ID A0A6G1P920_CHAAH Unreviewed; 1455 AA.
AC A0A6G1P920;
DT 12-AUG-2020, integrated into UniProtKB/TrEMBL.
DT 12-AUG-2020, sequence version 1.
DT 28-JAN-2026, entry version 20.
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=EXN66_Car002427 {ECO:0000313|EMBL:KAF3686755.1};
OS Channa argus (Northern snakehead) (Ophicephalus argus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Anabantiformes; Channoidei; Channidae; Channa.
OX NCBI_TaxID=215402 {ECO:0000313|EMBL:KAF3686755.1, ECO:0000313|Proteomes:UP000503349};
RN [1] {ECO:0000313|EMBL:KAF3686755.1, ECO:0000313|Proteomes:UP000503349}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OARG1902GOOAL {ECO:0000313|EMBL:KAF3686755.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:KAF3686755.1};
RA Zhou C., Xiao S.;
RT "Opniocepnalus argus genome.";
RL Submitted (FEB-2019) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000503349}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Zhou C., Xiao S.;
RT "Opniocepnalus argus Var Kimnra genome.";
RL Submitted (FEB-2019) to the EMBL/GenBank/DDBJ databases.
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 -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000256|ARBA:ARBA00004642}.
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DR EMBL; CM015713; KAF3686755.1; -; Genomic_DNA.
DR Proteomes; UP000503349; Chromosome 2.
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:0000278; P:mitotic cell cycle; IEA:TreeGrafter.
DR CDD; cd21993; HMG-box_WDHD1; 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; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR019775; WD40_repeat_CS.
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; PF24817; WD40_WDHD1_1st; 1.
DR SMART; SM00398; HMG; 1.
DR SMART; SM00252; SH2; 1.
DR SMART; SM00320; WD40; 5.
DR SUPFAM; SSF47095; HMG-box; 1.
DR SUPFAM; SSF55550; SH2 domain; 1.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS50118; HMG_BOX_2; 1.
DR PROSITE; PS50001; SH2; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 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};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW ProRule:PRU00267}; Reference proteome {ECO:0000313|Proteomes:UP000503349};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW SH2 domain {ECO:0000256|PROSITE-ProRule:PRU00191};
KW WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW ProRule:PRU00221}.
FT DOMAIN 256..307
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT REPEAT 323..355
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 446..480
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 556..590
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT DOMAIN 1345..1399
FT /note="HMG box"
FT /evidence="ECO:0000259|PROSITE:PS50118"
FT DNA_BIND 1345..1399
FT /note="HMG box"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00267"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 39..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 631..734
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1160..1455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..21
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 649..658
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1173..1187
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1200..1219
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1259..1271
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1282..1292
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1300..1311
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1357..1399
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1455 AA; 161431 MW; 2BE71F03A9AEF37C CRC64;
MELEEEAVMS EKKPRGSDTR PKCGLHSWIA DSYVWRGKKR SRSSCNGSSA GGLEAEGMED
QGVRSTSCPR WGRERKCSCS GIGDTLTSTE VDAVCRKALS RQSLRQKFQD AVGQCFPLRS
HHHHHHHHHH VPGSSRPFSV LFWSKRKIHV SELMQDKCPF SPKSELARCW HLIKKHAIQP
STLKDTEAPL KPNVSSFSTS PPQTPLSWED ICCSPGPGST SLDDWNPSCP HGAEGSCNNT
DYILVPDLLQ INNSPCYWGV LNRFEAEELL EGQPEGTFLL RDSAQDEFLF SVSFRRYSRS
LHARIEQNVW WFVKMPCERK PMRYGHSEGH TEVCFDETGK FIVTCGNDGD VRIWEGLDDD
DPKFITVGEK AYSLALKNGK LVTASSNNTV QIHTFPDGDP DGILTRFTTN ATHVTFNSSG
SRVAAGSSDF MVKVVEVSDS SQQKTLRGHE APVLSVTFDP KDDFLASASC DGSVVVWNIE
EQMLICFVFI QTQVISWPLL QKTNDVSNAK SLCRLAWQPR QTRFLAVPVE TKVHLYERGS
WNHVSNLTDD LLTQPINVLA WSPCGQFLAA GSVGGVLIVW DVKSKLSVER QKHEKGFTVC
GLAWHPSGSQ IAYTDIEGCL GLLDGLNPST SDTSATKAPA NKSTKDYDDL FDDDDDRLMD
EGLSDTNSPV KKPVAGHEED DDDDILMPAT GRVRNRGAIL DDENSLDTGS LKIGQDRFRD
NEEDDDDTGS TVLPAAAPLA PLRPVYEGPL PTPPQKAFQS GSTPAHLTHR FMMWNSVGIV
RCYNDEQDNA IDIEFHDTAV HHAMHLTNSL GHIIADLSQE AVLLACPSTD ELASKSFYLF
LSVFSKLQCL HFSSWDTNKE WMVDLPKGED VRVLCLGQGW AAVATSMLML RLFSIGGVQK
EIFSLPGPVV CMAGHGEQLL IVYHRATGFD GEQALGVQLL QFGQRKRKVI NGEPLPLSLK
SYLSWLGFTA EGTPCYVDSD GVVRILNRSL GNTWTPVCNT RETCKSKSDH YWVVGVHENP
QQLRCIPCKG SRYPPTLPRP AVAILPFKLP LCQTTTEKGQ MEEQFWRSVL FHNHYSFLSS
SGYEIDEDGQ NQSQKEQQEL LMKMFALSCK LEREFRCVEL AELMTQNAVT LAIRYASRSR
RMALAQRLSE IALEKANQIH VEGPDEQEEE TDYSSIRQSS GYGQSEATGG RYRNRQNQKE
EEEQEEEPED EPDGQEMETT ETRTRVNPFA KEAGSKAGCA NPFKVLGSGK PSASPGQPRM
TNILDNMTCS RKSAPVSGSA GKPNKSPALK PLAPKPKSKT QSTLLQMTGT KAPSKKTQEN
TEPAAAQQNK LDVPPPASPA DNSENKRPKT GFQLWLEENR KSIISDHPDM EETDVIKEAM
GHFRTLSPEE RLSWTERAKG QTGDAADLKK RKRAEGGGGD SENETGQSEA DENGAKKKKP
LDPSSKLSAF AFNKN
//
