ID A0A0G2I3V3_9PEZI Unreviewed; 1564 AA.
AC A0A0G2I3V3;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Putative dead deah box helicase {ECO:0000313|EMBL:KKY34635.1};
GN ORFNames=UCDDA912_g05387 {ECO:0000313|EMBL:KKY34635.1};
OS Diaporthe ampelina.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Diaporthaceae; Diaporthe.
OX NCBI_TaxID=1214573 {ECO:0000313|EMBL:KKY34635.1, ECO:0000313|Proteomes:UP000034680};
RN [1] {ECO:0000313|EMBL:KKY34635.1, ECO:0000313|Proteomes:UP000034680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DA912 {ECO:0000313|EMBL:KKY34635.1};
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.
RN [2] {ECO:0000313|EMBL:KKY34635.1, ECO:0000313|Proteomes:UP000034680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DA912 {ECO:0000313|EMBL:KKY34635.1};
RA Morales-Cruz A., Amrine K.C., Cantu D.;
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:KKY34635.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LCUC01000194; KKY34635.1; -; Genomic_DNA.
DR STRING; 1214573.A0A0G2I3V3; -.
DR OrthoDB; 33910at2759; -.
DR Proteomes; UP000034680; 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; cd18025; DEXHc_DDX60; 1.
DR CDD; cd18795; SF2_C_Ski2; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR44533; DEAD/H RNA HELICASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR44533:SF4; HELICASE ATP-BINDING DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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 Helicase {ECO:0000313|EMBL:KKY34635.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000034680}.
FT DOMAIN 525..698
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 979..1124
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 351..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 925..966
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1454..1475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1498..1534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..380
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 925..959
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1454..1469
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1564 AA; 174691 MW; 1C7A49E7AE4E5050 CRC64;
MASSTEHQVG PLGPDTWYKS LHPLQVDLVG DFAGKELFAI HGDALMLYCI TRAKVDLDSG
FQLLHAIHAV ESFLKKLQDR GLNFHIIWFR DHEALCLPRD ATDVLPPKYL LTRAVLIRHL
NRQQPSQDAI AFEDAKTISY EFGDLDSPSF QHYLANNAVH CFMCLDAPAF GACSDSSEEA
YLGIAHHFAA RGYCLAFIDR YVLSQKPQLP RSLLTEVHAF ANKIEELTSV SIAGSLPAPE
TSTGPVQRHV QNGEDTIIEH GVLPFNQPAL NGYLQDIHLV PMEGSDKETV PKIFRELTHW
HNARVSVANR RPPPPKNWRE MRADQKQMAS TIAYSASLTN ASGKRIEPEV IIGGINRDQS
SVPRKEAKKE AKKESQDTKP TKQAAQKGGK KGKAKSGKEL AREATSILIE AGDAPQTRQS
ITALIWSIVR SVDNSNLSPP TAKMLNLLAT SLQVPAEFAT DSSSSATRKL PFSCVFDAKT
GVTNLATVDL DFQLQHCGPF LERSFDPAPD PRVPFNPDGW QRNVLNAIDA DKSLFVVAPT
SAGKTFISFY AMRKVLKESD DGVLVYVAPT KALVNQIAAE IQARFTKSYK HDGRSVWSIH
TRDYRVNNPA GCQILVTVPH ILQIMLMAPS NAEHENSWSR RIKRIIFDEV HCIGQADDGV
IWEQLLLLAP CPIIALSATV GNPKEFRQWL ESAAKSKNLE FETIVHQTRY SDLRKFLWQP
SKQYTLDFLD PVERLPVPGL DDESTSSSNF FPIHPVATLV NRNRESLDDL TLEPRDCLLL
WKSMAKHQNA EYPLDRQLSP PHVFPKVATK PDVAKYEASL KKTLHAWMLD RNSPFDAVQK
DLRPQCHVPA SSRQELKDSA LPLLTDLRSQ GALPAILFNY DRVACEEIAF RILSDLQEAE
NTWKATDASW KKKVAKFEQF KKDQAKADSL RQKTTKAKAK GKRDEDDIGD GRMDDDPSTL
SSFDPEAPLE RFSLGDETKL TRSELEWMIW SLRWKNINPD ILNALRRGIG IHHAGMNRKY
RQIVEMLFRK GFLTVVVATG TLALGLNMPC KTVVFFGDSV FLTALNYHQA AGRAGRRGFD
LLGNVVFVGM PQERVYEIMS SRLPDLRGHF PLSTSLVLRT LSLLHHTNNS DFSVGAVRSL
LSQTRLYLGG PSGQLSIKHH LRFSIEYLRR QHLLSEDGAP LNFAGLVGHL YFTENSVFAF
HSLLKEGYFH KLCDKFRTAS EATMLEIVLV LSHIFGRIST NTFKKDWMGA VTRSDSIVFL
PPLPADALQT LRQHNQDTLD IFRTYVSTYV QQHLEDKPDM HLPFTKSEVG ASKRDLGEAG
LEGILGEGHN PPAKIRSPFH ALSGYGDNSF GSIHELCDTV RSDVFLEESA IPYIPLFPDD
TNGVPWNAYL YDFFKHGDME ALVRDNHIKK GDVWFLLKDF SLVLATIVTS ITNFLDLDAG
ADSDLAMMDV QDAEDAARET SDALEPDDGS DMAHGALTIQ DDGLKKLEVA AGVPKKTKKP
KVIDSWDDDG SSEDEAAAAE AAEAAAKAAG PAWEGDGERN LAQVLRMFRM VQQQFDEKFR
KQWA
//
