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Database: UniProt
Entry: A0A2K6DQV2_MACNE
LinkDB: A0A2K6DQV2_MACNE
Original site: A0A2K6DQV2_MACNE 
ID   A0A2K6DQV2_MACNE        Unreviewed;       312 AA.
AC   A0A2K6DQV2;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 22.
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   Name=HMCES {ECO:0000313|Ensembl:ENSMNEP00000038303.1};
OS   Macaca nemestrina (Pig-tailed macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9545 {ECO:0000313|Ensembl:ENSMNEP00000038303.1, ECO:0000313|Proteomes:UP000233120};
RN   [1] {ECO:0000313|Ensembl:ENSMNEP00000038303.1}
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; A0A2K6DQV2; -.
DR   Ensembl; ENSMNET00000062780.1; ENSMNEP00000038303.1; ENSMNEG00000042145.1.
DR   GeneTree; ENSGT00390000018439; -.
DR   Proteomes; UP000233120; Unplaced.
DR   Bgee; ENSMNEG00000042145; Expressed in thymus and 12 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; 2.
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; 2.
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:UP000233120}.
FT   REGION          250..285
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          293..312
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        251..265
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        266..285
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   312 AA;  35498 MW;  506E54986B534BD6 CRC64;
     MCGRTSCHLP RDVLTRACAY QDRRGQQRLP EWRDPDKYCP SYNKSPQSNS PVLLSRLHFE
     KDADSSERII APMRWGLVPS WFKESDPSKL QFSTTNCRSD TIMEKRSFKS GSTGAADSPE
     NWEKVWDNWR LLTMAGIFDC WEPPEGGDVL YSYTIITVDS CKGLSDIHHR MPAILDGEEA
     VSKWLDFGEV STQEALKLIH STENITFHAV SSVVNNSRNN TPECLAPVDL VVKKELKASG
     SSQRMLQWLA TKSPKKEDSK TPQKEESDVP QWSSQFLQKS SLPTKRGTAG LLEQWLKREK
     EEEPVAKRPY SQ
//
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