ID A0A0G2FQW0_9PEZI Unreviewed; 2185 AA.
AC A0A0G2FQW0;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE SubName: Full=Putative sec63-domain-containing protein {ECO:0000313|EMBL:KKY36597.1};
GN ORFNames=UCDDA912_g03370 {ECO:0000313|EMBL:KKY36597.1};
OS Diaporthe ampelina.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Diaporthaceae; Diaporthe.
OX NCBI_TaxID=1214573 {ECO:0000313|EMBL:KKY36597.1, ECO:0000313|Proteomes:UP000034680};
RN [1] {ECO:0000313|EMBL:KKY36597.1, ECO:0000313|Proteomes:UP000034680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DA912 {ECO:0000313|EMBL:KKY36597.1};
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:KKY36597.1, ECO:0000313|Proteomes:UP000034680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DA912 {ECO:0000313|EMBL:KKY36597.1};
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:KKY36597.1}.
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DR EMBL; LCUC01000113; KKY36597.1; -; Genomic_DNA.
DR STRING; 1214573.A0A0G2FQW0; -.
DR OrthoDB; 57056at2759; -.
DR Proteomes; UP000034680; 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; 5.
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; 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.
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:UP000034680}.
FT DOMAIN 539..723
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1365..1541
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT REGION 222..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 420..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 476..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..253
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..275
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..444
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 483..503
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2185 AA; 247211 MW; A91D0998BC1C9D10 CRC64;
MSGDNYQRDV SQYKYSAMSN LVLQADRRFV TRRTDEATGD PESLAGRLSI QEMGGRVARD
TAPKQKKSHI PAVERGSVRE GEDILRQQKK KGADLSRGGG ILSGAEALVE GLRYRPRTQA
TRATFDFILT IVAKNLGDVP QEVVRSAADA TLEYLKDEDL KDFDKKKEID DLLGASLNPK
EFNELVNLGK KITDYDAEDD DEEMEGADDD QEIDERQGVA VAFEEEDEDG EGIVNEVREE
SSEDEDEDEE DRPGLDKEAG AGGAAEDRDG DEAGVADGDA MVIDSAPAGK AQKKTQETNY
IPAFQIDAFW LQRQIGRLYP DAHIQHDKTI QALHILSGEP DEEGGDEKQL REIENDLMGL
FDYEHHEIVQ ELISNREKVV WLTRITRAEN PQARETLERE MVSEGLQWIL DEFHGKTGEE
KKGKLEIKMD LDQPEHKQES KPERPDGQLI GGLQPKKLIT LDNLIFDQGN HLMTNPKVRL
PEGSTKRAGK GYEEIHVPPP KKRSDPSDNL VPISEIPEWA REPFKSVKSL NKIQSKCYPS
AFEDDGNMLV CAPTGSGKTN VAFLAMLREI GKHRDPETGE IDLDSFKIVS IAPLKALVQE
QVGNFGGRLA PYGIKVSELT GDRQLTKQQI AETQIIVTTP EKWDVITRKA TDTSYTNLVR
LICIDEIHLL HDDRGPVLES IVARTIRKTE QTGEPVRILG LSATLPNYKD VASFLRVDPQ
KGMFHFDGSY RPCPLRQEFI GVTERKAIKQ LKVMNDVTYN KVLEHVGKNR NQMLIFVHSR
KETAKTARYI RDKALEMDTI NQILKSDVGS REILQATSDE ATDKDLKDLL PYGFGIHHAA
TLAWGVNLPA HTVIIKGTQV YSPEKGSWVE LSPQDVLQML GRAGRPQYDT FGEGIIITTQ
SEMQYYLSLM NQQLPIESQL VSRLVDNLNA EIVLGNVRSR DEGVDWLGYT YLFVRMLRSP
GLYSVGVEYE DDEGLEQKRV DLIHSAAHVL RKANLVKYDE KSGRMQATEL GRIASHYYIT
YGSMETYNAH IQPSITNIEL FRVFSLSSEF KYIPVRQEEK LELAKLLGRV PIPVKESIEE
PHCKINVLLQ AYISRLKLDG LALMADMVYV TQSAGRILRA IFEIALKKGW SSVAKTALNL
CKMAEKRMWP TMTPLRQFPN CPRDIVQKAE RTEVPWSSFF DLDPPRMGEL LGMPKAGKTV
VGLVNKFPRV EVQAQIQPLT RSMLRVELTI SPNFEWDEEV HGLAESFWIL VEDCDGEEIL
FHDTFLLRKD YAESETNEHI VEFTVPITEP MPPNYFISVV SDRWMHSETR VAVSFQKLIL
PEKFPPHTEL LDLQPLPPSA LKVKEYAALY PQWEYFNKVQ TQTFNTLYAT DNNVFIGAPT
GSGKTVCAEF ALLHLWSKPD AGRAVYIAPF QELVDIRLQD WQKRLSALRG GKDIMKLTGE
TAADIKILDA ADLVLATPTQ WDVLSRQWKR RKNVQTVELF IADELQLLGG SMGYVYEAIV
SRMHYIRSQT ELPMRIVGLG VSLANARDIG EWIGAKQHDI YNFSPHVRPV PLELHIQSYT
IPHFPSLMLA MARPTYLAIT QMSPDKPALV FVPNRKQTRA TTRDILTACL AEDDEDRFLH
VDVEQIKPLL ERVSEEALAE SLSHGVGYYH EALSTDDKRI VKYLYDNGAI QVLVASRDVC
WELDCTAHLV VVMGTQYFEG REHRYVDYPM TDVLQMFGKA LKSSKDGRGR GVLMLPGVKR
EYYKKFLNEA LPVESHLHSY LHDAFVTEIS TRMVESGDDA IAWMTFTYFY RRLLANPSFY
SLTSTTEDGL SQYLSDLVET TLRELDESKI IEFDEEDGSV TPQNAAMIGA YYNISYITMQ
TFLLSLSART KLKGILEIVT SATEFEAIQI RRHEDGLLRR IYDRVPVKMA QPDYDSPHFR
AFVLLQAHFS RMQLPIDLVK DQETIVSKVV SLLSATVDIL SSDGHLNAMN AMEMSQMVVQ
AMWDRDSPLK QIPHFTPEVV KAANSFGVKD VFDFMEAMNP EENPQYGELV KAMGLSQKQL
EDAARFTNQK YPDVSLEFEV VDPENLRAGE ASYLNIQIER EVEEGDEVDT VIHAPFYPGK
KLENWWLVVG EESTKTLLAI KRVTVGLKLN VKLEFTVPTP GQHELKLFLM SDSYIGVDQE
PSFEVTVAEG MEVDEDDEDD EDDDE
//
