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Database: UniProt
Entry: F6TIA5_MONDO
LinkDB: F6TIA5_MONDO
Original site: F6TIA5_MONDO 
ID   F6TIA5_MONDO            Unreviewed;      1014 AA.
AC   F6TIA5;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 2.
DT   27-MAR-2024, entry version 86.
DE   SubName: Full=Helicase like transcription factor {ECO:0000313|Ensembl:ENSMODP00000026570.3};
GN   Name=HLTF {ECO:0000313|Ensembl:ENSMODP00000026570.3};
OS   Monodelphis domestica (Gray short-tailed opossum).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Metatheria; Didelphimorphia; Didelphidae; Monodelphis.
OX   NCBI_TaxID=13616 {ECO:0000313|Ensembl:ENSMODP00000026570.3, ECO:0000313|Proteomes:UP000002280};
RN   [1] {ECO:0000313|Ensembl:ENSMODP00000026570.3, ECO:0000313|Proteomes:UP000002280}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17495919; DOI=10.1038/nature05805;
RA   Mikkelsen T.S., Wakefield M.J., Aken B., Amemiya C.T., Chang J.L., Duke S.,
RA   Garber M., Gentles A.J., Goodstadt L., Heger A., Jurka J., Kamal M.,
RA   Mauceli E., Searle S.M., Sharpe T., Baker M.L., Batzer M.A., Benos P.V.,
RA   Belov K., Clamp M., Cook A., Cuff J., Das R., Davidow L., Deakin J.E.,
RA   Fazzari M.J., Glass J.L., Grabherr M., Greally J.M., Gu W., Hore T.A.,
RA   Huttley G.A., Kleber M., Jirtle R.L., Koina E., Lee J.T., Mahony S.,
RA   Marra M.A., Miller R.D., Nicholls R.D., Oda M., Papenfuss A.T., Parra Z.E.,
RA   Pollock D.D., Ray D.A., Schein J.E., Speed T.P., Thompson K.,
RA   VandeBerg J.L., Wade C.M., Walker J.A., Waters P.D., Webber C.,
RA   Weidman J.R., Xie X., Zody M.C., Baldwin J., Abdouelleil A., Abdulkadir J.,
RA   Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., An P.,
RA   Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A.,
RA   Bayul T., Berlin A., Bessette D., Bloom T., Bloom T., Boguslavskiy L.,
RA   Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S.,
RA   Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M.,
RA   D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K.,
RA   Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J.,
RA   Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A.,
RA   Friedrich D., Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T.,
RA   Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B.,
RA   Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L.,
RA   Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D.,
RA   Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., LeVine R.,
RA   Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y.,
RA   Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C.,
RA   McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O.,
RA   Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L.,
RA   Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C.,
RA   Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L.,
RA   Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F.,
RA   Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T.,
RA   Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J.,
RA   Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S.,
RA   Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I.,
RA   Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M.,
RA   Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D.,
RA   Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J.,
RA   Chin C., Gnerre S., MacCallum I., Graves J.A., Ponting C.P., Breen M.,
RA   Samollow P.B., Lander E.S., Lindblad-Toh K.;
RT   "Genome of the marsupial Monodelphis domestica reveals innovation in non-
RT   coding sequences.";
RL   Nature 447:167-177(2007).
RN   [2] {ECO:0000313|Ensembl:ENSMODP00000026570.3}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   RefSeq; XP_007502123.1; XM_007502061.2.
DR   RefSeq; XP_007502124.1; XM_007502062.2.
DR   RefSeq; XP_007502125.1; XM_007502063.2.
DR   RefSeq; XP_016280727.1; XM_016425241.1.
DR   RefSeq; XP_016280728.1; XM_016425242.1.
DR   AlphaFoldDB; F6TIA5; -.
DR   STRING; 13616.ENSMODP00000026570; -.
DR   Ensembl; ENSMODT00000027046.4; ENSMODP00000026570.3; ENSMODG00000021258.4.
DR   GeneID; 100617443; -.
DR   KEGG; mdo:100617443; -.
DR   CTD; 6596; -.
DR   eggNOG; KOG1001; Eukaryota.
DR   GeneTree; ENSGT00910000144305; -.
DR   HOGENOM; CLU_000315_2_5_1; -.
DR   InParanoid; F6TIA5; -.
DR   OMA; ETTVWRL; -.
DR   OrthoDB; 200191at2759; -.
DR   TreeFam; TF332703; -.
DR   Proteomes; UP000002280; Chromosome 7.
DR   Bgee; ENSMODG00000021258; Expressed in spermatid and 21 other cell types or tissues.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IEA:Ensembl.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IBA:GO_Central.
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:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR   GO; GO:0042789; P:mRNA transcription by RNA polymerase II; IEA:Ensembl.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR   GO; GO:0050767; P:regulation of neurogenesis; IEA:Ensembl.
DR   CDD; cd18071; DEXHc_HLTF1_SMARC3; 1.
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; IPR049730; SNF2/RAD54-like_C.
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:SF17; 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   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002280};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          483..611
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          765..806
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          842..1001
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          344..409
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        344..365
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        367..387
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        388..409
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1014 AA;  114718 MW;  A1F2F26322097883 CRC64;
     MSWMFRRTDA PQVFFKVDPL WKYLQSFQYG VHGTFSHCTY PNLFSPFEPE DVIPPDDFVA
     GDEDLDSVLF GTLRGHVVGL RYYTGVVNNN EMVALQREPN NPYDKNAVKV NNVNGNQVGH
     IKKELAAPLA YIMDNKLAQV EGVVHYGASN AFTMPVQMSF WGKEENRKAV LDQLKKHGFK
     LGPPPKSSGF NFNSSWSSER AGPSYSVPVH AAVQMTTEQL KTEFDKLFED LKEDDKTREM
     EPAEAIETPL LPHQKQALAW MVSRENSKEL PPFWEQRNNS YYNTITNFSE KEPPENVLGG
     ILADDMGLGK TLAAIAVILT NFYDGNPLPV EKIKQLKEEH IIDRSAKQEE NDDSEQVKEP
     CKEGCTSNEE PSVSNVKEKS TDFMSEFTST RPKRRKATVK YTESSDSEDL ELNELPHKIK
     ARPRQEQPMT KGRIKRSSKA KEDADFECAL ESSAPLKKKA MKKGATLVQC SKKIDTAEKP
     RATLIICPLS VLSNWIDQFG QHIKSDVHLN LYVYYGPDRS KDPALLSKQD IVLTTYNILT
     YDYGSRGDSP LHKIRWLRVI LDEGHTIRNP NAQQTKAALD LEAERRWVLT GTPIQNSLKD
     LWSLLSFLKL KPFTDREWWH RTIQRPVTMG DEGGLRRLQS LIKNITLRRT KTSKIKGKPV
     LELPERKVFI QHITLTDEER QIYQSVKNEG RAAIGRYFNE GTVLAHYADV LGLLLRLRQL
     CCHPHLFTNT SSSSGPSGDD TPEELRKKLI SKMKLILSSG SDEECAICLD SLHIPVITHC
     AHVFCKPCIC QVIRSEQPNA KCPLCRNDLR AENLVECPPE ELNCNTEKKT DLEWMSSSKI
     NALMHALIEL RKKNPQIKSL VVSQFTTFLS LLETPLKASG FVFTRLDGSM AQKKRVESIQ
     CFQKTEAGSP TIMLLSLKAG GVGLNLCAAS RVFLMDPAWN PAAEDQCFDR CHRLGQKQEV
     VITKFIVKDS VEENMLKIQN KKRELAAGAF GTKKPNASEM KQAKINEIKT LIDL
//
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