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Database: UniProt
Entry: A0A3Q1HB65_ANATE
LinkDB: A0A3Q1HB65_ANATE
Original site: A0A3Q1HB65_ANATE 
ID   A0A3Q1HB65_ANATE        Unreviewed;       682 AA.
AC   A0A3Q1HB65;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Terminal nucleotidyltransferase 4B {ECO:0000313|Ensembl:ENSATEP00000004605.1};
OS   Anabas testudineus (Climbing perch) (Anthias testudineus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Anabantaria; Anabantiformes; Anabantoidei; Anabantidae; Anabas.
OX   NCBI_TaxID=64144 {ECO:0000313|Ensembl:ENSATEP00000004605.1, ECO:0000313|Proteomes:UP000265040};
RN   [1] {ECO:0000313|Ensembl:ENSATEP00000004605.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   AlphaFoldDB; A0A3Q1HB65; -.
DR   STRING; 64144.ENSATEP00000004605; -.
DR   Ensembl; ENSATET00000004665.2; ENSATEP00000004605.1; ENSATEG00000003179.2.
DR   GeneTree; ENSGT00940000158301; -.
DR   InParanoid; A0A3Q1HB65; -.
DR   OMA; KGGKARM; -.
DR   OrthoDB; 21395at2759; -.
DR   Proteomes; UP000265040; 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:SF51; TERMINAL NUCLEOTIDYLTRANSFERASE 4B; 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;
KW   Reference proteome {ECO:0000313|Proteomes:UP000265040}.
FT   DOMAIN          215..312
FT                   /note="Polymerase nucleotidyl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF01909"
FT   DOMAIN          377..437
FT                   /note="PAP-associated"
FT                   /evidence="ECO:0000259|Pfam:PF03828"
FT   REGION          62..87
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          528..682
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        544..604
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        611..627
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        640..661
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        667..682
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   682 AA;  75360 MW;  8ED587E78C982CF3 CRC64;
     MDPRIAWFQP EQRGPANNLW MQIWETTQGL GYLHVNNSYT TGSQSTPSLK ASINGASGAV
     LTSRNGAPDS NTGNGKVRTQ GMSTSVGDGE ITEQRDFIPL ETNSNHNNRA AGRGGVSAGG
     QQQGNGVAVL WRGLSDGHPN KRKRDNKAST FGFNSSPMNS AIGSNTGSYD GYTGTPWKVR
     NYSEGIIGLH EEINDFYDYI SPRPEEKKMR LEVVDRIKGV INDLWPSAEV QVFGSFSTGL
     YLPTSDIDLV VFGKWETLPL WTLEEALRKR NVADENSIKV LDKATVPIIK LTDSFTEVKV
     DISFNVKSGV KAAWLIKEFK EKYPVLPYLV LVLKQFLLQR DLNEVFTGGI GSYSLFLMAV
     SFLQLHYRED VCSPNINIGV LLIEFFELYG RQFNYLKTGI RIKDGGCYVA KDEVQKNMMD
     GYRPSMLYIE DPLQPDNDVG RSSYGAMQVK QAFDYAYVVL SHAVSPIAKY YPNNESESIL
     GRIIRVTQEV DEYRQWIQKN WGSPSQNDLP LNRNDVTLFE SQQLDECNNN VPDDDDVVVV
     LPSPPCSKTS SNSSSLSPSL RSSPSSSPLS PSSTSSSSSD ADSDGTPCKT AKQQSGQGST
     DHREKSAGVS NHRTQTHTTS TPSGRSKGGK ARMSRNHTKS GHHGQQSSSS STKSHPNNKT
     HQQGNSKKRK NVRDSTREDL CR
//
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