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Database: UniProt
Entry: D8RZ38_SELML
LinkDB: D8RZ38_SELML
Original site: D8RZ38_SELML 
ID   D8RZ38_SELML            Unreviewed;       432 AA.
AC   D8RZ38;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   RecName: Full=Peptidase M20 dimerisation domain-containing protein {ECO:0000259|Pfam:PF07687};
GN   ORFNames=SELMODRAFT_105028 {ECO:0000313|EMBL:EFJ22543.1};
OS   Selaginella moellendorffii (Spikemoss).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Lycopodiopsida; Selaginellales; Selaginellaceae; Selaginella.
OX   NCBI_TaxID=88036 {ECO:0000313|Proteomes:UP000001514};
RN   [1] {ECO:0000313|EMBL:EFJ22543.1, ECO:0000313|Proteomes:UP000001514}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21551031; DOI=10.1126/science.1203810;
RA   Banks J.A., Nishiyama T., Hasebe M., Bowman J.L., Gribskov M.,
RA   dePamphilis C., Albert V.A., Aono N., Aoyama T., Ambrose B.A., Ashton N.W.,
RA   Axtell M.J., Barker E., Barker M.S., Bennetzen J.L., Bonawitz N.D.,
RA   Chapple C., Cheng C., Correa L.G., Dacre M., DeBarry J., Dreyer I.,
RA   Elias M., Engstrom E.M., Estelle M., Feng L., Finet C., Floyd S.K.,
RA   Frommer W.B., Fujita T., Gramzow L., Gutensohn M., Harholt J., Hattori M.,
RA   Heyl A., Hirai T., Hiwatashi Y., Ishikawa M., Iwata M., Karol K.G.,
RA   Koehler B., Kolukisaoglu U., Kubo M., Kurata T., Lalonde S., Li K., Li Y.,
RA   Litt A., Lyons E., Manning G., Maruyama T., Michael T.P., Mikami K.,
RA   Miyazaki S., Morinaga S., Murata T., Mueller-Roeber B., Nelson D.R.,
RA   Obara M., Oguri Y., Olmstead R.G., Onodera N., Petersen B.L., Pils B.,
RA   Prigge M., Rensing S.A., Riano-Pachon D.M., Roberts A.W., Sato Y.,
RA   Scheller H.V., Schulz B., Schulz C., Shakirov E.V., Shibagaki N.,
RA   Shinohara N., Shippen D.E., Soerensen I., Sotooka R., Sugimoto N.,
RA   Sugita M., Sumikawa N., Tanurdzic M., Theissen G., Ulvskov P., Wakazuki S.,
RA   Weng J.K., Willats W.W., Wipf D., Wolf P.G., Yang L., Zimmer A.D., Zhu Q.,
RA   Mitros T., Hellsten U., Loque D., Otillar R., Salamov A., Schmutz J.,
RA   Shapiro H., Lindquist E., Lucas S., Rokhsar D., Grigoriev I.V.;
RT   "The Selaginella genome identifies genetic changes associated with the
RT   evolution of vascular plants.";
RL   Science 332:960-963(2011).
CC   -!- SIMILARITY: Belongs to the peptidase M20 family.
CC       {ECO:0000256|ARBA:ARBA00006153}.
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DR   EMBL; GL377595; EFJ22543.1; -; Genomic_DNA.
DR   RefSeq; XP_002976283.1; XM_002976237.1.
DR   AlphaFoldDB; D8RZ38; -.
DR   STRING; 88036.D8RZ38; -.
DR   MEROPS; M20.014; -.
DR   EnsemblPlants; EFJ22543; EFJ22543; SELMODRAFT_105028.
DR   GeneID; 9646586; -.
DR   Gramene; EFJ22543; EFJ22543; SELMODRAFT_105028.
DR   KEGG; smo:SELMODRAFT_105028; -.
DR   eggNOG; ENOG502QQEM; Eukaryota.
DR   HOGENOM; CLU_023257_0_0_1; -.
DR   InParanoid; D8RZ38; -.
DR   OMA; PECQTMG; -.
DR   OrthoDB; 3684955at2759; -.
DR   Proteomes; UP000001514; Unassembled WGS sequence.
DR   GO; GO:0010179; F:IAA-Ala conjugate hydrolase activity; IBA:GO_Central.
DR   GO; GO:0009850; P:auxin metabolic process; IBA:GO_Central.
DR   CDD; cd08017; M20_IAA_Hyd; 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; IPR044757; ILR1-like_Hyd.
DR   InterPro; IPR002933; Peptidase_M20.
DR   InterPro; IPR011650; Peptidase_M20_dimer.
DR   NCBIfam; TIGR01891; amidohydrolases; 1.
DR   PANTHER; PTHR11014:SF119; IAA-AMINO ACID HYDROLASE ILR1-LIKE 1; 1.
DR   PANTHER; PTHR11014; PEPTIDASE M20 FAMILY MEMBER; 1.
DR   Pfam; PF07687; M20_dimer; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   PIRSF; PIRSF005962; Pept_M20D_amidohydro; 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:UP000001514};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..432
FT                   /note="Peptidase M20 dimerisation domain-containing
FT                   protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003122260"
FT   DOMAIN          218..316
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   432 AA;  46022 MW;  2E33F4F4C3571BDC CRC64;
     MWFHSLLSLL LLVPLRSIRA HQECPSSSAG DAAIANSTLS SIGDGEDIRE WLVGIRRRIH
     QRPELGFQEF ETSALIRAEL DALGVPYEWP VAGTGVVATI GTGGPPIVAL RADMDALPLQ
     ELGNSEYKSQ VAGKMHACGH DAHVAMLLGA ARLLSRPAAV PRGTVRLLFQ PAEEGLYGAL
     AMVEGGALGD AQAIFGIHVT SERPVGTASS RAGPLLAGAG FLTATITGRG GHAALPHKTI
     DPILAASMVV ASLQQLVSRE SNPLESEVVS VTSIQTPDSF NVIPSTVTLK GTFRGYKKEG
     LERLKTRIEQ VITSQASVHQ CSASVDISNL QPATSNDPEL YHFFQGVAKD LLGEDKVTEM
     EPTMGAEDFA FYSDHVPTMF FFLGSGNDAE GFDNRPHSPY FDLDEDVLPI GAAMHAALAT
     NYIEKTATVS DI
//
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