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Database: UniProt
Entry: A0A1B8C4Z1_9PEZI
LinkDB: A0A1B8C4Z1_9PEZI
Original site: A0A1B8C4Z1_9PEZI 
ID   A0A1B8C4Z1_9PEZI        Unreviewed;      1325 AA.
AC   A0A1B8C4Z1;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OBT41875.1};
GN   ORFNames=VE00_07376 {ECO:0000313|EMBL:OBT41875.1};
OS   Pseudogymnoascus sp. WSF 3629.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1622147 {ECO:0000313|EMBL:OBT41875.1, ECO:0000313|Proteomes:UP000091997};
RN   [1] {ECO:0000313|EMBL:OBT41875.1, ECO:0000313|Proteomes:UP000091997}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WSF 3629 {ECO:0000313|EMBL:OBT41875.1,
RC   ECO:0000313|Proteomes:UP000091997};
RA   Palmer J.M., Drees K.P., Foster J.T., Lindner D.L.;
RT   "Comparative genomics of Pseudogymnoascus destructans, the fungus causing
RT   white-nose syndrome of bats.";
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000091997}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WSF 3629 {ECO:0000313|Proteomes:UP000091997};
RX   PubMed=29295979; DOI=10.1038/s41467-017-02441-z;
RA   Palmer J.M., Drees K.P., Foster J.T., Lindner D.L.;
RT   "Extreme sensitivity to ultraviolet light in the fungal pathogen causing
RT   white-nose syndrome of bats.";
RL   Nat. Commun. 9:35-35(2018).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC       {ECO:0000256|ARBA:ARBA00007025}.
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DR   EMBL; KV454648; OBT41875.1; -; Genomic_DNA.
DR   STRING; 1622147.A0A1B8C4Z1; -.
DR   OrthoDB; 200191at2759; -.
DR   Proteomes; UP000091997; 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   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
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   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 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   InterPro; IPR018957; Znf_C3HC4_RING-type.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR45626:SF24; ATP-DEPENDENT HELICASE ULS1; 1.
DR   PANTHER; PTHR45626; TRANSCRIPTION TERMINATION FACTOR 2-RELATED; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00176; SNF2-rel_dom; 1.
DR   Pfam; PF00097; zf-C3HC4; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000091997};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT   DOMAIN          483..671
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          831..882
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          1100..1258
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          72..177
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          213..281
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          299..318
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          902..968
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1014..1080
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1287..1325
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        76..137
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        142..156
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        157..177
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        213..230
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        261..281
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        911..936
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1044..1062
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1063..1080
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1290..1325
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1325 AA;  146637 MW;  43F9F4B7F40F9848 CRC64;
     MASASHLSPL EAYVSPDELA DELVLQKTLL FTLDNTTEGS ERAEADIKAE IARIETQLRA
     LRGGVTGPHI GASVLGGSIP QQQQTNNFES ASPFSSYNPT STGPFSSDTM DPSHPPSSSA
     SGSTSMKDSS ANFSLPSRKR SFDGLHGLDG SRKTGNKSRR TSPSPSTGVS TSYATTYTDP
     VTRELELHKI RQREIEEAAA KLKKDREYAR NLQDRYSASS PSQSDSRPAV SKRPSAYDRM
     MGTSHQPPPS RSKKHDSQNT NSQDSEVPVV TQGSQPGQRP HAYQSVDLTL NGPAFLSTRG
     SDTLPKIPGS YPDQDSDSDI EIISSADFRE NGRGHHLSRP PHPTNVGYGS YLSYTRQGPP
     STLPYLGGYP SNNSYYPNTY GQSISGAYPG MASPSMNAPL AQILNQTSAV DYVAMRDRLN
     QGLAGEIYNY VTDPRKTEKE IQDLLENIRP DTEIPVEDRE GTPEGLKYPL YEHQKLALTW
     LKAMEEGSNK GGILADDMGL GKTISTLALL LSRPSYNKAR KTTLIVGPVA LIRQWEREIL
     TKIVSSHRLS TFVYHSGKKA TWSTLRTHDV VLTTYGTLAA EYKRYMDIEK RKEAHPGMDD
     TPYQSTLPFL GRNSRWYRVV LDEAQCIKNR NTKSAQAASL LDAETRFCLT GTPMMNGVHE
     LYSLIHFLKI KPYNEYSRFS SEFSCLTKGT GSEYNMKRAM KKLQAVLKAI LLRRTKQSQI
     DGKPILVLPE KTEVVSNAIF NEDEQEYYTS LEKKTQLQFN KYLKAGTIGK NYSNILVLLL
     RLRQAACHPH LIMDYEEAPT EATAEEMLKL AKTLLPDVIG RIMDATVPFE CPVCYDPVPN
     PSIVVPCGHD TCAQCLVRIT SSFDQAIANG EDSTSAKCPT CRGAVDLKKI IDYETFQRAH
     MPNSESLTGN ADDIDDGDSD SYYSDSDSDS DNGLEEADEN GNIRDFIVPD DYETSSDEDD
     DLETRAKETK PKIEVDCKKE AIKYEEGSKE ALSKMLGGSD GSDDDLPADI FATFRGQPKR
     EDEKSQLASK SKPLGSKAIS QDKSKKSHRS KKLPRRKKSG KKPEDKHVSL AELKKKASKS
     ADGRRQYMRY LKKNWVSSSK IDKCMDILRN SAPDVKTIIF SQFTTLLDLM EVPIHSERIG
     FGRYDGGMSA DARNDAIVRF TDDPRCKILL VSLKAGNAGL NLVAASQVII LDPFWNPFVE
     MQAVDRAHRI GQQKPVSVHR ILVEGTVEDR IIELQNRKRK FVDAALDENA SRSVGRLGRD
     ELVFLFGNND GPSRATMDRP RVSHDTGMVN HGGLGSNTQS FRSDMPVYPS LGGSGSSSAF
     SSYSR
//
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