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Database: UniProt
Entry: A0A0G2GI49_9PEZI
LinkDB: A0A0G2GI49_9PEZI
Original site: A0A0G2GI49_9PEZI 
ID   A0A0G2GI49_9PEZI        Unreviewed;      1293 AA.
AC   A0A0G2GI49;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Putative atp-dependent rna helicase a {ECO:0000313|EMBL:KKY16655.1};
GN   ORFNames=UCDDS831_g06904 {ECO:0000313|EMBL:KKY16655.1};
OS   Diplodia seriata.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC   Diplodia.
OX   NCBI_TaxID=420778 {ECO:0000313|EMBL:KKY16655.1, ECO:0000313|Proteomes:UP000034182};
RN   [1] {ECO:0000313|EMBL:KKY16655.1, ECO:0000313|Proteomes:UP000034182}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DS831 {ECO:0000313|EMBL:KKY16655.1};
RA   Morales-Cruz A., Amrine K.C., Cantu D.;
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KKY16655.1, ECO:0000313|Proteomes:UP000034182}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DS831 {ECO:0000313|EMBL:KKY16655.1};
RA   Lawrence D.P., Travadon R., Rolshausen P.E., Baumgartner K.;
RT   "Distinctive expansion of gene families associated with plant cell wall
RT   degradation and secondary metabolism in the genomes of grapevine trunk
RT   pathogens.";
RL   Submitted (MAY-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:KKY16655.1}.
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DR   EMBL; LAQI01000166; KKY16655.1; -; Genomic_DNA.
DR   Proteomes; UP000034182; 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   CDD; cd17917; DEXHc_RHA-like; 1.
DR   CDD; cd18791; SF2_C_RHA; 1.
DR   Gene3D; 1.20.120.1080; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   Gene3D; 3.10.110.10; Ubiquitin Conjugating Enzyme; 1.
DR   InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR007502; Helicase-assoc_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR006575; RWD_dom.
DR   InterPro; IPR009060; UBA-like_sf.
DR   InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR   PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR   PANTHER; PTHR18934:SF145; ATP-DEPENDENT RNA HELICASE DHX29; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF21010; HA2_C; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF07717; OB_NTP_bind; 1.
DR   Pfam; PF05773; RWD; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00847; HA2; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF54768; dsRNA-binding domain-like; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF46934; UBA-like; 1.
DR   SUPFAM; SSF54495; UBC-like; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS50908; RWD; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Helicase {ECO:0000313|EMBL:KKY16655.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT   DOMAIN          425..524
FT                   /note="RWD"
FT                   /evidence="ECO:0000259|PROSITE:PS50908"
FT   DOMAIN          608..784
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          841..1012
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..78
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          218..252
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        37..76
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        218..238
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1293 AA;  143022 MW;  170AE37923ED737E CRC64;
     MPKNPHPPRG GGGSKKSAPA PLGAEDTSFI VFSNSKSDSK KSKKADPVAK NDTADKGKGK
     SKGAPEQPED APKKPDVRTV IGGASWTGKL PVNMLSEHCQ KQKWAKPEYT MTKVKDGFVS
     HVILKATNPK TRETTTLPPI RLPIEKQDLA VQPTALEARH FAATYTLFRI ASMKNIHMMM
     PPTYKDLWKG AFADMKKEDV KSGRGWMYEA DPFVAHKERE QAKAEAEKKR EEATKQRENA
     KNQPAGSSSN IMRGWTRVPK LDMGKRIRAE IEGLIRRDAV WNPHSVKISP AERSALIVEI
     VKLGFRKSHV EEAAEVCKDR EEILEWLLIH VPEDDLPPWS LPEGYTAGIS MASGNLKREA
     AIKRLAATGY AMELCEEALD TFDGDEAKAA GLLQARLLGD DELAEQLSGA TIGNETEPQE
     DVWAEEQVIL ASIYDEKYST TGQDQCQIRL EIVDGTKTGF LLNVRKPAEL YPNVLPIISI
     NAKIPAYIRL SIIRQALSHA RENFLGEQMI FNIVDWLEHE IPSIIDNPGR LTDVSSAISA
     ADTGVHAEAI KQKEKRQRRP KPVNLRPGSQ ISQRMLEQWR TKQASPDQQR MLRARQNLPA
     WKLLPDIVEA VKNYQVVIIS GETGSGKSTQ SVQFILDDMI QRQLGEAANI VCTQPRRISA
     LGLADRVADE RCTAVGDEVG YSIRGESRQK PGVTKLTFMT TGVLLRRLQT SGGRPDDVMA
     SLADITHVVV DEVHERSLDT DFLLVLLRDV LKKRNDLRVI LMSATLDADV FASFFKPAVG
     QVGMVEIAGR THPVTDYYVD DVIRMSGFNG HSADEDWEDE ESQKNIGGTL RSIGMRINYD
     LIAQTVHHID AELGAQDGAI LIFLPGTMEI DRTIQALRSM PNVYALPLHA SLLPVEQRRV
     FPPPPKGKRK VIASTNVAET SITIEDVVAV IDTGRVKETS FDPANNMVKL AETWASRAAC
     KQRRGRAGRV RAGTCYKLYT RNVERDKMME RPDPEIRRVP LEQLCLSVKA MGVQDVASFL
     AGALTPPDSI AVEGALELLG RMGAIDGDEM TALGRHLAVV PADLRCAKLM VYGATFGCLE
     SCLTIASILT VRSPFVSPQA KREESKAARS AFAKGQGDLI ADLRAYEQWS GFKEKGISFR
     DLRAFCEQNF LSLQTLNDIT STRRQYLSSL QETGFIPLRY SSYSDFGAQE VASLNRHGAN
     DALLRALVAG AFNPQIARID FPDKKFAASV SGAVELDPEA KTIKYFNQEN GRVFVHPSST
     VFDAQGFPGG ATFMSYFTKM ATSKVFMRDL TLH
//
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