ID A0A0B7NJK6_9FUNG Unreviewed; 895 AA.
AC A0A0B7NJK6;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=C5a peptidase {ECO:0000256|ARBA:ARBA00020956};
DE EC=3.4.21.110 {ECO:0000256|ARBA:ARBA00012942};
DE AltName: Full=SCP {ECO:0000256|ARBA:ARBA00030432};
GN Name=PARPA_11885.1 scaffold 44722 {ECO:0000313|EMBL:CEP17587.1};
OS Parasitella parasitica.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Parasitella.
OX NCBI_TaxID=35722 {ECO:0000313|EMBL:CEP17587.1, ECO:0000313|Proteomes:UP000054107};
RN [1] {ECO:0000313|EMBL:CEP17587.1, ECO:0000313|Proteomes:UP000054107}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 412.66 {ECO:0000313|EMBL:CEP17587.1,
RC ECO:0000313|Proteomes:UP000054107};
RA Ellenberger Sabrina;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: This virulence factor of S.pyogenes specifically cleaves the
CC human serum chemotaxin C5a at '68-Lys-|-Asp-69' bond near its C-
CC terminus, destroying its ability to serve as a chemoattractant.
CC {ECO:0000256|ARBA:ARBA00002909}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=The primary cleavage site is at 67-His-|-Lys-68 in human C5a
CC with a minor secondary cleavage site at 58-Ala-|-Ser-59.;
CC EC=3.4.21.110; Evidence={ECO:0000256|ARBA:ARBA00001404};
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC ProRule:PRU01240, ECO:0000256|RuleBase:RU003355}.
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DR EMBL; LN733710; CEP17587.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B7NJK6; -.
DR STRING; 35722.A0A0B7NJK6; -.
DR OrthoDB; 662485at2759; -.
DR Proteomes; UP000054107; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00538; PA; 1.
DR CDD; cd07489; Peptidases_S8_5; 1.
DR Gene3D; 3.50.30.30; -; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR Gene3D; 2.60.40.1710; Subtilisin-like superfamily; 1.
DR InterPro; IPR010435; Fn3_5.
DR InterPro; IPR046450; PA_dom_sf.
DR InterPro; IPR003137; PA_domain.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR InterPro; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR034187; Peptidases_S8_5.
DR PANTHER; PTHR43399; SUBTILISIN-RELATED; 1.
DR PANTHER; PTHR43399:SF4; TK-SUBTILISIN; 1.
DR Pfam; PF06280; fn3_5; 1.
DR Pfam; PF02225; PA; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52025; PA domain; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00136; SUBTILASE_ASP; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000054107};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}.
FT DOMAIN 129..558
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 347..433
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 589..713
FT /note="Fn3-like"
FT /evidence="ECO:0000259|Pfam:PF06280"
FT ACT_SITE 138
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 196
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 509
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 895 AA; 96241 MW; 7AC26B6131513C92 CRC64;
MLNGITALVN ATEESRNGYI IEFSSTDEAT AFVKQHTTDI QHERYIYNSE LFPAVSIEFK
DARTAQKLLR SSEIKKYWPI DHRSHLHAPV PEDSNSGDAE VTRFTPQKKD TIPLLTQAYD
KFRNLKSNGS GVKIGIIDTG VDYFHPALGG CFGKGCKVAY GYDLVGNNYN GTLGSIVESN
DPIDDCPANS TSATGHGTFI SGIIGAEDHI YNWTGVAPGA TLGMWKVYGC NSAISPNDVI
LKAMEMAYKA GMDVISISLG VSGGWQEDVL SVMADRLVSK GVHVITASGN SGTSGVFLTA
SPASSKNAIA VGSTMNSHVP GYVFKVDDND ITYRTFVNTA LVLNDTLPIV ATGSKFDQEN
DACKSLGKSS KYNDTIVLIH QGGCDSLTKI QHAHSAGAKA VILYTDIKNA TTSFETLPNA
VLPVAFINND DAKIVFTARK KQKPSKARFT NTLVAMPAPE GDVDSISSFS TLGPTNELEM
KPELVAVGGN VFSTVPRYQG SYQFGSGTSF SAPYVAANVA LFLANSKNKA NNSPDLVKNV
LMNFASTVRG PISASQYGDS PIRQGAGMVD VSQAIQGFAR FHVTPAKLSL NDTAHDQSLQ
QEITIYNHHS TSQTFTISHK PSLTATGYSL KGGNQSLAPV EPVGLYAGNE SSVATLHFDK
TSVTVAAGGS AKVHIRIEPP SKVFTMKNHV LYGGYIAISS KETTSLQATV PYFGMLGNMK
DLAVLDRSNK PSPLAPYQFP SIGLADGNST VQDGSVGHFN LTYYPENKMS SGGPSIITRL
LTGTALLQLQ ILDKDGSYIG DVPMTDARQY MMRNTLGVTE YSVPYYVWYW SGDYTPKDSS
LTTTAAAETE PKLLESGEYR LVVRALKVFG SVHNDADFDT WTSPRLKLDI QTATQ
//
