ID A0A1J4ME16_9CRYT Unreviewed; 628 AA.
AC A0A1J4ME16;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=E3 ubiquitin protein ligase {ECO:0000256|RuleBase:RU365038};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU365038};
GN ORFNames=cubi_00467 {ECO:0000313|EMBL:OII72472.1};
OS Cryptosporidium ubiquitum.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Cryptosporidiidae; Cryptosporidium.
OX NCBI_TaxID=857276 {ECO:0000313|EMBL:OII72472.1, ECO:0000313|Proteomes:UP000186176};
RN [1] {ECO:0000313|EMBL:OII72472.1, ECO:0000313|Proteomes:UP000186176}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=39726 {ECO:0000313|EMBL:OII72472.1};
RA Liu S., Roellig D.M., Guo Y., Li N., Frace M.A., Tang K., Zhang L.,
RA Feng Y., Xiao L.;
RT "Reductive evolution of mitochondrial metabolism and differential evolution
RT of invasion-related proteins in Cryptosporidium.";
RL Submitted (OCT-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|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:OII72472.1}.
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DR EMBL; LRBP01000022; OII72472.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J4ME16; -.
DR VEuPathDB; CryptoDB:cubi_00467; -.
DR OrthoDB; 53681at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000186176; 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; 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; PF13923; zf-C3HC4_2; 1.
DR SMART; SM00184; RING; 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 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 575..614
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 36..106
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 165..192
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 267..380
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 482..509
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..20
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 628 AA; 73752 MW; BAFC2EAC2680BA8C CRC64;
MISKRKREEN ELKRSSISSK TDDLPLDSQE LTNYHVVQLQ ESNKQYKRRI EELENQISKM
IGAFEKIEGE GKSEEENLIS KFEHVIQQKN DEILSLRNEN QRLNMQDIFK KFYLSGDSNS
DTNSSIYGKN NQTNSQGISL FGSISDDSTN ADRINIATSD IKSKLIEKEK QISELTTKNE
EISRENLELR RNLSIYSPCE SFDSELKDRE AKEGKFCRCV RSIINEVFEL RSQLNAEKLK
FVTLLENELL KNIKDFLANQ KSCEEHCKTT NKELEDIRGK YNTLKQDFFS MESVQKSLNA
RDREQKKKIK ELELENSKMR SEKVRVAEFI RTVSTKLEKG EKEEVVENLM NEYEELSNAF
EEKSLECDNL HHKLEEKEKE FGDYKIGIDD IKQALKEIET IKILYEEKLS LVRKTKSETL
KDIINSGTIQ PNQETKISKF LNRYLSFIGQ LGMNDQMDNQ IQLEKESFDS IYKSLIEQKS
ISERLNLDLE FYKAEYYKLR EKLESVEKDE SNYIATISIL KNRVQYILNR VNKLTNLEIN
FDNTEENEHL QIDDYDKEIN TLKSENQELL TLMKCSVCRD KVKDTVINRC GHLFCRECID
RNLSSRNRKC PLCHITFDKN DTGRIFLH
//
