UniProt: N4XAZ0

Database: UniProt
Entry: N4XAZ0_COCH4

LinkDB:  N4XAZ0_COCH4 
Original site:  N4XAZ0_COCH4

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Ontology (4)   
   GO (4)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (3)   
   InterPro (2)   
   Pfam (1)   
Literature (2)   
   PubMed (2)   
All databases (13)   

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ID   N4XAZ0_COCH4            Unreviewed;       507 AA.
AC   N4XAZ0;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=aspartyl aminopeptidase {ECO:0000256|ARBA:ARBA00011965};
DE            EC=3.4.11.21 {ECO:0000256|ARBA:ARBA00011965};
GN   ORFNames=COCC4DRAFT_56387 {ECO:0000313|EMBL:ENI10149.1};
OS   Cochliobolus heterostrophus (strain C4 / ATCC 48331 / race T) (Southern
OS   corn leaf blight fungus) (Bipolaris maydis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX   NCBI_TaxID=665024 {ECO:0000313|EMBL:ENI10149.1, ECO:0000313|Proteomes:UP000012338};
RN   [1] {ECO:0000313|EMBL:ENI10149.1, ECO:0000313|Proteomes:UP000012338}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C4 / ATCC 48331 / race T {ECO:0000313|Proteomes:UP000012338};
RX   PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA   Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA   Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA   LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA   Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA   Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA   Grigoriev I.V.;
RT   "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT   genomes of eighteen Dothideomycetes fungi.";
RL   PLoS Pathog. 8:E1003037-E1003037(2012).
RN   [2] {ECO:0000313|Proteomes:UP000012338}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C4 / ATCC 48331 / race T {ECO:0000313|Proteomes:UP000012338};
RX   PubMed=23357949; DOI=10.1371/journal.pgen.1003233;
RA   Condon B.J., Leng Y., Wu D., Bushley K.E., Ohm R.A., Otillar R., Martin J.,
RA   Schackwitz W., Grimwood J., MohdZainudin N., Xue C., Wang R., Manning V.A.,
RA   Dhillon B., Tu Z.J., Steffenson B.J., Salamov A., Sun H., Lowry S.,
RA   LaButti K., Han J., Copeland A., Lindquist E., Barry K., Schmutz J.,
RA   Baker S.E., Ciuffetti L.M., Grigoriev I.V., Zhong S., Turgeon B.G.;
RT   "Comparative genome structure, secondary metabolite, and effector coding
RT   capacity across Cochliobolus pathogens.";
RL   PLoS Genet. 9:E1003233-E1003233(2013).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of an N-terminal aspartate or glutamate from a
CC         peptide, with a preference for aspartate.; EC=3.4.11.21;
CC         Evidence={ECO:0000256|ARBA:ARBA00001335};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|ARBA:ARBA00008290, ECO:0000256|RuleBase:RU004386}.
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DR   EMBL; KB733445; ENI10149.1; -; Genomic_DNA.
DR   RefSeq; XP_014084058.1; XM_014228583.1.
DR   AlphaFoldDB; N4XAZ0; -.
DR   GeneID; 25846007; -.
DR   HOGENOM; CLU_019532_2_0_1; -.
DR   OrthoDB; 1156at2759; -.
DR   Proteomes; UP000012338; Unassembled WGS sequence.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd05658; M18_DAP; 1.
DR   Gene3D; 2.30.250.10; Aminopeptidase i, Domain 2; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR001948; Peptidase_M18.
DR   InterPro; IPR023358; Peptidase_M18_dom2.
DR   PANTHER; PTHR28570; ASPARTYL AMINOPEPTIDASE; 1.
DR   PANTHER; PTHR28570:SF3; ASPARTYL AMINOPEPTIDASE; 1.
DR   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
DR   SUPFAM; SSF101821; Aminopeptidase/glucanase lid domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW   ECO:0000256|RuleBase:RU004386};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU004386};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU004386};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW   ECO:0000256|RuleBase:RU004386};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU004386};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   507 AA;  55745 MW;  2C2AD89EA74F232E CRC64;
     MSSKPSLQAA EDFLSFVNAS PTPFHAVKSA KERLEKAGFK QIKERDSWAP TLQPGGKYYL
     TRNTSSIVAF AIGQKWKPGN PIAMIGAHTD SPCLRIKPVS KRQSDGFLQV ACETYGGGLW
     HTWFDRDLSI AGRAMVRTKD GNIEQRLVKV DRPILRIPTL AIHLDRQENF QFNKETQLFP
     ITGLVAAELN RQGKTEETKE ETKDADAEGS FEPLAAPTAR HHPYIVDIIA EEAGAEASDI
     VDFEMVLYDT QKSVIGGLNN ELIFSPRLDN LMMTYCSVEG LIKSLSSPSA LEKDSIIRLI
     ACFDHEEIGS QTAQGADSNL LPAVIRRLSV LPASESNSDK SYDKVEADTA TAFEQTLATS
     FLVSADMAHS VHPNYPAKYE SQHRPEMNKG TVIKINANAR YATNTPGIVL LQEAARRAKP
     ASYNLSSTKE GVPLQLFVVR NDSSCGSTIG PMLSAAMGAR TLDLGNPQLS MHSIRETGGA
     HDVEHAVNLF DSFFENYEEL EKKIIVD
//

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