ID A0A0D2AE19_9EURO Unreviewed; 1207 AA.
AC A0A0D2AE19;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KIW23142.1};
GN ORFNames=PV07_11365 {ECO:0000313|EMBL:KIW23142.1};
OS Cladophialophora immunda.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Cladophialophora.
OX NCBI_TaxID=569365 {ECO:0000313|EMBL:KIW23142.1, ECO:0000313|Proteomes:UP000054466};
RN [1] {ECO:0000313|EMBL:KIW23142.1, ECO:0000313|Proteomes:UP000054466}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 83496 {ECO:0000313|EMBL:KIW23142.1,
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KN847046; KIW23142.1; -; Genomic_DNA.
DR RefSeq; XP_016243358.1; XM_016398796.1.
DR AlphaFoldDB; A0A0D2AE19; -.
DR STRING; 569365.A0A0D2AE19; -.
DR GeneID; 27350559; -.
DR VEuPathDB; FungiDB:PV07_11365; -.
DR HOGENOM; CLU_000315_16_2_1; -.
DR OrthoDB; 5482994at2759; -.
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; 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; PTHR10799; SNF2/RAD54 HELICASE FAMILY; 1.
DR PANTHER; PTHR10799:SF964; SWI_SNF-RELATED MATRIX-ASSOCIATED ACTIN-DEPENDENT REGULATOR OF CHROMATIN SUBFAMILY A CONTAINING DEAD_H BOX 1; 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 610..778
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 962..1124
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 124..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 228..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 310..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1108..1130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1152..1207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..169
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..371
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1158..1207
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1207 AA; 135259 MW; 941572177C928A00 CRC64;
MPSDDSLSQS DDELFNPNYK PAHETVETLP LYRPNMSDAD SDIETLGILP VHPGAKSQNV
NSIRQTQPTQ IIDRTATTMS SSPLKPGVVQ VAASSPMTAP NPQRKPTGIL ASAMAPAGTM
FRKPYVAPQP RPVPITIDSD DDGPAYRGGS SDDDSHGVRS NDIKTSTFVR KKKSPGTIPE
SPQAAQNSAL NRFMEITARS MFRGSPNSMS SAGSNGVKRS ADVNANAYGS VSKRPRQTGP
ARALPVTSSP PAQQQEEMEL DDISDYGTRR KVNRLMSMLR AVTVRECYEA LMTKKGNYDD
AVDVLLVRSE KRQSQSKNSA VDLTGSDDEL MPTPAASRPV PQHTSVGRQQ AKVPQKSITE
KWSSTQNMRK PPKTIDVFET PPPKKKRTLV RGRKHSSSPQ PVPEGAVQKP KRVVAIQSDE
SDAGGLAVTS DDENRTGFQS RVLDLFNTCS AADLADIASI NRDLAEHFLS KRPFKNLMAI
RQIEDPKLKP TKTKRKTAPI GDRIVDKVED MLESYEAVDY LVKKCQTLAK PLSDEMRSWG
VNVTGSQEGE LDIASLQAPL PSHDSGIGTP VSDEEDIKRS GQKRFIGQPS IMADDIQMKD
YQVVGLNWLS LLYKKGLSCI LADDMGLGKT CQVIAFLAHL FEQGKMGPHL VVVPAATLEN
WLKEFQRFCP ALNVEPYYAT NPTERLTLRE FLDDNREDVN VIVTTYTIAK GKDDAPWLRS
FGFDCTIYDE GHVLKNADSQ VASKLVRIQC NFRLLLTGTP LQNNLKELIS LLAFLMPALF
REKAEALKNI FTHNFKALDN NHEMLLSAQR IQRAKSMLTP FILRRKKYQV LKDLPKKERR
VEFCDLSPEQ SEIYQMWLDK AYEIRARRER GENVSQESTN ILIKLRLAAI HPFLFRRLYP
DKQLPVIAKQ CLKVDLWRES NPDLIVTELV EYSDMEIHTL CDKHTQLRRF ALNGDEWRAS
GKIEKMIELL RKFISEGHRT LIFSQFVMVL DILELALERE GISSFRLDGA TKVSERQDLI
DEFSADDNDT PVFMLSTKAG GAGINLAKAN KVIIFDSGFN PQDDIQAENR AHRIGQEKDV
EVIRLISRGT VEEQIYAMGL TKLKLDEQVA GDGEEQPPRK ENEESEKEVE GRMMVEDMFF
KKIDVEPLEQ VKAEVSSPIK QRSDRRSPSL EREDLDVEGQ AARRGRKGSV DLPNRTRVRR
AKTKVED
//
