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Database: UniProt
Entry: A0A3B4GVL8_9CICH
LinkDB: A0A3B4GVL8_9CICH
Original site: A0A3B4GVL8_9CICH 
ID   A0A3B4GVL8_9CICH        Unreviewed;       355 AA.
AC   A0A3B4GVL8;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 24.
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   Pundamilia nyererei.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Haplochromini; Pundamilia.
OX   NCBI_TaxID=303518 {ECO:0000313|Ensembl:ENSPNYP00000027040.1, ECO:0000313|Proteomes:UP000261460};
RN   [1] {ECO:0000313|Ensembl:ENSPNYP00000027040.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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}.
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DR   AlphaFoldDB; A0A3B4GVL8; -.
DR   STRING; 303518.ENSPNYP00000027040; -.
DR   Ensembl; ENSPNYT00000027701.1; ENSPNYP00000027040.1; ENSPNYG00000020397.1.
DR   GeneTree; ENSGT00390000018439; -.
DR   Proteomes; UP000261460; Unplaced.
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}.
FT   REGION          21..51
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          144..178
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          274..355
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        274..314
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        315..332
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        333..355
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   355 AA;  40184 MW;  2673EC5FF30177AF CRC64;
     MCGRTACTLA PDELKRACSY RNRRGQRRQP RWRDGDADNY RPSYNKNPQS MSPVLLSQRH
     FDKDAPVDKC VLASMRWGLV PSWFKESDPS KMQYSTSNCR SENILQKKSY KDPMLKGQRC
     VILADGFYEW QKVEKGKQPF FIYFPQTQSG PSQEKRKNSD SESVRPPAKA SSGLMKGGEA
     AGEWTGWRLL TMAGVFDCWT PPGGGEPLYS YSVITVNASQ NLQSIHDRMP AILDGEEEVR
     QWLDFGEVKS LEALKLLQSK NILTFHPVSS FVNNTRNNSP ECLQPVDLNS KKEPKSTASS
     KMMASWLSSS SPSKRKESHT SESKEEQESK PLNQRKSAGG LQQWLQGTNK KPRTK
//
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