ID A0A2C9LN33_BIOGL Unreviewed; 1620 AA.
AC A0A2C9LN33;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Helicase-like transcription factor {ECO:0008006|Google:ProtNLM};
GN Name=106069768 {ECO:0000313|EnsemblMetazoa:BGLB033046-PA};
OS Biomphalaria glabrata (Bloodfluke planorb) (Freshwater snail).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Heterobranchia; Euthyneura; Panpulmonata; Hygrophila; Lymnaeoidea;
OC Planorbidae; Biomphalaria.
OX NCBI_TaxID=6526 {ECO:0000313|EnsemblMetazoa:BGLB033046-PA, ECO:0000313|Proteomes:UP000076420};
RN [1] {ECO:0000313|EnsemblMetazoa:BGLB033046-PA}
RP IDENTIFICATION.
RC STRAIN=BB02 {ECO:0000313|EnsemblMetazoa:BGLB033046-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR RefSeq; XP_013084958.1; XM_013229504.1.
DR STRING; 6526.A0A2C9LN33; -.
DR EnsemblMetazoa; BGLB033046-RA; BGLB033046-PA; BGLB033046.
DR GeneID; 106069768; -.
DR KEGG; bgt:106069768; -.
DR VEuPathDB; VectorBase:BGLB033046; -.
DR OrthoDB; 200191at2759; -.
DR Proteomes; UP000076420; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
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; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
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; PF00097; zf-C3HC4; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 3.
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 Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 1075..1206
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1369..1410
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 1456..1615
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 52..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 244..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 795..817
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1023..1042
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 795..812
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1620 AA; 181647 MW; B140FBDFF8314BD4 CRC64;
MLRMETNTNL RPPGQTSISE DDLEDLFSLN ISTDFYPSSN FDVLVEELDR YNGPSNSTRG
SEFTTSNAQS DSFSTGVMGL ETEAISNAVS ISHTSKDTRQ DVSESLYPTE EKLGEKSISN
FAQIPYSAKD VEYLPEADFN TGPSSYKTEA RRQETETNRN IGSCSYLTDM GQDAEINRNS
GLIKTRTDET LETNLNSVPI SYSTEDLSLE TNLNGVHYLR EDTAPERNPT SNTYTADMQQ
ERETNWNTGP NSYLAPDMES ERVSNSGSNS YLTENTEIEK TFNSNFNTPH HSVNMDSISH
FNTDDNIQTY TSQDIEPNLR RAYSPVGLRQ SNSNPHPSYS SVGYRPSSTL NVTPSTSFSS
IDLGIATSLG SPLKTAYSQQ EASNTNSNYP NIGHGSNSFD KHWSPHLAGI LDEDVQVFPN
SLRALNLLRR SDFPSVSPFS RQKEVFGTIN SEITSVYQYR GKVSDNETVY LQRAHNMFDR
TAIRVDNKSK EQVGVVKREH SSALTHIMDN NLATVEGKVV NYTADCVFRI PLEITLSGDP
SRKDEVLWYF KSNNIPVMAC YKSFSPIEVQ DRESPIPFDY DYDHVKSSRT YVTPAEMDNE
LDQMFKTLDE GDKVTEAEAS LAVKTQLYPH QKQALNWMIC KENKDSLPPF WVQRGHLYMN
TLSRKKTAEK PKSIYGGILA DDMGLGKTLE MISLIVTNFV NGKPIAEPLS GYTRDSFVKT
SKTGPLRIFK SEIENKESPE CNGAMNYSPL SPRLNLPNRI SPPSLASVSA EWHKSFNNMK
SEVVKSEIAS STTELKHSSS FPSLSPSRAM KRSNCEELND DSSNSIFGFA KGKGLGKKSK
FLELENTDSN QSADLSLDFV DLTLPETDLP SMQVDNHFDC DTTKGLTSAT HFPSMMKHRI
IELAYAAANK SGSRFDLNGA GTFSNNIDSA IDVDALPDIN KYEDITPVDS PEVFEVLNDS
PDAYSMSSMH RKNSDSDTRS SILESELSSK MKLPDKYAIV ISDSEDELPD IKPLDLTKKS
TFKKTISGSP HQRTKPDVAS ETVTSDVTNE TVTWKRREVI STHDPATGRT LTTGPRGTLI
ICPLSVISNW VEQFDEHVDR SVQINLHVYY GPKRTNDITF LLEQDVVITT YATLSSDFKR
GYLSPLHRIE WLRVVLDEGH TIRNPAAQQS KAIFELQADR RWVLTGTPIQ NSLKDLWSLI
NFLQVAPFTE KKTWNQIIAG PLVKRERQAL KRVSHLVRNL AMRRTKHQQL NGKPLISLPA
REVYLETVTL NAEERKIYDA MQINGQDLIG SYYRKGILLN NYGTVLTILL RLRQLCCHPQ
LVAIGALKKN PGAIFEDIIG TDQRPTHENK EKLIQQLKSV IESGSDEECS ICLESLKEPV
ITACAHIYCK LCIEAVIEKN EQETSCPMCR APLDKNELYG VEDSATDCPD KDQFHFNPDE
WHSSSKVDAL MKALNQLRQE DPSIKSVVVS QFTSLLTLLE TPLKEQGFVF ARLDGTMRAA
DRAKAVHDFA NPVPGGPTIF LLSLKAGGVG INLTAASRVF LLDPAWNPAA EDQCFDRCHR
LGQTRDVVIT KFVIEDSVEE RMLELQEKKK QLIRGVLDKK LSADQRRQKR IEEIKTLFNI
//
