ID A1CAF9_ASPCL Unreviewed; 674 AA.
AC A1CAF9;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE SubName: Full=Sister chromatid cohesion protein (Eso1), putative {ECO:0000313|EMBL:EAW12727.1};
GN ORFNames=ACLA_011540 {ECO:0000313|EMBL:EAW12727.1};
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612 {ECO:0000313|EMBL:EAW12727.1, ECO:0000313|Proteomes:UP000006701};
RN [1] {ECO:0000313|EMBL:EAW12727.1, ECO:0000313|Proteomes:UP000006701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1
RC {ECO:0000313|Proteomes:UP000006701};
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; DS027049; EAW12727.1; -; Genomic_DNA.
DR RefSeq; XP_001274153.1; XM_001274152.1.
DR AlphaFoldDB; A1CAF9; -.
DR STRING; 344612.A1CAF9; -.
DR EnsemblFungi; EAW12727; EAW12727; ACLA_011540.
DR GeneID; 4706806; -.
DR KEGG; act:ACLA_011540; -.
DR VEuPathDB; FungiDB:ACLA_011540; -.
DR eggNOG; KOG2095; Eukaryota.
DR HOGENOM; CLU_012348_7_1_1; -.
DR OMA; AWPCSNL; -.
DR OrthoDB; 118267at2759; -.
DR Proteomes; UP000006701; Unassembled WGS sequence.
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 PANTHER; PTHR45873; DNA POLYMERASE ETA; 1.
DR PANTHER; PTHR45873:SF1; DNA POLYMERASE ETA; 1.
DR Pfam; PF00817; IMS; 2.
DR Pfam; PF11799; IMS_C; 1.
DR Pfam; PF21704; POLH-Rev1_HhH; 1.
DR Pfam; PF18439; zf_UBZ; 1.
DR PIRSF; PIRSF036603; DPol_eta; 3.
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.
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 Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000006701};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 46..328
FT /note="UmuC"
FT /evidence="ECO:0000259|PROSITE:PS50173"
FT DOMAIN 595..629
FT /note="UBZ3-type"
FT /evidence="ECO:0000259|PROSITE:PS51907"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 570..595
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 629..674
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 570..586
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 637..652
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 674 AA; 76021 MW; E590FE2ED51E514C CRC64;
MSRSPSEPCA TPASSPSSSL KHRSQYTYRQ LQLLRQGSTA TPLRVIAHID LDAFYAQCEM
VRLAKPRETP LAVRQWDSLI AINYPARSFG ITRMMSADEA RKHCPEIVLQ HVATFREGEG
GQWAYRDDAF KNISTDKVCL DPYRAESRKI LKFTKEELSR WHADLVDGER GAGAQFQIQP
ASLEKASIDE VFIDLSPLVY GVLLQRYPEL RAGSQDDDRF TPLPRPPTTA LEWNPEDCLI
DLDENETEVD DPDWDDIAML IGSEIVRSVR KFVWDKLKYT CSGGVARNKM MAKLGSACNK
PNKQTIVRNR AVQNFLGGYK FTKIRMLGGK LGDQITASFG TEQVSDLLKV SHEQLRAKLD
DDTASWLYGI IRGEDKSEVN PRTQIKSMLS AKSFRPSINS VDQAEKWLRI FAADIYGRLV
EEGVLENRRR PRTVSLHHRQ GAQVRSKQLP IPGSATIDES LLFELGRTLL RQVIVDGRAW
PCANLSLSVG GFEDGVSKNK AIDSFLIRGE QAKNVVQPIR NQDIIGTMDT HQHDDKRRKA
EVNGIRRFFS IPPDTIQEAV SPDLNTIQHD RKKEEGSDHI PHHEQPSRSE QPVAAQEALY
TCNRCRQSLP IDGRNEHDDW HFAKDLEIEE RQAARNDQQA SRSVSDAGSS QPRGRAARTA
RGRSEKGQTR LSFG
//
