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Database: UniProt
Entry: A7TPM2_VANPO
LinkDB: A7TPM2_VANPO
Original site: A7TPM2_VANPO 
ID   A7TPM2_VANPO            Unreviewed;       740 AA.
AC   A7TPM2;
DT   02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT   02-OCT-2007, sequence version 1.
DT   24-JAN-2024, entry version 85.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EDO15767.1};
GN   ORFNames=Kpol_478p2 {ECO:0000313|EMBL:EDO15767.1};
OS   Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS   2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX   NCBI_TaxID=436907 {ECO:0000313|Proteomes:UP000000267};
RN   [1] {ECO:0000313|EMBL:EDO15767.1, ECO:0000313|Proteomes:UP000000267}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 /
RC   NRRL Y-8283 / UCD 57-17 {ECO:0000313|Proteomes:UP000000267};
RX   PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA   Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT   "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT   species descended from a whole-genome duplication.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(2007).
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}.
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DR   EMBL; DS480445; EDO15767.1; -; Genomic_DNA.
DR   RefSeq; XP_001643625.1; XM_001643575.1.
DR   AlphaFoldDB; A7TPM2; -.
DR   STRING; 436907.A7TPM2; -.
DR   MEROPS; M24.A10; -.
DR   GeneID; 5543885; -.
DR   KEGG; vpo:Kpol_478p2; -.
DR   eggNOG; KOG2413; Eukaryota.
DR   HOGENOM; CLU_011781_2_6_1; -.
DR   InParanoid; A7TPM2; -.
DR   OMA; YRPGKWG; -.
DR   OrthoDB; 869at2759; -.
DR   PhylomeDB; A7TPM2; -.
DR   Proteomes; UP000000267; Unassembled WGS sequence.
DR   GO; GO:0110165; C:cellular anatomical entity; IEA:UniProt.
DR   GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR   CDD; cd01085; APP; 1.
DR   Gene3D; 3.90.230.10; Creatinase/methionine aminopeptidase superfamily; 1.
DR   Gene3D; 3.40.350.10; Creatinase/prolidase N-terminal domain; 2.
DR   InterPro; IPR029149; Creatin/AminoP/Spt16_NTD.
DR   InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR   InterPro; IPR000587; Creatinase_N.
DR   InterPro; IPR000994; Pept_M24.
DR   InterPro; IPR033740; Pept_M24B.
DR   InterPro; IPR032416; Peptidase_M24_C.
DR   PANTHER; PTHR43763; XAA-PRO AMINOPEPTIDASE 1; 1.
DR   PANTHER; PTHR43763:SF6; XAA-PRO AMINOPEPTIDASE 1; 1.
DR   Pfam; PF01321; Creatinase_N; 1.
DR   Pfam; PF16189; Creatinase_N_2; 1.
DR   Pfam; PF00557; Peptidase_M24; 1.
DR   Pfam; PF16188; Peptidase_M24_C; 1.
DR   SUPFAM; SSF55920; Creatinase/aminopeptidase; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000000267}.
FT   DOMAIN          95..241
FT                   /note="Creatinase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01321"
FT   DOMAIN          451..665
FT                   /note="Peptidase M24"
FT                   /evidence="ECO:0000259|Pfam:PF00557"
FT   DOMAIN          678..740
FT                   /note="Peptidase M24 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16188"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..25
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   740 AA;  84576 MW;  4A55DE993C4760A9 CRC64;
     MSTAQSSRMA MAGGVPPSSS SVRGNRPFRP CDDCTCSPGL LSRHGKRSSI FFRQYENTRR
     RAHSSANNQL SASNESVYSS DTLCKNFKEV NTTERLLHLR NEMRSNDLCC YIVPSEDSHQ
     SEYVSEKDER RSFISGFTGS AGIACITRDL LNFNDEKEPT GKSILSTDGR YFNQALQELD
     YNWALLRQGE DKLNWQQWCC NEAIEMLKGL GLKSNKKPLK IGIDPKLITY EQVLNFKSTL
     EKMLSENSIN GNSSDYIQLV PITENLIDKI WGDFEPVPSR PSNDLILLDE SYHGEEFSSK
     RSRILKKLSS SKKSNDDSKI KNYFVTVALD EICWLLNLRG SEIDFNPVFY AYLLIDDQSD
     ETILFTDSKY DDKIKQYFES NRIVVKPYDQ FWESLSGFVT EATNDATTFI VPDNSSWQLI
     REVSKKTYKM LHSPVDVLKS VKNVTEIANA HRAQVLDSVC LTQYFAWLED RLIQHEALID
     EYTAAEKLTE IRKTKKTFIG NSFDTISSTG ANAAVIHYKP PKENSSMINP QKIYLCDSGS
     QFLEGTTDIT RTIHLDKPTE EEIKNYTLVL KGNLALERLI FPEGTNGYQI DVIARQYLWE
     QGLDYRHGTG HGIGAMLNVH EGPIGIGTKP TSIKYPLQAG NIISNEPGYY KDGEYGIRIE
     NDLLVEVVKP EMRFGDKKFL CFENITLVPY CRKLIDVKML DKREREQINE YHRKIFDTTV
     QFTQPQSISF KWLKRETAPL
//
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