ID   A0A2K6C0Y3_MACNE        Unreviewed;       883 AA.
AC   A0A2K6C0Y3;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   SubName: Full=Zinc finger CCCH-type containing 12C {ECO:0000313|Ensembl:ENSMNEP00000017334.1};
GN   Name=ZC3H12C {ECO:0000313|Ensembl:ENSMNEP00000017334.1};
OS   Macaca nemestrina (Pig-tailed macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9545 {ECO:0000313|Ensembl:ENSMNEP00000017334.1, ECO:0000313|Proteomes:UP000233120};
RN   [1] {ECO:0000313|Ensembl:ENSMNEP00000017334.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SIMILARITY: Belongs to the ZC3H12 family.
CC       {ECO:0000256|ARBA:ARBA00010922}.
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DR   RefSeq; XP_011759766.1; XM_011761464.1.
DR   AlphaFoldDB; A0A2K6C0Y3; -.
DR   Ensembl; ENSMNET00000041560.1; ENSMNEP00000017334.1; ENSMNEG00000032663.1.
DR   GeneID; 105493643; -.
DR   CTD; 85463; -.
DR   GeneTree; ENSGT00940000158397; -.
DR   OrthoDB; 180910at2759; -.
DR   Proteomes; UP000233120; Unplaced.
DR   Bgee; ENSMNEG00000032663; Expressed in skeletal muscle tissue and 12 other cell types or tissues.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd18729; PIN_Zc3h12-like; 1.
DR   Gene3D; 3.40.50.11980; -; 1.
DR   InterPro; IPR040546; Rege-1_UBA-like.
DR   InterPro; IPR040757; Regnase_1/ZC3H12_C.
DR   InterPro; IPR021869; RNase_Zc3h12_NYN.
DR   InterPro; IPR000571; Znf_CCCH.
DR   PANTHER; PTHR12876; N4BP1-RELATED; 1.
DR   PANTHER; PTHR12876:SF36; RIBONUCLEASE ZC3H12C-RELATED; 1.
DR   Pfam; PF18561; Regnase_1_C; 1.
DR   Pfam; PF11977; RNase_Zc3h12a; 1.
DR   Pfam; PF18039; UBA_6; 1.
DR   PROSITE; PS50103; ZF_C3H1; 1.
PE   3: Inferred from homology;
KW   Endonuclease {ECO:0000256|ARBA:ARBA00022759};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW   ProRule:PRU00723}; Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233120};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00723};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00723}.
FT   DOMAIN          410..435
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50103"
FT   ZN_FING         410..435
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT   REGION          52..110
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          138..158
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          456..556
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          717..738
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          754..775
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        70..85
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        456..480
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        513..546
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   883 AA;  99247 MW;  9DA29A6B98004F8E CRC64;
     MPGSGSQEYG VLCIQEYGKN SKVESSAHNS FMGLKDHLGH DLGHLYVEST DPQLSPAAPW
     STVERPSMDT VNAGKDEKEV SEENASSGDS EENTNSDHES EQSGSISVEP GLITKTHRQL
     CRSPCLQPHI LKRNEILQDF KPEESQTTSK EAKKPPDVVR EYQTKLEFAL KLGYSEEQVQ
     LVLNKLGTDA LINDILGELV KLGNKSEADQ TVSTINTITR ETSSLESQRS ESPMQEIVTD
     DGENLRPIVI DGSNVAMSHG NKEVFSCRGI KLAVDWFLER GHKDITVFVP AWRKEQSRPD
     ALITDQEILR KLEKEKILVF TPSRRVQGRR VVCYDDRFIV KLAFESDGII VSNDNYRDLA
     NEKPEWKKFI DERLLMYSFV NDKFMPPDDP LGRHGPSLDN FLRKKPIVPE HKKQPCPYGK
     KCTYGHKCKY YHPERGSQPQ RSVADELRAM SRNTAAKTAN EGGLVKSNSV PCSTKADSSS
     DVKRGAPKRQ SDPSIRTQVY QDLEEKLPTK NKLETRSVPS LVSIPATSTA KPQSTTSLSN
     GLPSGVHFPP QDQRPQGQYP PMMMATKNHG TLMPYEQYPK CDSPVDIGYY SMLNAYSNLS
     LSGPRSPERR FSLDTDYRIS SVASDCSSEG SMSCGSSDSY VGYNDRSYVS SPDPQLEENL
     KCQHMHPHSR LNPQPFLQNF HDPLTRVQSY SHEEPKFHHK PPLPHLALHL QHPAVGARSS
     CPGDYPSPPS SAHSKAPHLG RSLVATRIDS ISDSRLYDSS PSRQRKPYSR QEGLGGWERP
     GYGIDAYGYR QTYSLPDNST QPCYEQFTFQ SLPEQQEPAW RIPYCGMPQD PPRYQDNREK
     IYINLCNIFP PDLVRIVMKR NPHMTDAQQL AAAILVEKSQ LGY
//