Conserved Protein Domain Family
Hepsin-SRCR

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pfam09272: Hepsin-SRCR (This model is not part of the current CDD release)
Hepsin, SRCR domain
Members of this family form an extracellular domain of the serine protease hepsin. They are formed primarily by three elements of regular secondary structure: a 12-residue alpha helix, a twisted five-stranded antiparallel beta sheet, and a second, two-stranded, antiparallel sheet. The two beta-sheets lie at roughly right angles to each other, with the helix nestled between the two, adopting an SRCR fold. The exact function of this domain has not been identified, though it probably may serve to orient the protease domain or place it in the vicinity of its substrate.
Statistics
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PSSM-Id: 518793
Aligned: 7 rows
Threshold Bit Score: 150.731
Created: 15-Feb-2025
Updated: 28-Apr-2025
Structure
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Aligned Rows:
PubMed ReferencesClick to see Conserved Features Help

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
XP_006641623  50 RLYDVQINPADLRLSVFDRSDGRWKFVCSSSSDELVARISCEEMGFIRSLGYSVHPFSSVSGNtsEGFFCVDEKQLEFGK 129
3_pfamImport   1 ALYDVQISSADSRLLVYDRSEKVWRMVCESNLNLVLATMSCQAMGFVSSTSSRPLHLRSSASG--SHFDLTSPQILDHAR 78 
1_pfamImport   1 SFPAVQINSADQRLRVFDPAEKRWRQVCSSSANELLASISCEEVGFVSVVNYSVSSVPEASGDggE-FFCVRQQELSYGK 79 
4_pfamImport   1 SLYAVQVSPGDLRLTIYDENEGKWRLLCSSSHNAQVASLSCEEMGFVRSLSHSVLAADSAGSNgtSGYFCVDGSRLPYAR 80 
2_pfamImport   1 FLYLVQVSPGDSPLMLFDETGGTWWLLCSLCSNARVARLSCKEMGFLRALAHSELD-----GDgtLGF-CIDKGRLSHVR 74 
XP_006114828  50 GLYGVQVSSGDLRVTLYDESEGKWRLICSTPSNALVAALSCEEMGFVRSLWHSELDVELAGANgtSGYFCVDESRLPLAQ 129
XP_014452395  57 ALYGVQVSPADLRLTVFDEAEGRWRLVCSSPANALVAALSCEEMGFVRSLWHSELDVERAGANgtSGFFCVDEARLPLAS 136
XP_006641623 130 KIKEVLSACDCENGRILSVNCQDCGRRKLT 159
3_pfamImport  79 SLTLMSDVIECPSGRVLAVQCQDCGRRKVP 108
1_pfamImport  80 KIKDALFPCDCESREVLTLLCQDCGRRSFA 109
4_pfamImport  81 MLSEALVVCECPTGRFLATLCQDCGRRKLS 110
2_pfamImport  75 SLLEV-TLCDCPRGYFLATICQDCGCRKLP 103
XP_006114828 130 RLSEVVSICDCPMGQFLATLCQDCGRRKLS 159
XP_014452395 137 GLAEVVTACECPSGRFVATLCQECGRRKLP 166
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