ID I4YC36_WALMC Unreviewed; 447 AA.
AC I4YC36;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Leucine aminopeptidase {ECO:0000313|EMBL:EIM21528.1};
GN ORFNames=WALSEDRAFT_32687 {ECO:0000313|EMBL:EIM21528.1};
OS Wallemia mellicola (strain ATCC MYA-4683 / CBS 633.66) (Wallemia sebi (CBS
OS 633.66)).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Wallemiomycotina;
OC Wallemiomycetes; Wallemiales; Wallemiaceae; Wallemia.
OX NCBI_TaxID=671144 {ECO:0000313|EMBL:EIM21528.1, ECO:0000313|Proteomes:UP000005242};
RN [1] {ECO:0000313|EMBL:EIM21528.1, ECO:0000313|Proteomes:UP000005242}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4683 / CBS 633.66 {ECO:0000313|Proteomes:UP000005242};
RX PubMed=22326418; DOI=10.1016/j.fgb.2012.01.007;
RA Padamsee M., Kumar T.K.A., Riley R., Binder M., Boyd A., Calvo A.M.,
RA Furukawa K., Hesse C., Hohmann S., James T.Y., LaButti K., Lapidus A.,
RA Lindquist E., Lucas S., Miller K., Shantappa S., Grigoriev I.V.,
RA Hibbett D.S., McLaughlin D.J., Spatafora J.W., Aime M.C.;
RT "The genome of the xerotolerant mold Wallemia sebi reveals adaptations to
RT osmotic stress and suggests cryptic sexual reproduction.";
RL Fungal Genet. Biol. 49:217-226(2012).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the peptidase M17 family.
CC {ECO:0000256|ARBA:ARBA00009528}.
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DR EMBL; JH668232; EIM21528.1; -; Genomic_DNA.
DR RefSeq; XP_006958553.1; XM_006958491.1.
DR AlphaFoldDB; I4YC36; -.
DR STRING; 671144.I4YC36; -.
DR GeneID; 18471541; -.
DR KEGG; wse:WALSEDRAFT_32687; -.
DR eggNOG; KOG2597; Eukaryota.
DR HOGENOM; CLU_013734_2_2_1; -.
DR InParanoid; I4YC36; -.
DR OMA; MVTMKAD; -.
DR OrthoDB; 2899215at2759; -.
DR Proteomes; UP000005242; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00433; Peptidase_M17; 1.
DR Gene3D; 3.40.220.10; Leucine Aminopeptidase, subunit E, domain 1; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR011356; Leucine_aapep/pepB.
DR InterPro; IPR043472; Macro_dom-like.
DR InterPro; IPR000819; Peptidase_M17_C.
DR PANTHER; PTHR11963:SF52; CYTOSOL AMINOPEPTIDASE; 1.
DR PANTHER; PTHR11963; LEUCINE AMINOPEPTIDASE-RELATED; 1.
DR Pfam; PF00883; Peptidase_M17; 1.
DR PRINTS; PR00481; LAMNOPPTDASE.
DR SUPFAM; SSF52949; Macro domain-like; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS00631; CYTOSOL_AP; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW ECO:0000313|EMBL:EIM21528.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000005242};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 280..287
FT /note="Cytosol aminopeptidase"
FT /evidence="ECO:0000259|PROSITE:PS00631"
SQ SEQUENCE 447 AA; 48769 MW; 9F8EEFF2397C2FCB CRC64;
MSSIIEFQKA SANKLKLFYE APLKIINNLT NVTPETIKTA AGNSVKELQK HDEINTAKVD
ASQFPHQAAI GANLANFSYS LKKTQRSKLD IKPLEDNPSA EPLNWNTGEI YANAQNLARE
LMEMPPNYCT PTYFAERAAK EFEGIENIKL QVFDKDWAQS MKMNTFLSVA QGSTEPCKFL
QIEYNGSANK EDKPLALVGK GITMDTGGIS IKGGAGMDLM RGDCGGACTL LATTQAIAKL
KLPINVVFVA PLTENMPSGT ATKPGDIITS MSGLTVNVLN TDAEGRLVLA DALYYVSTKF
DPHTVIDCAT LTGAMMIALG EAYSGIFSTT DDLWKLLEDA GLAENDKFWR MPFDDFYLKQ
INNTAADLAN TGGRPAGACT AAIFLKQFVD GINFNAEEGE KPRRQYAHID IAGSMECTKP
ESYNTKGMSG RPTRALIEYA RRLAEKK
//
