ID   MPND_DANRE              Reviewed;         458 AA.
AC   Q08CH3;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=MPN domain-containing protein {ECO:0000305};
DE            EC=3.4.-.- {ECO:0000250|UniProtKB:Q5VVJ2};
GN   Name=mpnd; ORFNames=zgc:153076;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Ovary;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Probable protease (By similarity). Acts as a sensor of N(6)-
CC       methyladenosine methylation on DNA (m6A): recognizes and binds m6A DNA,
CC       leading to its degradation (By similarity).
CC       {ECO:0000250|UniProtKB:Q5VVJ2, ECO:0000250|UniProtKB:Q8N594}.
CC   -!- DOMAIN: The RAMA domain recognizes and binds N(6)-methyladenosine
CC       methylation on DNA (m6A). {ECO:0000250|UniProtKB:Q8N594}.
CC   -!- PTM: Degraded following binding to N(6)-methyladenosine methylated DNA
CC       (m6A). {ECO:0000250|UniProtKB:Q8N594}.
CC   -!- SIMILARITY: Belongs to the peptidase M67 family. {ECO:0000305}.
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DR   EMBL; BC124239; AAI24240.1; -; mRNA.
DR   RefSeq; NP_001070033.1; NM_001076565.1.
DR   AlphaFoldDB; Q08CH3; -.
DR   SMR; Q08CH3; -.
DR   STRING; 7955.ENSDARP00000083512; -.
DR   PaxDb; Q08CH3; -.
DR   PRIDE; Q08CH3; -.
DR   Ensembl; ENSDART00000089079; ENSDARP00000083512; ENSDARG00000061989.
DR   GeneID; 559169; -.
DR   KEGG; dre:559169; -.
DR   CTD; 84954; -.
DR   ZFIN; ZDB-GENE-060929-1162; mpnd.
DR   eggNOG; KOG1555; Eukaryota.
DR   GeneTree; ENSGT00940000160191; -.
DR   HOGENOM; CLU_037792_0_0_1; -.
DR   InParanoid; Q08CH3; -.
DR   OMA; MMLVEFY; -.
DR   OrthoDB; 590811at2759; -.
DR   PhylomeDB; Q08CH3; -.
DR   TreeFam; TF324811; -.
DR   PRO; PR:Q08CH3; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 8.
DR   Bgee; ENSDARG00000061989; Expressed in presomitic mesoderm and 27 other tissues.
DR   GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR   GO; GO:0070122; F:isopeptidase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0140492; F:metal-dependent deubiquitinase activity; IEA:InterPro.
DR   GO; GO:0003713; F:transcription coactivator activity; IBA:GO_Central.
DR   GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR000555; JAMM/MPN+_dom.
DR   InterPro; IPR037518; MPN.
DR   InterPro; IPR040843; RAMA.
DR   Pfam; PF01398; JAB; 1.
DR   Pfam; PF18755; RAMA; 1.
DR   PROSITE; PS50249; MPN; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase; Metal-binding; Metalloprotease; Protease; Reference proteome;
KW   Zinc.
FT   CHAIN           1..458
FT                   /note="MPN domain-containing protein"
FT                   /id="PRO_0000278806"
FT   DOMAIN          42..137
FT                   /note="RAMA"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          229..364
FT                   /note="MPN"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   REGION          1..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          147..175
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           306..319
FT                   /note="JAMM motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   COMPBIAS        147..163
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         306
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   BINDING         308
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   BINDING         319
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
SQ   SEQUENCE   458 AA;  51102 MW;  2A38082B6F88DE24 CRC64;
     MGSEPPSSPQ VVEEGADEED EELSGAEDAD LRSSSGRGSL LTRRGITLRV LLKDGLVEPG
     DGVLSIHYLG KKFVGDLLND GKIRWVETGQ IFNSPSAWAT HCKRLVNPAK KSGCGWASVR
     YRGQKLVQYK TTWLHKYQPS ADMSLISEGE DDEMGDDDEE EGKTTIPVED KNKKSKPELH
     EIGLTQRRDR ERIPVRYCTL GTRDAARDPH TLVELSAFSA INRFQPFNVA VSSNVLLLMD
     FHCHLTSSEV VGYLGGRWDT NTQLLTVLRA FPCRTRLADK DAAPAVEEEI CQNLFMRGLS
     LVGWYHSHPR GPALPSLQDI DSQMDHQLRL QGSSNGFQPC LGIICGPYYH GNQGVASTIT
     PFWVVPPPEQ RPNDHGIPVA VEVTYVQDNF LTTDVLNEMM LLVEFYRSAP DLVQFSQMWS
     PNTSILDKIK ASLSGHAPKD QAYAQILEHV YNQLRNTQ