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
//