (DUF5011); This entry represents a bacterial immunoglobulin-like domain.


The actual alignment was detected with superfamily member pfam16403:

Pssm-ID: 435320 [Multi-domain]  Cd Length: 71  Bit Score: 49.47  E-value: 5.82e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1125100809 268 DITITVGDTisYK-SGVTVSDNsGEDIEFTVDAS-AVNRNKAGTYKVKYTAADSSGNTAEEYRTVIV 332
Cdd:pfam16403   8 DITIELGTT--YEdPGATATDN-DGDLTDKVKVTgSVDTSKPGTYTLTYTVTDSDGNSATVTRTVTV 71
PLN02197 super family cl31838
pectinesterase
 111-149 1.51e-03

pectinesterase


The actual alignment was detected with superfamily member PLN02197:

Pssm-ID: 177848 [Multi-domain]  Cd Length: 588  Bit Score: 41.14  E-value: 1.51e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1125100809 111 RLTVCTYNRTVKVSVGSTEAVTVSDYIPTPGFAAKFVGF 149
Cdd:PLN02197  335 RKTVISYNRSVKLSPGTTTSLSGTVQVESEGFMAKWIGF 373
 
Name Accession Description Interval E-value
Transglut_core pfam01841
Transglutaminase-like superfamily; This family includes animal transglutaminases and other ...
 346-445 2.39e-09

Transglutaminase-like superfamily; This family includes animal transglutaminases and other bacterial proteins of unknown function. Sequence conservation in this superfamily primarily involves three motifs that centre around conserved cysteine, histidine, and aspartate residues that form the catalytic triad in the structurally characterized transglutaminase, the human blood clotting factor XIIIa'. On the basis of the experimentally demonstrated activity of the Methanobacterium phage pseudomurein endoisopeptidase, it is proposed that many, if not all, microbial homologs of the transglutaminases are proteases and that the eukaryotic transglutaminases have evolved from an ancestral protease.


Pssm-ID: 376628 [Multi-domain]  Cd Length: 108  Bit Score: 54.72  E-value: 2.39e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125100809 346 DLAKKIVNDGMTNDEKIKKIWNYTRLKIKYTgRSTKSDVYTAAYEGMTTGGGDCYTYYAINTLLFRHLGIE-------NT 418
Cdd:pfam01841   2 ALADRITGGATDPLEKARAIYDYVRKNITYD-LPGRSPGDGDAEEFLFTGKGDCEDFASLFVALLRALGIParyvtgyLR 80

                          90       100
                  ....*....|....*....|....*..
gi 1125100809 419 EVRRVEGKSRHWWSLVLFDDGKWYFVD 445
Cdd:pfam01841  81 GPDTVRGGDAHAWVEVYLPGYGWVPVD 107
YebA COG1305
Transglutaminase-like enzyme, putative cysteine protease [Posttranslational modification, ...
 344-445 9.42e-09

Transglutaminase-like enzyme, putative cysteine protease [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440916 [Multi-domain]  Cd Length: 174  Bit Score: 54.63  E-value: 9.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125100809 344 IADLAKKIVNDGMTNDEKIKKIWNYTRLKIKYTGRSTKSDvyTAAYEGMTTGGGDCYTYYAINTLLFRHLGI-------- 415
Cdd:COG1305    63 LRALAAELTGGATTPYEKARALYDWVRDNIRYDPGSTGVG--TTALETLERRRGVCRDFAHLLVALLRALGIparyvsgy 140

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1125100809 416 ---ENTEVRRVEGkSRHWWSLVLFDDGKWYFVD 445
Cdd:COG1305   141 lpgEPPPGGGRAD-DAHAWVEVYLPGAGWVPFD 172
DUF5011 pfam16403
Domain of unknown function (DUF5011); This entry represents a bacterial immunoglobulin-like ...
 268-332 5.82e-08

Domain of unknown function (DUF5011); This entry represents a bacterial immunoglobulin-like domain.


Pssm-ID: 435320 [Multi-domain]  Cd Length: 71  Bit Score: 49.47  E-value: 5.82e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1125100809 268 DITITVGDTisYK-SGVTVSDNsGEDIEFTVDAS-AVNRNKAGTYKVKYTAADSSGNTAEEYRTVIV 332
Cdd:pfam16403   8 DITIELGTT--YEdPGATATDN-DGDLTDKVKVTgSVDTSKPGTYTLTYTVTDSDGNSATVTRTVTV 71
PLN02197 PLN02197
pectinesterase
 111-149 1.51e-03

pectinesterase


Pssm-ID: 177848 [Multi-domain]  Cd Length: 588  Bit Score: 41.14  E-value: 1.51e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1125100809 111 RLTVCTYNRTVKVSVGSTEAVTVSDYIPTPGFAAKFVGF 149
Cdd:PLN02197  335 RKTVISYNRSVKLSPGTTTSLSGTVQVESEGFMAKWIGF 373
 
Name Accession Description Interval E-value
Transglut_core pfam01841
Transglutaminase-like superfamily; This family includes animal transglutaminases and other ...
 346-445 2.39e-09

Transglutaminase-like superfamily; This family includes animal transglutaminases and other bacterial proteins of unknown function. Sequence conservation in this superfamily primarily involves three motifs that centre around conserved cysteine, histidine, and aspartate residues that form the catalytic triad in the structurally characterized transglutaminase, the human blood clotting factor XIIIa'. On the basis of the experimentally demonstrated activity of the Methanobacterium phage pseudomurein endoisopeptidase, it is proposed that many, if not all, microbial homologs of the transglutaminases are proteases and that the eukaryotic transglutaminases have evolved from an ancestral protease.


Pssm-ID: 376628 [Multi-domain]  Cd Length: 108  Bit Score: 54.72  E-value: 2.39e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125100809 346 DLAKKIVNDGMTNDEKIKKIWNYTRLKIKYTgRSTKSDVYTAAYEGMTTGGGDCYTYYAINTLLFRHLGIE-------NT 418
Cdd:pfam01841   2 ALADRITGGATDPLEKARAIYDYVRKNITYD-LPGRSPGDGDAEEFLFTGKGDCEDFASLFVALLRALGIParyvtgyLR 80

                          90       100
                  ....*....|....*....|....*..
gi 1125100809 419 EVRRVEGKSRHWWSLVLFDDGKWYFVD 445
Cdd:pfam01841  81 GPDTVRGGDAHAWVEVYLPGYGWVPVD 107
YebA COG1305
Transglutaminase-like enzyme, putative cysteine protease [Posttranslational modification, ...
 344-445 9.42e-09

Transglutaminase-like enzyme, putative cysteine protease [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440916 [Multi-domain]  Cd Length: 174  Bit Score: 54.63  E-value: 9.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125100809 344 IADLAKKIVNDGMTNDEKIKKIWNYTRLKIKYTGRSTKSDvyTAAYEGMTTGGGDCYTYYAINTLLFRHLGI-------- 415
Cdd:COG1305    63 LRALAAELTGGATTPYEKARALYDWVRDNIRYDPGSTGVG--TTALETLERRRGVCRDFAHLLVALLRALGIparyvsgy 140

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1125100809 416 ---ENTEVRRVEGkSRHWWSLVLFDDGKWYFVD 445
Cdd:COG1305   141 lpgEPPPGGGRAD-DAHAWVEVYLPGAGWVPFD 172
DUF5011 pfam16403
Domain of unknown function (DUF5011); This entry represents a bacterial immunoglobulin-like ...
 268-332 5.82e-08

Domain of unknown function (DUF5011); This entry represents a bacterial immunoglobulin-like domain.


Pssm-ID: 435320 [Multi-domain]  Cd Length: 71  Bit Score: 49.47  E-value: 5.82e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1125100809 268 DITITVGDTisYK-SGVTVSDNsGEDIEFTVDAS-AVNRNKAGTYKVKYTAADSSGNTAEEYRTVIV 332
Cdd:pfam16403   8 DITIELGTT--YEdPGATATDN-DGDLTDKVKVTgSVDTSKPGTYTLTYTVTDSDGNSATVTRTVTV 71
CYK3 COG5279
Cytokinesis protein 3, contains TGc (transglutaminase/protease-like) domain [Cell cycle ...
 289-446 9.18e-04

Cytokinesis protein 3, contains TGc (transglutaminase/protease-like) domain [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444090 [Multi-domain]  Cd Length: 250  Bit Score: 41.15  E-value: 9.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125100809 289 SGEDIEFTVDASAVNRNKAGTYKVKYTAADSSGNTAEEYRTVIVIKLSIEKVEGMIadlaKKIVNDGMTNDEKIKKIWNY 368
Cdd:COG5279    36 LGSLYELAVLLFALLEGNSLAAFLKDAISSSTIYALKDEEGLLTEKATIADESKDD----DYIITPGMSDYEKVRAIHDW 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125100809 369 TRLKIKY---TGRSTKSDVYTAaYEGMTTGGGDCYTYYAINTLLFRHLGIENTEVR-----RVEGKSRHWWSLVLFDdGK 440
Cdd:COG5279   112 IVDNIEYdyeAYNSGKSDSHSA-YGALKNGKGVCEGYAKLFKLLCNKAGIECYIVTgyargSGGESGNHAWNAVKID-GK 189


                  ....*.
gi 1125100809 441 WYFVDS 446
Cdd:COG5279   190 WYLVDA 195
PLN02197 PLN02197
pectinesterase
 111-149 1.51e-03

pectinesterase


Pssm-ID: 177848 [Multi-domain]  Cd Length: 588  Bit Score: 41.14  E-value: 1.51e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1125100809 111 RLTVCTYNRTVKVSVGSTEAVTVSDYIPTPGFAAKFVGF 149
Cdd:PLN02197  335 RKTVISYNRSVKLSPGTTTSLSGTVQVESEGFMAKWIGF 373
HYR pfam02494
HYR domain; This domain is known as the HYR (Hyalin Repeat) domain, after the protein hyalin ...
 257-332 4.06e-03

HYR domain; This domain is known as the HYR (Hyalin Repeat) domain, after the protein hyalin that is composed exclusively of this repeat. This domain probably corresponds to a new superfamily in the immunoglobulin fold. The function of this domain is uncertain it may be involved in cell adhesion.


Pssm-ID: 460572 [Multi-domain]  Cd Length: 81  Bit Score: 36.21  E-value: 4.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125100809 257 DTEPPVFSGLHDI--TITVGDT---ISYKSgVTVSDNSGEDIEFTVDASAVNRNKAGTYKVKYTAADSSGNTAEEYRTVI 331
Cdd:pfam02494   2 DTTPPTVKCPNNIvrTVELGTStvrVFFTE-PTAFDNSGQAILVSRTAQPGDFFPVGTTTVTYVAYDNSGNRASCTFTVT 80


                  .
gi 1125100809 332 V 332
Cdd:pfam02494  81 V 81
 
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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