ID A0A2T4ANS9_TRIHA Unreviewed; 1671 AA.
AC A0A2T4ANS9;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:PTB58721.1};
GN ORFNames=M431DRAFT_75560 {ECO:0000313|EMBL:PTB58721.1};
OS Trichoderma harzianum CBS 226.95.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=983964 {ECO:0000313|EMBL:PTB58721.1, ECO:0000313|Proteomes:UP000241690};
RN [1] {ECO:0000313|EMBL:PTB58721.1, ECO:0000313|Proteomes:UP000241690}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 226.95 {ECO:0000313|EMBL:PTB58721.1,
RC ECO:0000313|Proteomes:UP000241690};
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; KZ679676; PTB58721.1; -; Genomic_DNA.
DR STRING; 983964.A0A2T4ANS9; -.
DR OrthoDB; 5482994at2759; -.
DR Proteomes; UP000241690; 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 CDD; cd18659; CD2_tandem; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 2.40.50.40; -; 2.
DR Gene3D; 6.10.140.1440; -; 1.
DR Gene3D; 1.10.10.60; Homeodomain-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; IPR025260; CHD1-like_C.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR023780; Chromo_domain.
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 PANTHER; PTHR45623:SF14; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 1; 1.
DR PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR Pfam; PF13907; CHD1-like_C; 1.
DR Pfam; PF00385; Chromo; 2.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00298; CHROMO; 2.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM01176; DUF4208; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF54160; Chromo domain-like; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS50013; CHROMO_2; 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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000241690};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 284..355
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 383..434
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 481..652
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 784..946
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1067..1109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1317..1435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1454..1523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1649..1671
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..75
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..115
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..140
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..177
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..217
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1069..1109
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1342..1357
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1358..1435
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1649..1663
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1671 AA; 192283 MW; 4FB11F943176225F CRC64;
MSSPSEGDPS NGNLSPDDSM TFSAVADQQG NDSDVSQGLN ATNSPPDHPS PSDPEASNDE
ATNHADADHA MSESEESSVA DASDDGDFDM QATSPSQHGN DEEDDNEDDN EDEDDVTAGR
ASSSESARAA KRKAPVEDEY MKANPELYGL RRSTRPREQR KIIESESESD VAPASRRQNK
RRRVGSSHAS SKRGTPVLQP STNDSDSDSS TYGGARAKSQ QKKARQQREM QPALALAEKR
WSNRRAAQQV QEGAYEESDV DEEDEEDAEL AASYYVDDYV DNSPYIEKVV KHRLRDGHEL
TYDSTRSDFE YFIKWQGKSH LHDTWELLDS LRSVRGFRKV ENYFRKFVDQ ELDIRFGDDI
PPETKEQFFL DRDRDEEALE DYTKVERVVA VRDGDEGDEY YVKWKGLTYE ECTWEAASDI
STLFQDKIDQ YIDRTSRSWL SDRKETSLDT RSKMTKLEKQ PDFIVGGELR EFQLKGLNFL
CLNWTRGNNV ILADEMGLGK TVQTVSFLSW LRNARRQEGP SLVVAPLSVI PAWCDTFNNW
SPDINYVVYL GPEDARNIIR ENELIINGNP KKPKFNVLVT SYEFILQDWQ FLQSIKWQVL
AVDEAHRLKN AESQLYQRLV GFGIPCKILI TGTPIQNNLA ELSALLDFLN PGKVTIDEDL
DSLSAADAQE KLQDLHRSIA PYILRRTKET VESDLPPKTE KIIRVELSDV QLDYYKNILT
RNYAALCDAT NGHKNSLLNI MMELKKVSNH PYMFPGAEER VLAGSTRRED QIKGLIASSG
KMMLIDQLLS KLKKDGHRVL IFSQMVRMLD ILGDYLSLRG YKFQRLDGTI AAGPRRMAIN
HFNAEDSEDF CFLLSTRAGG LGINLMTADT VIIFDSDWNP QADLQAMARA HRIGQKRPVN
IYRLVSKETV EEEVLERARN KLLLEYLTIQ AGVTDDGKAK FKEELNKKGI KIDGPSTSED
IQMVLKMRSS KMFEQSGNQQ RLEQLDIDSI LENAEITKTK VDDKINLSSG GIDWDNFMQI
TDVKVDDINL DWDQIIPAEK LAEIKAEEEK KQHDDYLAKV AAESAPRRAA VKSRNKDVER
ADRLKKRQRE QQQEEEEQRA YLADPKRPLN DKEQRNLIKA YFRFGSMEDR SADIIQEAKL
GERDPDFVKS VLDDFIKAAQ QAVDDNSAKL AEEEKKMGKT LTKKDKKAVL IDFGELKKVN
AETAIERPKQ LQLLRQVIRG HSDWKNFRVP DATKAANYSC PWGAKEDAML LVGIDKHGFG
AWAQIRDDSD LEMQEKLFLE EHRVGKKEER SKGNDKLKAP GAVHLVRRSE YLLSVLQSKH
SNDRSVHKAV ENHHRNNKKL HAVNGNRGSS STTTSTGIKR QRERERDHGS SEQRSHARED
GAPARPDFKR KHPSHDDARS PKHRRSEDPR RSSKAGDEYR DGRIEKRRHR EDDDRRHDRF
RREEYRRDDY RRDDRRDDRR DDYRRDDRRD DRRDRDRDRE RERERDRDRD HHRDRDRDRD
HNRDHNRDRD RDHHRDHRDR DHATRHLDER RVKALRRLDE LRRIGDDKDQ RAKDNDAMIW
FLLKPVRDNF EKILSTTKDS VKSSKERAAI FGAELVAIGS FLDEKLPATV ADDGLKNNFW
EFLAALWPVD DTSKSVTGDR LSSMYRTLHA RNKSKSSEPS AAKLNGTHAV R
//
