ID A0A2U9BH66_SCOMX Unreviewed; 307 AA.
AC A0A2U9BH66;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 08-NOV-2023, entry version 16.
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};
GN ORFNames=SMAX5B_014357 {ECO:0000313|EMBL:AWP03271.1};
OS Scophthalmus maximus (Turbot) (Psetta maxima).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Scophthalmidae;
OC Scophthalmus.
OX NCBI_TaxID=52904 {ECO:0000313|EMBL:AWP03271.1, ECO:0000313|Proteomes:UP000246464};
RN [1] {ECO:0000313|EMBL:AWP03271.1, ECO:0000313|Proteomes:UP000246464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Martinez P.;
RT "Integrating genomic resources of turbot (Scophthalmus maximus) in depth
RT evaluation of genetic and physical mapping variation across individuals.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CP026248; AWP03271.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U9BH66; -.
DR Proteomes; UP000246464; Chromosome 6.
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:UP000246464}.
FT REGION 20..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 147..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..41
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 307 AA; 34566 MW; 610075FCA3B3A164 CRC64;
MCGRTACTLA PDEVSRACSY RSRGGQRRQP RWRDGDADKY RPSYNKSPQS TSPVLLSQRH
FDKDAPVDEC VLASMRWGLV PAWFKEDDPR KMQYSTSNCR SENILEKKSY KSPLNKGQRC
VILADGFYEW RREEKSKQPF FIYFPQTPSG SSQEKTEDQD DLATSAQSKE TSERACSAEG
GAFDSTEEGE APCEWTGWRL LTMAGLFDCW TPPGGGEALY TYSVITVNAS PNLQSIHDRM
PAVLDGEEEV RRWLDFGEVK SPDALKLLQT KNSLTFHPVS SLVNNSRNNS AECLQPVDPG
CKKKCDI
//