ID F2Q1Y8_TRIEC Unreviewed; 293 AA.
AC F2Q1Y8;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Anaphase-promoting complex subunit 11 {ECO:0000256|ARBA:ARBA00013928};
GN ORFNames=TEQG_06907 {ECO:0000313|EMBL:EGE08156.1};
OS Trichophyton equinum (strain ATCC MYA-4606 / CBS 127.97) (Horse ringworm
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=559882 {ECO:0000313|Proteomes:UP000009169};
RN [1] {ECO:0000313|Proteomes:UP000009169}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4606 / CBS 127.97 {ECO:0000313|Proteomes:UP000009169};
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).
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DR EMBL; DS995773; EGE08156.1; -; Genomic_DNA.
DR AlphaFoldDB; F2Q1Y8; -.
DR VEuPathDB; FungiDB:TEQG_06907; -.
DR eggNOG; ENOG502RZA9; Eukaryota.
DR HOGENOM; CLU_037984_2_0_1; -.
DR Proteomes; UP000009169; Unassembled WGS sequence.
DR GO; GO:0005680; C:anaphase-promoting complex; IEA:InterPro.
DR GO; GO:0097602; F:cullin family protein binding; IEA:InterPro.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; IEA:InterPro.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR CDD; cd16494; RING-CH-C4HC3_ZSWM2; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR024991; RING-H2_APC11.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR007527; Znf_SWIM.
DR InterPro; IPR039903; Zswim2.
DR PANTHER; PTHR21540:SF0; E3 UBIQUITIN-PROTEIN LIGASE ZSWIM2; 1.
DR PANTHER; PTHR21540; RING FINGER AND SWIM DOMAIN-CONTAINING PROTEIN 2; 1.
DR Pfam; PF04434; SWIM; 1.
DR Pfam; PF12861; zf-ANAPC11; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
DR PROSITE; PS50966; ZF_SWIM; 1.
PE 4: Predicted;
KW Cell cycle {ECO:0000256|ARBA:ARBA00022776};
KW Cell division {ECO:0000256|ARBA:ARBA00022618};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Mitosis {ECO:0000256|ARBA:ARBA00022776};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT DOMAIN 111..143
FT /note="SWIM-type"
FT /evidence="ECO:0000259|PROSITE:PS50966"
FT DOMAIN 191..239
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..64
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 293 AA; 33140 MW; E657ED9EC0A32B58 CRC64;
MKRKRQTDVA SDQPGPARRA RKTQPVPRGA DVIEVTGEVA SKSPKKQKKA PRQKNEERRP
RAFRSKPPQT YLVKLDRART QRLFVLRRTR GGTEEVPEEY IDIAGSTGNI YQVVIGKEPS
CTCPDAKKGN QCKHVVYVLY HVLRAHEHLR YQLAFLSSEL HEIFENAPQN PAEAASTGNT
KGVRKEIDGD CPICFMPLEA ENESIVWCKA ACGNNVHQAC FQQWVSSQRG KEIRCVYCRT
PWEANNVPAL ENLLETGQVN SEGYLNVGAS LGLSCLRDCS TYHQPLGYRR RYR
//
