ID A0A3B4WLL2_SERLL Unreviewed; 543 AA.
AC A0A3B4WLL2;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Terminal nucleotidyltransferase 4A {ECO:0000313|Ensembl:ENSSLDP00000005524.1};
GN Name=TENT4A {ECO:0000313|Ensembl:ENSSLDP00000005524.1};
OS Seriola lalandi dorsalis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Carangidae; Seriola.
OX NCBI_TaxID=1841481 {ECO:0000313|Ensembl:ENSSLDP00000005524.1, ECO:0000313|Proteomes:UP000261360};
RN [1] {ECO:0000313|Ensembl:ENSSLDP00000005524.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; A0A3B4WLL2; -.
DR STRING; 1841481.ENSSLDP00000005524; -.
DR Ensembl; ENSSLDT00000005705.1; ENSSLDP00000005524.1; ENSSLDG00000004371.1.
DR GeneTree; ENSGT00940000157811; -.
DR Proteomes; UP000261360; Unplaced.
DR GO; GO:1990817; F:poly(A) RNA polymerase activity; IEA:InterPro.
DR GO; GO:0016070; P:RNA metabolic process; IEA:UniProt.
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 InterPro; IPR043519; NT_sf.
DR InterPro; IPR002058; PAP_assoc.
DR InterPro; IPR002934; Polymerase_NTP_transf_dom.
DR InterPro; IPR045862; Trf4-like.
DR PANTHER; PTHR23092; POLY(A) RNA POLYMERASE; 1.
DR PANTHER; PTHR23092:SF24; TERMINAL NUCLEOTIDYLTRANSFERASE 4A; 1.
DR Pfam; PF01909; NTP_transf_2; 1.
DR Pfam; PF03828; PAP_assoc; 1.
DR SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR SUPFAM; SSF81631; PAP/OAS1 substrate-binding domain; 1.
PE 4: Predicted;
FT DOMAIN 77..170
FT /note="Polymerase nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF01909"
FT DOMAIN 240..299
FT /note="PAP-associated"
FT /evidence="ECO:0000259|Pfam:PF03828"
FT REGION 368..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 462..543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..430
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 462..483
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 518..532
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 543 AA; 61253 MW; 9D8E0B9853863892 CRC64;
HTHNHHPGRR KSDNKASTYG MNYLLSNCTN GNYASTWTPW KTRKYNPGVM LHEEVMDFYN
FMSPRPEEAA MRKEVVNRIE MIIKELWPTA DVQIFGSFST GLYLPTDIDL VVFGKWERPP
LQELEQALRK HNVAEPFSIK VLDKATVPII KLTDQETEVK VDISFNVETG VKAASFIKDY
VKQKYPVLPY LIFVLKQFLL QRDLNEVFTG GISSYSLILM VISFLQQLHP RIDARNPNEN
LGVLLIEFFE LYGRHFNYLK TGIRIKNGGA YIAKEEIMKA MTNGYRPSML CIEDPLLPND
VGRGSYGAMH VKQVFDYAYT VLSHAVSPLA RSYPNKDCET LGRIIRLTQE VIDYREWIIK
KWGGRDLTRT DNRVSPPKEP VSEQDPSCVL RGGVGSEEQQ RDSVSPHSAD SPMSISSPQQ
HSSASSVSSL SARVSLPGGL AMHSIPGRQV CIDTGLPPFF HMPPPAHAHA PAPSSPQPPP
SPHSSHTHKN GTKFNVKGFH NPPLVNGPAL ANRGHTHAHT HTQYHRNTWR RRKRDSLPVS
LSR
//