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Database: UniProt
Entry: A0A2U9BH66_SCOMX
LinkDB: A0A2U9BH66_SCOMX
Original site: A0A2U9BH66_SCOMX 
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
//
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