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Conserved domains on  [gi|89363026|ref|NP_056232|]
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sperm flagellar protein 1 [Homo sapiens]

Protein Classification

calponin homology domain-containing protein( domain architecture ID 10533622)

calponin homology (CH) domain-containing protein may bind actin filaments or serve a regulatory function; such as mammalian sperm flagellar protein 1, a microtubule-associated protein involved in the stabilization of microtubules along the axis of migration during radial intercalation, and spermatogenesis-associated protein 4 that may play a role in apoptosis regulation

CATH:  1.10.418.10
Gene Ontology:  GO:0008017
PubMed:  12186940|11911887
SCOP:  3000264

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CH_2 pfam06294
CH-like domain in sperm protein; Spef is a region of sperm flagellar proteins. It probably ...
13-104 1.34e-45

CH-like domain in sperm protein; Spef is a region of sperm flagellar proteins. It probably exerts a role in spermatogenesis in that the protein is expressed predominantly in adult tissue. It is present in the tails of developing and epididymal sperm internal to the fibrous sheath and around the dense outer fibres of the sperm flagellum. The amino-terminal domain (residues 1-110) shows a possible calponin homology (CH) domain; however Spef does not bind actin directly under in vitro conditions, so the function of the amino-terminal calponin-like domain is unclear. Transcription aberrations leading to a truncated protein result in immotile sperm.


:

Pssm-ID: 461871  Cd Length: 91  Bit Score: 147.19  E-value: 1.34e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89363026    13 LYLWVDNIPLSRPKRNLSRDFSDGVLVAEVIKFYFPKMVEMHNYVPANSLQQKLSNWGHLnRKVLKRLNFSVPDDVMRKI 92
Cdd:pfam06294   1 LLKWLQSLDLSRPVRNIARDFSDGFLVAEILSRYYPKLVDLHNYSPGSSVAAKLNNWETL-EKVLKKLGIKLSKEDIEDL 79
                          90
                  ....*....|..
gi 89363026    93 AQCAPGVVELVL 104
Cdd:pfam06294  80 ANGKPGAAERLL 91
 
Name Accession Description Interval E-value
CH_2 pfam06294
CH-like domain in sperm protein; Spef is a region of sperm flagellar proteins. It probably ...
13-104 1.34e-45

CH-like domain in sperm protein; Spef is a region of sperm flagellar proteins. It probably exerts a role in spermatogenesis in that the protein is expressed predominantly in adult tissue. It is present in the tails of developing and epididymal sperm internal to the fibrous sheath and around the dense outer fibres of the sperm flagellum. The amino-terminal domain (residues 1-110) shows a possible calponin homology (CH) domain; however Spef does not bind actin directly under in vitro conditions, so the function of the amino-terminal calponin-like domain is unclear. Transcription aberrations leading to a truncated protein result in immotile sperm.


Pssm-ID: 461871  Cd Length: 91  Bit Score: 147.19  E-value: 1.34e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89363026    13 LYLWVDNIPLSRPKRNLSRDFSDGVLVAEVIKFYFPKMVEMHNYVPANSLQQKLSNWGHLnRKVLKRLNFSVPDDVMRKI 92
Cdd:pfam06294   1 LLKWLQSLDLSRPVRNIARDFSDGFLVAEILSRYYPKLVDLHNYSPGSSVAAKLNNWETL-EKVLKKLGIKLSKEDIEDL 79
                          90
                  ....*....|..
gi 89363026    93 AQCAPGVVELVL 104
Cdd:pfam06294  80 ANGKPGAAERLL 91
 
Name Accession Description Interval E-value
CH_2 pfam06294
CH-like domain in sperm protein; Spef is a region of sperm flagellar proteins. It probably ...
13-104 1.34e-45

CH-like domain in sperm protein; Spef is a region of sperm flagellar proteins. It probably exerts a role in spermatogenesis in that the protein is expressed predominantly in adult tissue. It is present in the tails of developing and epididymal sperm internal to the fibrous sheath and around the dense outer fibres of the sperm flagellum. The amino-terminal domain (residues 1-110) shows a possible calponin homology (CH) domain; however Spef does not bind actin directly under in vitro conditions, so the function of the amino-terminal calponin-like domain is unclear. Transcription aberrations leading to a truncated protein result in immotile sperm.


Pssm-ID: 461871  Cd Length: 91  Bit Score: 147.19  E-value: 1.34e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89363026    13 LYLWVDNIPLSRPKRNLSRDFSDGVLVAEVIKFYFPKMVEMHNYVPANSLQQKLSNWGHLnRKVLKRLNFSVPDDVMRKI 92
Cdd:pfam06294   1 LLKWLQSLDLSRPVRNIARDFSDGFLVAEILSRYYPKLVDLHNYSPGSSVAAKLNNWETL-EKVLKKLGIKLSKEDIEDL 79
                          90
                  ....*....|..
gi 89363026    93 AQCAPGVVELVL 104
Cdd:pfam06294  80 ANGKPGAAERLL 91
CAMSAP_CH pfam11971
CAMSAP CH domain; This domain is the N-terminal CH domain from the CAMSAP proteins.
14-85 1.34e-13

CAMSAP CH domain; This domain is the N-terminal CH domain from the CAMSAP proteins.


Pssm-ID: 432229  Cd Length: 85  Bit Score: 64.24  E-value: 1.34e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 89363026    14 YLWVDNIPLSRPKRNLSRDFSDGVLVAEVIKFYFPKMVEMHNYVPANSLQQKLS--NWGHLNRKVLKRLNFSVP 85
Cdd:pfam11971   1 PLSQRSLPLSPPVEDLLRDLSDGCALAALIHFYCPQLIDLEDICLKESMSLADSlyNIQLLQEFCQRHLGNRCC 74
 
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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