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Database: UniProt
Entry: K2RDZ3_MACPH
LinkDB: K2RDZ3_MACPH
Original site: K2RDZ3_MACPH 
ID   K2RDZ3_MACPH            Unreviewed;       886 AA.
AC   K2RDZ3;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   08-NOV-2023, entry version 38.
DE   RecName: Full=Aminopeptidase {ECO:0000256|RuleBase:RU364040};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU364040};
GN   ORFNames=MPH_11735 {ECO:0000313|EMBL:EKG11117.1};
OS   Macrophomina phaseolina (strain MS6) (Charcoal rot fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC   Macrophomina.
OX   NCBI_TaxID=1126212 {ECO:0000313|EMBL:EKG11117.1, ECO:0000313|Proteomes:UP000007129};
RN   [1] {ECO:0000313|EMBL:EKG11117.1, ECO:0000313|Proteomes:UP000007129}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MS6 {ECO:0000313|EMBL:EKG11117.1,
RC   ECO:0000313|Proteomes:UP000007129};
RX   PubMed=22992219; DOI=10.1186/1471-2164-13-493;
RA   Islam M.S., Haque M.S., Islam M.M., Emdad E.M., Halim A., Hossen Q.M.M.,
RA   Hossain M.Z., Ahmed B., Rahim S., Rahman M.S., Alam M.M., Hou S., Wan X.,
RA   Saito J.A., Alam M.;
RT   "Tools to kill: Genome of one of the most destructive plant pathogenic
RT   fungi Macrophomina phaseolina.";
RL   BMC Genomics 13:493-493(2012).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PIRSR:PIRSR634016-3,
CC         ECO:0000256|RuleBase:RU364040};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR634016-3,
CC       ECO:0000256|RuleBase:RU364040};
CC   -!- SIMILARITY: Belongs to the peptidase M1 family.
CC       {ECO:0000256|ARBA:ARBA00010136, ECO:0000256|RuleBase:RU364040}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EKG11117.1}.
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DR   EMBL; AHHD01000498; EKG11117.1; -; Genomic_DNA.
DR   AlphaFoldDB; K2RDZ3; -.
DR   STRING; 1126212.K2RDZ3; -.
DR   MEROPS; M01.007; -.
DR   VEuPathDB; FungiDB:MPH_11735; -.
DR   eggNOG; KOG1046; Eukaryota.
DR   HOGENOM; CLU_003705_0_1_1; -.
DR   InParanoid; K2RDZ3; -.
DR   OrthoDB; 3085317at2759; -.
DR   Proteomes; UP000007129; 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:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd09601; M1_APN-Q_like; 1.
DR   Gene3D; 1.25.50.20; -; 1.
DR   Gene3D; 2.60.40.1910; -; 1.
DR   Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR   Gene3D; 2.60.40.1730; tricorn interacting facor f3 domain; 1.
DR   InterPro; IPR045357; Aminopeptidase_N-like_N.
DR   InterPro; IPR042097; Aminopeptidase_N-like_N_sf.
DR   InterPro; IPR024571; ERAP1-like_C_dom.
DR   InterPro; IPR034016; M1_APN-typ.
DR   InterPro; IPR001930; Peptidase_M1.
DR   InterPro; IPR014782; Peptidase_M1_dom.
DR   InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR   PANTHER; PTHR11533:SF171; AMINOPEPTIDASE; 1.
DR   PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR   Pfam; PF11838; ERAP1_C; 1.
DR   Pfam; PF01433; Peptidase_M1; 1.
DR   Pfam; PF17900; Peptidase_M1_N; 1.
DR   PRINTS; PR00756; ALADIPTASE.
DR   SUPFAM; SSF63737; Leukotriene A4 hydrolase N-terminal domain; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|RuleBase:RU364040,
KW   ECO:0000313|EMBL:EKG11117.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU364040};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR634016-3};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW   ECO:0000256|RuleBase:RU364040};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU364040};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007129};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT   DOMAIN          19..217
FT                   /note="Aminopeptidase N-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17900"
FT   DOMAIN          257..474
FT                   /note="Peptidase M1 membrane alanine aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01433"
FT   DOMAIN          548..861
FT                   /note="ERAP1-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11838"
FT   ACT_SITE        330
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT   BINDING         329
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT   BINDING         333
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT   BINDING         352
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT   SITE            415
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ   SEQUENCE   886 AA;  99546 MW;  7ECCF6431B9405AA CRC64;
     MHAAMASDRD ILPDTVKPSN YAISLYDLEF GGAFGYQGTV TISSEIRKPT KEIVLNSHQL
     KIHEASVVTE HTKTQQSIKT TNISYDETNQ RATLAFDQEL PASSKAEVTI KFQGTINNLM
     AGFYRSKYKP AVTPAASVAK DDEYHYMFST QFESCDARRA FPCFDEPNLK ATFDFEIEVP
     EDQTALSNMP EKETKKASKS GFKVVSFEKT PVMSTYLLAW AVGDFEYVED FTRRKYNGKS
     LPVRVYTTRG LKEQGQFALE HAHKTVDYFS EIFRIEYPLP KVDLIAVHEF SHGAMENWGL
     ITYRTTAVLF DPEKSDQKYK NRVAYVVAHE LAHQWFGNLV TMDWWSELWL NEGFATWVGW
     LAVDHLHPEW NVWGQFCSES LQSAFNLDSL RNSHPIEVPV RNALEVDQIF DHISYLKGSS
     VIRMLSAHLG VETFLLGVSQ YLNAHKFGNA TTNDLWSALS KASGQDVNTF MDPWIRKIGF
     PVVTVAEEPG QISVQQRRFL LTGDVQAEED QTTWWIPLGL KTASKTESST AGALTTKEDT
     IRGVDDSFYK LNADQTGFYR TNYPPERLLK LGENKDKLSI EDKIGLIGDA AALAQSGDAN
     TAAFLALLGG FQSESEYIVW QQILLTLGNV RSIFSENEEI SKGLRLLTRK LVTPATDKIG
     WEFAENEDFL KGQLRSLLIS AAGLAGHEGV IKEAQRRFSA YQSGDKKAIH PSLRGPIFRI
     VVTEGGEQGF EAIKQEFLTN TSIDGREICL QALGRVQTPE LAKAYLDFLF SPAVPVQDMH
     SGAASLAANS KTRHTLWAYI KEHWDTKVYP ELSGNMVVLD RFIKLSLAKF ASFEVAKDVK
     TFFADKDCKG FDRALAQSDD IMTGGAKYRE RDSAVVKEWL SAHSYL
//
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