ID A0A194VYY1_9PEZI Unreviewed; 334 AA.
AC A0A194VYY1;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Non-structural maintenance of chromosomes element 1 homolog {ECO:0000256|ARBA:ARBA00019422, ECO:0000256|RuleBase:RU368018};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483, ECO:0000256|RuleBase:RU368018};
GN ORFNames=VM1G_04197 {ECO:0000313|EMBL:KUI69078.1};
OS Valsa mali.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Valsaceae; Valsa.
OX NCBI_TaxID=105487 {ECO:0000313|EMBL:KUI69078.1};
RN [1] {ECO:0000313|EMBL:KUI69078.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=03-8 {ECO:0000313|EMBL:KUI69078.1};
RA Yin Z., Liu H., Gao X., Li Z., Song N., Ke X., Dai Q., Wu Y., Sun Y.,
RA Xu J.-R., Kang Z.K., Wang L., Huang L.;
RT "Genome Sequence of Valsa Canker Pathogens Uncovers a Specific Adaption of
RT Colonization on Woody Bark.";
RL Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acts in a DNA repair pathway for removal of UV-induced DNA
CC damage that is distinct from classical nucleotide excision repair and
CC in repair of ionizing radiation damage. Functions in homologous
CC recombination repair of DNA double strand breaks and in recovery of
CC stalled replication forks. {ECO:0000256|RuleBase:RU368018}.
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 ECO:0000256|RuleBase:RU368018};
CC -!- SUBUNIT: Component of the Smc5-Smc6 complex.
CC {ECO:0000256|RuleBase:RU368018}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|RuleBase:RU368018}.
CC -!- SIMILARITY: Belongs to the NSE1 family. {ECO:0000256|ARBA:ARBA00010258,
CC ECO:0000256|RuleBase:RU368018}.
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DR EMBL; CM003101; KUI69078.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A194VYY1; -.
DR OrthoDB; 316902at2759; -.
DR Proteomes; UP000078559; Chromosome 4.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0030915; C:Smc5-Smc6 complex; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
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-UniRule.
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, ECO:0000256|RuleBase:RU368018};
KW DNA recombination {ECO:0000256|ARBA:ARBA00023172,
KW ECO:0000256|RuleBase:RU368018};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|RuleBase:RU368018};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU368018};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU368018};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU368018};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU368018};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU368018};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|RuleBase:RU368018}.
FT DOMAIN 238..282
FT /note="Non-structural maintenance of chromosomes element 1
FT RING C4HC3-type"
FT /evidence="ECO:0000259|Pfam:PF08746"
FT REGION 147..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 302..334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..167
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..321
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 334 AA; 37752 MW; 8A2402535DBEC9C7 CRC64;
MPEWEPILPD GWNHNHRAFV QAFMSRGTLT FPEGQKVIAA ILSAEDDGAR RVKPDSITEE
TFKFYISRTR EAIAPLDYDI RTTYHQIDRH QVWALINVHS DPSTQLATSR TPDEISFIKR
VLDAMFETYN TNRQEVMAVT AAQARKLARP PTMTNNGNQN GNADGDEATQ QRGADRGLKH
SEIERLLPSL VDEGWFEESD EGFYSLSPRS LLELKTWLVS TYNDPDAGEA SHQRIKFCKA
CKDIVTVGQR CPDRDCAIRI HDICSEAYWR TRRGGERTCP KCQTPWTGTN YVGERAVTET
AASHRRVGRK SGRKSDINDS TVDGVTEDVD DGEE
//
