ID S3DBE8_OPHP1 Unreviewed; 534 AA.
AC S3DBE8;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Peptide hydrolase {ECO:0000256|RuleBase:RU361240};
DE EC=3.4.-.- {ECO:0000256|RuleBase:RU361240};
GN ORFNames=F503_05980 {ECO:0000313|EMBL:EPE10885.1};
OS Ophiostoma piceae (strain UAMH 11346) (Sap stain fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Ophiostoma.
OX NCBI_TaxID=1262450 {ECO:0000313|EMBL:EPE10885.1, ECO:0000313|Proteomes:UP000016923};
RN [1] {ECO:0000313|EMBL:EPE10885.1, ECO:0000313|Proteomes:UP000016923}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 11346 {ECO:0000313|EMBL:EPE10885.1,
RC ECO:0000313|Proteomes:UP000016923};
RX PubMed=23725015; DOI=10.1186/1471-2164-14-373;
RA Haridas S., Wang Y., Lim L., Massoumi Alamouti S., Jackman S., Docking R.,
RA Robertson G., Birol I., Bohlmann J., Breuil C.;
RT "The genome and transcriptome of the pine saprophyte Ophiostoma piceae, and
RT a comparison with the bark beetle-associated pine pathogen Grosmannia
RT clavigera.";
RL BMC Genomics 14:373-373(2013).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the peptidase M28 family. M28A subfamily.
CC {ECO:0000256|ARBA:ARBA00005957}.
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DR EMBL; KE148146; EPE10885.1; -; Genomic_DNA.
DR AlphaFoldDB; S3DBE8; -.
DR STRING; 1262450.S3DBE8; -.
DR VEuPathDB; FungiDB:F503_05980; -.
DR eggNOG; KOG2195; Eukaryota.
DR HOGENOM; CLU_024336_0_1_1; -.
DR OMA; PNYEYEV; -.
DR OrthoDB; 51543at2759; -.
DR Proteomes; UP000016923; Unassembled WGS sequence.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008235; F:metalloexopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd03876; M28_SGAP_like; 1.
DR Gene3D; 3.50.30.30; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR045175; M28_fam.
DR InterPro; IPR041756; M28_SGAP-like.
DR InterPro; IPR046450; PA_dom_sf.
DR InterPro; IPR003137; PA_domain.
DR InterPro; IPR007484; Peptidase_M28.
DR PANTHER; PTHR12147:SF17; AMINOPEPTIDASE Y; 1.
DR PANTHER; PTHR12147; METALLOPEPTIDASE M28 FAMILY MEMBER; 1.
DR Pfam; PF02225; PA; 1.
DR Pfam; PF04389; Peptidase_M28; 1.
DR SUPFAM; SSF52025; PA domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW ECO:0000313|EMBL:EPE10885.1}; Hydrolase {ECO:0000256|RuleBase:RU361240};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU361240};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU361240};
KW Reference proteome {ECO:0000313|Proteomes:UP000016923};
KW Signal {ECO:0000256|RuleBase:RU361240};
KW Zinc {ECO:0000256|RuleBase:RU361240}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|RuleBase:RU361240"
FT CHAIN 20..534
FT /note="Peptide hydrolase"
FT /evidence="ECO:0000256|RuleBase:RU361240"
FT /id="PRO_5005146305"
FT DOMAIN 177..256
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 284..493
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
SQ SEQUENCE 534 AA; 56484 MW; 3152C733D1ABB818 CRC64;
MPAWKAPLAA SLLLSSASAL KIPGQQQLKS PGGIEDRGLI GNAIPADLAG CRPKGKPLVD
SAGLQSKISI KRLTSHADTL YNIATTSVAE YNHPTRVIGS AGHNGTLDYI HSVVSQLGVG
KPGSDGYYRV WNQSFPATTG NVRESRLVLN GTVFSGAAPM GLTPPTLNKE PVYANLTLVA
NNGCDATDFP ASVSGSIALI KRGTCTFGTK SDLAGKAGAV AAVVYNNEDG ALSGTLGTPS
PDHIATFGLS GAEGRPLALS LSNGTRIDGS AYIDSEVRTI QTTNILAQTV AGDPDNCIMV
GGHSDSVAEG PGINDDGSGS ITLLEVATQL SRYNVSNCVR FGWWAAEEEG LLGSDYYAEN
LTPEENLKIR AFLDYDMLAS PNFVYQVYNS VDSENPAGSE ALRNLYIDFY TQHGLNYTLV
PFDGRSDYDG FIRAGIPASG IATGAEGVKT EEEALIFGGT AGAWYDPCYH QLCDDTKNVN
LTAWEINSKL VAHSVATYAV SFEGFPNRTL DSISTRSASA YNQRTKYRHG KLII
//
