ID A0A3B3U1Q0_9TELE Unreviewed; 653 AA.
AC A0A3B3U1Q0;
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 Poecilia latipinna (sailfin molly).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48699 {ECO:0000313|Ensembl:ENSPLAP00000006526.1, ECO:0000313|Proteomes:UP000261500};
RN [1] {ECO:0000313|Ensembl:ENSPLAP00000006526.1}
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; A0A3B3U1Q0; -.
DR STRING; 48699.ENSPLAP00000006526; -.
DR Ensembl; ENSPLAT00000006100.1; ENSPLAP00000006526.1; ENSPLAG00000008701.1.
DR GeneTree; ENSGT00940000156988; -.
DR Proteomes; UP000261500; 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 307..322
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT DOMAIN 347..364
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT REGION 324..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 390..447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..349
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..418
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 426..444
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 653 AA; 72071 MW; 492298279362C84E CRC64;
DKAQLCLFGS SKNGFGFRDS DLDICMTLEG HETAEKLNCK EIIEGLAKVL KKHAGLRNIL
PITTAKVPIV KFEHRQSGLE GDISLYNTLA QHNTRMLATY AALDPRVQFL GYTIKVFAKR
CDIGDASRGS LSSYAYILMV LYFLQQRQPP VIPVLQEIFD GQTVPQRMVD GWNAFFCDDL
DKLRQRLADR QPNTESVGEL WLGLLRFYTE EFDFKEHVIS IRQHKRLTTF EKQWTSKCIA
IEDPFDLNHN LGAGVSRKMT NFIMKAFING RKLFGTPFIP IPGTEVEYFF DSKVLTDGEL
APNDRCCRIC GKIGHYMKDC PKRRRVKKKE NEKDEDSKED EREPKDRRCF QCGDMGHVRR
DCPENRHLKQ RNAAAPTPLM VRSVANSQSI PIPPAAADSP GRTRQPSECS DSRQTPPYSP
QPAAVPHGSP LSSGSPQTSH SKPGCVGPPQ VPLSLFSFPS SHPGQFHPAA LGALGLLPSH
QSHIASSSWP IHGPVLASSS AGGPSPPGLT FALRSVSANG SPTGTGGGGS VNLNDPSIIF
AQPAAGRQMG MAAAGRDGQW HNHMAQPGSL MGNGTVVKSE PGHQVQFEGV SQGSRLWEHN
KPPQFSLSPS WPYRMPQNFI QQGNGSVVHP NPNFPLVPHV RHPVNMNYIQ QKK
//
