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Database: UniProt
Entry: A0A177C0Q6_9PLEO
LinkDB: A0A177C0Q6_9PLEO
Original site: A0A177C0Q6_9PLEO 
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
//
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