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Database: UniProt
Entry: A0A0D2BW87_9EURO
LinkDB: A0A0D2BW87_9EURO
Original site: A0A0D2BW87_9EURO 
ID   A0A0D2BW87_9EURO        Unreviewed;      1090 AA.
AC   A0A0D2BW87;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KIW22660.1};
GN   ORFNames=PV07_10935 {ECO:0000313|EMBL:KIW22660.1};
OS   Cladophialophora immunda.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC   Cladophialophora.
OX   NCBI_TaxID=569365 {ECO:0000313|EMBL:KIW22660.1, ECO:0000313|Proteomes:UP000054466};
RN   [1] {ECO:0000313|EMBL:KIW22660.1, ECO:0000313|Proteomes:UP000054466}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 83496 {ECO:0000313|EMBL:KIW22660.1,
RC   ECO:0000313|Proteomes:UP000054466};
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 Cladophialophora immunda CBS83496.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; KN847046; KIW22660.1; -; Genomic_DNA.
DR   RefSeq; XP_016242876.1; XM_016398314.1.
DR   AlphaFoldDB; A0A0D2BW87; -.
DR   STRING; 569365.A0A0D2BW87; -.
DR   GeneID; 27350129; -.
DR   VEuPathDB; FungiDB:PV07_10935; -.
DR   HOGENOM; CLU_000315_2_7_1; -.
DR   OrthoDB; 200191at2759; -.
DR   Proteomes; UP000054466; 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: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:SF51; SINGLE-STRANDED DNA-DEPENDENT ATPASE (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   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054466}.
FT   DOMAIN          455..644
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          921..1073
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..101
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          125..161
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        28..64
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1090 AA;  122012 MW;  3270C2DD36917BFE CRC64;
     MASNAHLLLD PKSMKKMSKM SGGPGRRTPL GDQSSSEGPQ SPQKTGSTTS HSMSPSNSFN
     NVPKLPNAYD HRSLLDPGRS RQPLKSTTFL KGETGDKDSA QKSMLESIYG VEDRISNPRK
     KVKLTAEDQR EQTPKLGISS HRRGNGIVGE YMRPDPDQAP EVTKKSLVDL TNDEDDDGDD
     DDVQIVSSWS LDDQEVCYGH IATVAQAYLL PKPKVAGNIF HSEREWPVMK CTLVRKPSKD
     MIIDVQDPSD TAFARVHPDF AAVLAQAMDT MKGFRTQAKL INRRKKPDEW PHKACSEQLK
     MVVNVYGRRG DVDRVGRLFG NNNFWLRAPM ASEPGIPIVN PHAHNKSLFP TLRLTGQART
     LPDTRTLEEA TEAVSKLFDS FANSSRPLVE TSAPPSVVTT PLLSHQKQAL TFLLRQEQPR
     TFGSDEAENS SLWRRKQRRN GDFAYHEVVT GLSVKDEPEQ VLGGLLADVM GLGKTLEALS
     LIASTLEEAE SFANEKVVRD NQDMQHIILS NTKATLIVCP TSTVKNWEDQ IAQHIKPGTM
     DYHVYHGPNR EKNPYKLLRY EMIITTYGVV ASEFSKAAVT LSPLRQLKWF RIVLDEAHTI
     REQKALQSQA CYSLEAQRRW CLTGTPIQNR LDDLGSLTRF LRMYPYDTAG RFNQYIRGPA
     QAGDPAFLKA LRVFVDSFTL RRLRDRIDLP ERKDYVAKLT FSNEERILHD FFKGIAQVQI
     EQLSRTKEKN SGVQHHVLRG IMTLRLICAH GRELLKEKDL KLLKGISATD AIDVDEDAGP
     PTISRKAAYE ALNLRTEAEL DVCRNCERSI TKDVVKTEAD DEEQALRCFI LPCFDLVCAD
     CFNPAKASFD SVPDKEAVTC PFCSAQIAAQ YVGFSGSTAQ EILVAPDDTI AEPEEEDIVQ
     TYSGPHTKTK ALLADIEQMN QDSQALEAAG EAPLKCVVFS EFTSHLDLIE RALTDHGHSF
     VRIDGTMSLN SRKKSMDALA SDNNIRILLA SIKAAGQGLN LTAASRAFIM EPMWNPAAEA
     QAVDRIYRIG QKRPVLVKRY QIDNSIEGKI VELQKRKQQL ADVSVNQNYK QLSKQEVREQ
     HMKEILALFK
//
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