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Database: UniProt
Entry: F2PJG0_TRIEC
LinkDB: F2PJG0_TRIEC
Original site: F2PJG0_TRIEC 
ID   F2PJG0_TRIEC            Unreviewed;      1113 AA.
AC   F2PJG0;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   24-JAN-2024, entry version 61.
DE   SubName: Full=SNF2 family helicase/ATPase {ECO:0000313|EMBL:EGE02027.1};
GN   ORFNames=TEQG_01067 {ECO:0000313|EMBL:EGE02027.1};
OS   Trichophyton equinum (strain ATCC MYA-4606 / CBS 127.97) (Horse ringworm
OS   fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=559882 {ECO:0000313|Proteomes:UP000009169};
RN   [1] {ECO:0000313|Proteomes:UP000009169}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4606 / CBS 127.97 {ECO:0000313|Proteomes:UP000009169};
RX   PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA   Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA   Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA   Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA   Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA   Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT   "Comparative genome analysis of Trichophyton rubrum and related
RT   dermatophytes reveals candidate genes involved in infection.";
RL   MBio 3:E259-E259(2012).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. ISWI subfamily.
CC       {ECO:0000256|ARBA:ARBA00009687}.
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DR   EMBL; DS995720; EGE02027.1; -; Genomic_DNA.
DR   AlphaFoldDB; F2PJG0; -.
DR   VEuPathDB; FungiDB:TEQG_01067; -.
DR   eggNOG; KOG0385; Eukaryota.
DR   HOGENOM; CLU_000315_0_2_1; -.
DR   Proteomes; UP000009169; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0031491; F:nucleosome binding; IEA:InterPro.
DR   CDD; cd17997; DEXHc_SMARCA1_SMARCA5; 1.
DR   CDD; cd00167; SANT; 1.
DR   CDD; cd18793; SF2_C_SNF; 1.
DR   Gene3D; 1.10.10.60; Homeodomain-like; 2.
DR   Gene3D; 1.20.5.1190; iswi atpase; 1.
DR   Gene3D; 1.10.1040.30; ISWI, HAND domain; 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; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR044754; Isw1/2_DEXHc.
DR   InterPro; IPR015194; ISWI_HAND-dom.
DR   InterPro; IPR036306; ISWI_HAND-dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR001005; SANT/Myb.
DR   InterPro; IPR017884; SANT_dom.
DR   InterPro; IPR015195; SLIDE.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR000330; SNF2_N.
DR   PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR   PANTHER; PTHR45623:SF49; ISW-1; 1.
DR   Pfam; PF09110; HAND; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF09111; SLIDE; 1.
DR   Pfam; PF00176; SNF2-rel_dom; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00717; SANT; 2.
DR   SUPFAM; SSF101224; HAND domain of the nucleosome remodeling ATPase ISWI; 1.
DR   SUPFAM; SSF46689; Homeodomain-like; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51293; SANT; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Helicase {ECO:0000313|EMBL:EGE02027.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242}.
FT   DOMAIN          203..368
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          499..650
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   DOMAIN          860..912
FT                   /note="SANT"
FT                   /evidence="ECO:0000259|PROSITE:PS51293"
FT   REGION          1..73
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          131..174
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          818..839
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1036..1113
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        24..43
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        44..60
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        822..839
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1036..1067
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1080..1106
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1113 AA;  127667 MW;  5F8C2D00391C3B70 CRC64;
     MAPVQELPST GDEDVTMVDA AEYQPSDDAR DDQDMKEYQD TPDYTDSDTN PNTTASSVAG
     DTAPDGRKRR TEAFQLRKSV LGKKHGRLDE SMEDDSTRRF RYLLGLTDLF RHFIDTNPNP
     RIKEIMAEID RQNEAKSGSR KGATRKGGAA GERRRRTEQE EDAELLKDEK RGGKTETVFQ
     QSPSFIQGGE MRDYQIAGLN WLVSLHENGI SGILADEMGL GKTLQTISFL GYLRHICGIT
     GPHLVAVPKS TLDNWKREFG KWTPDVNVLV LQGAKDERHQ LINERLVDEK FDVCITSYEM
     ILREKSHLKK FAWEYIIIDE AHRIKNEESS LSQIIRVFKS RNRLLITGTP LQNNLHELWA
     LLNFLLPDVF GDSEAFDQWF SNQEADQDTV VQQLHRVLRP FLLRRVKSDV EKSLLPKKEL
     NLYVGMSEMQ VKWYQKILEK DIDAVNGAQG NRESKTRLLN IVMQLRKCCN HPYLFEGAEP
     GPPYTTDEHL IDNSGKMVIL DKLLNRLFKQ GSRVLIFSQM SRVLDILEDY CVFRGHEYCR
     IDGSTAHEDR IQAIDEYNRP GSKKFVFLLT TRAGGLGINL TTADIVILFD SDWNPQADLQ
     AMDRAHRIGQ TKQVVVFRFI TEKAIEEKVL ERAAQKLRLD QLVIQQGRAQ QQAKNAASKN
     ELLSMIQHGA SDVFSSTGGT FGSGKDISED DIEAILKKGE ERTAELKNKY EKLGIDDLQK
     FSSENAYEWN GKDFTNRKKD IGLNWINPAK RERKDQSYTI GSFYKQTFTK PAEPKPKVPK
     APKQTTIHDW QFFPPKLQEL QDKETAYFHK EIGYKAALPE GPEESVSDRE AERELEQQEI
     DNAVPLTTEE QEEKAKLSAE GFYNWNRRDF QQFINGSAKF GRTNYEDMAT EVDSKTPEEI
     KEYAKVFWKR YTEILDYPKY IRIIEQGEEK MRRMNQQRKL LRKKMGQYRV PLQQLKINYT
     VSTTNKKVYT EEEDRFLLVM LDRHGVDGEG LYEKIRDEIR ESPLFRFDWF FLSRTPVEIG
     RRCTTLLNTI AKEFEGDNKE TNGDNKAKAR TRDEETENGD DTGPAKKKSK GAAPAVNKKL
     KAVQSNSKAT STNTSRAGSV SSSGPTKSKS KKR
//
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