ID W5NB99_LEPOC Unreviewed; 368 AA.
AC W5NB99;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Abasic site processing protein HMCES {ECO:0000256|ARBA:ARBA00015888, ECO:0000256|RuleBase:RU364100};
DE Short=ES cell-specific 5hmC-binding protein {ECO:0000256|RuleBase:RU364100};
DE EC=3.4.-.- {ECO:0000256|RuleBase:RU364100};
DE AltName: Full=Embryonic stem cell-specific 5-hydroxymethylcytosine-binding protein {ECO:0000256|ARBA:ARBA00030390, ECO:0000256|RuleBase:RU364100};
DE AltName: Full=Peptidase HMCES {ECO:0000256|ARBA:ARBA00030898, ECO:0000256|RuleBase:RU364100};
DE AltName: Full=SRAP domain-containing protein 1 {ECO:0000256|ARBA:ARBA00031130, ECO:0000256|RuleBase:RU364100};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000017908.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000017908.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Sensor of abasic sites in single-stranded DNA (ssDNA)
CC required to preserve genome integrity by promoting error-free repair of
CC abasic sites. Acts as an enzyme that recognizes and binds abasic sites
CC in ssDNA at replication forks and chemically modifies the lesion by
CC forming a covalent cross-link with DNA: forms a stable thiazolidine
CC linkage between a ring-opened abasic site and the alpha-amino and
CC sulfhydryl substituents of its N-terminal catalytic cysteine residue.
CC The HMCES DNA-protein cross-link is then degraded by the proteasome.
CC Promotes error-free repair of abasic sites by acting as a 'suicide'
CC enzyme that is degraded, thereby protecting abasic sites from
CC translesion synthesis (TLS) polymerases and endonucleases that are
CC error-prone and would generate mutations and double-strand breaks. Has
CC preference for ssDNA, but can also accommodate double-stranded DNA with
CC 3' or 5' overhang (dsDNA), and dsDNA-ssDNA 3' junction.
CC {ECO:0000256|RuleBase:RU364100}.
CC -!- SIMILARITY: Belongs to the SOS response-associated peptidase family.
CC {ECO:0000256|ARBA:ARBA00008136, ECO:0000256|RuleBase:RU364100}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AHAT01014728; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01014729; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01014730; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_015203604.1; XM_015348118.1.
DR RefSeq; XP_015203605.1; XM_015348119.1.
DR AlphaFoldDB; W5NB99; -.
DR STRING; 7918.ENSLOCP00000017908; -.
DR Ensembl; ENSLOCT00000017940.1; ENSLOCP00000017908.1; ENSLOCG00000014549.1.
DR GeneID; 102691201; -.
DR KEGG; loc:102691201; -.
DR CTD; 56941; -.
DR eggNOG; KOG2618; Eukaryota.
DR GeneTree; ENSGT00390000018439; -.
DR HOGENOM; CLU_035990_1_0_1; -.
DR InParanoid; W5NB99; -.
DR OMA; SYNKGPQ; -.
DR OrthoDB; 204678at2759; -.
DR Proteomes; UP000018468; Linkage group LG5.
DR Bgee; ENSLOCG00000014549; Expressed in ovary and 13 other cell types or tissues.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0003697; F:single-stranded DNA binding; IEA:InterPro.
DR GO; GO:0006974; P:DNA damage response; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.90.1680.10; SOS response associated peptidase-like; 1.
DR InterPro; IPR003738; SRAP.
DR InterPro; IPR036590; SRAP-like.
DR PANTHER; PTHR13604:SF0; ABASIC SITE PROCESSING PROTEIN HMCES; 1.
DR PANTHER; PTHR13604; DC12-RELATED; 1.
DR Pfam; PF02586; SRAP; 1.
DR SUPFAM; SSF143081; BB1717-like; 1.
PE 3: Inferred from homology;
KW Covalent protein-DNA linkage {ECO:0000256|ARBA:ARBA00023124};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU364100};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU364100};
KW Reference proteome {ECO:0000313|Proteomes:UP000018468}.
FT REGION 30..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 294..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..322
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..360
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 368 AA; 41084 MW; 18436F23987B4AFE CRC64;
MCGRTACTLA PQELSRAACY RDRAGRRRRP EWRAGDADQY RPSYNKSPQS LSPVLLSRRH
LDKDAPVDEC VVAAMRWGLV PAWFQESDPQ KMQYSTSNCR SESLLQKKSY KEPLLKGQRC
VVLADGFYEW QRQKREKQPF FIYFPQSRTP GPAGAPDTPI AVSLDPETHT VGPNSFDTQD
NQTMEQEGCE WTGWRLLTLA GLFDCWSPPG GGTSLYTYTI ITVEASQNLQ SIHDRMPAVL
DGEEEVRRWL DFGEIRSLEA LSLLRPNNTL TFHPVSTLVN NSRNNSPECV QPVEVGVKKA
PPPSASSKAM MTWLQSASPQ KRKEQGPLAE REKPGERGGG TGAASASGRG TLQNWLIRTE
PSKKARTG
//
