ID A0A1Y2CAA3_9FUNG Unreviewed; 939 AA.
AC A0A1Y2CAA3;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
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 ORFNames=BCR33DRAFT_766156 {ECO:0000313|EMBL:ORY43959.1};
OS Rhizoclosmatium globosum.
OC Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC Chytridiomycota incertae sedis; Chytridiomycetes; Chytridiales;
OC Chytriomycetaceae; Rhizoclosmatium.
OX NCBI_TaxID=329046 {ECO:0000313|EMBL:ORY43959.1, ECO:0000313|Proteomes:UP000193642};
RN [1] {ECO:0000313|EMBL:ORY43959.1, ECO:0000313|Proteomes:UP000193642}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEL800 {ECO:0000313|EMBL:ORY43959.1,
RC ECO:0000313|Proteomes:UP000193642};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-2016) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ORY43959.1}.
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DR EMBL; MCGO01000023; ORY43959.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2CAA3; -.
DR STRING; 329046.A0A1Y2CAA3; -.
DR OrthoDB; 662485at2759; -.
DR Proteomes; UP000193642; 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 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 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:UP000193642};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..939
FT /note="C5a peptidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012395322"
FT DOMAIN 153..599
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 394..468
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 620..747
FT /note="Fn3-like"
FT /evidence="ECO:0000259|Pfam:PF06280"
FT ACT_SITE 162
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 215
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 547
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 939 AA; 98907 MW; 539DA786E2D354E3 CRC64;
MQLLSLLATL GAALGVAAQD DVFRAPRTGA PEGFDGIIPC TFFVEFPTSV VDPAAEVKNH
FTKYPTAKYA LRTSFSSELI SFASFELKGQ CDEDIVASIG GAIHYQAVTV RAPPVPVKDV
NPLKSGAPFV HKQDQIHDLT GVNKARNELG LTGKGVKVAV IDSGIYYLHP ALGGGIGPNF
KVVKGHDFVG NSFNGTAESI QESDDPLDNC SDVSHGTHVT GIIAGDARDI KDPKWAPKVP
FSGVAPDARI YGYRVFGCQG LTGGDIITKA IYMAAKDGVD IINMSLGGGP AFNDESDSLA
VDKVVAAQQI VVLASSGNSG SNGPFATGSP ANAKTGISVA SFDNGETYPH LGGIIEGSTY
PASLSIAEKV HLQDGQTVEL VAWNLTAAAD PNNISDGCFK PSNDVTGKAA FMRWGAGVCG
SVARCTNAYK AGAIACIIAK NKPVDNFGIT GYEKIPGMLL PQEAGDHIVR LMQAGKTVNV
TATYQVFAYG QSTGGTLSSF SSPGLDLELN LKPEIAGIGG NVLSTISPHS AEHEGSPEPY
IDMSGTSMSS PYTAGVVALL IEKRGKIPAA SFKAYLMNNA KPAPIYNTSL THSPSYQGAG
LVDAFGAATA QTIVTPPGLA LNDTVNIKNQ YTIKITNNYK VDVTYALQAK TAATSTQYLS
GDDFPEDQSG TLLTNDQHAT VTFLSNTCSE EDTTGTKTVL VRAGASVDVD IQFTPSALAP
AGNLPVYGGY ISITNSIDES ALSVPYVGMI GSWAEKPFWS RNSTSLLKQW LRTLVKGAQT
ATTGLYADTS FAPLVANDAV NATDGSFVLA IPTYTSRQAS VVVQYVGGDN AMVASGFSSN
IAYIKLYDAV SGDDQGPAYW QTFQRTSYQK AQGLPANLLY LWTGRAYDFD SKSKLPSLRS
QALPAGNFVM RFMGLKNFGD ITKPADWDVL ETVPFTLVY
//
