ID A0A2T4C9R8_TRILO Unreviewed; 1094 AA.
AC A0A2T4C9R8;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Chromatin remodeling factor mit1 {ECO:0008006|Google:ProtNLM};
GN ORFNames=M440DRAFT_1327913 {ECO:0000313|EMBL:PTB78317.1};
OS Trichoderma longibrachiatum ATCC 18648.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=983965 {ECO:0000313|EMBL:PTB78317.1, ECO:0000313|Proteomes:UP000240760};
RN [1] {ECO:0000313|EMBL:PTB78317.1, ECO:0000313|Proteomes:UP000240760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18648 {ECO:0000313|EMBL:PTB78317.1,
RC ECO:0000313|Proteomes:UP000240760};
RG DOE Joint Genome Institute;
RA Aerts A., Atanasova L., Chenthamara K., Zhang J., Grujic M., Henrissat B.,
RA Kuo A., Salamov A., Lipzen A., Labutti K., Barry K., Miao Y., Rahimi M.J.,
RA Shen Q., Grigoriev I.V., Kubicek C.P., Druzhinina I.S.;
RT "Multiple horizontal gene transfer events from other fungi enriched the
RT ability of initially mycotrophic Trichoderma (Ascomycota) to feed on dead
RT plant biomass.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; KZ679129; PTB78317.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T4C9R8; -.
DR STRING; 983965.A0A2T4C9R8; -.
DR Proteomes; UP000240760; 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:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd18660; CD1_tandem; 1.
DR CDD; cd17919; DEXHc_Snf; 1.
DR CDD; cd15489; PHD_SF; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 2.40.50.40; -; 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; IPR016197; Chromo-like_dom_sf.
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; IPR041684; Znf-PHD-like.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45623:SF13; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED; 1.
DR PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR Pfam; PF15446; zf-PHD-like; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00249; PHD; 2.
DR SUPFAM; SSF54160; Chromo domain-like; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 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 Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000240760};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 515..687
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 820..979
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 16..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1070..1094
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..87
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1094 AA; 124347 MW; 8B3896A87E8E2110 CRC64;
MSFNTSVVDQ EQDELALEAH QSSEDDNFLP VVSDLALKKG RPSRAVQRSR RLKKQQKEDN
TKRARTQLED SDIEFEQPRR SARATRNRTN MQDDAFMEDD DSFYVVDDKP AGTPKVISVR
EVFQPVAPDS DFGSVHMQSC HTCGGSRQRG QLLYCQGCCL AYHKNCIGYR SNREHLATKV
GEDDFVLQCR FCLNIYSKKD SSAPRHSACQ QCKKDGRSCA PFSQKKTARQ EEKLRVENGG
VDPVTPVSPE LINNSDNVLF RCSMCHRGWH VDHLPPTGTD AIETDVKSER LKEYSVDWRC
TDCSSAKGKM HRLIAWRPVS QTDDRPAYAD VSEDDREYLI KWQDMSYRHC SWAPGAWVFG
VSAGAMRTSF AKRALEQDLL KFTTEEAIPD EYITPDIIFK VKMDRSGAMG KTKADDLANV
SHVKKILVKF HGLGYDDVVW DSPPSPENPR VYSAFVEAYR EYVEGKHFEP GSANKMKERI
KLYKNSPFVE VDTQPSGLTR GKLMGYQIEG LNWLLQNFHQ NRSVVLADEM GLGKTVQVVG
LVTSLILDAP KCWPFLIVVP NATCSNWRRE FKQWAPGVRV VAYHGGREPQ ELAYKYELFP
DGSTDMKAQV VIMSYDSAQD PRTSALFKSV SWKGLVVDEG QRLKNDQNLL YTALRAMKVP
FRLLLTGTPL QNNKRELFNL LQFIDEKQNA EKLDEEYAVL DKDNLPKLHE KIRPYFLRRT
KLGVLKFLPP MAQIILPVTM TVIQEKLSKS IMAKNPQLIR AVFANSKMNA KDRGSLNNIL
MQLRKCLCHP FMYSEAIEER HNDPTVVHRN LVEASAKLLL LEIMLPKLKE RGHRVLIFSQ
FLQQLDIVED FLNGMGYGYR RLDGSISSLE KQRRIDAFNE PGSELFAFLL STRAGGVGIN
LATADTVIIM DPDFNPHQDI QALSRAHRIG QKNKVLCFQL MTKDSVEERI MEIGRKKMAL
DHALIESMDD DELEGADLES ILKHGAQALF DEGYQKTAIH YDSASVDKLL DRSQMEKSAA
VDDNSAEGQF TYARVWSNDK LGFEETADLT EEQAPEPIGS SVWDQILAQR EEEARREAET
SKEVLGRGAR RRMV
//
