ID A0A0G2DY44_9EURO Unreviewed; 974 AA.
AC A0A0G2DY44;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=UCRPC4_g06474 {ECO:0000313|EMBL:KKY15046.1};
OS Phaeomoniella chlamydospora.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Phaeomoniellales; Phaeomoniellaceae; Phaeomoniella.
OX NCBI_TaxID=158046 {ECO:0000313|EMBL:KKY15046.1, ECO:0000313|Proteomes:UP000053317};
RN [1] {ECO:0000313|EMBL:KKY15046.1, ECO:0000313|Proteomes:UP000053317}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCRPC4 {ECO:0000313|EMBL:KKY15046.1};
RA Lawrence D.P., Travadon R., Rolshausen P.E., Baumgartner K.;
RT "Distinctive expansion of gene families associated with plant cell wall
RT degradation and secondary metabolism in the genomes of grapevine trunk
RT pathogens.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KKY15046.1, ECO:0000313|Proteomes:UP000053317}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCRPC4 {ECO:0000313|EMBL:KKY15046.1};
RA Morales-Cruz A., Amrine K.C., Cantu D.;
RL Submitted (MAY-2015) 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 -!- SIMILARITY: Belongs to the ZNF598/HEL2 family.
CC {ECO:0000256|ARBA:ARBA00035113}.
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:KKY15046.1}.
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DR EMBL; LCWF01000196; KKY15046.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G2DY44; -.
DR OrthoDB; 3059402at2759; -.
DR Proteomes; UP000053317; Unassembled WGS sequence.
DR GO; GO:0001405; C:PAM complex, Tim23 associated import motor; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0072344; P:rescue of stalled ribosome; IEA:InterPro.
DR CDD; cd16615; RING-HC_ZNF598; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR013875; Pam17.
DR InterPro; IPR041888; RING-HC_ZNF598/Hel2.
DR InterPro; IPR044288; ZNF598/Hel2.
DR InterPro; IPR013087; Znf_C2H2_type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR22938:SF0; E3 UBIQUITIN-PROTEIN LIGASE ZNF598; 1.
DR PANTHER; PTHR22938; ZINC FINGER PROTEIN 598; 1.
DR Pfam; PF08566; Pam17; 1.
DR Pfam; PF13920; zf-C3HC4_3; 1.
DR SMART; SM00355; ZnF_C2H2; 4.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000053317};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT TRANSMEM 868..889
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 50..90
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 325..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 522..626
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 642..693
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 782..808
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 327..341
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..395
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 528..564
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 591..618
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 642..680
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 974 AA; 107320 MW; B84BEA15081E2347 CRC64;
MGLDAGQPPE LDGGRSDDQA SADSNCTLVL GSKRNENGIS AEEEEEGDTC FICASNIDHI
SIAPCNHQTC HICALRLRAL YKTRACAHCR TESNFVVFTD DPTKRYEDFK DSDFVKTDDN
LGIRYEKEEI FEDTVLLLRY NCPDKTCDVA CLGWPHLHRH VKAKHGKTMC DLCTRNKKVF
THEHELFTFG ELRRHERYGD DNPGALDQSG FKGHPECGFC RERFYGDDEL YVHCREKHER
CHICDRRNNG RQPQYYLNYE ALEEHFRKDH FLCLDQECLG KKFVVFDSEM DLKAHQLAEH
PNGLSKDARR DARLVDISGF DYRAPYQAQR GRREGRGGGR GRDPNSEPLP VSSAQPLRRD
ELAYQRQMAI QSAQSSSTRT FGGQLTQSVR EPVRPAPSTQ PTPPLPAVEN LSISDPQSMA
TLSPQEQARR LRHNAVIERA SNLLGNDALK LNEFRSKVSA YKNSTITATN LIDAFFSLFD
TSSAEMGKLV KELADIYENE TKRTELLKSW NDWRAINEDY PSLPGPNGTV PGMTSDAISG
SSSGRRVLRL KSSTAQSSRS AVGSGNPFPP LGRPTNAAAK KSPAWGALAK ANGSASSSAS
SSRTPSRHPT TSSSSEAFPA LPAAAKPNTL MAGLTKGSIR WQDTKSQPPA ANAWNPSGGA
PSAQVPATGN ASLPSQSDES TTAKKKGKKA KGQVHLNTSA VVVSGWDEDI MQQPIRIASL
GYRAAKQNVP SAGIRVPTAV STQTAPKRAL SCSSVSPRSL KIPSAFCTNE QLPKTIVITA
TARSHQKSNT SSSPLTRLRH VSTSTPPPAE QNLDWQTFFR LRTSRRRYSL IASIASSLAT
SWGAIVAINT TPLSDTLTSI SPIPDPFVSL GLFTFATAGV GWLIGPFFGQ AVWRMSHRQQ
VPGFMVREKD FYERVKRYRV DPRGASAQNP VPDYYGEKVG SRDEWRTWLK DQRAFNRKRE
GRGAGAGGSV FAGF
//
