ID A0A1X0QBM4_9MICR Unreviewed; 507 AA.
AC A0A1X0QBM4;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=E3 ubiquitin protein ligase {ECO:0000256|RuleBase:RU365038};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU365038};
GN Name=BRE1 {ECO:0000313|EMBL:ORD97199.1};
GN ORFNames=HERIO_933 {ECO:0000313|EMBL:ORD97199.1};
OS Hepatospora eriocheir.
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Hepatosporidae;
OC Hepatospora.
OX NCBI_TaxID=1081669 {ECO:0000313|EMBL:ORD97199.1, ECO:0000313|Proteomes:UP000192356};
RN [1] {ECO:0000313|EMBL:ORD97199.1, ECO:0000313|Proteomes:UP000192356}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GB1 {ECO:0000313|EMBL:ORD97199.1,
RC ECO:0000313|Proteomes:UP000192356};
RX PubMed=28345194; DOI=10.1111/1462-2920.13734;
RA Wiredu Boakye D., Jaroenlak P., Prachumwat A., Williams T.A., Bateman K.S.,
RA Itsathitphaisarn O., Sritunyalucksana K., Paszkiewicz K.H., Moore K.A.,
RA Stentiford G.D., Williams B.A.;
RT "Decay of the glycolytic pathway and adaptation to intranuclear parasitism
RT within Enterocytozoonidae microsporidia.";
RL Environ. Microbiol. 19:2077-2089(2017).
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|RuleBase:RU365038};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906, ECO:0000256|RuleBase:RU365038}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|RuleBase:RU365038}.
CC -!- SIMILARITY: Belongs to the BRE1 family. {ECO:0000256|ARBA:ARBA00005555,
CC ECO:0000256|RuleBase:RU365038}.
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:ORD97199.1}.
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DR EMBL; LVKB01000036; ORD97199.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X0QBM4; -.
DR VEuPathDB; MicrosporidiaDB:A0H76_1613; -.
DR VEuPathDB; MicrosporidiaDB:HERIO_933; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000192356; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniRule.
DR CDD; cd16499; RING-HC_Bre1-like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR013956; E3_ubiquit_lig_Bre1.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR23163:SF0; E3 UBIQUITIN-PROTEIN LIGASE BRE1; 1.
DR PANTHER; PTHR23163; RING FINGER PROTEIN-RELATED; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853,
KW ECO:0000256|RuleBase:RU365038};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|RuleBase:RU365038};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU365038}; Nucleus {ECO:0000256|RuleBase:RU365038};
KW Reference proteome {ECO:0000313|Proteomes:UP000192356};
KW Transferase {ECO:0000256|RuleBase:RU365038};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU365038};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU365038};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 455..494
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT COILED 94..172
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 204..238
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 272..404
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 507 AA; 60123 MW; DC12271E1ADCCCEE CRC64;
MVKMKGIKDK IGKKRFDEIQ MTLKKMVEKH NISNIKDNLS KSTDLTTSTN IQDEQNTQLA
NDSTVNKDLS VNKQSLIGKT DLQEDLEDDN SWNVKKIKFT LKEKNDRIRE LEQKLLKQTN
ENKKLVEAEN KVVFSKVEVE FNRETDILIS KYTKLIEEND SLRKELNNLD KRYFEEMRMY
KSDLEKVKYE LKLVNEPKEK KFDIQEYFVR FDESQNEIAK LNEKLLEKDR MLQMAKKDNN
ILENSSINLS RQLEIAHKRL ERSLNIKGVS ANQILEDEVA SMTVAIKELS LENKKMQSTI
ENIEMKSKTT ESELIRVRGQ LKTNIKLEER LENNKKRLEN VKKDIINQIE KYENKYSNFE
RIEANLNEKI IENKKNVNSY KSDMMYCEKK ISDLIEERKK YENDLYDVKV RNLEIEKENK
VLKSKVYAYE SVIENGTKTT ELFNQIDILR QYVICPLCKT NFKSHIIDKC MHCFCKDCLL
DRLKVRVRNC PKCNVGYSEE DIKKIYL
//
