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Conserved domains on  [gi|1200742288|ref|NP_001339028|]
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vezatin isoform j [Homo sapiens]

Protein Classification

vezatin family protein( domain architecture ID 10576871)

vezatin family protein similar to vezatin that plays a pivotal role in the establishment of adherens junctions and their maintenance in adult life; it bridges myosin VIIA to the cadherin-catenins complex

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Vezatin pfam12632
Mysoin-binding motif of peroxisomes; Vezatin is a peroxisome transmembrane receptor that is ...
12-304 1.90e-104

Mysoin-binding motif of peroxisomes; Vezatin is a peroxisome transmembrane receptor that is involved in membrane-membrane and cell-cell adhesions. In the movement of peroxisomes it binds to class V and class VIIa myosins to guide the organelle through the microtubules and allow pathogens to internalize themselves into host cells. Vezatin is crucial for spermatozoan production. In mouse cells it interacts with the cadherin-catenin complex bridging it to the C-terminal FERM domain of myosin VIIA.


:

Pssm-ID: 463650  Cd Length: 282  Bit Score: 318.18  E-value: 1.90e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200742288  12 LFAFISLLVMLPTWWIVSSWLVWGVILFVYL---VIRALRLWRTAKLQVTLKKYSVHLEDMATNSRAFTNLVRKALRLIQ 88
Cdd:pfam12632   1 LIALIIFLLKQARYWLSSSSLFKGFKLLLLIsskLVRLYAYWRRQRLQIIRHKALNQLEEFVANSQAFDKLVRKALILIQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200742288  89 ETEVISRGFTLlldrVSAACPFNKAG-QHPSQHLIGLRKAVYRTLRANFQAARLATLYMLKNyplnSESDNVTNYICVVP 167
Cdd:pfam12632  81 EVELVSRGYRL----SSPLPPFSRIEdQSQSRRCIGLRKALYSTLSFLFLNLRQAISKLLPL----SEGDNLEKYCDIYN 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200742288 168 FKELGLglSEEQISEEEAHNFTDGFSLPALKVLFQLWVAQSSEFFRRLALLLSTANSPPGPLLTPALLPHRILSDVTQGL 247
Cdd:pfam12632 153 INELGL--SEESLSLEEAEELTDSESLPALKFLFQLFNGLRKEFLCRLLALLSDGSKPNFFRWKVADLFHRILSELLQGL 230
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1200742288 248 PHAHSACLEELkrsyefYRYFETQHQ-SVPQCLSKTQQKSRELNNVHTAVRSLQLHLK 304
Cdd:pfam12632 231 SHALGSCLEEL------HRIFETQESfTTPDRRERARAQSRKLNSLSTLIRSLQLHLK 282
 
Name Accession Description Interval E-value
Vezatin pfam12632
Mysoin-binding motif of peroxisomes; Vezatin is a peroxisome transmembrane receptor that is ...
12-304 1.90e-104

Mysoin-binding motif of peroxisomes; Vezatin is a peroxisome transmembrane receptor that is involved in membrane-membrane and cell-cell adhesions. In the movement of peroxisomes it binds to class V and class VIIa myosins to guide the organelle through the microtubules and allow pathogens to internalize themselves into host cells. Vezatin is crucial for spermatozoan production. In mouse cells it interacts with the cadherin-catenin complex bridging it to the C-terminal FERM domain of myosin VIIA.


Pssm-ID: 463650  Cd Length: 282  Bit Score: 318.18  E-value: 1.90e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200742288  12 LFAFISLLVMLPTWWIVSSWLVWGVILFVYL---VIRALRLWRTAKLQVTLKKYSVHLEDMATNSRAFTNLVRKALRLIQ 88
Cdd:pfam12632   1 LIALIIFLLKQARYWLSSSSLFKGFKLLLLIsskLVRLYAYWRRQRLQIIRHKALNQLEEFVANSQAFDKLVRKALILIQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200742288  89 ETEVISRGFTLlldrVSAACPFNKAG-QHPSQHLIGLRKAVYRTLRANFQAARLATLYMLKNyplnSESDNVTNYICVVP 167
Cdd:pfam12632  81 EVELVSRGYRL----SSPLPPFSRIEdQSQSRRCIGLRKALYSTLSFLFLNLRQAISKLLPL----SEGDNLEKYCDIYN 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200742288 168 FKELGLglSEEQISEEEAHNFTDGFSLPALKVLFQLWVAQSSEFFRRLALLLSTANSPPGPLLTPALLPHRILSDVTQGL 247
Cdd:pfam12632 153 INELGL--SEESLSLEEAEELTDSESLPALKFLFQLFNGLRKEFLCRLLALLSDGSKPNFFRWKVADLFHRILSELLQGL 230
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1200742288 248 PHAHSACLEELkrsyefYRYFETQHQ-SVPQCLSKTQQKSRELNNVHTAVRSLQLHLK 304
Cdd:pfam12632 231 SHALGSCLEEL------HRIFETQESfTTPDRRERARAQSRKLNSLSTLIRSLQLHLK 282
 
Name Accession Description Interval E-value
Vezatin pfam12632
Mysoin-binding motif of peroxisomes; Vezatin is a peroxisome transmembrane receptor that is ...
12-304 1.90e-104

Mysoin-binding motif of peroxisomes; Vezatin is a peroxisome transmembrane receptor that is involved in membrane-membrane and cell-cell adhesions. In the movement of peroxisomes it binds to class V and class VIIa myosins to guide the organelle through the microtubules and allow pathogens to internalize themselves into host cells. Vezatin is crucial for spermatozoan production. In mouse cells it interacts with the cadherin-catenin complex bridging it to the C-terminal FERM domain of myosin VIIA.


Pssm-ID: 463650  Cd Length: 282  Bit Score: 318.18  E-value: 1.90e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200742288  12 LFAFISLLVMLPTWWIVSSWLVWGVILFVYL---VIRALRLWRTAKLQVTLKKYSVHLEDMATNSRAFTNLVRKALRLIQ 88
Cdd:pfam12632   1 LIALIIFLLKQARYWLSSSSLFKGFKLLLLIsskLVRLYAYWRRQRLQIIRHKALNQLEEFVANSQAFDKLVRKALILIQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200742288  89 ETEVISRGFTLlldrVSAACPFNKAG-QHPSQHLIGLRKAVYRTLRANFQAARLATLYMLKNyplnSESDNVTNYICVVP 167
Cdd:pfam12632  81 EVELVSRGYRL----SSPLPPFSRIEdQSQSRRCIGLRKALYSTLSFLFLNLRQAISKLLPL----SEGDNLEKYCDIYN 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200742288 168 FKELGLglSEEQISEEEAHNFTDGFSLPALKVLFQLWVAQSSEFFRRLALLLSTANSPPGPLLTPALLPHRILSDVTQGL 247
Cdd:pfam12632 153 INELGL--SEESLSLEEAEELTDSESLPALKFLFQLFNGLRKEFLCRLLALLSDGSKPNFFRWKVADLFHRILSELLQGL 230
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1200742288 248 PHAHSACLEELkrsyefYRYFETQHQ-SVPQCLSKTQQKSRELNNVHTAVRSLQLHLK 304
Cdd:pfam12632 231 SHALGSCLEEL------HRIFETQESfTTPDRRERARAQSRKLNSLSTLIRSLQLHLK 282
 
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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