ID   A0A3B3C820_ORYME        Unreviewed;       627 AA.
AC   A0A3B3C820;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=CCHC-type domain-containing protein {ECO:0000259|PROSITE:PS50158};
OS   Oryzias melastigma (Marine medaka).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC   Oryzias.
OX   NCBI_TaxID=30732 {ECO:0000313|Ensembl:ENSOMEP00000014076.1, ECO:0000313|Proteomes:UP000261560};
RN   [1] {ECO:0000313|Ensembl:ENSOMEP00000014076.1}
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   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
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DR   AlphaFoldDB; A0A3B3C820; -.
DR   STRING; 30732.ENSOMEP00000014076; -.
DR   PaxDb; 30732-ENSOMEP00000014076; -.
DR   Ensembl; ENSOMET00000021880.1; ENSOMEP00000014076.1; ENSOMEG00000015574.1.
DR   GeneTree; ENSGT00940000156988; -.
DR   OMA; ARNYNHQ; -.
DR   Proteomes; UP000261560; Unplaced.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0016779; F:nucleotidyltransferase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd05402; NT_PAP_TUTase; 1.
DR   Gene3D; 1.10.1410.10; -; 1.
DR   Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR   Gene3D; 4.10.60.10; Zinc finger, CCHC-type; 1.
DR   InterPro; IPR043519; NT_sf.
DR   InterPro; IPR002058; PAP_assoc.
DR   InterPro; IPR002934; Polymerase_NTP_transf_dom.
DR   InterPro; IPR001878; Znf_CCHC.
DR   InterPro; IPR036875; Znf_CCHC_sf.
DR   PANTHER; PTHR12271; POLY A POLYMERASE CID PAP -RELATED; 1.
DR   PANTHER; PTHR12271:SF49; TERMINAL URIDYLYLTRANSFERASE 4; 1.
DR   Pfam; PF01909; NTP_transf_2; 1.
DR   Pfam; PF03828; PAP_assoc; 1.
DR   Pfam; PF00098; zf-CCHC; 2.
DR   SMART; SM00343; ZnF_C2HC; 2.
DR   SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR   SUPFAM; SSF81631; PAP/OAS1 substrate-binding domain; 1.
DR   SUPFAM; SSF57756; Retrovirus zinc finger-like domains; 2.
DR   PROSITE; PS50158; ZF_CCHC; 2.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00047};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00047};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00047}.
FT   DOMAIN          295..310
FT                   /note="CCHC-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50158"
FT   DOMAIN          335..352
FT                   /note="CCHC-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50158"
FT   REGION          312..341
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          375..453
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          473..505
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          528..560
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        313..341
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        393..433
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        539..560
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   627 AA;  69925 MW;  A2113DC48A5EE4B9 CRC64;
     EKAQLCLFGS SKNGFGFRDS DLDICMTLEG HDSAEKLNGK EIIEGLAKVL KKHAGLRNIL
     PITTAKVPIV KFEHRQSGLE GDISLYNTLA QHNTRMLATY AALDPRVQFL GYTMKVFAKR
     CDIGDASRGS LSSYAYILMV LYFLQQRQPP VIPVLQEIFD GSTVPQRMVD GWNAFFFDDI
     LDLRQRLAGR QLNRESVGEL WLGLLRFYTE EFDFKEHVIS IRQRKRLTTF EKQWTSKCIA
     IEGDFIMTNF IMKAFINGRK LFGTPFYPLP GTEVDYFFDS KVLTDGELAP NDRCCRICGK
     IGHYMKDCPK RRRMKKKEND KDEDVKEEER EPKDRRCFQC GDPGHVRRDC PEYRHLKQRN
     AGAPVPHMVR PMVSSQSIPV PQTGVDGPGR TRQPSECSDS RQTPPYSPQP GSAPQSSSQP
     SGSPQSSHSK ISGGLPKQPA HPQVPFSLFS FPSSSPGQYH PGALTALGLL PHPQHQSHQS
     QGLKFAMRSA AGSAGSGGNP TPMNLNDPSI IFAQPAGRQG HWRNHMAQPG ALMGNGTVGK
     SESGHQAQPS SVSQGSRLWD HNKAPQYTLS PSWPYRMPQS FIQQGNGGFQ PGKPFIAPGS
     VVHPNPNFPL VPHVRHQVNL NFIQQKK
//