ID E3QUM0_COLGM Unreviewed; 903 AA.
AC E3QUM0;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 52.
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=GLRG_09702 {ECO:0000313|EMBL:EFQ34558.1};
OS Colletotrichum graminicola (strain M1.001 / M2 / FGSC 10212) (Maize
OS anthracnose fungus) (Glomerella graminicola).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum graminicola species complex.
OX NCBI_TaxID=645133 {ECO:0000313|Proteomes:UP000008782};
RN [1] {ECO:0000313|Proteomes:UP000008782}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M1.001 / M2 / FGSC 10212 {ECO:0000313|Proteomes:UP000008782};
RX PubMed=22885923; DOI=10.1038/ng.2372;
RA O'Connell R.J., Thon M.R., Hacquard S., Amyotte S.G., Kleemann J.,
RA Torres M.F., Damm U., Buiate E.A., Epstein L., Alkan N., Altmueller J.,
RA Alvarado-Balderrama L., Bauser C.A., Becker C., Birren B.W., Chen Z.,
RA Choi J., Crouch J.A., Duvick J.P., Farman M.A., Gan P., Heiman D.,
RA Henrissat B., Howard R.J., Kabbage M., Koch C., Kracher B., Kubo Y.,
RA Law A.D., Lebrun M.-H., Lee Y.-H., Miyara I., Moore N., Neumann U.,
RA Nordstroem K., Panaccione D.G., Panstruga R., Place M., Proctor R.H.,
RA Prusky D., Rech G., Reinhardt R., Rollins J.A., Rounsley S., Schardl C.L.,
RA Schwartz D.C., Shenoy N., Shirasu K., Sikhakolli U.R., Stueber K.,
RA Sukno S.A., Sweigard J.A., Takano Y., Takahara H., Trail F.,
RA van der Does H.C., Voll L.M., Will I., Young S., Zeng Q., Zhang J.,
RA Zhou S., Dickman M.B., Schulze-Lefert P., Ver Loren van Themaat E.,
RA Ma L.-J., Vaillancourt L.J.;
RT "Lifestyle transitions in plant pathogenic Colletotrichum fungi deciphered
RT by genome and transcriptome analyses.";
RL Nat. Genet. 44:1060-1065(2012).
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; GG697381; EFQ34558.1; -; Genomic_DNA.
DR RefSeq; XP_008098578.1; XM_008100387.1.
DR AlphaFoldDB; E3QUM0; -.
DR STRING; 645133.E3QUM0; -.
DR EnsemblFungi; EFQ34558; EFQ34558; GLRG_09702.
DR GeneID; 24415067; -.
DR VEuPathDB; FungiDB:GLRG_09702; -.
DR eggNOG; KOG4266; Eukaryota.
DR HOGENOM; CLU_003559_2_1_1; -.
DR OrthoDB; 662485at2759; -.
DR Proteomes; UP000008782; 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; cd02124; PA_PoS1_like; 1.
DR CDD; cd07489; Peptidases_S8_5; 1.
DR Gene3D; 3.50.30.30; -; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR010435; Fn3_5.
DR InterPro; IPR013783; Ig-like_fold.
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:UP000008782};
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..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..903
FT /note="C5a peptidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003180859"
FT DOMAIN 143..532
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 358..439
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 598..721
FT /note="Fn3-like"
FT /evidence="ECO:0000259|Pfam:PF06280"
FT ACT_SITE 152
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 202
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 515
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 903 AA; 96084 MW; E14AC282D0EB1D2E CRC64;
MRISATVSAF ALALHLGGVT ALSPRQEPDS NTAKATAFVA KSFIIEYAPG SSARLRRQNV
ASTDGIKVVK EFASDVFSGA SIETDTFTID TLQALPEVLN VWVNEEVKLD PTEPQAAAPE
DAPTYSTHNA TGVSKLHALG IYGKGVKVGV VDTGIWYDHP ALGGGFGPGF KVAAGYDFVG
DGSYPASGPK APDDDPVDTR GHGTHVAGII AGKTDSWVGT APEATLHAYK VFSNAASTDT
ATLIEAFLAA YSDGVDIITA SIGGANGWSN NAWAEVASRL VDEGVVVTIS AGNSGANGPF
YGSSGSSGKN VIAVASVETE VFPAIPFEAT FGGSETSRVG YLPSAGYFPP TVVDWPIVAL
STDTSAPADG CTPYPPGSPD LTGKIPLVRR GTCNFQVKQE NLAALGAEYI LIYNNESPMT
TPGTGNTDTM IALITAESGA SFINAIKANT TVTADFSVNP EIPIALDYPA GNRPNIFTSW
GLLYDNQLKP DIAAPGGNIF STYLDGEYAI LSGTSMACPY VAGVAALYIG QHGGRSVQGK
GFARALSRRI ISSGYALPWS DGTATDYGYT APPAQVGNGQ IDAWKVLNYG TQLEFDKIQL
NDTRYFSRYH DVTVTNNGKS DVTYKFSVQP NAGVDALAWV PATGGLPGTK RVKTFAQLRP
KTYTPEISFP RDFTLKPGES KTVSVNFKNP DNLGWNATGL PLYGGKVIIQ GSNGELVSVP
YAGVGADLRN TLGGVHEAGW PQSTSTVDDT PIAEKATYSF DLSIEAQDFP KIFQKLIWGT
RQTRWDVFDA SWTERQWVYP PVEGQNGYIG SVASWVGSGE VQTFDPAQYD PDETFTYPIT
DVYRNAGAQY HEHWWFGKLG NGSQIAPGEY QFRFAALRPF GDPTHADNWD VYKTPKITIT
GQY
//
