ID A0A1Y1XA21_9FUNG Unreviewed; 639 AA.
AC A0A1Y1XA21;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=E3 ubiquitin-protein ligase CHFR {ECO:0000256|ARBA:ARBA00017908};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
DE AltName: Full=Checkpoint with forkhead and RING finger domains protein {ECO:0000256|ARBA:ARBA00031332};
DE AltName: Full=RING-type E3 ubiquitin transferase CHFR {ECO:0000256|ARBA:ARBA00029800};
GN ORFNames=BCR32DRAFT_267576 {ECO:0000313|EMBL:ORX82567.1};
OS Anaeromyces robustus.
OC Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC Chytridiomycota incertae sedis; Neocallimastigomycetes; Neocallimastigales;
OC Neocallimastigaceae; Anaeromyces.
OX NCBI_TaxID=1754192 {ECO:0000313|EMBL:ORX82567.1, ECO:0000313|Proteomes:UP000193944};
RN [1] {ECO:0000313|EMBL:ORX82567.1, ECO:0000313|Proteomes:UP000193944}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S4 {ECO:0000313|EMBL:ORX82567.1,
RC ECO:0000313|Proteomes:UP000193944};
RG DOE Joint Genome Institute;
RA Haitjema C.H., Gilmore S.P., Henske J.K., Solomon K.V., De Groot R.,
RA Kuo A., Mondo S.J., Salamov A.A., Labutti K., Zhao Z., Chiniquy J.,
RA Barry K., Brewer H.M., Purvine S.O., Wright A.T., Boxma B., Van Alen T.,
RA Hackstein J.H., Baker S.E., Grigoriev I.V., O'Malley M.A.;
RT "A Parts List for Fungal Cellulosomes Revealed by Comparative Genomics.";
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ORX82567.1, ECO:0000313|Proteomes:UP000193944}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S4 {ECO:0000313|EMBL:ORX82567.1,
RC ECO:0000313|Proteomes:UP000193944};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SUBCELLULAR LOCATION: Nucleus, PML body
CC {ECO:0000256|ARBA:ARBA00004322}.
CC -!- SIMILARITY: Belongs to the CHFR family.
CC {ECO:0000256|ARBA:ARBA00005797}.
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:ORX82567.1}.
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DR EMBL; MCFG01000092; ORX82567.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y1XA21; -.
DR STRING; 1754192.A0A1Y1XA21; -.
DR OrthoDB; 1462937at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000193944; Unassembled WGS sequence.
DR GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR Gene3D; 2.60.200.20; -; 1.
DR Gene3D; 3.30.40.140; -; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR019406; APLF_PBZ.
DR InterPro; IPR040909; CHFR_Znf-CRD.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR16079:SF4; E3 UBIQUITIN-PROTEIN LIGASE CHFR; 1.
DR PANTHER; PTHR16079; UBIQUITIN LIGASE PROTEIN CHFR; 1.
DR Pfam; PF00498; FHA; 1.
DR Pfam; PF13923; zf-C3HC4_2; 1.
DR Pfam; PF10283; zf-CCHH; 1.
DR Pfam; PF17979; zf-CRD; 1.
DR SMART; SM00240; FHA; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR PROSITE; PS50006; FHA_DOMAIN; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000193944};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 42..94
FT /note="FHA"
FT /evidence="ECO:0000259|PROSITE:PS50006"
FT DOMAIN 188..227
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 373..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 442..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 384..408
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..430
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 639 AA; 74673 MW; 1FB2643A661EC5FB CRC64;
MFIKNIVQKI ASISNLNNSN AWGVLKSLNE NSKDINLIND YYIIGRKKDP KNDKLITLSD
NRISHKHIKI FLSENKVHLQ DISRNGTFIN NTLVGKGNIV TLNDNDIIKF GHLDNMPQYQ
IIINTFNTET SDSEYSDITI EDNNENDIND NNKRVLDNSV DINPTKKIKA EVKGKEKIDD
MLDDELKCGI CYDIMYNATT CSPCMHSFCA GCLSQWINNL KECPHCRTKI SEIRKNNQTN
NIINAFLLAH PEKKRPADEL ADLDKFDTIK NNIIRYEEEN GNDIKYLYKD EYEFHYLSCP
NCPSNDDDVN NNNNNNNDNA PIVFRRYDDA ANINYRVKRK ALPQYADYRC PPRSIHILCH
ACRQQMPLRC KPNRQRRVNE DEDEDRESEF ESEEDNSESE DENSENEEEN NNNNNNNNNN
NNVNTSSNIN NNNSIVILDV RNNENNNNNN NDNNNDNDNN SDNNNNINSS NNPTNEPVIP
QQCFVCNNYY CDKYMENGCE NIKGRLDKLE DITMAEIPPS AFRWNNFEKQ ILINYLDSKN
LNINECWKVC VANLLNKKFT LDNMFLQNIQ KDTYICYDCS RQIFSELVYQ YREKEVNKDD
LPENIRKRPD CWYGRKCRTQ TNKQDHARNY NHICEQTHF
//
