ID A0A3Q2V8S3_HAPBU Unreviewed; 1619 AA.
AC A0A3Q2V8S3;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 18-JUN-2025, entry version 31.
DE SubName: Full=Cullin 9 {ECO:0000313|Ensembl:ENSHBUP00000007060.1};
OS Haplochromis burtoni (Burton's mouthbrooder) (Chromis burtoni).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Haplochromis.
OX NCBI_TaxID=8153 {ECO:0000313|Ensembl:ENSHBUP00000007060.1, ECO:0000313|Proteomes:UP000264840};
RN [1] {ECO:0000313|Ensembl:ENSHBUP00000007060.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2025) to UniProtKB.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SIMILARITY: Belongs to the cullin family. {ECO:0000256|PROSITE-
CC ProRule:PRU00330, ECO:0000256|RuleBase:RU003829}.
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DR STRING; 8153.ENSHBUP00000007060; -.
DR Ensembl; ENSHBUT00000004266.1; ENSHBUP00000007060.1; ENSHBUG00000008650.1.
DR GeneTree; ENSGT00940000153954; -.
DR OMA; SEAPRRC; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000264840; Unplaced.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR CDD; cd20347; BRcat_RBR_CUL9; 1.
DR CDD; cd20359; Rcat_RBR_CUL9; 1.
DR Gene3D; 1.20.120.1750; -; 1.
DR Gene3D; 1.20.1310.10; Cullin Repeats; 1.
DR Gene3D; 3.30.230.130; Cullin, Chain C, Domain 2; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR004939; APC_su10/DOC_dom.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR056405; ARM_CUL7_CUL9.
DR InterPro; IPR047561; BRcat_RBR_CUL9.
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; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR047560; Rcat_RBR_CUL9.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR22771:SF4; CULLIN 7-RELATED; 1.
DR PANTHER; PTHR22771; CULLIN AND GALACTOSE-BINDING DOMAIN-CONTAINING; 1.
DR Pfam; PF03256; ANAPC10; 1.
DR Pfam; PF24742; ARM_CUL7_CUL9; 1.
DR Pfam; PF00888; Cullin; 1.
DR Pfam; PF10557; Cullin_Nedd8; 1.
DR Pfam; PF01485; IBR; 1.
DR Pfam; PF22191; IBR_1; 1.
DR SMART; SM01337; APC10; 1.
DR SMART; SM00884; Cullin_Nedd8; 1.
DR SMART; SM00647; IBR; 2.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF75632; Cullin homology domain; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF57850; RING/U-box; 2.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS50069; CULLIN_2; 1.
DR PROSITE; PS51284; DOC; 1.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000264840};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 298..477
FT /note="DOC"
FT /evidence="ECO:0000259|PROSITE:PS51284"
FT DOMAIN 676..924
FT /note="Cullin family profile"
FT /evidence="ECO:0000259|PROSITE:PS50069"
FT DOMAIN 1175..1393
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 1346..1389
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1541..1619
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1545..1557
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1567..1609
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1610..1619
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1619 AA; 183410 MW; CA953EE3AEC8BD9D CRC64;
MLKYEWRVSF ATEGGVKAIL SCMQEFSGVV HVQQLALAVR KLLVIAHLSP PLSESGTQMM
LEIFASIGSA TPEGSRGLLD AIPAAIDLML TTKGCVPSVR NGLLVIIMLI SNHKSLAEQL
VACDVTSVLK KCLSLSRAET MLAIIALNHI SMVHKLESKG CSCLIGSLRS RRILNKFLDN
YQEDVLPWHE SIEPCLSSMT AFINDREVVQ LFIRFLYRLA SLNKDYAVVM CRLGTKEALV
KALDKHSTNL LLVTELRDLI TDCEKYASLY KKMTTSVLAG CIQMVLGQIE EHRRSHQPIN
IPFFDVFLRN LCQGSSVELK EDKCWEKVEV SSNHHRANKL TDKNPKTYWE SNGCTGSHFI
NIFMHRGVII RQLAILVASE DSSYMPARIL VLGGDEPTNI NTELNTVNVP PSASRVVLLE
NMTRFWPIVQ IRVKRCQQGG IDTRIHGFEV LGPKPTFWPV FKEQLCCRTY LFYSTKAHTW
CQEVMEDKTQ LLQLFNNVSA QPRETRQAAL TAFQSVLVNT LLLHLVNPLS WLLSEYLDNS
EAPRRCKSRA TIFNSRVRRL THLLVHVDTS RVDGEELKPP VKSSESDIEQ SPVPVCPSDQ
NILRGGELNV TPSPQVKKFL EASCTLPDFV ERYRRLYLRL KNAMEELFGQ QTAFVLALRH
GFSAALLQLS ILRAMHVSER FAQYIDQMIQ ASGMASGCVE TLERLQQFLE PMLFLSGLEL
ASTFEHFYRY YLGDRLLAQG NVWLEHAVAE QIGSCFPSRF PQQMLKNLSE SSELQQEFHL
YRLQQLDRSL QEHDQEEWAE LEEEAEVQVL VLSPRCWAVS SLCYLDEPAK HLPPELCSYL
NQFTQFYTHS QSIYGLSHSK PRRLQWTWLG HAELQFGGWT LHVSTLQMFV LLQFNSQQEV
RVDALLQASG LSATVLLHAL LPLIGEGGPL TCSHPDDPAR GVLQLNEQVA SRSQEGAPAS
VWLLPKQTYL NVDEDAAGTL ERKRNYIYCL IVHIMKQEKE MHIDNLVFKV LDSCQKQEAS
RSPGSGRFSC STSDVLSCIM HVISKGCIRR NDENPHIVEF VPEDPSTPQK GQAQFSFSRA
DIGKDATSDS RDGVLDTVLF SMGRTMTQDE VRQLMQRTVQ QVAGTLSLDL DRAEHLLIHC
KWNVDLLVQR YTDDPDAIIV AAGLKFLNPQ TPPSPASTCP VCLSPWSCGM ELVPSLSCMH
YCCRSCWQEY LTARIEQNLI MNCNCPITDC QAQPTSQFFL SVLTDKDTIA KYENALLRGY
VECCSNLTWC TNPQGCDQIL CKENTGSMAT CSKCCWSSCF SCNFPEAHYP ASCSHMSQWM
DDGGYYEGMS MEAQSKHLAK LISKRCPSCQ AQIEKNEGCL HMTCAKCNHG FCWRCLKPWK
PTHKDYYNCS AMVSKAARQE KKFQDYNERC TFHHQAKDFA INLENKVSSI NEALQMKSLT
FVIDACKVLA QARKVLAYSC VYSYYNQETE KMDVMEQQTE ALDLHTNALQ ILLEETLLQC
TDLASCVRLL KPEHLNTGLE LIRRIQERLL AILQHSTQVL APEPVRSKSD RASHSGDSDN
NNYTGEEGGD EAEDDDDEYD EEYVPEWHED YDEDDIDEDD FFSDDDESEN LERDFSPFD
//
