ID U4L5E6_PYROM Unreviewed; 1241 AA.
AC U4L5E6;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Anaphase-promoting complex subunit 11 {ECO:0000256|ARBA:ARBA00013928};
GN ORFNames=PCON_11615 {ECO:0000313|EMBL:CCX12021.1};
OS Pyronema omphalodes (strain CBS 100304) (Pyronema confluens).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC Pezizales; Pyronemataceae; Pyronema.
OX NCBI_TaxID=1076935 {ECO:0000313|EMBL:CCX12021.1};
RN [1] {ECO:0000313|EMBL:CCX12021.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS100304 {ECO:0000313|EMBL:CCX12021.1};
RC TISSUE=Vegetative mycelium {ECO:0000313|EMBL:CCX12021.1};
RX PubMed=24068976; DOI=10.1371/journal.pgen.1003820;
RA Traeger S., Altegoer F., Freitag M., Gabaldon T., Kempken F., Kumar A.,
RA Marcet-Houben M., Poggeler S., Stajich J.E., Nowrousian M.;
RT "The genome and development-dependent transcriptomes of Pyronema confluens:
RT a window into fungal evolution.";
RL PLoS Genet. 9:E1003820-E1003820(2013).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; HF935675; CCX12021.1; -; Genomic_DNA.
DR AlphaFoldDB; U4L5E6; -.
DR STRING; 1076935.U4L5E6; -.
DR eggNOG; KOG2066; Eukaryota.
DR OMA; CYIRLQD; -.
DR OrthoDB; 8838at2759; -.
DR Proteomes; UP000018144; Unassembled WGS sequence.
DR GO; GO:0005680; C:anaphase-promoting complex; IEA:InterPro.
DR GO; GO:0005768; C:endosome; IEA:UniProt.
DR GO; GO:0099023; C:vesicle tethering complex; IEA:UniProt.
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 GO; GO:0006886; P:intracellular protein transport; IEA:UniProtKB-UniRule.
DR GO; GO:0006623; P:protein targeting to vacuole; IEA:InterPro.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR000547; Clathrin_H-chain/VPS_repeat.
DR InterPro; IPR024991; RING-H2_APC11.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR045111; Vps41/Vps8.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR12616; VACUOLAR PROTEIN SORTING VPS41; 1.
DR PANTHER; PTHR12616:SF1; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 41 HOMOLOG; 1.
DR Pfam; PF00637; Clathrin; 1.
DR Pfam; PF12861; zf-ANAPC11; 1.
DR SMART; SM00299; CLH; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS50236; CHCR; 1.
PE 4: Predicted;
KW Cell cycle {ECO:0000256|ARBA:ARBA00022776};
KW Cell division {ECO:0000256|ARBA:ARBA00022618};
KW Mitosis {ECO:0000256|ARBA:ARBA00022776}.
FT DOMAIN 1152..1231
FT /note="RING-type"
FT /evidence="ECO:0000259|SMART:SM00184"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 92..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 428..454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..39
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1241 AA; 138135 MW; 03FA71304E102579 CRC64;
MPPPHDNDHD DHADEEPTDN ASVVDSGDEE EEEEEEDDEE PRLKYTRLTK SLGGVYRNGD
AVSTTVVFGD RMHILSLPSL TPLRTYHAHS ASVTSISISP PPPPPVAIPT KRHKDAYHDR
HISVASASID GLVCTVPLLP STPPAPGQSL STVPYAKSEI TLKNFKRPIL AVALSPNFRA
DRTFLSGGLA GNLVLSVAPT GGVAGGSWMT LGLSGGAKDT ILHSGEGAIS AIAWSKESPR
YVAWANEQGI KIMRSHITPP TLQAQTQAQT QGPAATTEEI TGNPGLIGWI PGFGSGPISG
NETAWKRISA IERPENIPEE LASLHKPRLE WIDRRALLTS DPDDAATGTT LNVKDVDWGD
KEKLLVGWGG TVWVIDVFPG SGEPGEENSN GWAQITHILQ TDCTISGLYM YTPSLILMLA
YLTNTEAPTE EEVETPPTSP TSPRSPRASP RFRRGRTNAL IPELRFIDLE TSEEVSADEL
MMSRFESLAV GDYHLGILPA TPTSVHPPTP DNEQAEGGLG ASLWTAALAP TQLFNSGAQS
IRSFGTGSRR DSIAASGFSS ATAALRGARA KEVTWGEDEK GTKIYITSPY DVVFATERSQ
KDHLSWMLDR KKYADAWHLI DKHPEVVDPD TTSLSMYDEE ERKVIVHLDD DYDSDSTVTS
SVRQRSVKRY TVAEKEKRRI GELWLRDLID AGEWKRAGEV CGQVLGLSSR WEYWVWVFEA
AKKIEEITNY IPTTQLSPPL PSVIYEIVLA YYLNHDRRRF RELLLEIWKP EGSHTLYDAR
TLVDTIILKI ENREDEIHKG DTDWRLLQEC LARLYMVLRE PRNALRRYMI LKDADEAFRL
IRDYRLVDTV KDDIASLIML RVTDKQLAIA PIKELEKATY EAISLLINES DRGILSPKQV
VEQLSSDKIV AGRLFLYFYL RRLWKNQHDQ MFTTTGGALA EFEDLMVELF AEYDRPLLME
FLKDSHNYSL EKASAVCERR NYIPELVHLL SKTGQTKRAL FLIIDKLADV TQAISFAKQQ
DDPDLWNDLL DYSMDKPKFI RGLLENVGTA IDPITLVRRI PAGLQIEGLK EALAKILKEY
AVQWSICDGV AKAMTSEVAR GMESLRHGQR RGVKFQVGEI APLPVTPDNI EIALERAMET
ERVNSANPNE VCGICEKRFS GHNGKQRTLV AFACGHVFHL HCISRPVTAA DEEDDEHEEE
IVQSGYGRSV GAKVTRAALL GEKVKKGCSV CAKRKREEIM V
//
