ID A0A0C3JNW2_PISTI Unreviewed; 512 AA.
AC A0A0C3JNW2;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Peptidase M20 dimerisation domain-containing protein {ECO:0000259|Pfam:PF07687};
GN ORFNames=M404DRAFT_995298 {ECO:0000313|EMBL:KIO10838.1};
OS Pisolithus tinctorius Marx 270.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Sclerodermatineae; Pisolithaceae; Pisolithus.
OX NCBI_TaxID=870435 {ECO:0000313|EMBL:KIO10838.1, ECO:0000313|Proteomes:UP000054217};
RN [1] {ECO:0000313|EMBL:KIO10838.1, ECO:0000313|Proteomes:UP000054217}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Marx 270 {ECO:0000313|EMBL:KIO10838.1,
RC ECO:0000313|Proteomes:UP000054217};
RG DOE Joint Genome Institute;
RA Kuo A., Kohler A., Costa M.D., Nagy L.G., Floudas D., Copeland A.,
RA Barry K.W., Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A.,
RA Lipzen A., Lundell T., Morin E., Murat C., Sun H., Tunlid A., Henrissat B.,
RA Grigoriev I.V., Hibbett D.S., Martin F., Nordberg H.P., Cantor M.N.,
RA Hua S.X.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000054217}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Marx 270 {ECO:0000313|Proteomes:UP000054217};
RG DOE Joint Genome Institute;
RG Mycorrhizal Genomics Consortium;
RA Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase M20A family.
CC {ECO:0000256|ARBA:ARBA00006247}.
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DR EMBL; KN831951; KIO10838.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C3JNW2; -.
DR STRING; 870435.A0A0C3JNW2; -.
DR HOGENOM; CLU_031812_1_1_1; -.
DR InParanoid; A0A0C3JNW2; -.
DR OrthoDB; 1074531at2759; -.
DR Proteomes; UP000054217; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR CDD; cd05672; M20_ACY1L2-like; 1.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR017439; Amidohydrolase.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR NCBIfam; TIGR01891; amidohydrolases; 1.
DR PANTHER; PTHR30575; PEPTIDASE M20; 1.
DR PANTHER; PTHR30575:SF0; XAA-ARG DIPEPTIDASE; 1.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000054217}.
FT DOMAIN 277..368
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
FT REGION 31..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..56
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 512 AA; 55240 MW; 2C1007BE6715F2B4 CRC64;
MSHKMLDDHN KVGCLSLKRL FRLPPIGRSL SIRSPTKIDQ RNSSEESEDH DKQPSSDRPS
TFVNSEPVHF ESCCDFSARR SLPSSVDPPP KYLDSSTSVQ SMSTVMSVIE STMQALDNDL
RALSLQIHDH PELMFEERYA HDLLCDFMER HGFAVTRHYL GLETAWRAEF THGKGGRTLG
INSEMDALPV IGHACGHNLI AVSGVGVAIA VKSALQTYDV PGTVVLLGTP GEEGGAGKAV
MLERGGYRDI DVCLMCHPAT GPAGSVSLGS CLAMQSLEAE FFGRSAHAGN APWDGTNALD
AAFLAYSSIS VLRQQIKPDH RIHGVIQGSK SAVNVIPDYA GMRWLVRAPT KDQLSVLVER
VKACFEGAAL ATSCRFKLTE GIPYHDLRQN NVLAACFSHA VSNSFGMNIG QRGFGASTDF
GNVSYALPSL HPSFAIPTVA NGGNHTPAFA ESARSTDAHK ATMTVSKGLA WTGFRVIADD
ELFQQVRGAY ESGPAGVQQL ILSDSDTHQT EL
//
