ID   V5EUC3_KALBG            Unreviewed;      1410 AA.
AC   V5EUC3;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=aspartyl aminopeptidase {ECO:0000256|ARBA:ARBA00011965};
DE            EC=3.4.11.21 {ECO:0000256|ARBA:ARBA00011965};
GN   ORFNames=PSEUBRA_SCAF3g04254 {ECO:0000313|EMBL:EST06743.1};
OS   Kalmanozyma brasiliensis (strain GHG001) (Yeast) (Pseudozyma brasiliensis).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Kalmanozyma.
OX   NCBI_TaxID=1365824 {ECO:0000313|EMBL:EST06743.1, ECO:0000313|Proteomes:UP000019377};
RN   [1] {ECO:0000313|Proteomes:UP000019377}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GHG001 {ECO:0000313|Proteomes:UP000019377};
RX   PubMed=24356824; DOI=10.1128/genomea.00920-13;
RA   Oliveira J.V.D.C., dos Santos R.A.C., Borges T.A., Riano-Pachon D.M.,
RA   Goldman G.H.;
RT   "Draft genome sequence of Pseudozyma brasiliensis sp. nov. strain GHG001, a
RT   high producer of endo-1,4-xylanase isolated from an insect pest of
RT   sugarcane.";
RL   Genome Announc. 1:E0092013-E0092013(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}.
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DR   EMBL; KI545873; EST06743.1; -; Genomic_DNA.
DR   RefSeq; XP_016291732.1; XM_016438191.1.
DR   STRING; 1365824.V5EUC3; -.
DR   MEROPS; M18.A01; -.
DR   GeneID; 27420869; -.
DR   eggNOG; KOG2596; Eukaryota.
DR   eggNOG; KOG3729; Eukaryota.
DR   HOGENOM; CLU_004237_0_0_1; -.
DR   OMA; GPNKTQK; -.
DR   OrthoDB; 5478811at2759; -.
DR   Proteomes; UP000019377; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
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; cd07993; LPLAT_DHAPAT-like; 1.
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; IPR045520; GPAT/DHAPAT_C.
DR   InterPro; IPR041728; GPAT/DHAPAT_LPLAT.
DR   InterPro; IPR001948; Peptidase_M18.
DR   InterPro; IPR023358; Peptidase_M18_dom2.
DR   InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR   PANTHER; PTHR28570; ASPARTYL AMINOPEPTIDASE; 1.
DR   PANTHER; PTHR28570:SF3; ASPARTYL AMINOPEPTIDASE; 1.
DR   Pfam; PF01553; Acyltransferase; 1.
DR   Pfam; PF19277; GPAT_C; 1.
DR   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
DR   SMART; SM00563; PlsC; 1.
DR   SUPFAM; SSF101821; Aminopeptidase/glucanase lid domain; 1.
DR   SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|ARBA:ARBA00022438};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019377};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EST06743.1};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          263..390
FT                   /note="Phospholipid/glycerol acyltransferase"
FT                   /evidence="ECO:0000259|SMART:SM00563"
FT   REGION          1..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1410 AA;  155145 MW;  9C71557657DDEE15 CRC64;
     MGSQSRRGAD QQSASTSAAG SSSSAPTDDR SDSTGSRSGP PSEGRLPSVQ HESNVLSKQL
     GDLGSSRRQD RNLADQKGIL TSEEHKLGDL NVVAAYKAHF RESPFEFLQQ FVAYGQGTGW
     RGYSNYIGAP ILYKGCAEES IRAVLNSDQV QERIRALASS RVDHLLPEQP PLSPTGPNKT
     QKNLAVFKER KKRQIEQQLR DEALAILQVS VARVDSLPFV KFFAATVNNI LARMYHQGIH
     ISVPQVLELR RVAAYAAERK QSILFLPCHK SHIDYLTVSW LMFRLGIGLP HIIAGENLDL
     PVLGDVLRKG GAFFIRRTFS GDQLYPAVIK EYVETLLASG KNLECFIEGT RSRTGKLLPP
     KLGILKYVVE GLLNGRTDDV WICPVSLQYD SVIESGTYVS ELLGKPKEAE SLLGLLSDSS
     SLLQLKMGRI DIRFDTPWSL QGFIKEQKDR RAAPGLKGEK VELDPVNNEV HKVLLLKALG
     YRVLADINKV SVVMPAALIG TVVLTLRGRG VSRSELIRRV DWLRSAIIKK GFTVADFGTM
     KTGEVVDRAL NTVMKGLITE QKDVMEPTFV PDKHFELSFY RNQVIHIFVS ESLAAAALYT
     KVKQGGTAPM QRMTRKELLN ECMFISSVLR NEFVFGVDTL ETNVDRTIDG MVADGVLDKH
     ADIKPEDGGS IELSAKEREN GRENYDSFLF LIWPFIEGYW LAAVSLFSLI PKGAEAHGYP
     TDKLPWFAAK DFEKHTQLLG KTLYAQGELS YLESINAATL SQAFTRMEEM SMILRKKSSH
     QKPIPIMALN PNFWPSQTSN LAAYIDRLSQ FRREGKDRRE KSVGAKVRQY TTMYTPSVPA
     VVLLAFTLHH QLTHSLRRIA SRHTLALDPS LHSNKLSAQA FFKLVSAASV RLSQNSVASR
     SSAAAAAMST SSTAAAVAAG TSGKADDIAA ARRFLEYVDA SPTPFHAVAT TSAMLDAAGF
     ERIRENDLWD SKVQRGGKYY FTRNQSAIVA FAVGAKYEPG NGVHVVGAHT DSPNFQIKPV
     SRKAKEGYLQ CGVETYGGGI WASWFDRDLG VAGRVIVSDS KNHDAFTGKL VHIKRPIMRI
     PTLAIHLNRT VNEAFKFNVE DNTVPILGLA TEQLNKRADE AAAAAKSTPQ AVGTPVMAEK
     HHSVLLDLLA SELGISVEQI QDFELSLYDT QPASIGGINN EFIHSPRLDN QMSCFCATEA
     LIDSLTSADS LNASSSIRAI ALFDNEEVGS VSTHGAESNM LPSLIQRLVA LPVSSSPASA
     SKPAASNLYE QAVARSFLLS SDMAHGFHPN YPSFYEENHR PKINGGPVLK TNVKQRYATT
     GPTAFLIRRI AQRAQVPLQS FVVKNDMPCG STIGPMLSKL GIRTLDLGNP QLSMHSIRET
     CGTKDVEYKI QLFKHFFDSF EEVDAQLVID
//