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Database: UniProt
Entry: A0A151NAY5_ALLMI
LinkDB: A0A151NAY5_ALLMI
Original site: A0A151NAY5_ALLMI 
ID   A0A151NAY5_ALLMI        Unreviewed;       990 AA.
AC   A0A151NAY5;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Helicase-like transcription factor {ECO:0000313|EMBL:KYO33941.1};
GN   Name=HLTF {ECO:0000313|EMBL:KYO33941.1};
GN   ORFNames=Y1Q_0024550 {ECO:0000313|EMBL:KYO33941.1};
OS   Alligator mississippiensis (American alligator).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC   Alligator.
OX   NCBI_TaxID=8496 {ECO:0000313|EMBL:KYO33941.1};
RN   [1] {ECO:0000313|EMBL:KYO33941.1, ECO:0000313|Proteomes:UP000050525}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KSC_2009_1 {ECO:0000313|EMBL:KYO33941.1};
RX   PubMed=22293439; DOI=10.1186/gb-2012-13-1-415;
RA   St John J.A., Braun E.L., Isberg S.R., Miles L.G., Chong A.Y., Gongora J.,
RA   Dalzell P., Moran C., Bed'hom B., Abzhanov A., Burgess S.C., Cooksey A.M.,
RA   Castoe T.A., Crawford N.G., Densmore L.D., Drew J.C., Edwards S.V.,
RA   Faircloth B.C., Fujita M.K., Greenwold M.J., Hoffmann F.G., Howard J.M.,
RA   Iguchi T., Janes D.E., Khan S.Y., Kohno S., de Koning A.J., Lance S.L.,
RA   McCarthy F.M., McCormack J.E., Merchant M.E., Peterson D.G., Pollock D.D.,
RA   Pourmand N., Raney B.J., Roessler K.A., Sanford J.R., Sawyer R.H.,
RA   Schmidt C.J., Triplett E.W., Tuberville T.D., Venegas-Anaya M.,
RA   Howard J.T., Jarvis E.D., Guillette L.J.Jr., Glenn T.C., Green R.E.,
RA   Ray D.A.;
RT   "Sequencing three crocodilian genomes to illuminate the evolution of
RT   archosaurs and amniotes.";
RL   Genome Biol. 13:415-415(2012).
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:KYO33941.1}.
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DR   EMBL; AKHW03003627; KYO33941.1; -; Genomic_DNA.
DR   RefSeq; XP_014458311.1; XM_014602825.2.
DR   AlphaFoldDB; A0A151NAY5; -.
DR   STRING; 8496.A0A151NAY5; -.
DR   GeneID; 102570682; -.
DR   KEGG; amj:102570682; -.
DR   CTD; 6596; -.
DR   eggNOG; KOG1001; Eukaryota.
DR   OrthoDB; 200191at2759; -.
DR   PhylomeDB; A0A151NAY5; -.
DR   Proteomes; UP000050525; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProt.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
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; 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   Helicase {ECO:0000313|EMBL:KYO33941.1};
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:UP000050525};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          404..587
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          741..782
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          818..990
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          348..411
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          430..450
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        348..368
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        372..411
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   990 AA;  111011 MW;  74048CA7F745A96A CRC64;
     MFAKNYGSST GYGGNRTYSC SSSGDVDSAL GFEDFLYTDD TSGTDEDLDL FVLFGNLRGN
     VVGLRYYTGV VNNNEMVALQ REPNNPYDKN AVKVNNVNGD QVGHIKKELA APLAYIIDNK
     LARVEGIVPY GAKNTFTMPV QMSFWGKEEN KQAVLDRLKM HGFKMAPPLK SSELGFGSNL
     FSGRAGPSYS APGHTAVQMT TEQLKSEFDK LFEDLKEDDK TREIQGPEVI GTQLLPHQKQ
     ALAWMVLREN NKELPPFWEE RNNFFYNTLT NFAEKERPEN VLGGILADDM GLGKTLTTIA
     LILANFHNGK PLPVEKIKRD QLYKEFGATS VKNEGDLPFK DLNCNLESST SSGKNETVQS
     QLSSSYPKRT KAKKPKYSES SDSEESEEWL PQETRINTKK DLPTTRKRSK ASCNFQEDTG
     FASALAAPSP TLKKKAKKKG TSSIQLAKKD DSEEGQRTTL IICPLSVLSN WIDQLEQHIS
     PDVHLNVYVY YGPDRSKDPA LLSRQDIVLT TYNILASDYG SRGDSPLHKL KWLRVVLDEG
     HTIRNPNALQ TKAALNLEAQ RRWILTGTPI QNSLKDLWSL LSFLKLKPFA DREWWHRTIQ
     RPVMMGDQGG LRRLQSLIKN ITLRRTKMSK IKGKPVLELP ERKVFIQHVT LTEEERQIYQ
     AVKNEGKLAI SRYFSEGTVL AHYADVLGVL LRLRQLCCHP HLCTNASSFS GTGVNNTPEE
     LREKLVNKMK LVLSSGSDEE CAVCLDSLTF PVITHCAHVF CKPCICEVIQ SEQPNAKCPL
     CRNELRLEHL IECPPEESDF ESVKKSDREW IPSSKINALM HALIELRKEN PVVKCLIVSQ
     FTTFLSLIET PLRESGFVFT RLDGSMPQKK RVEAIQCFQS SQAGSPTIML LSLKAGGVGL
     NLTAASRVFL MDPAWNPAAE DQCFDRCHRL GQKQAVIITK FVVKNSVEEN MLSIQNKKRK
     LAAGAFATKK PTASEVKQTK INEIKTLIDL
//
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