ID   A0A1B7N7W0_9AGAM        Unreviewed;       834 AA.
AC   A0A1B7N7W0;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Creatinase aminopeptidase {ECO:0000313|EMBL:OAX40913.1};
GN   ORFNames=K503DRAFT_848715 {ECO:0000313|EMBL:OAX40913.1};
OS   Rhizopogon vinicolor AM-OR11-026.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Boletales; Suillineae; Rhizopogonaceae; Rhizopogon.
OX   NCBI_TaxID=1314800 {ECO:0000313|EMBL:OAX40913.1, ECO:0000313|Proteomes:UP000092154};
RN   [1] {ECO:0000313|EMBL:OAX40913.1, ECO:0000313|Proteomes:UP000092154}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AM-OR11-026 {ECO:0000313|EMBL:OAX40913.1,
RC   ECO:0000313|Proteomes:UP000092154};
RG   DOE Joint Genome Institute;
RA   Mujic A.B., Kuo A., Tritt A., Lipzen A., Chen C., Johnson J., Sharma A.,
RA   Barry K., Grigoriev I.V., Spatafora J.W.;
RT   "Comparative genomics of the ectomycorrhizal sister species Rhizopogon
RT   vinicolor and Rhizopogon vesiculosus (Basidiomycota: Boletales) reveals a
RT   divergence of the mating type B locus.";
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
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; KV448196; OAX40913.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1B7N7W0; -.
DR   STRING; 1314800.A0A1B7N7W0; -.
DR   InParanoid; A0A1B7N7W0; -.
DR   OrthoDB; 869at2759; -.
DR   Proteomes; UP000092154; Unassembled WGS sequence.
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.
DR   SUPFAM; SSF53092; Creatinase/prolidase N-terminal domain; 1.
DR   SUPFAM; SSF101447; Formin homology 2 domain (FH2 domain); 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000313|EMBL:OAX40913.1};
KW   Hydrolase {ECO:0000313|EMBL:OAX40913.1};
KW   Protease {ECO:0000313|EMBL:OAX40913.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000092154}.
FT   DOMAIN          214..339
FT                   /note="Creatinase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01321"
FT   DOMAIN          533..743
FT                   /note="Peptidase M24"
FT                   /evidence="ECO:0000259|Pfam:PF00557"
FT   DOMAIN          757..814
FT                   /note="Peptidase M24 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16188"
FT   REGION          1..188
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        27..83
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        97..117
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        138..154
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        163..188
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   834 AA;  94239 MW;  F4380FB33C5D4ADF CRC64;
     MPPPPPPPPP PPPPPMCFPF ANRSRTREAS PPISVHSYRG SQRSDNISNN SNRSKRSHHS
     TGSQNKLVRS GSYSPTKTLA SDAEKLSFDS DSEAYDVPAL PNNQSRSKFS QHSRNESKSV
     LTRVDSKKSS KWGYGWGLGK VKEREREMLE RSPSVDSERP PLYKSPTRTS SRSSESKRPP
     FYSNDSSSTL VGSAYERKIN DIEPIKEKID TADRLEDIRK LMAKDKLDYY VVPSEDAHQS
     EYVAASDKRR EWISGFTGSA GQAVVSKTAA YLITDSRYWL QARTELDSNW HLIPAGAVDG
     PKDWIDWLVD RAKDANIGID ARMISHDKAA SLNSQLKNKS SRLIYPPQNY IDLAWKEKPQ
     RSKEPVFIQS LEFTGREAST KIAEVRAWIR AQPASVPSYS KASPTPAQIH IGTLITSLSS
     IAWLLNLRGS DIPFNPLFCG YLFISLDRVV LFLDAVKLTD EVEDHLRALN VERKEYNDIW
     AFLRRRDWGE GKVLISPETS YAISLMLTHF RYTVAPSFID SIKAIKNEVE LEGLRRAYLR
     DGAAYVRWLA WLEHKIQQGY DITEYEAAWR LTEYRRQNKH YWGLAYENIS ASGPNAALPH
     YSPTKSGARM IDRDTPYLND SGGQYRDGTC DTTRTVHFGR PSPDQSEAYT RVLQGHIAID
     SAIFPEGTTG SQLDVLARRA LWKDGLNYMH GTGHGFGSFL NVHEGPHGFS SSVPLVPGHV
     ITNEPGFYLE GRWGMRIESA LAIRRVKTKG EFNGDIWLGF ERLTCVPIQT RMVKESMLTK
     EEKQWLKDHN KKCLERLEPF LKDDKRALKW LKRESDRGIG IAAAGPGGIT IDWD
//