ID A0A168FDG5_CORDF Unreviewed; 676 AA.
AC A0A168FDG5;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Sister chromatid cohesion protein Eso1 {ECO:0000313|EMBL:OAA75030.1};
GN ORFNames=LEL_07018 {ECO:0000313|EMBL:OAA75030.1};
OS Akanthomyces lecanii RCEF 1005.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Akanthomyces;
OC Cordyceps confragosa.
OX NCBI_TaxID=1081108 {ECO:0000313|EMBL:OAA75030.1, ECO:0000313|Proteomes:UP000076881};
RN [1] {ECO:0000313|EMBL:OAA75030.1, ECO:0000313|Proteomes:UP000076881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCEF 1005 {ECO:0000313|EMBL:OAA75030.1,
RC ECO:0000313|Proteomes:UP000076881};
RX PubMed=27071652; DOI=10.1093/gbe/evw082;
RA Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT "Divergent and convergent evolution of fungal pathogenicity.";
RL Genome Biol. Evol. 8:1374-1387(2016).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OAA75030.1}.
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DR EMBL; AZHF01000005; OAA75030.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A168FDG5; -.
DR STRING; 1081108.A0A168FDG5; -.
DR OrthoDB; 118267at2759; -.
DR Proteomes; UP000076881; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0070987; P:error-free translesion synthesis; IEA:UniProt.
DR Gene3D; 3.30.70.270; -; 1.
DR Gene3D; 3.40.1170.60; -; 1.
DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR Gene3D; 3.30.1490.100; DNA polymerase, Y-family, little finger domain; 1.
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; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR041298; UBZ3.
DR InterPro; IPR001126; UmuC.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR45873; DNA POLYMERASE ETA; 1.
DR PANTHER; PTHR45873:SF1; DNA POLYMERASE ETA; 1.
DR Pfam; PF00817; IMS; 1.
DR Pfam; PF11799; IMS_C; 1.
DR Pfam; PF21704; POLH-Rev1_HhH; 1.
DR Pfam; PF18439; zf_UBZ; 1.
DR PIRSF; PIRSF036603; DPol_eta; 2.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR SUPFAM; SSF100879; Lesion bypass DNA polymerase (Y-family), little finger domain; 1.
DR PROSITE; PS50173; UMUC; 1.
DR PROSITE; PS51907; ZF_UBZ3; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 4: Predicted;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000076881};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 48..310
FT /note="UmuC"
FT /evidence="ECO:0000259|PROSITE:PS50173"
FT DOMAIN 585..620
FT /note="UBZ3-type"
FT /evidence="ECO:0000259|PROSITE:PS51907"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 413..435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 500..521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 626..676
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..432
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 505..521
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 635..676
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 676 AA; 74704 MW; D254D88A0C1A732B CRC64;
MPSSPEHYAP LSSAEQHDDG THRTRSQFTY RHLSQMAGYV ASSPLRVIAH VDLDAFYAQC
EMVRLGLPDD QPLAVQQWQS LIAINYPARK GGIGGRLGSV ADAKKVCPNL IAQHVATWRE
GDDKWAYRDD AAANIATDKV SLDPYRLESR KILALIKEHL PQNLQRVEKA SVDEVFLDLS
AQVHSILLER FPELQQPPPY NDPAERLPLP SISALDWQAD ALIDLDEERE GKDPDWDDVA
ILLGSEIVRE VRAEIRKQLR YTCSGGVACN KLLSKLGSGY KKPNRQTVVR NRAVGIFLHE
FKLTRIRNLG GKLGEQVVNV FGTELVKDLL PVPVEQLKAK LGEETGIWLY NTIRGVDTSE
VNPRTQIKSM LSAKSFRPYI NTHDQAVKWL RIFVGDIFNR LLEEGVLENK RRPKTVHLSA
RQPTQTRSKQ IPIPQGRPID DAMLMNLAKE LLSQILGDGS IWPCSNLSLT VGGFEDGIKN
NMGIGAFLVK GDAAISLKAA DHGNSESTSS ERPHKRARAD EAGIQRFFAK DQREKTPSAE
ADATVAHADI HDGDNVDFRS NHKSDADAEA EAEVEACIRI QHGQPQPASL LCARCNASFE
MPEALQSHMD WHMAKDIQDE ERVKPAFAER SRNGIAVRGT SSKGPTGSSS SRRGGRGGGG
SSSSKLEQGQ SKLKFG
//
