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}.
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; 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
//