ID A0A0F4Z860_9PEZI Unreviewed; 2201 AA.
AC A0A0F4Z860;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KKA26729.1};
GN ORFNames=TD95_000873 {ECO:0000313|EMBL:KKA26729.1};
OS Thielaviopsis punctulata.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Microascales; Ceratocystidaceae; Thielaviopsis.
OX NCBI_TaxID=72032 {ECO:0000313|EMBL:KKA26729.1, ECO:0000313|Proteomes:UP000033483};
RN [1] {ECO:0000313|EMBL:KKA26729.1, ECO:0000313|Proteomes:UP000033483}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CR-DP1 {ECO:0000313|EMBL:KKA26729.1};
RA Radwan O., Al-Naeli F.A., Rendon G.A., Fields C.;
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
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:KKA26729.1}.
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DR EMBL; LAEV01001983; KKA26729.1; -; Genomic_DNA.
DR OrthoDB; 57056at2759; -.
DR Proteomes; UP000033483; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProt.
DR CDD; cd18019; DEXHc_Brr2_1; 1.
DR CDD; cd18021; DEXHc_Brr2_2; 1.
DR CDD; cd18795; SF2_C_Ski2; 1.
DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 2.
DR Gene3D; 2.60.40.150; C2 domain; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 4.
DR Gene3D; 1.10.3380.10; Sec63 N-terminal domain-like domain; 2.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041094; Brr2_helicase_PWI.
DR InterPro; IPR048863; BRR2_plug.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR004179; Sec63-dom.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR47961; DNA POLYMERASE THETA, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G05260)-RELATED; 1.
DR PANTHER; PTHR47961:SF4; U5 SMALL NUCLEAR RIBONUCLEOPROTEIN HELICASE; 1.
DR Pfam; PF21188; BRR2_plug; 1.
DR Pfam; PF00270; DEAD; 2.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF18149; Helicase_PWI; 1.
DR Pfam; PF02889; Sec63; 2.
DR PIRSF; PIRSF039073; BRR2; 1.
DR SMART; SM00382; AAA; 2.
DR SMART; SM00487; DEXDc; 2.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00973; Sec63; 2.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 4.
DR SUPFAM; SSF158702; Sec63 N-terminal domain-like; 2.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 2.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000033483}.
FT DOMAIN 533..717
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 756..964
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1384..1560
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT REGION 30..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 197..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 222..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..94
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..214
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..256
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2201 AA; 249065 MW; B0B1F5350B6FE5D0 CRC64;
MSGANRDVSQ YKYSAMSNLV LQADRRFVTR RNDEATGDPE SLSGRLKISD MGSRVERDTM
PKSKKTSVLP NIERGSAQDG KDILEREKRK SKASSGLSRG LSAADIAVEG IQYRPRTVET
RATFNFILTI VANNLGDVSY DVVRSAADAV LEYLKDEDMK DFDKKKEIDD ILGTSLGPKE
FNELINLSKK ITDYDAQDDE SQVSAMDVDE NDELDDRQGV AVTFEDDDED ENGGFVDEVR
DQSSDDEEDE DEASQEKADD KQDGGMSDDD EMLLDSAPAV ASTDNSKTAS KSIPAREIDA
YWLQRLIGKL YEDPHEQHDK TQEALRILSG EPDEPGGDEK QLREIENDLM ELFDFEHHEL
VNKMIANREK IVWLTRLARA EGEEKRLGIE REMASEGLQW ILNELHGKGS SDAKLKKEIK
MDIDVPNDMI AAPAKSEKAE GQLVGGLHPR KTINLENLVF DQGNHLMTNP KVRLPEGSTK
RTFKGYEEIH VPPPKKRNDP NDPLIPISDL PEWARLPFST TKSLNRIQSK CFPTAFEDDG
NMLVCAPTGS GKTNVSMLTI LREIGKHRDP ETGIIDLDSF KIVYIAPLKA LVQEQVGNFG
KRLEPYGITV AELTGDRQLT KQQIAETQII VTTPEKWDVI TRKATDLTYT NLVRLIIIDE
IHLLHDDRGP VLESIVARTI RKTEQSGEPV RIVGLSATLP NYRDVASFVR ADPKTGVFHF
DGSFRPCPLR QEFIGVTDRK PIKQLKIMND VCYNKVIEHV GTNHNQMLIF VHSRKETAKT
ARYIRDKALE LGTINQILRH DAGSREVLRE AAEDATDKDL KDLLPQGFGI HHAGMNRMDR
SDVEDLFARG AIQVLVCTAT LAWGVNLPAH TVIIKGTQVY SPEKGSWVEL SPQDVLQMLG
RAGRPQFDTY GEGIIITSQS EIQYYLSLMN QQLPIESQLV SRLVDNLNAE VVLGNVRTRD
EGVEWLGYTY LFVRMLRSPG LYQVGAEYED DDALEQKRVD LIHSAALILR KSHLIRYDEK
SGKIQSTELG RIASHYYITH DSMETYNTLI QPSITVIDFF RIFALSAEFK YIPVRQDEKV
ELAKLLQTVP IPVKESIEEP HTKINVLLQA YISRLKLDGL ALVADMVYVT QSAGRILRAV
FEIAMRKGWS SVAKTALDLC KMAEKRMWPT MSPLRQFPGC PRDIVHKMER IEAPWGAYFD
LDPPRMGELL GMPRAGKTVC ELVAKFPRLE VQAFAKPITR SLLHVGLSIT PNFEWDDDVH
GTSEGFWIVV EDCDGEEILF YDQFLLRKDY ALSEDNEHLV DFTVPITDPM PPNYFISVIS
DRWMHSETRL PISFQKLILP EKFPPHTELL ELQPLPVSAL KLKDYQALYP DWDHFNRIQT
QTFNSLFTTD QNVLVAAPTG SGKTVCAEFS ILRLWAQKEP GRAVYVAPTQ ELVDIRHQDW
QKRLSGIRGG KEVVKLTGET TRDLKLLEQG DLILATPSQW DVLSRQWRRR KNVQTVELFI
ADELHLLGGN QGYIYEVVVS RMHFIRTQTE LPLRILGLSV SLANARDIGE WIGAKKHDIY
NFSPHVRPIP LELHVQAYSV PHFPSLMLAM AKPTYLSILQ LSLSQPAIVF VPSRKQTRAT
ARDLLAACLV DDDEDRFLHA DPEQLKRILE HVHEEALAEA ISHGVGYYHE ALSQNDKKIV
KHLYDNGAIQ VLVASRDVCW ELNSTAHLVV VMGTQYFEGR EHRYVDYPMA EVLHMFGKAL
KPSKDGRSRG VLMVPTARRE YFKKFLNEAL PIESHLHNYL NDAFVTEVST KMIESIDDAI
NWTTFTYFYR RLLANPSYYA LTDTSHDGLS TYISDLVETA ITELSEAKII DFDEEDGSVS
PQNAAMIAAY YNISNVTMQT FLMSLKATTK LKGILEIVTS ATEFEALQSR RHEEGLLRKI
YNMLPVKMAD ANAESAHFKA FVLLQAHFSR MQLPIDLAKD QEIILTKVLS LLSATVDILS
SEGWLNAMNA MEMSQMVVQA MWDRDSPLKQ IPHFFPEVIK AANESGVKDV FDFMEAMNPE
DSRYKPLIKS LGLTNNQLVE VAKFTNEKYP DIELEHEILD ADEIQAGEPA YLQVNITRNI
DEGDEFDATV HAPFYPAKKM ENWWLVVGEE ATKSLLAIKR VTVGTELKMK LEFTVPTAGM
HSCKLFLMSD SYMGVDQEQE FEVTAAEAMD VDSDEEEDEE E
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