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
//