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Database: UniProt
Entry: W5MLN3_LEPOC
LinkDB: W5MLN3_LEPOC
Original site: W5MLN3_LEPOC 
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
//
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