ID A0A1R2C2H8_9CILI Unreviewed; 727 AA.
AC A0A1R2C2H8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Cullin family profile domain-containing protein {ECO:0000259|PROSITE:PS50069};
GN ORFNames=SteCoe_15910 {ECO:0000313|EMBL:OMJ83197.1};
OS Stentor coeruleus.
OC Eukaryota; Sar; Alveolata; Ciliophora; Postciliodesmatophora;
OC Heterotrichea; Heterotrichida; Stentoridae; Stentor.
OX NCBI_TaxID=5963 {ECO:0000313|EMBL:OMJ83197.1, ECO:0000313|Proteomes:UP000187209};
RN [1] {ECO:0000313|EMBL:OMJ83197.1, ECO:0000313|Proteomes:UP000187209}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WM001 {ECO:0000313|EMBL:OMJ83197.1};
RA Slabodnick M., Ruby J.G., Reiff S.B., Swart E.C., Gosai S., Prabakaran S.,
RA Witkowska E., Larue G.E., Fisher S., Freeman R.M., Gunawardena J., Chu W.,
RA Stover N.A., Gregory B.D., Nowacki M., Derisi J., Roy S.W., Marshall W.F.,
RA Sood P.;
RT "The macronuclear genome of Stentor coeruleus: a giant cell with tiny
RT introns.";
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SIMILARITY: Belongs to the cullin family.
CC {ECO:0000256|ARBA:ARBA00006019, ECO:0000256|PROSITE-ProRule:PRU00330,
CC ECO:0000256|RuleBase:RU003829}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OMJ83197.1}.
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; MPUH01000312; OMJ83197.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R2C2H8; -.
DR OrthoDB; 21270at2759; -.
DR Proteomes; UP000187209; Unassembled WGS sequence.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:InterPro.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR Gene3D; 1.20.1310.10; Cullin Repeats; 4.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR045093; Cullin.
DR InterPro; IPR016158; Cullin_homology.
DR InterPro; IPR036317; Cullin_homology_sf.
DR InterPro; IPR001373; Cullin_N.
DR InterPro; IPR019559; Cullin_neddylation_domain.
DR InterPro; IPR016159; Cullin_repeat-like_dom_sf.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR11932; CULLIN; 1.
DR PANTHER; PTHR11932:SF168; CULLIN-3; 1.
DR Pfam; PF00888; Cullin; 1.
DR Pfam; PF10557; Cullin_Nedd8; 1.
DR SMART; SM00182; CULLIN; 1.
DR SMART; SM00884; Cullin_Nedd8; 1.
DR SUPFAM; SSF75632; Cullin homology domain; 1.
DR SUPFAM; SSF74788; Cullin repeat-like; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS50069; CULLIN_2; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000187209}.
FT DOMAIN 376..598
FT /note="Cullin family profile"
FT /evidence="ECO:0000259|PROSITE:PS50069"
SQ SEQUENCE 727 AA; 85503 MW; 85CA641A14EB03E6 CRC64;
MSKRVSGIPF VKIAMPVPRE QAEETWKSLD HSIGLIFDFQ ASKLSFEELY RKAYDLIIHK
YGDLLYNGLT DSFHRQCSII LKKLRSEVSG NLFEVLLQSW TNFKMFINMI KDILMYMDRN
YVSSKNLLPA YELGLSIFKS DIILDADISI KIRIWILENI KNDRNMQMIS TEKCLIKNII
NMLAELNPRE KNIYISIFEN PFIEESRNFF TQEAQEWIAS DSCPEYLKKV ERRLKEEQER
VEQLMDPRTE NLILKIVDEC FIKAHARTLV SMEGSGCSRM IDNLQLDDLK RMYWLFSRVP
ECRKEISFHL SSSIEAEGSK IISLVDYKKN YKQLMDDLLK IREKYDLIVT KSFEKDPIMQ
TCMNLSFEKC INKNAKTALA LTLYIDNLLT KGIKSMNENQ IETIFDHAIL IFRYISDKDI
FEAYYKQNLS KRLLGSSSLS DDAERLMIRK LKIECGSHYT SKIEGMLIDM RLSKDSLKDF
INPNDIIDFK VLTAAFWPQA QVQPIILPVE FSTKIERFRR LYLNKYSGRT LIWTTNLGNA
EIKSYLGDNR EKHDLVVSTY QMIVLLMYND KTAYRYEEIY ESLNIDDKEF EFHVLGLVKC
GILVKKNNEK KLENDTVLML NADFKYKMYK IKVPILQKKE NTDDVCENEI PEIVEDDRKH
MIEAIIVKIM KSRRVIGHQQ LISEVSKMIS WKFVASNKQI KGRIENLIER EFLQRDPKDS
NVYLYIV
//
