ID A0A8J6L2Y7_MICOH Unreviewed; 884 AA.
AC A0A8J6L2Y7;
DT 25-MAY-2022, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 1.
DT 28-JAN-2026, entry version 14.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=LTLLF_205275 {ECO:0000313|EMBL:KAH0520806.1};
OS Microtus ochrogaster (Prairie vole).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Arvicolinae; Microtus.
OX NCBI_TaxID=79684 {ECO:0000313|EMBL:KAH0520806.1, ECO:0000313|Proteomes:UP000710432};
RN [1] {ECO:0000313|EMBL:KAH0520806.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=LTLLF {ECO:0000313|EMBL:KAH0520806.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:KAH0520806.1};
RA Glass D.;
RT "Studies in the Genomics of Life Span.";
RL Submitted (MAR-2020) 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: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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:KAH0520806.1}.
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DR EMBL; JAATJU010000500; KAH0520806.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A8J6L2Y7; -.
DR Proteomes; UP000710432; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0043022; F:ribosome binding; IEA:TreeGrafter.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:TreeGrafter.
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; IPR057634; PAH_ZNF598/HEL2.
DR InterPro; IPR041888; RING-HC_ZNF598/HEL2.
DR InterPro; IPR056437; Znf-C2H2_ZNF598/HEL2.
DR InterPro; IPR044288; ZNF598/HEL2.
DR InterPro; IPR013087; Znf_C2H2_type.
DR InterPro; IPR059042; Znf_C2H2_ZNF598.
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; PF23202; PAH_ZNF598; 1.
DR Pfam; PF25447; RING_ZNF598; 1.
DR Pfam; PF23230; zf-C2H2_13; 1.
DR Pfam; PF23208; zf_C2H2_ZNF598; 1.
DR SMART; SM00355; ZnF_C2H2; 5.
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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 10..51
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 276..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 334..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 443..642
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 665..693
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..313
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..370
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 466..482
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 483..492
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 513..522
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 629..642
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 676..693
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 884 AA; 97642 MW; 1C96A19CBEC123EC CRC64;
MRVLCEQRYC AVCREELRQA TALGRCDHPV CYRCSTKMRV LCEQRYCAVC REELRQVVFG
KKLPAFAMIP IHQLQHEKKY DIYFADGKVF ALYRQLLQHE CPRCPHLPSF GLFGDLEQHM
RKQHELFCCK LCLKHLKIFT YERKWYSRKD LARHRMQGDP DDTSHRGHPL CKFCDERYLD
NDELLKHLRR DHYFCHFCDS DGAQDYYSDY AYLREHFREK HFLCEEGRCS TEQFTHAFRT
EIDLKAHKTA CHSRSRAEAR QNRQIDLQFS FAPRHSRRSE GVVSGEDYEE VDRYNRQGRA
GRASGRGAQQ NRRGSWRYKR EEEDREVAAA IRASVAAQQQ EDTHRAEDRE EGSRPKKEDA
AARGSEEPRG SRRLPRTQGE GTGSKEASTN GPVSQEAFPT TGPGPVAAPS NTLPPPNPKL
KDEDFPSLCA STSSCCTAVT PGSVGLALAY PGPPRGKNTF QEEDFPALVS SAPKPSSVPS
SLISAWNSSC SKKGNPPTPG AQAVVGGSQP PRKAGKGSRG GRKGGPASVD EEEGGGLTVQ
ELRSVPTTVA VSSLLAPTAN QSSTKVGKKK KVGSEKTGAA SSPLLPPDHI PKPSGAEQAP
DSSLSKAEVP VTIVNGHSEG PALARSTPKE PPGLPRPLGP LPCPIAQEDF PSLGGPCPPR
MPPPGFNTVV FSKSTPSPPP LPPGLVPPVS KPPPGFSSFL PSSHSACIPS PTTTSMKAPR
LTPTPRAYLV PENFRERNLQ LIQSIKDFLQ SEACFSKFKS HSGEFRQGMI SAAQYYKSCR
DLLGENFQKI FSELLALLPD IAKQQELLSA HTDFCSREKP PSSKSKKNKK NVWQTSTQQL
GLDCCVCPTC QQVLAHGDIS SHQALHTARD DDFPSLQAIA RIIT
//
