ID A0A0A2VPU4_BEABA Unreviewed; 759 AA.
AC A0A0A2VPU4;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=BBAD15_g6327 {ECO:0000313|EMBL:KGQ08377.1};
OS Beauveria bassiana D1-5.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX NCBI_TaxID=1245745 {ECO:0000313|EMBL:KGQ08377.1, ECO:0000313|Proteomes:UP000030106};
RN [1] {ECO:0000313|EMBL:KGQ08377.1, ECO:0000313|Proteomes:UP000030106}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D1-5 {ECO:0000313|EMBL:KGQ08377.1,
RC ECO:0000313|Proteomes:UP000030106};
RA Li Q., Wang L., Zhang Z., Wang Q., Ren J., Wang M., Xu W., Wang J., Lu Y.,
RA Du Q., Sun Z.;
RT "Genome sequencing and analysis of entomopathogenic fungi Beauveria
RT bassiana D1-5.";
RL Submitted (OCT-2012) 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: Nucleus {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:KGQ08377.1}.
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DR EMBL; ANFO01000585; KGQ08377.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A2VPU4; -.
DR STRING; 1245745.A0A0A2VPU4; -.
DR EnsemblFungi; BB8028_0002g04840.1; BB8028_0002g04840.1; BB8028_0002g04840.
DR eggNOG; KOG4718; Eukaryota.
DR HOGENOM; CLU_376819_0_0_1; -.
DR Proteomes; UP000030106; 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:UP000030106};
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 666..691
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 267..309
FT /note="Non-structural maintenance of chromosomes element 1
FT RING C4HC3-type"
FT /evidence="ECO:0000259|Pfam:PF08746"
FT REGION 182..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 372..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 433..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 709..759
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 471..485
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 731..759
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 759 AA; 83837 MW; 387C9C108D5F8E1D CRC64;
MLGASREDQR ETNILLDKTS GVGTFLYGSK NHTFCTMETL AETQYSNKNR AFLQAMLARS
SMTFRESRPV IAAILNADNN GSLVRPEQVT EETFDIFMRT AREAASLFDY EIRRTQHQVT
KERVYAFVNT ASDAQTQLAT TFSHDELAFI KRALEAMFDK YNTARMEVIA LTDMQAVKLA
RPNRRESAVD RTEDEPEQSQ AITDKGLKHS EVETVLQNLV GGGWFEKSRE GFYSLTPRSL
LELRPWLLGT FNYPDAEEGE WQRIKFCEAC KDIVTVGVRC ADPDCNIRVH AICEEAFWRT
RRNKNCPGCS KEWTGNLNLI ITDAPVHVLA HCSCTMEIQG GKPHAKGGWA RPPAPPTMIE
YFTYKKVKKH NAQKKAKQEA DNAKASANDA TTADDIDHGT AKLLKGKERD DGSGDVDAVL
REDDERFIAN LLAEHDGPAP PLPPRIDVSD LDWPSDNDAA AAAGPAAAEK NEVATKEEAK
ADKKPNRFSL LFTRHKKAED GLKPQDAQLA TTEAEREKKD LGNVLDRLNL SAKNNKIVPG
GGDSAALLAK FTQVFKDLVN GVPTAVDDLT SLIEDRDGTI AKGFDKLPSS LKKLVTQLPD
KVTATLGPEI LAAAAASQGI KANTDDGLKG TAKKIFLPQN IIELVTKPGA VVAMLRAIVE
ALKTRWPAFI GMNVLWSVAL SLLLFVLWYC YKRGREVRLE REKTENVIDG SDRFEELPDD
PMLPEPSQAE VTPPEETTAA SSSRELTEGE VVATSSKAK
//
