ID A0A177C0Q6_9PLEO Unreviewed; 675 AA.
AC A0A177C0Q6;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=DEAD/DEAH box helicase-like protein {ECO:0000313|EMBL:OAG00996.1};
GN ORFNames=CC84DRAFT_1101246 {ECO:0000313|EMBL:OAG00996.1};
OS Paraphaeosphaeria sporulosa.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Didymosphaeriaceae;
OC Paraphaeosphaeria.
OX NCBI_TaxID=1460663 {ECO:0000313|EMBL:OAG00996.1, ECO:0000313|Proteomes:UP000077069};
RN [1] {ECO:0000313|EMBL:OAG00996.1, ECO:0000313|Proteomes:UP000077069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AP3s5-JAC2a {ECO:0000313|EMBL:OAG00996.1,
RC ECO:0000313|Proteomes:UP000077069};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KV441558; OAG00996.1; -; Genomic_DNA.
DR RefSeq; XP_018031361.1; XM_018174904.1.
DR AlphaFoldDB; A0A177C0Q6; -.
DR STRING; 1460663.A0A177C0Q6; -.
DR GeneID; 28758390; -.
DR InParanoid; A0A177C0Q6; -.
DR OrthoDB; 1358472at2759; -.
DR Proteomes; UP000077069; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR CDD; cd18799; SF2_C_EcoAI-like; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR006935; Helicase/UvrB_N.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR47396:SF1; ATP-DEPENDENT HELICASE IRC3-RELATED; 1.
DR PANTHER; PTHR47396; TYPE I RESTRICTION ENZYME ECOKI R PROTEIN; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF04851; ResIII; 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:ARBA00022806, ECO:0000313|EMBL:OAG00996.1};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:OAG00996.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022806,
KW ECO:0000313|EMBL:OAG00996.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000077069}.
FT DOMAIN 67..233
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 288..445
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 439..462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 654..675
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..453
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 661..675
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 675 AA; 74725 MW; 67BA5A7F67CB69E2 CRC64;
MFRFFQCVPS ILRRAAPVAH PFAVPRRCVS TAVKSAPTTT PPPSLPSSPL KITLREYQEE
CIQSVLAYLA KGHKRLGVSL ATGSGKTVIF THLIDRLPAT GDASQTLILA HRRELVEQAA
RHCALAYPNK HVDLEMGNHR ASGTADITVA SIQSIMSSGR VAKFDPARYK LVLVDEAHHI
VSQQYLDLLE HFGLRHTADW KKVPAPALVG VSATFSRFDG RKLGAVIDHI VYHRDYVDMI
EDNWLSDVVF TTVEIKADLN TVSTTANGDF KTAALSRVVN TEQTNDLLIK AWLAKAQSRN
STIVFCVDLS HVSNLTARFR QHGIAAEFVT GDTPSKIRSA RVDAFRRGDF PVLLNCGVFT
EGTDIPNIDC VLLARPTKSR NLLVQMIGRG MRLHPGKENC HIIDMVSALS TGVVSTPTLF
GLDPAEILEK ANTKDMMELK ERKEEESKRE QAAADTAARP LSAKPPGSIT FTDYDSVHDL
IADTSSDHVI RRISQLAWVA VGEGRFVLST NGGAYLVIDP TGNDNQTFRV KHYWRLPAGT
RSKSPYATPR VIAQSDSFEH VVHAADTFAM EAFEFIWISK NQPWRRSPAS QTQIDYLNKF
RPEEDHLKSK DLTKGKAGDM ITRIKHGTTG KFKKAHAKQK SALKVQERAD TLKDRLQGQT
RVGPLSANNF RGLSE
//