ID A0A498L895_LABRO Unreviewed; 1522 AA.
AC A0A498L895;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=Nuclear factor of activated T-cells 5-like isoform X2 {ECO:0000313|EMBL:RXN03573.1};
GN ORFNames=ROHU_035789 {ECO:0000313|EMBL:RXN03573.1};
OS Labeo rohita (Indian major carp) (Cyprinus rohita).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Labeoninae; Labeonini; Labeo.
OX NCBI_TaxID=84645 {ECO:0000313|EMBL:RXN03573.1, ECO:0000313|Proteomes:UP000290572};
RN [1] {ECO:0000313|EMBL:RXN03573.1, ECO:0000313|Proteomes:UP000290572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DASCIFA01 {ECO:0000313|EMBL:RXN03573.1};
RC TISSUE=Testis {ECO:0000313|EMBL:RXN03573.1};
RA Das P., Kushwaha B., Joshi C.G., Kumar D., Nagpure N.S., Sahoo L.,
RA Das S.P., Bit A., Patnaik S., Meher P.K., Jayasankar P., Koringa P.G.,
RA Patel N.V., Hinsu A.T., Kumar R., Pandey M., Agarwal S., Srivastava S.,
RA Singh M., Iquebal M.A., Jaiswal S., Angadi U.B., Kumar N., Raza M.,
RA Shah T.M., Rai A., Jena J.K.;
RT "Draft genome sequence of Rohu Carp (Labeo rohita).";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RXN03573.1}.
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DR EMBL; QBIY01013480; RXN03573.1; -; Genomic_DNA.
DR STRING; 84645.A0A498L895; -.
DR Proteomes; UP000290572; Unassembled WGS sequence.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0004422; F:hypoxanthine phosphoribosyltransferase activity; IEA:InterPro.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0009653; P:anatomical structure morphogenesis; IEA:UniProt.
DR GO; GO:0060429; P:epithelium development; IEA:UniProt.
DR GO; GO:0006166; P:purine ribonucleoside salvage; IEA:InterPro.
DR CDD; cd06223; PRTases_typeI; 1.
DR CDD; cd07882; RHD-n_TonEBP; 1.
DR Gene3D; 3.40.50.2020; -; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 2.60.40.340; Rel homology domain (RHD), DNA-binding domain; 1.
DR InterPro; IPR005904; Hxn_phspho_trans.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR008366; NFAT.
DR InterPro; IPR015646; NFAT5_RHD_DNA-bd.
DR InterPro; IPR008967; p53-like_TF_DNA-bd_sf.
DR InterPro; IPR000836; PRibTrfase_dom.
DR InterPro; IPR029057; PRTase-like.
DR InterPro; IPR011539; RHD_DNA_bind_dom.
DR InterPro; IPR037059; RHD_DNA_bind_dom_sf.
DR NCBIfam; TIGR01203; HGPRTase; 1.
DR PANTHER; PTHR12533; NFAT; 1.
DR PANTHER; PTHR12533:SF10; NUCLEAR FACTOR OF ACTIVATED T-CELLS 5; 1.
DR Pfam; PF00156; Pribosyltran; 1.
DR Pfam; PF00554; RHD_DNA_bind; 1.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF49417; p53-like transcription factors; 1.
DR SUPFAM; SSF53271; PRTase-like; 1.
DR PROSITE; PS50254; REL_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000290572}.
FT DOMAIN 265..444
FT /note="RHD"
FT /evidence="ECO:0000259|PROSITE:PS50254"
FT REGION 40..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 88..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 132..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 611..643
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 844..876
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 895..916
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1011..1031
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1098..1188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 705..787
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 132..146
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..201
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1522 AA; 165454 MW; C236BB554E608C78 CRC64;
MEMLLLACCR ILSLLKILLF FVKSVYDLLP KELQLPSVVQ QDNPTMSQKS GGEAGPPPPA
ALASDAAATC AAASSPGGLS STLPSCPSML SATSAQEQAS RLHGGPAAEG MPERMGVEPG
SVVAISAVDT VGATQSQATP SKRRTVLSIS PPPEDLLDDS RMSCQDDLLP NQDSEQSGSM
WMDDSVSNFS MGSSNSYNDN TEVPRKSRKR TPRQRPGPKP AARDEAGMDV FDADSAKAPH
FVLSQLGSDA KVTPKVSSLE VSNNQKGGIL SIQYPQKSEG KELKILVQPE TQHRARYLTE
GSRGSVKDRT QQGFPTIKLE GVSEPVVLQV FVANDAGRVK PHGFYQACRV TGRNTTACKE
VDIEGTTVIE VNLEPTNSMT LAVDCVGILK LRNADVEARI GVAGSKKKST RARLAFRVNI
PRADGSVLTL QALSSPILCT QPAGVPEILK KSLHSCTVAG GEEVFIIGKN FLKGTKVLFQ
ENSTAMQTET SCLNNVLMLP MVKREEPMEV SCNAAPSDIF KPVEALSSTQ QILEISTVLP
SATKSFPSPV ALQSVDSQQP SAQIFTTQET LSTIQKQDIP SPASFQVSLS EDTTVLQPVP
PQVPQQFLRE TPETLSPEDS SADGSGMVLV GIDSRNPPSQ RPQVQALLPQ DGVAQLERAV
RELQAQQQLN SVLYSPTPSA ESLQQHVQEN MNSLRLGGNE TTLTNQQQQQ QEQNILENLQ
QQQQKALVDL QHQQTVLENL QQHQKVLENL QQQALGNIQQ QQTHKVLENL QHQQQHHQKV
LENIQQQSSI VTLQHQKVLD NLQQQQQHQQ HLETLQHQEV LENLKQQLES ELLQTQIPMQ
CTPSFASEQQ SSTQTNTLSQ PSEGFLQNPP QQQLQQQTAL FQQTGGLMTI QTSSFLQQPP
SQPSPPQPLF QGHNPLTETQ DSQTVLFGTT KPPQVQATLF PGTMTMLTST NLPTDQQAPS
ASLFIAQSVL PSQLSSDSNQ NQQQQQIAFL TPMQTSGTEA QTVSLFQGQA QLSTPMEQQQ
SPQQQQMATP QQAPLFPNIA TISPNQAQQQ PQTGILFCTT TINPHDLPQA LLFSGQNQAP
LGSDRLPENI FQEQQPMQVV PSSENVTVNN PSNQPTASAA QPTPNPSIIF PQASVAQQDS
AEPMSFQDQS TVVSDSSASM PSTRTELFQD QQPMQVVPSA TSVTPVSPTD QPSVNIFLPQ
SAISALQGGV GAQELPPTAT AATIFSGQSG VAVGGLQNTS SSAPQQPPSQ LFQTAIGGNL
SQPGQPGQAG IFLFEIPSVL YFICQYSERW NDGFCPPSLC YKMEIVICLI ADDSKGHELS
LFCVPKHYEE DLDSVIIPNG LIKDRTERLA RDIVRDMGGH HIVALCVLKG GYKFFADLMD
YIKTLNQNSD KSVPLTVDFI RLKSYSNDQS TNCVKVIGGD ELSALAGKNV LIVEDIVETG
KTMETLLKLL NECHPKMVKV VSLLVKRTPR SSGYRPDYIG FEVPDKFLVG YALDYNEYFR
DLSVSVSSCS VLFCSYLIVC NA
//
