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Database: UniProt
Entry: M5FPM2_DACPD
LinkDB: M5FPM2_DACPD
Original site: M5FPM2_DACPD 
ID   M5FPM2_DACPD            Unreviewed;       505 AA.
AC   M5FPM2;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 46.
DE   SubName: Full=Creatinase/aminopeptidase {ECO:0000313|EMBL:EJT96514.1};
DE   Flags: Fragment;
GN   ORFNames=DACRYDRAFT_120060 {ECO:0000313|EMBL:EJT96514.1};
OS   Dacryopinax primogenitus (strain DJM 731) (Brown rot fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC   Dacrymycetales; Dacrymycetaceae; Dacryopinax.
OX   NCBI_TaxID=1858805 {ECO:0000313|EMBL:EJT96514.1, ECO:0000313|Proteomes:UP000030653};
RN   [1] {ECO:0000313|EMBL:EJT96514.1, ECO:0000313|Proteomes:UP000030653}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DJM-731 SS1 {ECO:0000313|EMBL:EJT96514.1,
RC   ECO:0000313|Proteomes:UP000030653};
RX   PubMed=22745431; DOI=10.1126/science.1221748;
RA   Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA   Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA   Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA   Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA   Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA   Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA   Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA   Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA   Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA   Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA   Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA   Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA   Hibbett D.S.;
RT   "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT   31 fungal genomes.";
RL   Science 336:1715-1719(2012).
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; JH795897; EJT96514.1; -; Genomic_DNA.
DR   AlphaFoldDB; M5FPM2; -.
DR   STRING; 1858805.M5FPM2; -.
DR   HOGENOM; CLU_017266_1_2_1; -.
DR   OMA; ESKHINH; -.
DR   OrthoDB; 1377484at2759; -.
DR   Proteomes; UP000030653; 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; 2.
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:SF1; XAA-PRO DIPEPTIDASE; 1.
DR   Pfam; PF05195; AMP_N; 1.
DR   Pfam; PF00557; Peptidase_M24; 2.
DR   SMART; SM01011; AMP_N; 1.
DR   SUPFAM; SSF55920; Creatinase/aminopeptidase; 2.
DR   SUPFAM; SSF53092; Creatinase/prolidase N-terminal domain; 1.
DR   PROSITE; PS00491; PROLINE_PEPTIDASE; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000313|EMBL:EJT96514.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU000590}; Protease {ECO:0000313|EMBL:EJT96514.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030653}.
FT   DOMAIN          5..165
FT                   /note="Aminopeptidase P N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01011"
FT   REGION          233..253
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          455..491
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        460..485
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         505
FT                   /evidence="ECO:0000313|EMBL:EJT96514.1"
SQ   SEQUENCE   505 AA;  55524 MW;  6463EF009BC2FAE1 CRC64;
     MDSHYPAHKH AINVLNNLIP LLSKQHRCKP QLLLLRSKPV TYRDDTDREL PYRQESNFYY
     LSGCLVPDST LVVSYTPPNA TPNANANAEG EEEVDVGVHP DSVQTTLFIP PEDPIEVLWS
     PAPPSLAETV LSHQVTSVLP TPSLPAQLFT LLQSSPVLHL LPESSFPLLP GSISGLVKEY
     KGEGTRRDCL LPALHLARLI KDEHEIELIR RANAISSRAH ELVMRLLGEH AHRARTRTRT
     REGEGEEGEG GKVEMPGEWR IESEQEAEAV FVAACRREGA KHQAYLPIVA SSTRASTLHY
     CCNDKSFAWG PLPSPSHPHS HSHSALGGLG SLLHGDGNGN GKEEGLQAQV LLIDAGCEWD
     CYASDITRVT PIGNNGHFSP QARDIYLTVL HMQTTAISLL RPGLHWDVVQ LSMHRILVQS
     FLKLGIFRGE EDEVLKSGVS AAFFPHGVGH SLGLDVHDVP SASKPERPEG DRPGEKGEGE
     KGGEGGENPE FYTWLRLRLP LRKGM
//
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