ID A0A1U8BYZ4_MESAU Unreviewed; 1023 AA.
AC A0A1U8BYZ4;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=DNA cross-link repair 1A protein {ECO:0000313|RefSeq:XP_005063481.1, ECO:0000313|RefSeq:XP_012968758.1};
GN Name=Dclre1a {ECO:0000313|RefSeq:XP_005063481.1,
GN ECO:0000313|RefSeq:XP_012968758.1};
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036 {ECO:0000313|Proteomes:UP000189706, ECO:0000313|RefSeq:XP_012968758.1};
RN [1] {ECO:0000313|RefSeq:XP_005063481.1, ECO:0000313|RefSeq:XP_012968758.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the DNA repair metallo-beta-lactamase (DRMBL)
CC family. {ECO:0000256|ARBA:ARBA00010304}.
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DR RefSeq; XP_005063481.1; XM_005063424.3.
DR RefSeq; XP_012968758.1; XM_013113304.2.
DR STRING; 10036.ENSMAUP00000008094; -.
DR GeneID; 101830910; -.
DR KEGG; maua:101830910; -.
DR CTD; 9937; -.
DR eggNOG; KOG1361; Eukaryota.
DR OrthoDB; 23465at2759; -.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.12650; -; 1.
DR Gene3D; 3.60.15.10; Ribonuclease Z/Hydroxyacylglutathione hydrolase-like; 1.
DR InterPro; IPR011084; DRMBL.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR006642; Rad18_UBZ4.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR PANTHER; PTHR23240:SF6; DNA CROSS-LINK REPAIR 1A PROTEIN; 1.
DR PANTHER; PTHR23240; DNA CROSS-LINK REPAIR PROTEIN PSO2/SNM1-RELATED; 1.
DR Pfam; PF07522; DRMBL; 1.
DR Pfam; PF12706; Lactamase_B_2; 1.
DR SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1.
DR PROSITE; PS51908; ZF_UBZ4; 1.
PE 3: Inferred from homology;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|PROSITE-
KW ProRule:PRU01256};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|PROSITE-
KW ProRule:PRU01256}; Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000189706};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU01256}.
FT DOMAIN 122..152
FT /note="UBZ4-type"
FT /evidence="ECO:0000259|PROSITE:PS51908"
FT REGION 14..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 79..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 183..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 243..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 281..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 416..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 510..536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 548..680
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..65
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..94
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..205
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..264
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..305
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..438
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..457
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 513..536
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 560..574
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 591..608
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1023 AA; 112552 MW; 1EC165DD7BCE37CE CRC64;
MLEDTFWEEE IWDYKSKRKP KPAHPNSCSQ NIPESVGRTA DGNDQSKGKK GNKKRNAEDK
GKTRDHTVCL GEADCQIAVG SSQNPSGRDE TQQAQSKDTT PRKHCRTHKN KQVSPRARPV
YDGHCPCCQM PFSSLLGQTP RWHVFECLDS PPVSDTECPE GVLCTSTIPS HYKKYTHLLL
AQSRASNEPP SSPSRVPTGR STAAKPASCN PEERWPVHLK AESLRVLDDS LLMIQCLKTS
ALPPETDRKS PSCANSQMSP APQCTESVKK DKFVRGGLHL PEDAFNSQST SQGTTSLPSP
ETDCGSCEIS YSPLQSDKET YDDSQRELFC TQSSKDSSLE DDGPAVFENF HNPFPRELEG
VCPTAESLVT QADCNALYKI SALSDSFQLL SQTESRLSQD AGVLLFSPAL AAGPAASNCQ
ARKAKPGDPE EPRSLGSSHQ KGKMETSAVG NQIPLPSPLP TSAMPKPLEK EGGERRPLHP
TQNQIRGLRN EVLGATVANS ACACRKVEKL SSTPPAKSLN PLPSSPKCSA SQPSKKVMKQ
MDIGVFFGLP PKRLEPSPSE SASGGRNVNP VASPNKRQPR PCKRKAENSL SNLESDSGDL
NESQRSVEQP GERAQRRRKR HKMSDSPQEG AHQRRSGHPM NNPELGAVSL NKGRAFGRRT
HGRPQRGSTD TPGSSRAGEL RRTCPFYKRI PGTGFTVDAF QYGEVEGCTA YFLTHFHSDH
YAGLSKDFAL PIYCSEITGN LLKKKLRVQE QYIHQLPMDT ECTVDGVKVV LLDANHCPGA
AMILFRPPNG AAVLHTGDFR ADPSMERSLL AGRKVHTLFL DTTYCSPEYT FPSQQEVIQF
AINAAFEAVT LNPRALIVCG TYCIGKEKVF LAIADVLGSK VGMSPEKYKT LQCLNIPEVN
SLITTDMCSS LVHLLPMMQI NFKGLQSHLK KCGGKYDQIL AFRPTGWTHS NNITSIADIT
PQTKGNISIY GIPYSEHSSY LEMKRFVQWL KPQKIIPTVN VGTFQSRSTM EKHFREWRLE
AGY
//
