ID W5MLN3_LEPOC Unreviewed; 1002 AA.
AC W5MLN3;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 54.
DE SubName: Full=Helicase like transcription factor {ECO:0000313|Ensembl:ENSLOCP00000009292.1};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000009292.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000009292.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUL-2023) to UniProtKB.
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DR EMBL; AHAT01015276; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; W5MLN3; -.
DR Ensembl; ENSLOCT00000009303.1; ENSLOCP00000009292.1; ENSLOCG00000007640.1.
DR GeneTree; ENSGT00910000144305; -.
DR HOGENOM; CLU_000315_2_5_1; -.
DR Proteomes; UP000018468; Linkage group LG14.
DR Bgee; ENSLOCG00000007640; Expressed in testis and 13 other cell types or tissues.
DR GO; GO:0005634; C:nucleus; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:InterPro.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd16509; RING-HC_HLTF; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 3.30.70.2330; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR014905; HIRAN.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR45626:SF22; HELICASE-LIKE TRANSCRIPTION FACTOR; 1.
DR PANTHER; PTHR45626; TRANSCRIPTION TERMINATION FACTOR 2-RELATED; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF08797; HIRAN; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR Pfam; PF13923; zf-C3HC4_2; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00910; HIRAN; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000018468};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 474..602
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 756..797
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 829..1000
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 316..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 395..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 958..1002
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 332..357
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..417
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1002 AA; 112732 MW; 426A2C75D733ED80 CRC64;
FSTSFQKVTN WWSFQIVSLP VNWKSSHVQY CYWQGQYEKS STVPGEDDQE ALVLFGSLRG
NVVGLRYYTG VVNKREMVSL VREPQNPYDK NAVQVANVYG HQVGHIKREL AAPMAYIMDN
KLAKVEGIVP FGATNTFAMP VQLFFWGQKE NKAAVMNKLG QHGFRLGPTS EVLGFGGKSA
KASGPTIDKF FPPLRGSPAA IPLTREQLQN VFDKLFDNLM EEKIQEMEPA EAVGTPLLPH
QKQALAWMVL RENNNDLPPF WEQKNNLYFN VLTNFAVKEK PEKVHGGILA DDMGLGKTLT
TIALILSNFH NGRPLPTETL STENALAPGS SASKERKERK RTRKGTTFPE ELEKKQSKAL
EEQTSQFVRK SFLCLSLFSL SFLKRSKVKV KYTYSSDSEG SDSGVSPKKK NKSDQGEAKR
VQGGFSALKD DADFAAALEG FIAERPLQKK APKKGVPKTS FKGSRTETKI ARATLIICPL
SVLSNWMDQF EQHVRADVSL NVYLYYGSDR SRDASFLAKQ DVVLTTYNVL AVDYGNKNSS
PLHRMEWLRV VLDEGHTIRN PNALQSRAVL DLTAQRRWIL TGTPIQNSLK DVWTLIAFLK
LKPFDVKEWW NRIIQRPVTM GDKDGLQHLQ ALIKGITLRR TKASTIKGKP VVELPQRNVR
VQHVTLTEDE RRVYEAVQKE GRSIIRRYFR EGTVLTNYAD VLAILVRLRQ VCCHPGLLRN
SPGAAGPTED ATPSELREKL INKINMVLNS GSDEECAICL ESLRLPVITQ CAHVYCKPCI
CEVIRAEQQN AKCPLCRGEI KVEELVEYPG EKAELESEEA GDGFLSSSKV DALMIQLQKI
RDKDPNIKSL VVSQFTKFLS LIEIPLRERG FSFTRLDGSM NQKRRVAALQ AFQNTNPGTP
TILLLSLKAG GVGLNLTAAS RIFLMDPAWN PAAEDQCFDR CHRIGQKRDV VITKFIVKNS
VEENMIKIQK KKRDLVAKAF GLKNLNERKQ ARIEEIKTLM EI
//