ID A0A0N0NRU3_9EURO Unreviewed; 991 AA.
AC A0A0N0NRU3;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Putative ATP-dependent helicase {ECO:0000313|EMBL:KPI45491.1};
GN ORFNames=AB675_966 {ECO:0000313|EMBL:KPI45491.1};
OS Phialophora attinorum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Phialophora.
OX NCBI_TaxID=1664694 {ECO:0000313|EMBL:KPI45491.1, ECO:0000313|Proteomes:UP000038010};
RN [1] {ECO:0000313|EMBL:KPI45491.1, ECO:0000313|Proteomes:UP000038010}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 131958 {ECO:0000313|EMBL:KPI45491.1,
RC ECO:0000313|Proteomes:UP000038010};
RA Moreno L.F., Stielow B.J., de Hoog S., Vicente V.A., Weiss V.A.,
RA de Vries M., Cruz L.M., Souza E.M.;
RT "Draft genome of the ant-associated black yeast Phialophora attae CBS
RT 131958.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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:KPI45491.1}.
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DR EMBL; LFJN01000001; KPI45491.1; -; Genomic_DNA.
DR RefSeq; XP_018005454.1; XM_018150225.1.
DR AlphaFoldDB; A0A0N0NRU3; -.
DR STRING; 1664694.A0A0N0NRU3; -.
DR GeneID; 28742094; -.
DR OrthoDB; 200191at2759; -.
DR Proteomes; UP000038010; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR CDD; cd18008; DEXDc_SHPRH-like; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR45626:SF14; ATP-DEPENDENT DNA HELICASE (EUROFUNG); 1.
DR PANTHER; PTHR45626; TRANSCRIPTION TERMINATION FACTOR 2-RELATED; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000313|EMBL:KPI45491.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000038010}.
FT DOMAIN 273..458
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 751..913
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 195..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 584..613
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 673..744
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 935..991
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..51
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..69
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..92
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..139
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..156
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..217
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 673..691
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 700..738
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 948..964
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 966..980
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 991 AA; 109928 MW; 39094ABA1166720A CRC64;
MPLSPSGGNV GYPSLGDTDS PTFGKPSALG TTASSHTKQN SQSNSSAQRA PVQKKYDHLF
VKTDRKPQYH KPQVSSNPFH QLKNQVVEKA QETINKLTDR SDKPSNGAGS QSDPFIIPDP
MRQQSYQPRP APPPAPMYSS AVNTNPYFKP ASTSNFVYPT ASASHSQFDD FSSSDPLTYM
DAGKANDNIK ALLEGAFEDE EEKKPRTRRK DKPQNGDVDA LAAKLGDVKV DDKGDESEEE
ENDGSVEGLK VKLLPHQIDG VEWMKHKELG TRKTRGVFPL GGILADDMGL GKTIQSIALI
LSNKKPTAEE IEAHPKRKLP QGVNKGTLVV APLALIKQWE GELKDRIEDS HALRICVHHG
PKRAKSSKDL KGYDVVITTY STLTSEHADS GGDLKTGCFG LHWWRVILDE AHSIKNRNAK
ATKAACALDA HYRWCLTGTP MQNNLDELQS LIHFLRIKPY DDLNVWREQI TKPMNGGRGG
LAIKRLRAYL GAFMKRRTKD ILKQDGGLTT GTKATGKGKE AFKIVKRTVD HIEADFTPQE
RAFYTKLESR TDKSLELMMA GSKISYASAL VLLMRLRQAC NHPRLTGSDL SKEKDSAAGS
GNQTPSRKKA TDDDMDAIAG LLGGLSVETK LCDMCQIELT SEQSSAGNVR CDECEADLQD
DAFTIKNFKS KDKAKKHRKA SMAKPLREKR RQARKAIIDS DDEDEEDVVP AKDESESESG
DDDDDEESED DEIYGSSEDD NPQTDLIAST KIRHLLKILS TDSAEHKYIV FSFFTSMLDL
IEPFLAAQHI NFVRYDGAMR NDAREASLES LRTNAKTRVL LCSLRAGSLG LNLTAASRVV
ILEPFWNPFV EEQAIDRVHR LNQTKDVKVY KMTIKDTVEA RILELQEKKR ELANATIEGQ
KAGGVKLTLQ DMLNLFKHDG GADDKRLDMI GMKPSAGLLE KGESTRERST PPVSINSYNH
SNGGRRILSE AEKERQKQRQ EAASGVYGRR Y
//
