ID T5A5S4_OPHSC Unreviewed; 422 AA.
AC T5A5S4;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=Prolidase {ECO:0000256|ARBA:ARBA00032413};
GN ORFNames=OCS_06334 {ECO:0000313|EMBL:EQK97953.1};
OS Ophiocordyceps sinensis (strain Co18 / CGMCC 3.14243) (Yarsagumba
OS caterpillar fungus) (Hirsutella sinensis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Ophiocordyceps.
OX NCBI_TaxID=911162 {ECO:0000313|EMBL:EQK97953.1, ECO:0000313|Proteomes:UP000019374};
RN [1] {ECO:0000313|EMBL:EQK97953.1, ECO:0000313|Proteomes:UP000019374}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Co18 / CGMCC 3.14243 {ECO:0000313|Proteomes:UP000019374};
RC TISSUE=Fruit-body {ECO:0000313|EMBL:EQK97953.1};
RX DOI=10.1007/s11434-013-5929-5;
RA Hu X., Zhang Y., Xiao G., Zheng P., Xia Y., Zhang X., St Leger R.J.,
RA Liu X., Wang C.;
RT "Genome survey uncovers the secrets of sex and lifestyle in caterpillar
RT fungus.";
RL Chin. Sci. Bull. 58:2846-2854(2013).
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SIMILARITY: Belongs to the peptidase M24B family.
CC {ECO:0000256|ARBA:ARBA00008766, ECO:0000256|RuleBase:RU000590}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KE655960; EQK97953.1; -; Genomic_DNA.
DR AlphaFoldDB; T5A5S4; -.
DR eggNOG; KOG2413; Eukaryota.
DR HOGENOM; CLU_011781_2_5_1; -.
DR Proteomes; UP000019374; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR CDD; cd01085; APP; 1.
DR Gene3D; 3.90.230.10; Creatinase/methionine aminopeptidase superfamily; 1.
DR Gene3D; 3.40.350.10; Creatinase/prolidase N-terminal domain; 1.
DR InterPro; IPR029149; Creatin/AminoP/Spt16_NTD.
DR InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR InterPro; IPR000994; Pept_M24.
DR InterPro; IPR033740; Pept_M24B.
DR InterPro; IPR032416; Peptidase_M24_C.
DR InterPro; IPR001131; Peptidase_M24B_aminopep-P_CS.
DR PANTHER; PTHR43763; XAA-PRO AMINOPEPTIDASE 1; 1.
DR PANTHER; PTHR43763:SF6; XAA-PRO AMINOPEPTIDASE 1; 1.
DR Pfam; PF16189; Creatinase_N_2; 1.
DR Pfam; PF00557; Peptidase_M24; 1.
DR Pfam; PF16188; Peptidase_M24_C; 1.
DR SUPFAM; SSF55920; Creatinase/aminopeptidase; 1.
DR PROSITE; PS00491; PROLINE_PEPTIDASE; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000313|EMBL:EQK97953.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU000590}; Protease {ECO:0000313|EMBL:EQK97953.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000019374}.
FT DOMAIN 130..348
FT /note="Peptidase M24"
FT /evidence="ECO:0000259|Pfam:PF00557"
FT DOMAIN 359..421
FT /note="Peptidase M24 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16188"
SQ SEQUENCE 422 AA; 46703 MW; 587976361FE2A970 CRC64;
MLDEVAWLFN LRGSDIPYNP VFFSYATITP RAATLYTDVS KLSETCKSHL ANNDIHVKPY
HAFLSDARSH HAQVSDKDTA PGCTTQQTFL ISNKGSWALQ RALGGDGCVE EIRSPVGDAK
AIKNETEMGG MRACHTRDGA ALIEFFAWLE HQLLVERATL DEVQAADKLE ELRSTKQHFV
GLSFPTISST GPNAAVIHYG PERGSCATID PQSVYLCDSG AQFLDGTTDT TRTLHFGNPS
DAEKKAYTLV LKGVIALDTV IFPRGTTGFA LDCLARQHLW KTGLDYRHGT GHGVGSYLNV
HEGPIGIGTR VQYAEVPLAH GNVLSNEPGY YEDGQFGIRI ENVMLVREVE TEHCFGDKPF
LGFTHVTMVP YCQNLIDRAL LTVEEKEWIN VYNAEILDKT KVFFENDALT MAWLTRETRP
LG
//
