ID T0QG49_SAPDV Unreviewed; 522 AA.
AC T0QG49;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Cytosol aminopeptidase domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=SDRG_05746 {ECO:0000313|EMBL:EQC36919.1};
OS Saprolegnia diclina (strain VS20).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Saprolegnia.
OX NCBI_TaxID=1156394 {ECO:0000313|EMBL:EQC36919.1, ECO:0000313|Proteomes:UP000030762};
RN [1] {ECO:0000313|EMBL:EQC36919.1, ECO:0000313|Proteomes:UP000030762}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VS20 {ECO:0000313|EMBL:EQC36919.1,
RC ECO:0000313|Proteomes:UP000030762};
RG The Broad Institute Genome Sequencing Platform;
RA Russ C., Nusbaum C., Tyler B., van West P., Dieguez-Uribeondo J.,
RA de Bruijn I., Tripathy S., Jiang R., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA Berlin A., Chapman S.B., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Larimer J., McCowen C., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Saprolegnia declina VS20.";
RL Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase M17 family.
CC {ECO:0000256|ARBA:ARBA00009528}.
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DR EMBL; JH767146; EQC36919.1; -; Genomic_DNA.
DR RefSeq; XP_008609700.1; XM_008611478.1.
DR AlphaFoldDB; T0QG49; -.
DR STRING; 1156394.T0QG49; -.
DR MEROPS; M17.006; -.
DR EnsemblProtists; EQC36919; EQC36919; SDRG_05746.
DR GeneID; 19946473; -.
DR VEuPathDB; FungiDB:SDRG_05746; -.
DR eggNOG; KOG2597; Eukaryota.
DR InParanoid; T0QG49; -.
DR OMA; MVCEQSD; -.
DR OrthoDB; 2899215at2759; -.
DR Proteomes; UP000030762; 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; 3.40.630.10; Zn peptidases; 1.
DR Gene3D; 3.40.50.10590; Zn-dependent exopeptidases; 1.
DR InterPro; IPR011356; Leucine_aapep/pepB.
DR InterPro; IPR041417; NPEPL1_N.
DR InterPro; IPR000819; Peptidase_M17_C.
DR PANTHER; PTHR11963:SF4; AMINOPEPTIDASE NPEPL1-RELATED; 1.
DR PANTHER; PTHR11963; LEUCINE AMINOPEPTIDASE-RELATED; 1.
DR Pfam; PF18295; Pdase_M17_N2; 1.
DR Pfam; PF00883; Peptidase_M17; 1.
DR PRINTS; PR00481; LAMNOPPTDASE.
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 Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000030762}.
FT DOMAIN 18..155
FT /note="Probable aminopeptidase NPEPL1 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18295"
FT DOMAIN 201..510
FT /note="Cytosol aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF00883"
SQ SEQUENCE 522 AA; 55379 MW; 7BF79AC715471C37 CRC64;
MVRYLANVGR IARATALPKV VLIGTKETNS LDLGSKILAQ LKREARPLDP LARRLLAHTI
DELRPTADVP VSAHVYLPLG DDDGIVSCTV ATLPTAISRH NAFARPHAIS SIVKAHMADA
GRTLVGVDLP SHATLQPWKT AGFAVARAIP TYKHTSTTRA GVITDGVATS IPADDVDVVF
SHDLSANEVA FLNATADGIH LAQRLVDAPP NELTTETFVE EARAVATRIG AEFTLIQGTE
LRDRGFGGLY NVGKASLHPP ALAVLSYYPN DASRTERSIA LVGKGLVYDT GGLDLKVGGH
MAGMKADMGG AAGLLGAFDA AVRSGNVRTR PLHCILCIAE NAVGPNATRP DEVHTFYSGK
TVEVNDTDAE GRLVLADGVA YAVKHLHPAL LLDMATLTGA QGIATGSHMG ALYTNTDDLE
AMAVAAGKAS GDLVHPVPYV PEFFRPEYKS HVADMKNYMS NPRNAGVSCG GQFIANHMTD
YLDGDGQWMH IDMASPVEHS DKRATGYGVG FVQSLLEQLH KL
//
