ID   A0A2K6GFN3_PROCO        Unreviewed;       883 AA.
AC   A0A2K6GFN3;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=Zinc finger CCCH-type containing 12C {ECO:0000313|Ensembl:ENSPCOP00000025037.1};
GN   Name=ZC3H12C {ECO:0000313|Ensembl:ENSPCOP00000025037.1};
OS   Propithecus coquereli (Coquerel's sifaka) (Propithecus verreauxi
OS   coquereli).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lemuriformes;
OC   Indriidae; Propithecus.
OX   NCBI_TaxID=379532 {ECO:0000313|Ensembl:ENSPCOP00000025037.1, ECO:0000313|Proteomes:UP000233160};
RN   [1] {ECO:0000313|Ensembl:ENSPCOP00000025037.1}
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   AlphaFoldDB; A0A2K6GFN3; -.
DR   Ensembl; ENSPCOT00000035726.1; ENSPCOP00000025037.1; ENSPCOG00000024737.1.
DR   GeneTree; ENSGT00940000158397; -.
DR   Proteomes; UP000233160; Unplaced.
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:UP000233160};
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          62..109
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          138..157
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          456..501
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          524..546
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          714..738
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          754..777
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        754..769
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   883 AA;  99594 MW;  88A10DB04FDE8E87 CRC64;
     QPASGCQEYG VLCIQEYRKN NKVESSTLNS FMGLKDHLGH DLSHLYVENT DPQLSAAVPW
     STVDKPTMDT VNAGKDEKEV SEENASSGDS EESTNSDHES EQLSSISVEP CSLTKTHRQL
     CRSPCLEPHI LKRNEILQDF KPEESQTTSK EGKKPPDVVR EYQTKLEFAL KLGYSEEQVQ
     LVLNKLGTDA LINDILGELV KLGNKSEADQ TVSTINSIMR ETSSLESQRS ESPMQEIVTD
     DGENLRPIVI DGSNVAMSHG NKEVFSCRGI KLAVDWFLER GHKDVTVFVP AWRKEQSRPD
     ALITDQEILR KLEKEKILVF TPSRRVQGRR VVCYDDRFIV KLAFESDGII VSNDNYRDLA
     NEKPEWKKFI DERLLMYSFV NDKFMPPDDP LGRHGPSLDN FLRKKPIVPE HKKQPCPYGK
     KCTYGHKCKY YHPERGSQPQ RSVADELRAM SRNTAAKTAN EGGLVKSNSV PCSTKADSTS
     DVKRGAPKRQ SDPSIRTQVY QDLEEKLPTK NKLETRSVPS LVSIPATSTA KPQSTASLSN
     GLPSGVHFPP QDQRPQGQYP PMMMATKNHG TPMPYEQYPK CDSPVDIGYY SMLNAYSNLS
     ISGPRSPERR FSLDTDYRIS SVASDCSSEG SMSCGSSDSY VGYNDRSYVS SPDPQLEENL
     KCQHMHPHSR LNSQPFLQNF HDPLTRVQSY SHEEPKFHHK PPLPHLAMHL QHPTVGARSS
     CPGDYPSPPS SAHSKAPHLG RSLVATRIDS ISDSRLYDSS PSRQRKPYSR QEGMGSWDRP
     SYGMDAYGYR QTYSLPDNST QPCYEQFTFQ SLPEQQEPTW RIPYCGMPQD PPRYQDNREK
     IYINLCNIFP PDLVRIVMKR NPHMTDAQQL AAAILVEKSQ LGY
//