ID A0A423WH50_9PEZI Unreviewed; 1379 AA.
AC A0A423WH50;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ROW02708.1};
GN ORFNames=VSDG_01681 {ECO:0000313|EMBL:ROW02708.1};
OS Valsa sordida.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Valsaceae; Valsa.
OX NCBI_TaxID=252740 {ECO:0000313|EMBL:ROW02708.1, ECO:0000313|Proteomes:UP000284375};
RN [1] {ECO:0000313|EMBL:ROW02708.1, ECO:0000313|Proteomes:UP000284375}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YSFL {ECO:0000313|EMBL:ROW02708.1,
RC ECO:0000313|Proteomes:UP000284375};
RA Yin Z., Huang L.;
RT "Host preference determinants of Valsa canker pathogens revealed by
RT comparative genomics.";
RL Submitted (SEP-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:ROW02708.1}.
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DR EMBL; LJZO01000004; ROW02708.1; -; Genomic_DNA.
DR STRING; 252740.A0A423WH50; -.
DR Proteomes; UP000284375; Unassembled WGS sequence.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; 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; IPR002464; DNA/RNA_helicase_DEAH_CS.
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; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF46934; UBA-like; 1.
DR SUPFAM; SSF54495; UBC-like; 1.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000284375}.
FT DOMAIN 614..789
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 857..1023
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 COILED 207..234
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 22..45
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1379 AA; 152251 MW; B6134B547AB7BAAF CRC64;
MAKKGKEKAP ASGSSTAKKS AKKAPAPEDD LLIFTTDKKK SKGGPSNKPG DSAGSAAGGP
DGPPEPPKPT VKQIIGGSSW TGKLPVNLLS EHCQRMKWER PDYDMRKTAE GYSSMVTLGA
KNSKTQEVTK LPTFKLPPTH VHLAHKPTAL EARHFAATYA LFRVCSMKNM SMILPPDYRS
LWKEFEALKK QDVKEGKAWM YDADPFKALE EREAAKVLAE KKRKEQQAAK EKAASMPGAS
GLVLRSNAAA SGGGGGFNPM KGWTTVPKIE MGNKTRQHLE NLLRRDTVWN PHGVVMKPEV
RGSIIKEFKD LGFRPSHVEE AVGECKDREE ALEWLLIHVP EDDLPKWALP GNYTSGVSVA
ATDLRKEGAV KRLAQSGYSI ELCRKVYDDS GGDEGKAAET LQKILLNSGS DAETEVASND
VMSNEDRDQL WEDELGSLES LYGEQYSRLG SDVCQIRLDS VTNGANKNIE AYIQFRKAPH
YPSQLIISVV ADLPSYLKLS IIKKALAYMS ETLQGEEMKM FYVISWVQEN TNEIIDKPGA
LREIAAVSST ASEEKNVSAK RRAKRPQRHP NPISWIPEST SIQNWMQRQK AASFQKMLAQ
RQKLPAWQVR ETIVQTVDDN QVTIISGETG SGKSTQSMQF VLDDLYDRGY AKCANIIVTQ
PRRISALGLA DRVSDERCTT VGQEVGYSIR GENRTSRDTK ITFVTTGVLL RRLQTSGGKI
DDVVASLADV SHVVIDEVHE RSLDTDFLLS IIRDVLKKRK DLKLILMSAT LDSATFGSYF
KADGLQVGSV EIAGRTFPVQ DFYLDDIIHM TGFTGQHDIY EAKGSDKPMD DDQRVNKIIQ
SLGMRINYNL LMETAKAIDS DLTQTQKSGG ILIFLPGVAE INQICRLLSS VASLYVLPLH
ASLETKEQKR VFSAAPPGKR KVVVATNVAE TSITIDDIVA VIDSGRVKET SFDPQTNMRK
LGETWASRAA CKQRRGRAGR VQAGKCYKMY TQNLEEQTMQ ERPEPEIRRV PLEQLCLSVR
AMGNKDVGEF LGRTPTPPEA LAVEGAIKML RRMGALDGDE LTALGQQLAM IPADLRCGKL
MVYGAIFGCL DDCVTIAAIL STKSPFLSPP DKRELAKQAK MRFAQGDGDL LTDLRAFKHW
DEMMQDRMPQ RQVRGFCEES FLSYNTMADI ASTRSQYYSA LAEVGIASAA DAYAGRHRNT
SPSMPLLRAL TASAFSPQIA RIQFPDKKYM ASVSGAVELD PEAKTIKYFT QENGRVFVHP
SSTLFDSHGF SGNAAFVSYF TLMSTSKIFV RDLTPFNAYT LLLFSGAIEL DTLGRGLVVD
GWLRLRGWAR VGVLVSRLRG IIDNIIAKKV ENGSAAMDPR DDEVIKAVVK LIELDGLDA
//
