ID K8FC50_9CHLO Unreviewed; 1450 AA.
AC K8FC50;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=Anaphase-promoting complex subunit 2 {ECO:0000256|ARBA:ARBA00016068};
GN OrderedLocusNames=Bathy13g02800 {ECO:0000313|EMBL:CCO19253.1};
OS Bathycoccus prasinos.
OC Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales;
OC Bathycoccaceae; Bathycoccus.
OX NCBI_TaxID=41875 {ECO:0000313|EMBL:CCO19253.1, ECO:0000313|Proteomes:UP000198341};
RN [1] {ECO:0000313|EMBL:CCO19253.1, ECO:0000313|Proteomes:UP000198341}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCC 1105 {ECO:0000313|EMBL:CCO19253.1,
RC ECO:0000313|Proteomes:UP000198341};
RA Genoscope - CEA;
RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the cullin family. {ECO:0000256|PROSITE-
CC ProRule:PRU00330, ECO:0000256|RuleBase:RU003829}.
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DR EMBL; FO082266; CCO19253.1; -; Genomic_DNA.
DR RefSeq; XP_007509450.1; XM_007509388.1.
DR STRING; 41875.K8FC50; -.
DR GeneID; 19012232; -.
DR KEGG; bpg:Bathy13g02800; -.
DR eggNOG; KOG2165; Eukaryota.
DR OrthoDB; 2786196at2759; -.
DR Proteomes; UP000198341; Chromosome_13.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:InterPro.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR Gene3D; 1.20.1310.10; Cullin Repeats; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR044554; APC2-like.
DR InterPro; IPR014786; APC2_C.
DR InterPro; IPR016158; Cullin_homology.
DR InterPro; IPR036317; Cullin_homology_sf.
DR InterPro; IPR001373; Cullin_N.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR45957; ANAPHASE-PROMOTING COMPLEX SUBUNIT 2; 1.
DR PANTHER; PTHR45957:SF1; ANAPHASE-PROMOTING COMPLEX SUBUNIT 2; 1.
DR Pfam; PF08672; ANAPC2; 1.
DR Pfam; PF00888; Cullin; 2.
DR SMART; SM01013; APC2; 1.
DR SMART; SM00182; CULLIN; 1.
DR SUPFAM; SSF75632; Cullin homology domain; 2.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS50069; CULLIN_2; 1.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW Cell division {ECO:0000256|ARBA:ARBA00022618};
KW Mitosis {ECO:0000256|ARBA:ARBA00022776};
KW Reference proteome {ECO:0000313|Proteomes:UP000198341};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 955..1307
FT /note="Cullin family profile"
FT /evidence="ECO:0000259|PROSITE:PS50069"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 106..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 179..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 247..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 354..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 638..662
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 681..723
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 763..793
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 872..909
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1116..1148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1161..1215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..213
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..263
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..403
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 681..706
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 707..723
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 872..892
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1170..1184
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1450 AA; 163177 MW; EAE49333DE9AB771 CRC64;
MKTTRTRTRR QKSVGEEEEE EEEETTMRVA FLLQERFKAY REMLSKSSSS KSSSVEDGEG
VCGAIDAFVD EDDDDDENAK VFFFDDSFRE EFRECCFSAA TLTKNQTRTR RRKEEEEEEE
EEEGAAAATT TTLLKSIFEM RRAFKDICVE QFLREAKAYV LRSPLRELTE TLRKIEKEEG
EAESLSAVIA NALDREEEEE EEDDDEEDDE EEASSPGFRC LRAFSAFARK VERLKAIASE
VAEMVLVGEE EEEKDDDDKD DDGADGKENE KIISAAKGSR SSVKSGNLLP LDAQSQKKKF
EKKFDDLIAE LIVSCGPRNA TRVLSAYYAK VIVKFRNKCA FPLDEEEFYA SLEEEKKSGR
SRRPATLNTT TSTKTDENNE EESMQLSDDD DNGGDDDDDD EENEVQQYRK FVKNVRKHLR
NCASPTKMLG KLECAQIERV HKDAILKHFK RYSYEAFEIA SDFAIKHFAL KFAASNFKAS
ALKCVALYSR VVPLQIAKTV FGFESVQFGN EAPSQFHRKF ISSSKEHLGA LRIEELFDIV
VDHPDSLGAV KDLRMCLSDD RQFGLRESLV SSFNEQLRRR LLHPGARTAD VISQYIGTIK
TMRDLDPSGI VLDLVSGPIR KYLRKRKDTI RCVVTMLTDD GSGDRNDNND GDGDGGGGDA
STANALFAEL GAMAREELKN TNDNADDANP HHHDRRRRKA SGGDIVDEDG DESESSELDE
DDGASFNQFN EQEFNAFKAN ENRKKYQEYQ MQMRNTFQGV EDYDMDDADE GANNKDGNGS
DESESESEGS EDRGLDEFAH FYPAPKKSTS LLKSQNSGMD AIMDYESKQL SRTLTSFGVD
QLQNLVLDRT ESGMTWGKNF GTPVPVDILS REQSRKMQQQ QQQQQQEQQH QEQRHQNLQK
AGELESLIPG RKSASAPKKI LKRFPGDAWD PEPVVSEATK LRSRKRRQLR DIIGLLVGIY
GGKELFVNEY RLMLADKLLQ KSNYDAERET LALELLKNKF GETHLHDCEV MLRDVNDSRR
VNANVKTRPA EGTPLAKEGI RTTEMLKESP VQALILSKLF WPKDIAKSAA TIVAPASTQA
SLPHPVSTPS IVPSLGQEQE PVQMTMNTNE MYVGEEEEVD GLNDPTSAAA AANTAPTSPP
PEGDASVLDD DIDAQLQQQL RDQEEGDEGT PSLLSRSLST SPPRDPGVSG ERENERMKRT
TVGARPPFPS AHNDIILPPA IDQAMRAYEE RYHELKAPRK MTWMRSLGRV VVEVSLINEK
PFEIVVSPLH AAILYHFTER EKWTAEELAK VLNATTKAVR QRMVLWMNRG VVSETSEATY
ELNTVASSAT NNKMMEHRRA TGSLKTTIAT DGGGGGPGEN DDDDDDFLHR AGSSAEEVEA
AEMKVYEQYV MGMLTNFPSM PIERIHNMLK MFVVEPAYDK TQAQLEKFLM SLVRAEKLAH
DGENFSKRKE
//
