ID J4UUS0_BEAB2 Unreviewed; 736 AA.
AC J4UUS0;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 43.
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=BBA_01722 {ECO:0000313|EMBL:EJP69757.1};
OS Beauveria bassiana (strain ARSEF 2860) (White muscardine disease fungus)
OS (Tritirachium shiotae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX NCBI_TaxID=655819 {ECO:0000313|EMBL:EJP69757.1, ECO:0000313|Proteomes:UP000002762};
RN [1] {ECO:0000313|EMBL:EJP69757.1, ECO:0000313|Proteomes:UP000002762}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 2860 {ECO:0000313|EMBL:EJP69757.1,
RC ECO:0000313|Proteomes:UP000002762};
RX PubMed=22761991; DOI=10.1038/srep00483;
RA Xiao G., Ying S.H., Zheng P., Wang Z.L., Zhang S., Xie X.Q., Shang Y.,
RA St Leger R.J., Zhao G.P., Wang C., Feng M.G.;
RT "Genomic perspectives on the evolution of fungal entomopathogenicity in
RT Beauveria bassiana.";
RL Sci. Rep. 2:483-483(2012).
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: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the NSE1 family.
CC {ECO:0000256|ARBA:ARBA00010258}.
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DR EMBL; JH725152; EJP69757.1; -; Genomic_DNA.
DR RefSeq; XP_008595041.1; XM_008596819.1.
DR AlphaFoldDB; J4UUS0; -.
DR STRING; 655819.J4UUS0; -.
DR GeneID; 19884734; -.
DR HOGENOM; CLU_376819_0_0_1; -.
DR InParanoid; J4UUS0; -.
DR OrthoDB; 2099840at2759; -.
DR Proteomes; UP000002762; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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: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 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; 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; PF07574; SMC_Nse1; 1.
DR Pfam; PF08746; zf-RING-like; 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|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000002762};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {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 643..668
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 231..273
FT /note="Non-structural maintenance of chromosomes element 1
FT RING C4HC3-type"
FT /evidence="ECO:0000259|Pfam:PF08746"
FT REGION 146..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 347..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 410..462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 686..736
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 448..462
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 686..700
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 711..736
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 736 AA; 81497 MW; D9064F5FF51A93F5 CRC64;
METLSETQYS NKNRAFLQAM LARSSMTFRE SRPVIAAILN ADNNGSLVRP EQVTEETFDI
FMRTAREAAS LFDYEIRRTQ HQVTKERVYA FVNTASDAQT QLATTFSHDE LAFIKRALEA
MFDKYNTPRM EVIALTDMQA VKLARPNRRE SAVDRTEDEP EQSQAITDKG LKHSEVETVL
QNLVGGGWFE KSREGFYSLT PRSLLELRPW LLGTFNYPDA EEGEWQRIKF CEACKDIVTV
GVRCADPDCN IRVHAICEEA FWRTRRNKNC PGCSKEWTGN LRARACACAL QLHDGNPRRK
AACQGGAGRS LFAPVRTVCE RKNETHRPAP APPTMIEYFT YKKVKKHNAQ KKAKQEADNA
KASANDATTA DDIDHGTAKL LKGKERDDGN GDVDAVLRED DERFIANLLA EHDGPAPPLP
PRIDVSDLDW PSDNDAAAAA GPAAAEKNEV ATKEEAKADK RPNRFSLLFT RHKKAEDGLK
PQDAQLATTE AEREKKDLGN VLDRLNLSAK NNKIVLGGGD SAALLAKFTQ VFKDLVNGVP
TAVDDLTSLI EDRDGTIAKG FDKLPSSLKK LVTQLPDKVT ATLGPEILAA AAASQGIKAN
TDDGLKGTAK KIFLPQNIIE LVTKPGAVVA MLRAIVEALK TRWPAFIGMN VLWSVALSLL
LFVLWYCYKR GREVRLEREK TENVIDGSDR FEELPDDPML PEPSRAEVTP PEETTAASSS
RELTEGEVVA TSSKAK
//
