ID S0EE51_GIBF5 Unreviewed; 438 AA.
AC S0EE51;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Related to ECM14-involved in cell wall biogenesis and architecture {ECO:0000313|EMBL:CCT72112.1};
GN ORFNames=FFUJ_13888 {ECO:0000313|EMBL:CCT72112.1};
OS Gibberella fujikuroi (strain CBS 195.34 / IMI 58289 / NRRL A-6831) (Bakanae
OS and foot rot disease fungus) (Fusarium fujikuroi).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium fujikuroi species complex.
OX NCBI_TaxID=1279085 {ECO:0000313|EMBL:CCT72112.1, ECO:0000313|Proteomes:UP000016800};
RN [1] {ECO:0000313|Proteomes:UP000016800}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 195.34 / IMI 58289 / NRRL A-6831
RC {ECO:0000313|Proteomes:UP000016800};
RX PubMed=23825955; DOI=10.1371/journal.ppat.1003475;
RA Wiemann P., Sieber C.M., von Bargen K.W., Studt L., Niehaus E.M.,
RA Espino J.J., Huss K., Michielse C.B., Albermann S., Wagner D.,
RA Bergner S.V., Connolly L.R., Fischer A., Reuter G., Kleigrewe K., Bald T.,
RA Wingfield B.D., Ophir R., Freeman S., Hippler M., Smith K.M., Brown D.W.,
RA Proctor R.H., Munsterkotter M., Freitag M., Humpf H.U., Guldener U.,
RA Tudzynski B.;
RT "Deciphering the cryptic genome: genome-wide analyses of the rice pathogen
RT Fusarium fujikuroi reveal complex regulation of secondary metabolism and
RT novel metabolites.";
RL PLoS Pathog. 9:E1003475-E1003475(2013).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the peptidase M14 family.
CC {ECO:0000256|ARBA:ARBA00005988}.
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DR EMBL; HF679030; CCT72112.1; -; Genomic_DNA.
DR AlphaFoldDB; S0EE51; -.
DR STRING; 1279085.S0EE51; -.
DR EnsemblFungi; CCT72112; CCT72112; FFUJ_13888.
DR VEuPathDB; FungiDB:FFUJ_13888; -.
DR HOGENOM; CLU_019326_1_1_1; -.
DR OrthoDB; 3540647at2759; -.
DR Proteomes; UP000016800; Chromosome 8.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd03860; M14_CP_A-B_like; 1.
DR Gene3D; 3.30.70.340; Metallocarboxypeptidase-like; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR036990; M14A-like_propep.
DR InterPro; IPR000834; Peptidase_M14.
DR PANTHER; PTHR11705:SF91; CARBOXYPEPTIDASE A1 (PANCREATIC)-RELATED; 1.
DR PANTHER; PTHR11705; PROTEASE FAMILY M14 CARBOXYPEPTIDASE A,B; 1.
DR Pfam; PF00246; Peptidase_M14; 1.
DR PRINTS; PR00765; CRBOXYPTASEA.
DR SMART; SM00631; Zn_pept; 1.
DR SUPFAM; SSF54897; Protease propeptides/inhibitors; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS00132; CARBOXYPEPT_ZN_1; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000016800};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..438
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004495890"
FT DOMAIN 163..185
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|PROSITE:PS00132"
SQ SEQUENCE 438 AA; 49580 MW; 6C65E3A302AA517C CRC64;
MRYSIVSLLT LALGALAVPK TEIKSYDGYK VFRVNTHGKA AIKEKLTPVT FDEWEHGYQH
VDIVVAPNDI SAFESLKLDY TTLHENLGTS ITGESVSRKK WKRQADDDSW FDEFHNYEDH
IDYFRDLQAQ FPNNSKLVSS GKSYQKRNIY GLHLWGDDGP GKPAVLYHGT VHAREWISGP
TLEYITLQLV KGFKSGDEDV QTYLNKYDFY IFPFVNPDGF VYSTTADRLW RKNRQPPPAT
AANQSCYGRD INRNWEFGWD SNKRGASTDP CSQVYRGEKP ADTPENQGLD KFVRQLRDTV
GIALYIDWHS YGQYILSPFG YKEDLYAPEL GKWTKAAALV SEAIRESTDD HTTYTFGPSG
AVLYVTTGAA PDHVYSVGGA KFSYTIEQRD TGENGFVLPP EQIRPNAEEQ WAGQKVLLSL
LDETFFDGKG PALYQGQT
//
