ID F2RNC5_TRIT1 Unreviewed; 642 AA.
AC F2RNC5;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Sister chromatid cohesion protein {ECO:0000313|EMBL:EGD92824.1};
GN ORFNames=TESG_00391 {ECO:0000313|EMBL:EGD92824.1};
OS Trichophyton tonsurans (strain CBS 112818) (Scalp ringworm fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=647933 {ECO:0000313|Proteomes:UP000009172};
RN [1] {ECO:0000313|Proteomes:UP000009172}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 112818 {ECO:0000313|Proteomes:UP000009172};
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; GG698477; EGD92824.1; -; Genomic_DNA.
DR AlphaFoldDB; F2RNC5; -.
DR HOGENOM; CLU_012348_7_1_1; -.
DR OrthoDB; 118267at2759; -.
DR Proteomes; UP000009172; 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 Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 39..323
FT /note="UmuC"
FT /evidence="ECO:0000259|PROSITE:PS50173"
FT DOMAIN 584..618
FT /note="UBZ3-type"
FT /evidence="ECO:0000259|PROSITE:PS51907"
FT REGION 504..549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 617..642
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..523
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 524..540
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 642 AA; 72259 MW; 55D51D35E71E1908 CRC64;
MATGPASFHD EDSRPSSRFT YRHFQLLRSF STRTPLRVIA HIDLDAFYAQ CEMIRLNTPR
DQPLAVQQWQ SLIAVNYAAR PFGVSRMITA AEARKLCPQL LTPHVATFRE GEGENWAYRE
GDYSVQKDKV SLDPYRAESR KILAVMKTTL LTWAEGVYEG CRGQFSEPSD MVRLEKAGID
EVFVDLSALV FGTLLHRYEI LQQAATLEVS KDGHSAFLPR PETTALIWGE DDELIDLDTG
ESEEDDPEWD DIVIQVGAEI VKFVRTAVWD QLKYTCSGGI ARNKMMAKLG SACNKPNRQT
IVRNRAIQQF LSGYKFTKIR SLGGKLGKKI SSEFETDKIS DLLTIPLDQL KNKLDDDTGM
WLYQIIRGED DSEVTPRTEI KSMISAKSFN PKLASLDQAE KWMRIFVAEI YGRLVDEGVL
ENKRRPKMIT VHHYGPNQDK SRQTHIPTGG AIDQVMLFEL AKNLLQQVVS WPCSHLSLTV
SGFESGITGN KKLDSFFIRG AGETPVSQRD GSMPNSSCQR ELHGDNSAHQ RKKQKVGEAH
RQPPSKGAGF FARYKTSAKQ ILLEPCPENT GESLANLQTN PTSYYSTQDV CSRCGETVPE
FMQSEHDDWH LAKDLESQEQ QSLNAARARS SGKTRQTRLA FG
//
