ID A0A1V8SGU3_9PEZI Unreviewed; 1168 AA.
AC A0A1V8SGU3;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Helicase ATP-binding domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=B0A48_15623 {ECO:0000313|EMBL:OQN98356.1};
OS Rachicladosporium antarcticum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Cladosporiales; Cladosporiaceae; Rachicladosporium.
OX NCBI_TaxID=1507870 {ECO:0000313|EMBL:OQN98356.1, ECO:0000313|Proteomes:UP000192596};
RN [1] {ECO:0000313|Proteomes:UP000192596}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCFEE 5527 {ECO:0000313|Proteomes:UP000192596};
RA Coleine C., Masonjones S., Stajich J.E.;
RT "Genomes of endolithic fungi from Antarctica.";
RL Submitted (MAR-2017) 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:OQN98356.1}.
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DR EMBL; NAJO01000046; OQN98356.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V8SGU3; -.
DR STRING; 1507870.A0A1V8SGU3; -.
DR InParanoid; A0A1V8SGU3; -.
DR OrthoDB; 200191at2759; -.
DR Proteomes; UP000192596; 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: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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000192596}.
FT DOMAIN 420..610
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 942..1103
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 36..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 239..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 749..768
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 824..858
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 878..941
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 352..389
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 74..89
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..144
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..190
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..270
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 750..765
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 834..858
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 900..917
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1168 AA; 128398 MW; C03B8E58BC9248B7 CRC64;
MTSGAQQQFV DVMAAPRSDM IAPCDSAYDW MTEPKQRSPV RGTFKPLNTL AAHTPPFHST
AASLAKAGSV SPSPDPGNED TSPITRILAG RSPSRSRPPE IQVRTTQAGS IHRDSAQAAG
QGSRMVSERD PSRTSSSTYL SPQKQDHRLP LANISAKMQS PSPQASAPAR VADNVISKPS
QPQFGTASPL RNPLQKKKPD PFFVPQVRTT YQRSPPVASA ATQRTVAPPV PVENRAFYLP
GQVPRPTNPP NATTQRAPAP MFSSLGPKTT YQPFVPPRQV VDLTRKDDDE DRFDPDAAIR
AESRSFGAAD PYMYVDSAQA SENLKNLLEG AFDDEEEKSS TRLRTRAARK ATKEAEKQTK
SLAAQLAALE VKVTKKEEAE EEEAEEDEED GTVEGLTVKL LPHQVEGVKW MIDKEIGQRK
RNGVLPHGGI LADDMGLGKT VQSVALLLTN PRPAADAKPD FPKQKMPGKG VTKCTLVVAP
LALIKQWEGE IKSKVTRSHS MKVLIHHGPS RTKSAAELKK YDVVITTYQI LASEHAGSSL
DRPGGPRIGC FGVHWYRLIL DEAHTIKNRN AKSTQACYAL ESWYRWCLTG TPMQNNLDEL
QSLIKFLRVK PYCEMSEWKN SITGPMKNGR GGIAMKRLQL FLQAFMKRRT KNILKKEGAL
NFGGKTDEDG KPKSGGMQIV KREVFTTECV FDDAEQQFYD RLSARAESRL KDIQESGKGD
YIGALVILLR LRQACNHPHL IEAAMSKDKD ALTTGSTQSG AQTPRKMKVD TDEMDDLASL
MGGVTVQNKS CDVCQADLSA QATKSGAGRC EDCEEDLRVL RGKERKKKQE KRAKRESIKT
EESRAAPARR NRKVLIDSDD EDDAGEWIAA GPERYIDYGR AGGTDDEDAE GGGDTLGSVD
TGDEDSEPSD SVSENDEDSG PDSPIIGNLA PSHKPAHKPS TKIRHLLRIL HAETPKHKTI
VFSQFTSMLD LIEPHMRHAS IRFVRYDGSM RPDAREASLN SLKTDPKTRV LLCSLKCGSL
GLNLTAASRV VIVEPFWNPF VEEQAIDRVH RLNQTVDVKV FRLTVLNTVE ERILALQEKK
RELAAAALEG GKTVGKLSMQ DIMSLFRRDA EIGGSKEDVE FEKKFGKESS VLHGERSQEG
GFVSGVAGDA RGGGEAIRGE HAIFGRRW
//
