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Database: UniProt
Entry: A0A8T2N8P3_9TELE
LinkDB: A0A8T2N8P3_9TELE
Original site: A0A8T2N8P3_9TELE 
ID   A0A8T2N8P3_9TELE        Unreviewed;      1400 AA.
AC   A0A8T2N8P3;
DT   12-OCT-2022, integrated into UniProtKB/TrEMBL.
DT   12-OCT-2022, sequence version 1.
DT   28-JAN-2026, entry version 14.
DE   RecName: Full=WD repeat and HMG-box DNA-binding protein 1 {ECO:0000256|ARBA:ARBA00069769};
DE   AltName: Full=Acidic nucleoplasmic DNA-binding protein 1 {ECO:0000256|ARBA:ARBA00080131};
GN   ORFNames=JZ751_003057 {ECO:0000313|EMBL:KAG9336709.1};
OS   Albula glossodonta (roundjaw bonefish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Albuliformes; Albulidae; Albula.
OX   NCBI_TaxID=121402 {ECO:0000313|EMBL:KAG9336709.1, ECO:0000313|Proteomes:UP000824540};
RN   [1] {ECO:0000313|EMBL:KAG9336709.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=HI-2016 {ECO:0000313|EMBL:KAG9336709.1};
RA   Pickett B.D.;
RT   "Applications of and Algorithms for Genome Assembly and Genomic Analyses
RT   with an Emphasis on Marine Teleosts.";
RL   Thesis (2021), BYU ScholarsArchive, Provo, UT, USA.
CC   -!- FUNCTION: Core replisome component that acts as a replication
CC       initiation factor. Binds directly to the CMG complex and functions as a
CC       hub to recruit additional proteins to the replication fork.
CC       {ECO:0000256|ARBA:ARBA00056293}.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC       {ECO:0000256|ARBA:ARBA00004642}.
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:KAG9336709.1}.
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DR   EMBL; JAFBMS010000102; KAG9336709.1; -; Genomic_DNA.
DR   OrthoDB; 427368at2759; -.
DR   Proteomes; UP000824540; Unassembled WGS sequence.
DR   GO; GO:0043596; C:nuclear replication fork; IEA:TreeGrafter.
DR   GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003682; F:chromatin binding; IEA:TreeGrafter.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006281; P:DNA repair; IEA:TreeGrafter.
DR   GO; GO:0006261; P:DNA-templated DNA replication; IEA:InterPro.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   GO; GO:0000278; P:mitotic cell cycle; IEA:TreeGrafter.
DR   GO; GO:0009968; P:negative regulation of signal transduction; IEA:UniProtKB-KW.
DR   CDD; cd21993; HMG-box_WDHD1; 1.
DR   CDD; cd00200; WD40; 1.
DR   FunFam; 1.10.750.20:FF:000002; Suppressor of cytokine signaling 2; 1.
DR   FunFam; 1.10.30.10:FF:000028; WD repeat and HMG-box DNA-binding protein 1; 1.
DR   FunFam; 2.130.10.10:FF:001715; WD repeat and HMG-box DNA-binding protein 1; 1.
DR   Gene3D; 1.10.30.10; High mobility group box domain; 1.
DR   Gene3D; 3.30.505.10; SH2 domain; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR   InterPro; IPR055339; HMG-box_WDHD1.
DR   InterPro; IPR009071; HMG_box_dom.
DR   InterPro; IPR036910; HMG_box_dom_sf.
DR   InterPro; IPR000980; SH2.
DR   InterPro; IPR036860; SH2_dom_sf.
DR   InterPro; IPR022252; SOCS4/SOCS5_dom.
DR   InterPro; IPR001496; SOCS_box.
DR   InterPro; IPR036036; SOCS_box-like_dom_sf.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   InterPro; IPR001680; WD40_rpt.
DR   InterPro; IPR057646; WD40_WDHD1_1st.
DR   InterPro; IPR022100; WDHD1/CFT4_beta-prop_2nd.
DR   InterPro; IPR048591; WDHD1/CFT4_hel.
DR   PANTHER; PTHR19932; WD REPEAT AND HMG-BOX DNA BINDING PROTEIN; 1.
DR   PANTHER; PTHR19932:SF10; WD REPEAT AND HMG-BOX DNA-BINDING PROTEIN 1; 1.
DR   Pfam; PF20946; Ctf4_C; 1.
DR   Pfam; PF24815; HMG_WDHD1; 1.
DR   Pfam; PF12341; Mcl1_mid; 1.
DR   Pfam; PF00017; SH2; 1.
DR   Pfam; PF12610; SOCS; 1.
DR   Pfam; PF07525; SOCS_box; 1.
DR   Pfam; PF24817; WD40_WDHD1_1st; 1.
DR   SMART; SM00398; HMG; 1.
DR   SMART; SM00252; SH2; 1.
DR   SMART; SM00253; SOCS; 1.
DR   SMART; SM00969; SOCS_box; 1.
DR   SMART; SM00320; WD40; 5.
DR   SUPFAM; SSF47095; HMG-box; 1.
DR   SUPFAM; SSF55550; SH2 domain; 1.
DR   SUPFAM; SSF158235; SOCS box-like; 1.
DR   SUPFAM; SSF50978; WD40 repeat-like; 1.
DR   PROSITE; PS50118; HMG_BOX_2; 1.
DR   PROSITE; PS50001; SH2; 1.
DR   PROSITE; PS50225; SOCS; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 3.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE   4: Predicted;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PROSITE-
KW   ProRule:PRU00267}; Growth regulation {ECO:0000256|ARBA:ARBA00022604};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW   ProRule:PRU00267}; Reference proteome {ECO:0000313|Proteomes:UP000824540};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   SH2 domain {ECO:0000256|ARBA:ARBA00022999, ECO:0000256|PROSITE-
KW   ProRule:PRU00191};
KW   Signal transduction inhibitor {ECO:0000256|ARBA:ARBA00022700};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW   WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW   ProRule:PRU00221}.
FT   DOMAIN          252..347
FT                   /note="SH2"
FT                   /evidence="ECO:0000259|PROSITE:PS50001"
FT   DOMAIN          342..391
FT                   /note="SOCS box"
FT                   /evidence="ECO:0000259|PROSITE:PS50225"
FT   REPEAT          406..438
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   REPEAT          529..570
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   REPEAT          630..664
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   DOMAIN          1291..1359
FT                   /note="HMG box"
FT                   /evidence="ECO:0000259|PROSITE:PS50118"
FT   DNA_BIND        1291..1359
FT                   /note="HMG box"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00267"
FT   REGION          1..65
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          208..230
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1132..1300
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1333..1385
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        7..20
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1153..1163
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1173..1184
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1198..1215
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1260..1276
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1333..1345
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1400 AA;  155015 MW;  C85EB9644513FFE3 CRC64;
     MNSGKAEMSE KKSRNSDTRP KCIRSWSADS YAWSNKKRSR SAHNEMGVSS TEGEGSEDQA
     GRSASCPRRR RERKCSCATL GEGDTELPCR KALTRRSLRQ KFQDAVGQCF PLRTHHHHHH
     HHHHHHQAGA SRPFSVLLWS KRKIHVSELM QDKCPFSPKS ELAHCWHLIK KHVSQSGNSI
     SVAAEHKGSS CPSSSFSSTP PLISWEEISS GGTQGGSLDD WDPSRPGERA QGCSHTDYIL
     VPDLLQINNS PCYWGVLDRF EAEELLEGQP EGTFLLRDSA QDEFLFSVSF RRYSRSLHAR
     IEQNGKRFSF DGRDPCVYRD PSVTGLLKHY SDPATCLFFE PLLSRPLPRN FPFSLQHLCR
     AVICSCTTYQ GIEALPLPHP LRDYLRQYHY KCNGACKMPA ERKPMRYGHS EGHTDVCFDD
     TGKYIVTSGS DGDVRIWESL DDDDPKSINV GEKVHSLALM SGKLVTAVSN NTVQIHTFPE
     GDPDGILTRF TTNANHVTFN SIGSRVAAGS SDFMVKVVEV SDSSQQKTLR GHDGPVLSVA
     FDPNDEFLGS SSCDGTVAVW KIEDQVQVSN WKILQKSNDI SNAKSLCRLA WQPGRAKLLA
     VPLDTTVQLY ERDSWNHVGT LSDDFITHPV NVVTWSPCGK FLAAGTIGGF LTVWDVETKL
     CVEREKHEKG YTVCGLAWHP SGGQIAYTDT EGCLGLLDGV SASSSSSAST KSSNKVNVAS
     VKLGSDKFGD DDGGSTILPA VTPAVPRPIY EGPMPTPPQK PFQPGSTPSH LMHRFMVWNS
     VGIVRGYNDE QDNAIDVEFH DTAVHHAMHL TNSLGHSLAD LSQEAVLLAC EATDELASKL
     QCLHFSSWDT NKEWMVDLPK GEEVKALCLG QGWAAAATST QLVRVFSIGG VQREVFCLPG
     PVVCMAGHGE QIVIVYHRGT GFDGEQALGI QLLNFGLKKR QVIHGEPLSL SKKSYLSWLG
     FTAEGTPCFV DSEGVVRMLN RSLGNTWTPV CNTRENCKGK SDHNWVVGVH ENPQQLRCIP
     CKGSRFPPTL PRPAVTILPF KLPLCQTTTE KGQMEEQYWR SVLFHNHFDF LSSSGYEIDE
     EAKNQAQKEQ QELLMKMFAR LSELALEKAA IEQRGEEQEE EELEYASAMR ASGYSRAAGE
     RGESRQWSLR ESQEEEACEE EDGQQQMDTV EAVESRKASS KEGRVNPFKV SGTGKPNGLS
     SGQPRVSNVL DTMTASGRKP SLMGNSGAKQ SKGPVLKPLV PRPKSKATLL QMGSSRVASK
     RQEEREPAPQ PERQRNTDGG SPAPLSDNSE NRKPKTGFQL WLEENRKSIL ADNPDLDETD
     VVKEAMGRFR ALSAEDRLTW TDRAKGGQLP EVADLKKRKR EDDESEEGAN NGQNERENSL
     KKKKPLDATA KLSAFAFNKD
//
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