ID A0A165Y3U7_9AGAM Unreviewed; 1278 AA.
AC A0A165Y3U7;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=DNA repair protein {ECO:0000313|EMBL:KZV71579.1};
GN ORFNames=PENSPDRAFT_751674 {ECO:0000313|EMBL:KZV71579.1};
OS Peniophora sp. CONT.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Russulales; Peniophoraceae; Peniophora.
OX NCBI_TaxID=1314672 {ECO:0000313|EMBL:KZV71579.1, ECO:0000313|Proteomes:UP000077086};
RN [1] {ECO:0000313|EMBL:KZV71579.1, ECO:0000313|Proteomes:UP000077086}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CONT {ECO:0000313|EMBL:KZV71579.1,
RC ECO:0000313|Proteomes:UP000077086};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC -!- SIMILARITY: Belongs to the DNA polymerase type-Y family.
CC {ECO:0000256|ARBA:ARBA00010945}.
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DR EMBL; KV424511; KZV71579.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165Y3U7; -.
DR STRING; 1314672.A0A165Y3U7; -.
DR InParanoid; A0A165Y3U7; -.
DR OrthoDB; 169741at2759; -.
DR Proteomes; UP000077086; Unassembled WGS sequence.
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 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; 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:UP000077086}.
FT DOMAIN 213..301
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT DOMAIN 529..719
FT /note="UmuC"
FT /evidence="ECO:0000259|PROSITE:PS50173"
FT REGION 24..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 123..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 333..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 940..961
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 990..1016
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..60
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..167
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..362
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1278 AA; 140783 MW; 0AE724DA5096A109 CRC64;
MAALSADDSF DYFGSEDSAF LRELQDVQLP GDARQAGDTS KPSLLNPDSE LDQSGDSDLL
PRNRTLDITF GGPPCAQPSK RRRLSDTPPV SPLRSHDPPA AKRPRHDINL SIFADLSSDI
SFNELSPPLP QSDADPAPVQ LPSQVQSPRK AGGSNTKRNP NSNGAYNALQ TDDDNYLGED
IYGAAHFGDF GEYMRRKRAK LQIQNTELDE GTERNQIFRG VSIYINGRTK PSVQELRKLI
VDYGGVFQAY LDKKALVTHV ITCSLTPAKV REFQHMKVVR PEWLVDSVQK GALLPWHDYI
FQTGGRIEGS MQGRTMQPSM HTFPAQRAQT SAQGFASSRA QSTMYGVQTT RASTSGRNYA
ASKRPRSPSP DADYGFDESF PDDDWERSFD ADEAGLPPVY RIPQWKSTIP AKPATKPVQP
PPASKAPVYA NGPNTHAARA MQDPAWRAAH TSVAPGFIEG YYRNSRLHYL STWKTELRVL
VADAQDRAER GDVPGVEARL ASQGLSMRGA KLTSPKGKGR AREGSQRVIM HVDFDAFFVS
VGLLDRPEMR GKPVVVCHSQ GGAGGASSTS EIASASYEAR EFGIKNGMSL QQARQLCPSI
STIPYEFEKY KKLSLKFYTI LMSVADDLQA VSVDEALIDV TSSVEQMVSS NPAKDFAESV
RAQVKEATGC TVSIGIAHNI MMARLATRKA KPAGSFHLTE DEIPALMGTL DIKDLHGFGS
AACDKAQEKL GSTNLGELAK RSRGVLCDAL GKGTGETLWK AIRGIDERKL ESDKPRKSVS
CEINYGIRFE DNEQAERFVH QMAEEVTRRL QAINKKGRSL TLKVMQRDPE APVEAPKFMG
HGICITHNRQ SPLSGALGRA TDDSNIIGAL SWKLLRSMNI PPQELRGLGI QIQKLDDEVV
VVPAGQGRLQ FKSKDGKSYA GQGRIHDPLE RLVAELDVLP TPAAMPPPHG APATRPDVDL
PNLSQLDQSV YNALPDDIRA ELSQEYKRRS VTPAPGHNAA REPSAGPSNV GTDAPAPNLA
RITRALAPRS RPHISPQKRL YGLLARPAQK VKIPPPRVDE AELVALGLDP GVFAVLPVKI
QREQLAQARG VATRLSQRPA EAVKPLKAPK KLGERFRYFD PLNEIIPPPP PPFAVHVELP
TLRKPKKNAR QVQEDAQALL AAWLQGFQAH VPHRRDVDHF AKYLSLCVES DLGIEQATAL
MRWWRILLRR SLGLWEGMEL DEDVEQMLEE WVAGNRTFEG VRVSEELLGC AWWVAFEEIK
CKMNEVARKR YGGSLSFR
//