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Database: UniProt
Entry: A0A0D2DPJ6_9EURO
LinkDB: A0A0D2DPJ6_9EURO
Original site: A0A0D2DPJ6_9EURO 
ID   A0A0D2DPJ6_9EURO        Unreviewed;      1333 AA.
AC   A0A0D2DPJ6;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KIW64157.1};
GN   ORFNames=PV04_09111 {ECO:0000313|EMBL:KIW64157.1};
OS   Phialophora macrospora.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Phialophora.
OX   NCBI_TaxID=1851006 {ECO:0000313|EMBL:KIW64157.1, ECO:0000313|Proteomes:UP000054266};
RN   [1] {ECO:0000313|EMBL:KIW64157.1, ECO:0000313|Proteomes:UP000054266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 27337 {ECO:0000313|EMBL:KIW64157.1,
RC   ECO:0000313|Proteomes:UP000054266};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Capronia semiimmersa CBS27337.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KN846961; KIW64157.1; -; Genomic_DNA.
DR   STRING; 5601.A0A0D2DPJ6; -.
DR   HOGENOM; CLU_001832_4_0_1; -.
DR   OrthoDB; 53793at2759; -.
DR   Proteomes; UP000054266; Unassembled WGS sequence.
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; 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; 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   SMART; SM00591; RWD; 1.
DR   SUPFAM; SSF54768; dsRNA-binding domain-like; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF54495; UBC-like; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS50908; RWD; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT   DOMAIN          402..500
FT                   /note="RWD"
FT                   /evidence="ECO:0000259|PROSITE:PS50908"
FT   DOMAIN          585..756
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          814..977
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          206..228
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..21
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        29..51
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        206..220
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1333 AA;  147319 MW;  26128B7981614147 CRC64;
     MAPKKASTSS KGNSSKNLSL GVPDSEHIVF TNKKGDKKKQ EQKDPEGPPR PDAKKIIGGA
     SWTGKLPVNL LSELCQRQKW NKPDYQMRQV PSQNGSEKVY RACVVLSKTD PKSGEITKLP
     PFQLPATDVH LADQPSALEA RHLAAAYTLY RLQSMKNLSM ALPPTYRDLW KGDFQRLKDE
     DVKEGRAWKY DADPFAAESK RQEIKTAMEK RKEEQARKPP KPESVSLVGL GSSSVGAKGW
     DRAPRIELGQ DARTRIESLI RTHSVWNRSA LAMSERDKAS LEIDLAKSGF QHSHIQEALD
     CCGTREEVLE WLLIHVPEDC LPAWSFPPGY SAGVTLVTSD LATDAKVKRL ALGGYATQLC
     LQALRDNDGD EAQAAEALQS KLVPPKEAAS LGVTSDAHVW EEEMNALESI LDDRFKASGP
     DQCSIRPDPA SDIPATYHFR RPVSGYPHVP PMVTIEAPSL PSYVRLSAVK KAITYAQDSL
     LGDSMVFNIL EWLQSSMPDI TQNPGKLSDL EIVSGSMRKE LPLTKTNAQM LPLRSRTAER
     INLKDSRSNQ VMFDTWNARQ SSDSQRKMNA ARQRLPAWSK QAEIVRVVNG AQVTLVTGET
     GSGKSTQAIQ FILDDAIQNM RGSSANLICT QPRRVAALSL SERVSAERCC NEGDEVGYII
     RGDSKTSSRT KITFQTTGVL LRRLQSSPSI KAALAGVTHV FIDEVHERSL DTDFLLALLR
     DGLPMLPHLK VVLMSATLDA DIFANYFGGD RVGRVHIEGR TYPVEDYYLD DVLRLTGSGN
     KRDFDADGEQ GIGKAIQGLG IGLNYELIAS LVRHIDRELS NARGGILIFM PGTMEIDRCI
     KSLADMANIH VLPLHASLTP AEQRLVFKQP PAGKRKVVVA TNVAETSITI EDIVAVIDSG
     KVKETNYDPI SNIVRLEEVW ASRAACKQRR GRAGRVQAGN CYKLFTKNVE ANMAAAAAPE
     IHRTPLEQLC LSVKATGSDR KVEEFLARTV SPPDSRAVAT AMKTLQRMGA LEHDRLTGLG
     TYLAMIPADL RCAKLLVYGV LFDCVETCLT MAAVLATKSP FVSPRDKRDE AKDARMSFPT
     SEGDLMLDSA AFDQWKELFV TSRYRDMQNW CSSKFLSQQT LRDIDSTRRQ LLDSLIEAGL
     LPPAYHNNSS EGNRHKGNNM LLRALVAGAL YPQIARIQMP DKKYIASMSG AKELDPEAKT
     IKYFNEENGR VFVHPSSVLF DAQSFSGNAS FVSYFTKMET SKTFIRDLTP LNAYALLLFG
     GPIEVDTSGQ GVIVDGWLRL KGWARIGVLA SRLRALLDDE LRRRIDARGA VVADDTGLFE
     IVRHLVEFNG QDR
//
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