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Database: UniProt
Entry: A0A3Q3FAH2_9LABR
LinkDB: A0A3Q3FAH2_9LABR
Original site: A0A3Q3FAH2_9LABR 
ID   A0A3Q3FAH2_9LABR        Unreviewed;       923 AA.
AC   A0A3Q3FAH2;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Probable ribonuclease ZC3H12C {ECO:0000313|Ensembl:ENSLBEP00000016453.1};
OS   Labrus bergylta (ballan wrasse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Labriformes; Labridae; Labrus.
OX   NCBI_TaxID=56723 {ECO:0000313|Ensembl:ENSLBEP00000016453.1, ECO:0000313|Proteomes:UP000261660};
RN   [1] {ECO:0000313|Ensembl:ENSLBEP00000016453.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-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; A0A3Q3FAH2; -.
DR   STRING; 56723.ENSLBEP00000016453; -.
DR   Ensembl; ENSLBET00000017394.1; ENSLBEP00000016453.1; ENSLBEG00000012710.1.
DR   GeneTree; ENSGT00940000155107; -.
DR   InParanoid; A0A3Q3FAH2; -.
DR   OrthoDB; 180910at2759; -.
DR   Proteomes; UP000261660; 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:UP000261660};
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          401..434
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50103"
FT   ZN_FING         401..434
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT   REGION          52..120
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          131..150
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          453..499
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          513..551
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        52..83
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        90..108
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        136..150
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        453..482
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        516..538
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   923 AA;  102211 MW;  0A1345B3CBBA9ACA CRC64;
     MGVKNHLEDG KGHILSLGLD LDYLHVEGAE RQSSLSIVTG NIGVLQVGSG SLNNSSNSIG
     STSFSTHSNY SSSSSCSNFS EEGAVSDSED ERLQNGSGVE PQNPMQDQPS HLHHKESPSV
     SQMVRLDLAP KQSFEDPAQP ETSPTNPATD YRNKVEFALK LGYPEELVLL VLRKLGPDAL
     INDVLGELVK LGTKTTMEQQ GGSIVSQFSS SSSSLDCSSS SSNSSLDSCR QLCPSHLLED
     KENIRPVVVD GSNVAMSHGN KEVFSCQGIQ LAVDWFLERG HRDITVFVPA WRKEQSRPDA
     LITDQEILRR LEKDKVLVFT PSRRVQGRRV VCYDDRFIVK LAYESDGIIV SNDNYRDLAN
     EKPEWKKFID ERLLMYSFVN DKFMPPDDPL GRHGPSLENF LRKRPVIPEH RKQSCPYGKK
     CTYGHKCKFY HPERGTQPQR AVADELRASA KMSSVASRSL QEDSLMAKSQ SSGQQERMAE
     AEPSQNTPKK HPYPSPRFSF NDLLEDRLRI QSKAEGRRGS NCSSSSSCSS SFQGQHAPGG
     PPSSGGLERW EHSGISEGGC SRFSGASGPS FGDTHHRCES PDLGYNSLIK SYSGLSLVVP
     NSPECFFPAD LRAASLVSDC SSEGSVSSDS FSPDPLLDEC SKCHHHQQHP HHHHHCPGQY
     AHPVNRVPPG LGHHVSQGFQ VPTRRQHGFG LEDPAISVTS HASPRPFKIP SAYISSQPQH
     PLLSSFPEEF PVCPPQTSTA HSFSQSSPLR RNFMGSLWQE GGLQDSQVYK GSPIISRRNH
     LGINQQPQYQ QNWDPHYQQS PKPSFDPFTF KSIPQVQERA WHSPWERQVH STPHGLSSSS
     LPSLPLLSLP SISSHKSPLS PVPQHQEPPA LGRYQDVREK VFLNLCRIFP SDLVRMVMTR
     NPHVMDAQEL AAAILMEKSQ HCS
//
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