ID A0A093HA61_STRCA Unreviewed; 1005 AA.
AC A0A093HA61;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Helicase-like transcription factor {ECO:0000313|EMBL:KFV76295.1};
DE Flags: Fragment;
GN ORFNames=N308_12841 {ECO:0000313|EMBL:KFV76295.1};
OS Struthio camelus australis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Palaeognathae; Struthioniformes; Struthionidae;
OC Struthio.
OX NCBI_TaxID=441894 {ECO:0000313|EMBL:KFV76295.1, ECO:0000313|Proteomes:UP000053584};
RN [1] {ECO:0000313|EMBL:KFV76295.1, ECO:0000313|Proteomes:UP000053584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N308 {ECO:0000313|EMBL:KFV76295.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KL205889; KFV76295.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093HA61; -.
DR STRING; 441894.ENSSCUP00000000948; -.
DR Proteomes; UP000053584; 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; 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:KFV76295.1};
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:UP000053584};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 473..601
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 755..796
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 833..992
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFV76295.1"
FT NON_TER 1005
FT /evidence="ECO:0000313|EMBL:KFV76295.1"
SQ SEQUENCE 1005 AA; 112130 MW; F2131160E69C1100 CRC64;
FCRSPAWGCS PRNTYKGERN YSDYSSSEFY SSLGLEDFSI GDASGTDEDI DSAILYGTLR
GTIVGLRYYK GVVNNNEMVA LQREPNNPYD KNAVKVNNVN GDQVGHIKKE LAAALAGIMD
NKLAVVEGVV PYGAKNVFTM PVQMSFWGRE ENKEAVLDQL KMHGFKLAPP LKECGFGSKW
ISGKAGPTYS APVHAAVHLT SEQLKSEFDK LFEDLKEDDK TCEMEGAEAV GTLLLPHQKQ
ALAWMVSREN SNDLPPFWEE RNNFYYNILT NFAVKERPKN VLGGILADDM GLGKTLTTIA
LILTNFQDGQ PLPVEKITKE DKVPPEKSGF GNILQCVGVV TELQQNSFCK RCSLSFSISS
ALTRFLFAFA SCVLFLAECR GTSSVIQEDT GFGSVLVASP TPLKRKTKRK GNEENKFDHV
NFWVTSGIHV NSVSFCFALK WTVTPLNVTS VFSGTASVQS AEKKCSEDGP RATLIICPLS
VLSNWIDQFE QHVSQDFHLN IYVYYGSDRN KDPAVLSEQD VILTTYNVLA TDYGTGGDSP
LHKIKWLRIV LDEGHTIRNP NAQQTKAVLS LEAHRRWILT GTPIQNSVKD LWSLISFLKL
KPFTDREWWH RTIQRPVTMG TPGGLRRLQS LIKSITLRRT KISKVKGKPI LELPERKVLI
QHVTLTEEER QIYQSVKKEG KAAVNRFFRE GTVLARYADI LGVLLRLRQL CCHPRLCTNT
SSSSFSAGNN APEELREMLV NKMKLVLSSG SDEECAVCLE SLTLPVITHC AHVFCKPCIY
EVIRSEQPNA SCPLCRNELR VEHLVECPLE EGLDCSNEKK GDQEWISSSK INALMHALIE
LRRENPTTKC LVVSQFTTFL SLIENPLKKS GFAFTRLDGS MAQKKRIEAI QCFQSSQAGS
PTVMLLSLKA GGVGLNLTAA SRVFLMDPAW NPAAEDQCFD RCHRLGQKYN VVITKFIVKD
SVEENMLKIQ NKKRELAVGA FATKKPSASE IKQTKINEIK ALIDL
//
