ID   A0A2K6TE54_SAIBB        Unreviewed;       883 AA.
AC   A0A2K6TE54;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=Zinc finger CCCH-type containing 12C {ECO:0000313|Ensembl:ENSSBOP00000017916.1};
GN   Name=ZC3H12C {ECO:0000313|Ensembl:ENSSBOP00000017916.1};
OS   Saimiri boliviensis boliviensis (Bolivian squirrel monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC   Saimiriinae; Saimiri.
OX   NCBI_TaxID=39432 {ECO:0000313|Ensembl:ENSSBOP00000017916.1, ECO:0000313|Proteomes:UP000233220};
RN   [1] {ECO:0000313|Ensembl:ENSSBOP00000017916.1}
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; A0A2K6TE54; -.
DR   Ensembl; ENSSBOT00000034731.1; ENSSBOP00000017916.1; ENSSBOG00000025582.1.
DR   GeneTree; ENSGT00940000158397; -.
DR   Proteomes; UP000233220; 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:UP000233220};
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          69..101
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          456..545
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        69..85
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        87..101
FT                   /note="Polar 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..545
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;  99330 MW;  723881017DC011AB CRC64;
     QPASGCQEYG VLCIQEYRKN SKVESSTRNS FMGLKDHLGH DLSHLYVESS DPQLSAAVPW
     SAVEKPTMDT VHAGKDEKEV SEENASSGDS EENTNSDHES VQLGSISVEP GLLTKTHRQL
     CRSPCLEPHI LKRNEILQDF KPDESQTTSK EAKKPPDVVR EYQTKLEFAL KLGYSEEQVQ
     LVLNKLGTDA LINDILGELV KLGNKSEADQ TVSTINTVTR ETSSLESQRS ESPMQEIVTD
     DGENLRPVVI DGSNVAMSHG NKEVFSCRGI KLAVDWFLER GHKDITVFVP AWRKEQSRPD
     ALITDQEILR KLEKEKILVF TPSRRVQGRR VVCYDDRFIV KLAFESDGII VSNDNYRDLA
     NEKPEWKKFI DERLLMYSFV NDKFMPPDDP LGRHGPSLDN FLRKKPIVPE HKKQPCPYGK
     KCTYGHKCKY YHPERGSQPQ RSVADELRAM SRNTAAKTAN EGGLVKSNSV PCSTKADSTS
     DVKRGAPKRQ SDPSIRTQVY QDLEEKLPTK NKLETRSVPS LVSIPATSAA KPQSTTSLSN
     GLPSGVHFPP QDQRPQGQYP PMIMATKNHG TPMPYEQYPK CDSPVDIGYY SMLNAYSNLS
     LSGPRSPERR FSLDTDYRIS SVASDCSSEG SMSCGSSDSY VGYNDRSYVS SPDPQLEENL
     KCQHMHPHSR LNSQPFLQNF HDPLTRVQSY SHEEPKFHHK PPLPHLALHL QHPAVGARSS
     CPGDYPSPPS SAHSKAPHLG RSLVATRIDS ISDSRLYDSS PSRQRKPYSR QEGLGSWERP
     GYGIDAYGYR QTYSLPDNST QPCYEQFTFQ SLPEQQDPAW RIPYCGMPQD PPRYQDNREK
     IYINLCNIFP PDLVRIVMKR NPHMTDAQQL AAAILVEKSQ LGY
//