ID A0A166ASW5_9AGAM Unreviewed; 1699 AA.
AC A0A166ASW5;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Chromatin remodeling factor mit1 {ECO:0008006|Google:ProtNLM};
GN ORFNames=SISSUDRAFT_153305 {ECO:0000313|EMBL:KZT35641.1};
OS Sistotremastrum suecicum HHB10207 ss-3.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Trechisporales; Trechisporales incertae sedis; Sistotremastrum.
OX NCBI_TaxID=1314776 {ECO:0000313|EMBL:KZT35641.1, ECO:0000313|Proteomes:UP000076798};
RN [1] {ECO:0000313|EMBL:KZT35641.1, ECO:0000313|Proteomes:UP000076798}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB10207 ss-3 {ECO:0000313|EMBL:KZT35641.1,
RC ECO:0000313|Proteomes:UP000076798};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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DR EMBL; KV428133; KZT35641.1; -; Genomic_DNA.
DR STRING; 1314776.A0A166ASW5; -.
DR Proteomes; UP000076798; 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; cd18793; SF2_C_SNF; 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; 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 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 SUPFAM; SSF54160; Chromo domain-like; 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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000076798}.
FT DOMAIN 906..1083
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1219..1371
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 54..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 155..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 451..535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 667..715
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 734..772
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1477..1655
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..182
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..202
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..243
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..514
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 756..771
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1492..1519
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1627..1655
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1699 AA; 190909 MW; B76A58B7E8494A33 CRC64;
MSRDRASSPL SSLLSSVVPE TPQGSPEPEI SSPNQDPFAV EILKARESSL EKYQPLGGIP
YQSSESGSEE PHMNKPLQIV GEHGTGNDLH YYALFSNDVV RRFNPIHTKN SWPDLLDEYL
TKKGMDELDD FDPWSTQVHP EDRPVKKALR QLRLIVHPPK PQAAPERSTS KSKRKSKKSY
EPDESEDDDD DVADSDDFED DMPVEEPTRR SSRIQVAPKR RYNEVEEDSP VKTRKSRRIG
SNVVESDSDD FMAYESPAPK TKGKLVRKKR TVQPGYGVIR DVDELGVTDD EGDDAALRSH
RKICEKCRLG PSHELLQKHR KSKKGKRAKT RDEFEMSDSE KFESLGGWVR CLKCCVVAHW
KCVATDQRDQ IIFAVRQNED ADGPKRKGIN IEETTDFLCN HCSNGGICID CKEPAIAPEL
LAKLRPGAAN ADAKVEEGGV QDQPMDIVKE EPKEATPGGG KDDPIALDDS DDDADAMEVD
GELQKSVKPP STQRSVTDPE RSLNAEEPPK TPDITEGESE LSGSPPPDPE KPQPVDQSRL
LFRCITCKRP IHYEHLPTPF GMVDPSLEET AQYYQDDWQC HDCKNFADND VDLIVAWRPY
PADAPQPKDD DVVYTANLPR EYLIKWQERG YNRCSWVPHM WLLSLAKAKL KNFTAHGTKV
KLLERPIQDE DAKSRESSAF NIGDDGPADP ETKPDLLEDY SGYQGPEPEA ERRIPPAWKT
VDVILDVYLW HPPQKKSKKP VKKSKKGSKR RVADSEDEDE EDEEEDELEG MDERLFAYRD
GVQPDDKYLE TIGQYEKRTK RKLTVDDANR VIWAYIKWDE LLYEEATWDA PPEENSTGWI
RFLEAWQRFL FARTVHIPKR IPDSAIRASP EVEKKNFKAL KSTPHLGQKD TYRLMDFQIE
GVSWLLGNWC IDQHSILADE MGLGKTIQIA VFLGVLFKNR KAAPSLIVVP NSTITNWLRE
LARWAPNLRA VPFYGPAKSR KVIQNYELYH ENPTNAEVGT KYHVMVTTYE TVTSAAGAAA
VFGKVPRWEC LIVDEGQRLK SDSSLIFKKL SSLNSEHRII MTGTPLNNNI RELFNLMNFL
DPVNWQNLEE LEKQHEELTH ELVLELHEKL RPYFLRRLKA EVLNLPPKNE VIVPVSMTAL
QKQLYKSILQ QNIGDINLLI QGSNAAAKKK SVSKLNNVLM QLRKCLQHPY LIDQGLEPAG
LSDAEAHKQL IDASAKLLLL KTMLPILKQR GHRVLLFSQF KIALDIIEDF ITGEGYKFCR
LDGDTPGADR QKGMDEYNKP NSDKFIYLLT TRAGGVGINL STADTVIMFD PDFNPHQDLQ
AIARSYRYGL KKTCLVFKLM VRASAEERII QTGKKKMALD HLIVQKMEDE EGPGENIQSI
LTFGAQALFA EDAESMATQN VVYSEQDILR LIEKTEVEGD DTAPKEKNTA FDFAKVWTAD
RETFEDVDDG EAAPTDDSWA VLLAKAEVAA KQQAIKEEVT GRGARRRATT RPTNYYDGSP
EKQALVTSTH GSQDGSEDFD YANSVHASEI DSDGGDDTFA EPKNNLASPG KAKKRSELIQ
GHTNHRNVTP QAADSTKAVA KHALPSQTAA ATLVPQAPKG QAARTVPVVK PVKKSTAPPQ
PIKQSAAPPS KPSRTLSQTS SNATEPVASS GAGNQNDMQL CRLCRKLHGH PCPSINQEEK
LLELRRQIAD SDSKKKHKV
//
