ID W6YYM8_COCMI Unreviewed; 2213 AA.
AC W6YYM8;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Sec63-domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=COCMIDRAFT_6252 {ECO:0000313|EMBL:EUC44467.1};
OS Bipolaris oryzae ATCC 44560.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX NCBI_TaxID=930090 {ECO:0000313|EMBL:EUC44467.1};
RN [1] {ECO:0000313|EMBL:EUC44467.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 44560 {ECO:0000313|EMBL:EUC44467.1};
RX PubMed=23357949; DOI=10.1371/journal.pgen.1003233;
RA Condon B.J., Leng Y., Wu D., Bushley K.E., Ohm R.A., Otillar R., Martin J.,
RA Schackwitz W., Grimwood J., MohdZainudin N., Xue C., Wang R., Manning V.A.,
RA Dhillon B., Tu Z.J., Steffenson B.J., Salamov A., Sun H., Lowry S.,
RA LaButti K., Han J., Copeland A., Lindquist E., Barry K., Schmutz J.,
RA Baker S.E., Ciuffetti L.M., Grigoriev I.V., Zhong S., Turgeon B.G.;
RT "Comparative genome structure, secondary metabolite, and effector coding
RT capacity across Cochliobolus pathogens.";
RL PLoS Genet. 9:E1003233-E1003233(2013).
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DR EMBL; KI964004; EUC44467.1; -; Genomic_DNA.
DR RefSeq; XP_007689019.1; XM_007690829.1.
DR STRING; 930090.W6YYM8; -.
DR GeneID; 19124896; -.
DR KEGG; bor:COCMIDRAFT_6252; -.
DR eggNOG; KOG0951; Eukaryota.
DR HOGENOM; CLU_000335_1_0_1; -.
DR OrthoDB; 57056at2759; -.
DR Proteomes; UP000054032; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase 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; 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; SM00487; DEXDc; 2.
DR SMART; SM00490; HELICc; 2.
DR SMART; SM00973; Sec63; 2.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 3.
DR SUPFAM; SSF158702; Sec63 N-terminal domain-like; 2.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 2.
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}.
FT DOMAIN 543..727
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 766..974
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1394..1570
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT REGION 53..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 197..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2193..2213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..97
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 199..214
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..259
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2198..2213
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2213 AA; 249125 MW; 98E8E093D4445E03 CRC64;
MSKDQNNLAQ FKYAAMSNLV LQADRRFTSR RPDEHTGDPE SLAGRINIRD MGARTARDSA
SAQTKKLKGP GVERGNLGEG GDVLEREQRK RKRDDGTSAF GAIATADLNI EGLTYKPRTP
ATRQTFELIT TIVSRALGDV DPATTRSAAD QVLEYLKDDS MKDFDKKKEV DDLLGTSMGA
KEFNELVNLG KKITDYDAQD DEEGGDEEMA DGDGADNGDN QGVAVVFDDE EEDEDGPQTF
EIRDADSSDE EDEAEAPIEQ IGGDDAKDAG FADTEETIIQ GDAATSDRKN GADQLIPAHE
IDAYWLQRQI GQIYEDAHIQ QEKTQEALKF LAGVSEDGEE KELREIENDL MDLFDYEHHE
LVAKLVLNRD RVVWVTRWRR AAEDNDERTA VEREMKAAGQ QQILQELRAR ETGIKAEEGA
GTGKMKFNLK DISLPEASND VEMADAKPEG IVGGLQPSSR LVNLDNIVFD QGNHLMTNAS
VKLPQGSTRR QFKGYEEIHV PAPKAKRDPN EPPLMPTSEL PDWARPGFGN SKSLNRIQTK
CFPTAFNDDG NMLICAPTGS GKTNVAMLTM LREIGKHRNP TTGEIALDDF KIIYIAPLKA
LVAEQVGNFG KRLEPYGIKV SELTGDRQLT KQQIAETQII VTTPEKYDVI TRKATDTSYI
NLVRLICIDE IHLLHDDRGP VIESIVSRTL RRSEQTGDHV RIVGLSATLP NYRDVASFLR
VDPDKGLFHF DGTFRPCPLK QEFIGVTDKK AIKQLKTMND VCYTKVLEQV GEHRNQMLIF
VHSRKETAKT AKYIRDKALE EETIGKILRS DAASREILRE ESESIQNADL KDVMPYGFGI
HHAGMSRADR TSVEDLFADG SIQVLVCTAT LAWGVNLPAH TVIIKGTQIY SPEKGSWVEL
SPQDVLQMLG RAGRPQYDTY GEGIIITTQS EIQYYLSLLN QQLPIESQLI SKLADNLNAE
IVLGNVRSRD EAVDWLGYTY LFVRMLRSPA LYRVGPEYEN DTVLEQRRVD LIHAAAHVLE
KCSLIKYDRK TGALNPTELG RIASHYYITH NSMATYNMHV QPGISAIELF RVFALSEEFK
YIPVRQDEKL ELAKLLGKVP IPVKEGVEEP QAKINVLLQA YISRLKLEGL ALMADLVYVT
QSAGRILRAI FEICLKKGWS QVAKLALDMC KMAEKRMWPT MTPLRQFPTC PRDIVQKAER
IDVSWSSYFG LDPPSMGELL GMPKAGRLVC GLVEKFPRLQ IEATPRPVTR SLLRLELTIR
PDFVWDNELH GTSEAFWILV EDCDGEQVLF HDTFILRRDY ADGDVNEHLL EITVPIDEPM
PPNYFVTVLS DRWMASETKL AVSFQKLILP AKFPAHTPVL DLQPLPVSAL KRKEYMGLYE
NIGRFNKVQT QTFNTLYTTD DNALIGASAG IGKTICAEFA ILRHWGSGDE GRIVYLAPFQ
ELVDNQYKNW NERLSGLSGG KDVVKLTGET TADLRLLEKG DLILATPSQW DSLSRQWQRR
KNVQSVSLLI ADELHMLGGS NGHVYEIVVS RMQAMATQLE SKLRIVGLSV SLSNARDIGE
WIGANKHTIY NFSPAIRAVP LELKIQSFTI PHFPSLMMAM ARPTYSAITQ MSPDKPAMVF
VANRKQARNS AADLFNACIA DDDEDRFLNV DLSEIQPILE KINEQALATS LSHGIGYFHE
ALNSFDKRAV QHLFKVGAIQ VMIVSRDSCW EIDSSAHLVV VQGTQFYEGR EHRYVDYPIS
DILQMFGKAG RVGLDKSAKG VLMLPAVKRE YYKKFLNEAL PIESYLHDYL HDAFVAEISA
KTIESTQEAV DWSTYTYFYR RLLANPSYYN LHDTSHEGLS AHLSDMVEQT LKELTDANLI
EHDEDEDAIT PLNPCMIAAY YNISFITMQT LMMSLNGRTS LKGVLEIITA ATEFEDIQIR
RHEDHILQRI YDRVPFKMQE PNFETPHFKA FVLLQAHFSR MQLPIDLAKD QETVLRKVLT
ILSASVDVLS SEAHLNAMSA MELSQMVVQA MWQKDSPLKQ IPHFDADTIK AAQKFGINDV
DDFINAMDED ENPDYKQLIS ALNVDQRQLA DIANFTNNFY PNVELEHQLV DPENIASNTP
AQLKVRVTRN LEEDEEPKTE VHAPFYPADK TESWWLVLGD QKERTLLAIK KVPILRKLET
VLEFTLEKPG SHELTLYLVS DSYLGVDQAP TFQVEAAEGM EEDSEEEEEE DEE
//
