ID A0A067PY50_9AGAM Unreviewed; 1237 AA.
AC A0A067PY50;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=DNA repair protein REV1 {ECO:0008006|Google:ProtNLM};
GN ORFNames=JAAARDRAFT_126496 {ECO:0000313|EMBL:KDQ59748.1};
OS Jaapia argillacea MUCL 33604.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Jaapiales; Jaapiaceae; Jaapia.
OX NCBI_TaxID=933084 {ECO:0000313|EMBL:KDQ59748.1, ECO:0000313|Proteomes:UP000027265};
RN [1] {ECO:0000313|Proteomes:UP000027265}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MUCL 33604 {ECO:0000313|Proteomes:UP000027265};
RX PubMed=24958869; DOI=10.1073/pnas.1400592111;
RA Riley R., Salamov A.A., Brown D.W., Nagy L.G., Floudas D., Held B.W.,
RA Levasseur A., Lombard V., Morin E., Otillar R., Lindquist E.A., Sun H.,
RA LaButti K.M., Schmutz J., Jabbour D., Luo H., Baker S.E., Pisabarro A.G.,
RA Walton J.D., Blanchette R.A., Henrissat B., Martin F., Cullen D.,
RA Hibbett D.S., Grigoriev I.V.;
RT "Extensive sampling of basidiomycete genomes demonstrates inadequacy of the
RT white-rot/brown-rot paradigm for wood decay fungi.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:9923-9928(2014).
CC -!- SIMILARITY: Belongs to the DNA polymerase type-Y family.
CC {ECO:0000256|ARBA:ARBA00010945}.
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DR EMBL; KL197715; KDQ59748.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A067PY50; -.
DR STRING; 933084.A0A067PY50; -.
DR HOGENOM; CLU_003901_0_3_1; -.
DR InParanoid; A0A067PY50; -.
DR OrthoDB; 169741at2759; -.
DR Proteomes; UP000027265; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR GO; GO:0070987; P:error-free translesion synthesis; IEA:UniProt.
DR CDD; cd17719; BRCT_Rev1; 1.
DR CDD; cd01701; PolY_Rev1; 1.
DR CDD; cd19318; Rev1_UBM2; 1.
DR Gene3D; 3.30.70.270; -; 1.
DR Gene3D; 3.40.1170.60; -; 1.
DR Gene3D; 6.10.250.1490; -; 1.
DR Gene3D; 6.10.250.1630; -; 1.
DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR Gene3D; 3.40.50.10190; BRCT domain; 1.
DR Gene3D; 3.30.1490.100; DNA polymerase, Y-family, little finger domain; 1.
DR Gene3D; 1.20.58.1280; DNA repair protein Rev1, C-terminal domain; 1.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR036775; DNA_pol_Y-fam_lit_finger_sf.
DR InterPro; IPR017961; DNA_pol_Y-fam_little_finger.
DR InterPro; IPR031991; Rev1_C.
DR InterPro; IPR038401; Rev1_C_sf.
DR InterPro; IPR047346; Rev1_UBM1/2.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR001126; UmuC.
DR PANTHER; PTHR45990; DNA REPAIR PROTEIN REV1; 1.
DR PANTHER; PTHR45990:SF1; DNA REPAIR PROTEIN REV1; 1.
DR Pfam; PF16589; BRCT_2; 1.
DR Pfam; PF00817; IMS; 1.
DR Pfam; PF11799; IMS_C; 1.
DR Pfam; PF16727; REV1_C; 1.
DR SMART; SM00292; BRCT; 1.
DR SUPFAM; SSF52113; BRCT domain; 1.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR SUPFAM; SSF100879; Lesion bypass DNA polymerase (Y-family), little finger domain; 1.
DR PROSITE; PS50172; BRCT; 1.
DR PROSITE; PS50173; UMUC; 1.
PE 3: Inferred from homology;
KW DNA synthesis {ECO:0000256|ARBA:ARBA00022634};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000027265}.
FT DOMAIN 127..215
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT DOMAIN 435..642
FT /note="UmuC"
FT /evidence="ECO:0000259|PROSITE:PS50173"
FT REGION 46..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 245..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 842..867
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 942..961
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1056..1094
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1181..1200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..74
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..303
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..328
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1076..1090
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1182..1200
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1237 AA; 135688 MW; 9D4EDFACAA4E72F8 CRC64;
MGPPLVSSGA STDYFGDEDP SFLEALNKAV FPGDLDDSMV VDSEVCIEET TRATSKRPRS
PDDWEEEDVQ SEGGSHQLEE IPPNYTDDST IYGASRFGEF GEYMRRKRAK LQIQNTEMDG
EGQASDSSRK IFRGLAIYIN GWTDPSVQDL RQLIIKHGGA YHAYLDKKAL VTHIITCSLT
PAKIREFKHM KVVKPSWLVD SAKAGQLLPW QEFKYKPGER LEDSQGKKAP QASLLNGFVS
QRQRESQVAE AVESAPIGAS GSKTQQPEES IPEPPHTPPR IPRSKPPLFP KAPTSPTSPS
HIPPTTDPTS KSNPYASSKS NPNASRAMAN PAWRQAHTSV APDFIEGYYK HSRLHHLSIW
KAELKELVAE AQERAEKGLM EGVDSEEGEG GGKKVGGGID DYTMRGAELV LVSPKGKGKA
KARDLDEDVE GERVIMHCDF DCFFVSAGLV DRPHLRGKPV VVCHSQGAQG GMSSTSEIAS
ASYEAREFGI KGGMSLQQAR KLCPGILTIP YEFEKYKQYS LLFYTILMTH ADDLQAVSVD
EALIDVSSSV ARLKANRARI QQQSTSESEL ASVHPAKELA EVIRAQVRKA TSCEVSIGIS
HNILLARLAT RRAKPSGSYH LLPPSIPTFL APLEINDLHG FGRSIRQKAE EKLGSVVLGE
LALKSKGVLC EVLGKGTGET LYNAIRGVDH KKLDSNKPRK SVSCEINYGI RFEGNKQAEE
FVYRLAEEVA ARLDKVEMLG KSLILKVMKR DATAPVEPAK FLGHGPCDTF NKQTPLIGPG
GRATSDAKVI GEVAWRLLKS FDFDPVELRG VGIHVTKLEK SSGVEVTMQP GQAKLSFKVP
IVDGGGGDRQ EGPSISVQPI HGAGGDDEDD DVVEIIPQPP KAQEIPETLE IPTHLDLPSF
SQVDKSVFDA LPADLRQELE AEYARRSASP APHLFKVPAL PTHHHQQPQT AGPSRLSPPK
PKLMVKGTTT TNVKRITQQL APRSRPSISP TKTKLFVGKR ENGLKISDAE LLKLGVDPDV
FGLLPVDLQR EQLAIARQSK GGFGLGLTDN NSVNTAHQKI IIKPRNRRST RSPSITHPRR
PPPPQALYPP LPTIKQRGPN KGEKLVFCET DDVQRVIGEW VERCRESVVN ERDVEYFGRY
LVGCCESGGG RGVERGVEVM KWWMVLLRGY WGVWEGGGEG DVEMGEGGKG RDGEGRDGEG
RVTSEIVGRA WWKAFWEVKG RMDEVVRKKI GGSLSLK
//
