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Database: UniProt
Entry: A0A2S7P6C6_9HELO
LinkDB: A0A2S7P6C6_9HELO
Original site: A0A2S7P6C6_9HELO 
ID   A0A2S7P6C6_9HELO        Unreviewed;      1261 AA.
AC   A0A2S7P6C6;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Chromo domain-containing protein {ECO:0000313|EMBL:PQE09843.1};
GN   ORFNames=CJF30_00010323 {ECO:0000313|EMBL:PQE09843.1};
OS   Rutstroemia sp. NJR-2017a BBW.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Rutstroemiaceae; Rutstroemia.
OX   NCBI_TaxID=2070414 {ECO:0000313|EMBL:PQE09843.1, ECO:0000313|Proteomes:UP000238072};
RN   [1] {ECO:0000313|EMBL:PQE09843.1, ECO:0000313|Proteomes:UP000238072}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NJR-2017a BBW {ECO:0000313|EMBL:PQE09843.1,
RC   ECO:0000313|Proteomes:UP000238072};
RA   Gaut B.S., Morton B.R., Clegg M.T., Duvall M.R.;
RL   Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PQE09843.1}.
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DR   EMBL; NJPT01000063; PQE09843.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S7P6C6; -.
DR   STRING; 2070414.A0A2S7P6C6; -.
DR   Proteomes; UP000238072; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006338; P:chromatin remodeling; IEA:UniProt.
DR   GO; GO:0043170; P:macromolecule metabolic process; IEA:UniProt.
DR   CDD; cd18966; chromodomain; 1.
DR   Gene3D; 2.40.50.40; -; 1.
DR   Gene3D; 4.10.1000.10; Zinc finger, CCCH-type; 2.
DR   InterPro; IPR016197; Chromo-like_dom_sf.
DR   InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR   InterPro; IPR023780; Chromo_domain.
DR   InterPro; IPR000571; Znf_CCCH.
DR   InterPro; IPR036855; Znf_CCCH_sf.
DR   PANTHER; PTHR22812; CHROMOBOX PROTEIN; 1.
DR   Pfam; PF00385; Chromo; 1.
DR   Pfam; PF00642; zf-CCCH; 1.
DR   SMART; SM00298; CHROMO; 1.
DR   SMART; SM00356; ZnF_C3H1; 5.
DR   SUPFAM; SSF90229; CCCH zinc finger; 3.
DR   SUPFAM; SSF54160; Chromo domain-like; 1.
DR   PROSITE; PS50013; CHROMO_2; 1.
DR   PROSITE; PS50103; ZF_C3H1; 4.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW   ProRule:PRU00723}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000238072};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00723};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00723}.
FT   DOMAIN          35..93
FT                   /note="Chromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50013"
FT   DOMAIN          400..428
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50103"
FT   DOMAIN          442..470
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50103"
FT   DOMAIN          495..522
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50103"
FT   DOMAIN          532..560
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50103"
FT   ZN_FING         400..428
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT   ZN_FING         442..470
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT   ZN_FING         495..522
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT   ZN_FING         532..560
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          131..312
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1235..1261
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        137..163
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        164..209
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1261 AA;  140303 MW;  D2211896E43A28B5 CRC64;
     MASKEVPGRR ASEDRISVAS IETSEDEQYS TDHEFLVECI LSEKVQDGRT LYLLDWTGYP
     REMATWEPPE NIQDPGIIQT WEERKILQQK GVEAVFDVDA FEAEKKEYAE AKALRSRLRH
     EKRMAIRLGL GVSGNEPNEN EMGSVYGSEQ TVGSLQSPKR PSPPRQSVDE RRSSERQNER
     QEATARAKAN KRIRSDSDSS DDEPLISRKS RAPIPKSAPA AIPLSRGMPS PKQNFQVRGA
     ALADRIHRPG TKTAPDNEIE GPANAANRGG RGATRGGSSL LSKNVFAGGR TRRRKPTLIE
     SATDSNKSQK HFSQLRMVRR AELAGRQLAD KAPDIEALPG GLFDPSKNSH VQPIRPGTVK
     RHSFAYQEDE DMLQSRQQRQ QETSIEPAKP KEIRWQDIPW ERRTICFWWS RNIRCEYGSN
     CKFLHINDLS LPVAPPPDNW VEYAKPVCAY YNKPGGCNKG DSCNFLHEDA GNTATNGGLD
     LQSAHPLPMS SSVVEKTSIC YWWFGHGNCT KGDKCKFAHI LDSTRTVKVP HPKAREPCIA
     SLRGECRYSR EDCLKLHAHP SHDPEPVAPV APMAPMVSGA PLVAPNFTAT PGFATAYNAK
     YSNQPANSAV KLREADVCLY WKDGNCRNSA ATCRWAHTFY AETPTSNQSY IEAAMQPKAT
     RTARPTVRFA TDISEYSADY DMPSIENTDD IIMLSPDQNS NTVPMLNPSE SDVTRLKSKP
     LDLDKSRREI DLEGSNTRLK RVIFGADSDG QRISVDFGEL PAGSLWSETC AKLEVIRFDQ
     MCAAQDFYFK YKSPQQLWEG NLGIDHADSD SKMVVGQVAE NLRLGSTGLL ALCEEVAILL
     HPTSAEDWNY LGSTASSSSD LELRYLVFDL DKLIASSTTS PALITAPDAD QLSSRNEHIM
     PPPCRSKVVK TLYGLNYRTL RDLDYENLRP SKKSRNADNF FLIFPTSATY LADFIATWLR
     SCRKECKVYS SQVDGAWDHF VHSSSITAGA ILVYETALTS LSELPWTRDL TVQNSFLFWS
     IGDSISSAPL SLHPKVNGVP NLGQITITPL LPFGAAIFVT PSFLVAEPAM TYKLLKWFQT
     RLRNATPGSY KLVSCHDLRS YLLDLAVQKS RERDDLLEKN DHKPEKHAIA SEKGLSHEDC
     QLRFDVFRLF VDILENDLSS GLSAIDLDPS EDAFIPVRYA PASIDPDNEK DLVSWFAGWT
     ILNLSTYRKF YVVGSSTKNS TRAVKMVPEI RTDIPSLSTS NMPATPSSEL IGAHPGGSGE
     A
//
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