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Database: UniProt
Entry: A0A0F2M9C2_SPOSC
LinkDB: A0A0F2M9C2_SPOSC
Original site: A0A0F2M9C2_SPOSC 
ID   A0A0F2M9C2_SPOSC        Unreviewed;      1507 AA.
AC   A0A0F2M9C2;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=ATP-dependent helicase STH1/SNF2 {ECO:0000313|EMBL:KJR85679.1};
GN   ORFNames=SPSK_08306 {ECO:0000313|EMBL:KJR85679.1};
OS   Sporothrix schenckii 1099-18.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Sporothrix.
OX   NCBI_TaxID=1397361 {ECO:0000313|EMBL:KJR85679.1, ECO:0000313|Proteomes:UP000033710};
RN   [1] {ECO:0000313|EMBL:KJR85679.1, ECO:0000313|Proteomes:UP000033710}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1099-18 {ECO:0000313|EMBL:KJR85679.1,
RC   ECO:0000313|Proteomes:UP000033710};
RX   PubMed=25351875; DOI=10.1186/1471-2164-15-943;
RA   Teixeira M.M., de Almeida L.G., Kubitschek-Barreira P., Alves F.L.,
RA   Kioshima E.S., Abadio A.K., Fernandes L., Derengowski L.S., Ferreira K.S.,
RA   Souza R.C., Ruiz J.C., de Andrade N.C., Paes H.C., Nicola A.M.,
RA   Albuquerque P., Gerber A.L., Martins V.P., Peconick L.D., Neto A.V.,
RA   Chaucanez C.B., Silva P.A., Cunha O.L., de Oliveira F.F., dos Santos T.C.,
RA   Barros A.L., Soares M.A., de Oliveira L.M., Marini M.M.,
RA   Villalobos-Duno H., Cunha M.M., de Hoog S., da Silveira J.F., Henrissat B.,
RA   Nino-Vega G.A., Cisalpino P.S., Mora-Montes H.M., Almeida S.R.,
RA   Stajich J.E., Lopes-Bezerra L.M., Vasconcelos A.T., Felipe M.S.;
RT   "Comparative genomics of the major fungal agents of human and animal
RT   Sporotrichosis: Sporothrix schenckii and Sporothrix brasiliensis.";
RL   BMC Genomics 15:943-943(2014).
RN   [2] {ECO:0000313|EMBL:KJR85679.1, ECO:0000313|Proteomes:UP000033710}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1099-18 {ECO:0000313|EMBL:KJR85679.1,
RC   ECO:0000313|Proteomes:UP000033710};
RX   PubMed=25480940;
RA   Teixeira Mde M., Rodrigues A.M., Tsui C.K., de Almeida L.G.,
RA   Van Diepeningen A.D., van den Ende B.G., Fernandes G.F., Kano R.,
RA   Hamelin R.C., Lopes-Bezerra L.M., Vasconcelos A.T., de Hoog S.,
RA   de Camargo Z.P., Felipe M.S.;
RT   "Asexual propagation of a virulent clone complex in a human and feline
RT   outbreak of sporotrichosis.";
RL   Eukaryot. Cell 14:158-169(2015).
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:KJR85679.1}.
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DR   EMBL; AXCR01000007; KJR85679.1; -; Genomic_DNA.
DR   RefSeq; XP_016588355.1; XM_016734909.1.
DR   GeneID; 27670186; -.
DR   KEGG; ssck:SPSK_08306; -.
DR   VEuPathDB; FungiDB:SPSK_08306; -.
DR   OrthoDB; 5482994at2759; -.
DR   Proteomes; UP000033710; 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:0042393; F:histone binding; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd04369; Bromodomain; 1.
DR   CDD; cd17996; DEXHc_SMARCA2_SMARCA4; 1.
DR   CDD; cd18793; SF2_C_SNF; 1.
DR   Gene3D; 1.20.5.170; -; 1.
DR   Gene3D; 1.20.920.10; Bromodomain-like; 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; IPR001487; Bromodomain.
DR   InterPro; IPR036427; Bromodomain-like_sf.
DR   InterPro; IPR014978; Gln-Leu-Gln_QLQ.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR014012; HSA_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR029295; SnAC.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR049730; SNF2/RAD54-like_C.
DR   InterPro; IPR000330; SNF2_N.
DR   PANTHER; PTHR10799:SF973; ATP-DEPENDENT HELICASE BRM; 1.
DR   PANTHER; PTHR10799; SNF2/RAD54 HELICASE FAMILY; 1.
DR   Pfam; PF00439; Bromodomain; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF07529; HSA; 1.
DR   Pfam; PF08880; QLQ; 1.
DR   Pfam; PF14619; SnAC; 1.
DR   Pfam; PF00176; SNF2-rel_dom; 1.
DR   PRINTS; PR00503; BROMODOMAIN.
DR   SMART; SM00297; BROMO; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00951; QLQ; 1.
DR   SMART; SM01314; SnAC; 1.
DR   SUPFAM; SSF47370; Bromodomain; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS50014; BROMODOMAIN_2; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51204; HSA; 1.
DR   PROSITE; PS51666; QLQ; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW   ProRule:PRU00035}; Helicase {ECO:0000313|EMBL:KJR85679.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242}.
FT   DOMAIN          157..192
FT                   /note="QLQ"
FT                   /evidence="ECO:0000259|PROSITE:PS51666"
FT   DOMAIN          407..480
FT                   /note="HSA"
FT                   /evidence="ECO:0000259|PROSITE:PS51204"
FT   DOMAIN          590..755
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          901..1052
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   DOMAIN          1353..1416
FT                   /note="Bromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50014"
FT   REGION          69..153
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          519..550
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1174..1305
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1324..1345
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1446..1507
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        69..83
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1182..1203
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1205..1222
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1223..1269
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1325..1340
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1451..1466
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1478..1500
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1507 AA;  168591 MW;  690000784E333E09 CRC64;
     MASVQASAAA MPLANTAPPN GITPQQVQEV YSRFRQMKEQ GVPQTDPDFI KTQQFLLNIQ
     QQQAFKRQMQ HQRDTQQAAQ QAAAAAANGA IMNGGGAPHP GRQAPGFPGT PMGRPMPPNA
     AAGGAAPATP GSAGSGAPAG AGAGAGAGTA ASPVTGHFSQ QQLSLLRHQI QAFKHLSRNA
     GVPMQTQQVI FGQRARRQIA SVSEKLAGTK TPATPTTAAA RKGAAAAASG GADAAKADAD
     GAAPGSQELT APGRKVKSFK TVQSPYESGA VRKTISYFDH GRRINRPVIP GILPTGIDFD
     ALRTEREKIV FNRMSARYAE LKSLPSNISH WDTATNSLTP DDTIKRKAYI EMKCLGLYSL
     QRALRDKIGR QMMHYDNLAM TTNRSNYRRM KRQNVREARI TEKLEKQQRD AREHREKKRH
     SDFLAAVTKH RAELTTTANQ QRNKMQKLGR IMYTQHFNIE KEEQKRIERN AKQRLQALKA
     NDEEAYLKLL DQAKDTRITH LLRQTDGFLH QLASSVKAQQ RDAAERYGGD PNLRPDEPES
     DDDSEDDDRT KKIDYYAVAH RVREEVTEQA NMLVGGRLKE YQVKGLQWMI SLYNNNLNGI
     LADEMGLGKT IQTISLICYL IERKHQPGPY LVIVPLSTLT NWNLEFEKWA PSIARIVYKG
     PPTTRKAQQD KIRQGRFQVL LTTYEYIIKD RPLLSKIKWF HMIVDEGHRM KNSNSKLSAT
     ISQYYHTRFR LILTGTPLQN NLGELWAMLN FVLPNIFKSA TTFDDWFNTP FANTGGQDRM
     ELNEEEQILV IRRLHKVLQP FLLRRLKKDV EKDLPDKTEK VIKCKFSALQ ARLYKEMLNN
     NKLIVGDGKG GKTSARGLSN IIMQLRKLCN HPFVFDEIET VMNPQSISND LLWRTAGKFE
     LLERILPKYK ATGHRVLMFF QMTAIMDIME DYLRYRGFQY LRLDGTTKAD ERSDLLRDFN
     HPDSPYFMFL LSTRAGGLGL NLQTADTVII YDSDWNPHQD LQAQDRAHRI GQKNEVRILR
     LITSTSVEEK ILERARYKLD MDGKVIQAGR FDNKSSETDR DAMLRTLLES ADLQESGDQE
     EMDDEELNMI LARSENELAT FQKMDEERFH DPVYGTAPGC QAVPRLMAEN ELPDIYLADP
     NAVEEEVEVV LGRGARERTK VKYDDGLTEE QWLMAVDDDD DSPEAAAARK QARKDKREQN
     RLKRLANANP LTGSVENTPE GSRASSEEAE PEPEPEPETP VKKRGRKPNA KNEKRKADDE
     DEPAPPAKKR RGPIGRPKAV AAADRAVSGG AASPAGSPKA SMTPQLRGRL QENLRKLYDG
     LMTLEVDDPE PEDPEDKDKD EDDEPLKRII IGPFVKLPSK RDYGDYYVII QKPICMNQIH
     ARIKKGEYHK LTDMQADIKL LCNNCRTYND DGSLLYADAN TIEEFFNAKI AETLAAHPEL
     QALEPGGATK ASSEAPTTTN STPAPAATPL PKIKLVSNGV SLNKSANGSS NGNGEATNGT
     STKTEDE
//
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