ID G3AQZ3_SPAPN Unreviewed; 506 AA.
AC G3AQZ3;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=Aminopeptidase P N-terminal domain-containing protein {ECO:0000259|SMART:SM01011};
GN ORFNames=SPAPADRAFT_141091 {ECO:0000313|EMBL:EGW31655.1};
OS Spathaspora passalidarum (strain NRRL Y-27907 / 11-Y1).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Spathaspora.
OX NCBI_TaxID=619300 {ECO:0000313|Proteomes:UP000000709};
RN [1] {ECO:0000313|EMBL:EGW31655.1, ECO:0000313|Proteomes:UP000000709}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-27907 / 11-Y1 {ECO:0000313|Proteomes:UP000000709};
RX PubMed=21788494; DOI=10.1073/pnas.1103039108;
RA Wohlbach D.J., Kuo A., Sato T.K., Potts K.M., Salamov A.A., LaButti K.M.,
RA Sun H., Clum A., Pangilinan J.L., Lindquist E.A., Lucas S., Lapidus A.,
RA Jin M., Gunawan C., Balan V., Dale B.E., Jeffries T.W., Zinkel R.,
RA Barry K.W., Grigoriev I.V., Gasch A.P.;
RT "Comparative genomics of xylose-fermenting fungi for enhanced biofuel
RT production.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:13212-13217(2011).
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SIMILARITY: Belongs to the peptidase M24B family.
CC {ECO:0000256|ARBA:ARBA00008766, ECO:0000256|RuleBase:RU000590}.
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DR EMBL; GL996503; EGW31655.1; -; Genomic_DNA.
DR RefSeq; XP_007376433.1; XM_007376371.1.
DR AlphaFoldDB; G3AQZ3; -.
DR STRING; 619300.G3AQZ3; -.
DR GeneID; 18870342; -.
DR KEGG; spaa:SPAPADRAFT_141091; -.
DR eggNOG; KOG2414; Eukaryota.
DR HOGENOM; CLU_017266_1_1_1; -.
DR InParanoid; G3AQZ3; -.
DR OMA; DSYFWYL; -.
DR OrthoDB; 1377484at2759; -.
DR Proteomes; UP000000709; Unassembled WGS sequence.
DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR Gene3D; 3.90.230.10; Creatinase/methionine aminopeptidase superfamily; 1.
DR Gene3D; 3.40.350.10; Creatinase/prolidase N-terminal domain; 1.
DR InterPro; IPR007865; Aminopep_P_N.
DR InterPro; IPR029149; Creatin/AminoP/Spt16_NTD.
DR InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR InterPro; IPR000994; Pept_M24.
DR InterPro; IPR001131; Peptidase_M24B_aminopep-P_CS.
DR PANTHER; PTHR43226; XAA-PRO AMINOPEPTIDASE 3; 1.
DR PANTHER; PTHR43226:SF4; XAA-PRO AMINOPEPTIDASE 3; 1.
DR Pfam; PF05195; AMP_N; 1.
DR Pfam; PF00557; Peptidase_M24; 1.
DR SMART; SM01011; AMP_N; 1.
DR SUPFAM; SSF55920; Creatinase/aminopeptidase; 1.
DR SUPFAM; SSF53092; Creatinase/prolidase N-terminal domain; 1.
DR PROSITE; PS00491; PROLINE_PEPTIDASE; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU000590};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000000709}.
FT DOMAIN 50..187
FT /note="Aminopeptidase P N-terminal"
FT /evidence="ECO:0000259|SMART:SM01011"
SQ SEQUENCE 506 AA; 56412 MW; EECBBCE5120BA3C9 CRC64;
MIKTKAPSIF RRFINIQTRP PHQSVLRAGQ PLHETRPHYL PTPGFLTPGI SAQEYYERRL
QLSRQMPAKS VAIIVGNTVQ FASGSVFYDF QQDNDLFYLT GWNEPDAIAV IEKRGENDED
DVYLHMLVPP RNPAKELWEG PKSGLEGAVE YFNADLVEDI SRAPLYLKNL IHDADLIYYD
NKFASKEEEP IKSFFSILGT SDLNGVISKS NKRISPLSPK LAELRAIKSP AEIKVMHAAA
KISSRAINKA MAKVGSDSPI LSERTLAKFL EYQFVKGGCD KQAYIPVIAS GRNALTIHYT
RNDDLLYKDE MVFIDAAGKV GGYNADISRT WPNSPQGFTD PQRDIYEAVL NTNKACIELC
AQSFGYSMHD LQEFAVRQLT QELNNITGFI VNTTEVTRYL YPHYIGHHLG LDLHDVPTCS
KYKSLVAGNV ITIEPGLYIP ENDRWPKAFR GIGVRVEDDI VVGHTGADIL NLTSGCVKEV
ADIEALISSG KCTTPGIDDE LVVLDI
//
