ID A0A364MYB2_9PLEO Unreviewed; 816 AA.
AC A0A364MYB2;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Non-structural maintenance of chromosomes element 1 homolog {ECO:0000256|ARBA:ARBA00019422};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=DDE83_006601 {ECO:0000313|EMBL:RAR07164.1};
OS Stemphylium lycopersici.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Stemphylium.
OX NCBI_TaxID=183478 {ECO:0000313|EMBL:RAR07164.1, ECO:0000313|Proteomes:UP000249619};
RN [1] {ECO:0000313|Proteomes:UP000249619}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIDEFI 213 {ECO:0000313|Proteomes:UP000249619};
RA Medina R., Franco M.E.E., Lucentini C.G., Saparrat M.C.N., Balatti P.A.;
RT "Draft genome sequence of Stemphylium lycopersici strain CIDEFI 213.";
RL Submitted (MAY-2018) 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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the NSE1 family.
CC {ECO:0000256|ARBA:ARBA00010258}.
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:RAR07164.1}.
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DR EMBL; QGDH01000104; RAR07164.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A364MYB2; -.
DR STRING; 183478.A0A364MYB2; -.
DR Proteomes; UP000249619; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProt.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0030915; C:Smc5-Smc6 complex; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
DR CDD; cd16493; RING-CH-C4HC3_NSE1; 1.
DR Gene3D; 3.90.1150.220; -; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR011513; Nse1.
DR InterPro; IPR014857; Nse1_RING_C4HC3-type.
DR InterPro; IPR002227; Tyrosinase_Cu-bd.
DR InterPro; IPR007305; Vesicle_transpt_Got1/SFT2.
DR InterPro; IPR013272; Vps72/YL1_C.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR20973; NON-SMC ELEMENT 1-RELATED; 1.
DR PANTHER; PTHR20973:SF0; NON-STRUCTURAL MAINTENANCE OF CHROMOSOMES ELEMENT 1 HOMOLOG; 1.
DR Pfam; PF04178; Got1; 1.
DR Pfam; PF07574; SMC_Nse1; 1.
DR Pfam; PF08265; YL1_C; 1.
DR Pfam; PF08746; zf-RING-like; 1.
DR SMART; SM00993; YL1_C; 1.
DR PROSITE; PS00498; TYROSINASE_2; 1.
PE 3: Inferred from homology;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA recombination {ECO:0000256|ARBA:ARBA00023172};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000249619};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT TRANSMEM 307..327
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 334..352
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 358..381
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 204..215
FT /note="Tyrosinase copper-binding"
FT /evidence="ECO:0000259|PROSITE:PS00498"
FT REGION 52..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 436..456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 618..658
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 791..816
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..79
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..456
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 816 AA; 90305 MW; AD13F29FC832C562 CRC64;
MAPLTAASDD KTHQALLDKL DIYAVEKPFR NPNWKPPQRR NKNLKQILGE ASRKEASVMA
TQNNSGMSTP AVATEGATSA ASGGRQANIA QAAHSLSALV LEKNGRAAAG GNAAGPAPTY
TNIESAPSFH PSSQKKYCDI TGLPAPYTDP KTRLRYHNKE VFGGIRTMPQ NVSEGYLAAR
VKLLSTHHMP FSLWLKEVLR LNRDPVFFCA HKTVDQGYGF GARYTLRLGI SLVPSAPPGY
CLNSFYLHHL ARRELYPPTN IQHADHVAFR YPKYDARTPR ALFRVLANMM GRDWGGLLFR
GLAMGNILFI IGLTLIIGTT KTVAFFARKQ KWKGTLAFVA GISLILMRWA FIGFLVELYG
ILVLFGDFLA TIAGFVSNVP IIGPYIAKAL NAISGATRNA DLPPRENPAV SNYVFTCFRV
LAFRNSPPPL EFNWIDHSPR HENPPNPTSK QTNPGTRRCT RAAAIANPPM SQSASPSVRA
PAGDEEYNDM HRAFLQAFQT NGVLTTEEMK EILAHIMTAY DPERPWTRSD ITGPHLTSTL
QLINAKLEAF DYEIRSTRDQ ESRTPIYAFV NNTSDALTQF ATTFSANEMA YIRRLLDAMF
ETNNTKVRET MAVRHTEASQ LARVSRRSRQ SQLPNGGGGG DDDDDEVVEA TQQGQAETSI
SISDADAVLE SLVALRFFRK SPAGYYSLAP RALVELRAYL KETYNETADE AGRDLYRIRD
CEGCREIVTI GLRCDNRECG VRWHDACAKA YYHSAGRRRR KGGDGAAAAE NKCPRCDIPF
TETVFVGERA ERVGSSRASL VVGRGEDEDE EMEEDD
//
