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Database: UniProt
Entry: A0A672UNN5_STRHB
LinkDB: A0A672UNN5_STRHB
Original site: A0A672UNN5_STRHB 
ID   A0A672UNN5_STRHB        Unreviewed;      1606 AA.
AC   A0A672UNN5;
DT   17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 1.
DT   18-JUN-2025, entry version 25.
DE   SubName: Full=Cullin 9 {ECO:0000313|Ensembl:ENSSHBP00005016515.1};
GN   Name=LOC115613592 {ECO:0000313|Ensembl:ENSSHBP00005016515.1};
OS   Strigops habroptila (Kakapo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Australaves;
OC   Psittaciformes; Psittacidae; Strigops.
OX   NCBI_TaxID=2489341 {ECO:0000313|Ensembl:ENSSHBP00005016515.1, ECO:0000313|Proteomes:UP000472266};
RN   [1] {ECO:0000313|Ensembl:ENSSHBP00005016515.1, ECO:0000313|Proteomes:UP000472266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Jarvis E.D., Howard J., Rhie A., Phillippy A., Korlach J., Digby A.,
RA   Iorns D., Eason D., Robertson B., Raemaekers T., Howe K., Lewin H.,
RA   Damas J., Hastie A., Tracey A., Chow W., Fedrigo O.;
RT   "Strigops habroptila (kakapo) genome, bStrHab1, primary haplotype, v2.";
RL   Submitted (NOV-2019) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSSHBP00005016515.1}
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 RBR family. Ariadne subfamily.
CC       {ECO:0000256|ARBA:ARBA00005884}.
CC   -!- SIMILARITY: Belongs to the cullin family. {ECO:0000256|PROSITE-
CC       ProRule:PRU00330, ECO:0000256|RuleBase:RU003829}.
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DR   Ensembl; ENSSHBT00005019775.1; ENSSHBP00005016515.1; ENSSHBG00005014362.1.
DR   GeneTree; ENSGT00940000153954; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000472266; Chromosome 11.
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   CDD; cd16624; RING-HC_RBR_CUL9; 1.
DR   Gene3D; 1.20.120.1750; -; 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; IPR048962; ARIH1-like_UBL.
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; IPR047562; RING-HC_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; PF01485; IBR; 1.
DR   Pfam; PF22191; IBR_1; 1.
DR   Pfam; PF21235; UBA_ARI1; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000472266};
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          328..507
FT                   /note="DOC"
FT                   /evidence="ECO:0000259|PROSITE:PS51284"
FT   DOMAIN          725..977
FT                   /note="Cullin family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50069"
FT   DOMAIN          1213..1430
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51873"
FT   DOMAIN          1383..1426
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   COILED          1512..1550
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1606 AA;  178435 MW;  A968BF7916D6403B CRC64;
     ALGSSEGLSE RGSLAKIAAT VDVIQSSSSE LGLRLAGLKH ILKILEEEPE RLLPRCPFPC
     REKLVKVAVE LLGTEAAEKA VVVVTLRLLA VLMAKHDWRV TFAMEGGVRA VLACMQQHAS
     SALVQQAGLA ALKVLVGAVA GEPGGAGGKL LPLKQADAQL IREIFASIGS ASSKGSASLL
     SAIPAALSTM QSVPGGPPLS LRILNKILDG YQEDVLPWHE CVEPCVSSLS AHSSDREVLQ
     EVVGFLHRLA TTSKDCAVVM CCVGTHEALS KALNKHSTAP PLAPALLALV GDCEKHADIS
     KKLMTSILAG CIQLVLGQIE EHRRSHHPIS IPLFDVFLHN LCRGSSMEVK EERCWEKVEV
     SSNPHRASKL TDRNPKTYWQ SNSSSGSHFI TVHMQCGVVV REMSMLVASE DSSYMPARVV
     VLGGDSPATV RTELNAVTIL PSDSRVILLE NMSRFWPVIQ IRVKRCQQGG IDTRVRGIEV
     LGPKPTFWPI FKEKLCQRTF LSCTARTHAW CQEICRDRGR LLQLFGRLNR ALRHEQSFAN
     RFLPDNEAAR ALGRTCWEAL VTPLVQSITS PDPDGVSPLA WLLSQYLESV EPPCCTRSPG
     AAFGSRVRRL TQLLVHVDPG GWEPEEARAA GEHGAPARPA KVVVEKSSSL WGISQCWRGV
     VQQQVQRFLE AAGQAPDLVE RYCGLYQRLR GATEELFGQQ AAFALALGQG FAGALLQLSF
     LTALHVSEQF ARYLDRQIQE LRGAVGSTGP LQQILEPFVV FSGLELAHSF EHFYRHYLGD
     RLLVQGPSWL EGAVVEQIGL CFPSRFPQDM LSNLAESEEL QRQFRLYQLQ EQDKRLLELD
     MAALLPPCQA LGTASVADVP EVTVLALSPR CWPVSPLCHM DRPRRLFSAA LSCPLDEFAD
     FCRRSECGEP PGPPWRLQWT WLGHAELQFG DCVLHVSTLQ MYILLCFNSA EEVAVEALLQ
     VTGLPADLVH HALAPLTHGE GVLVWSRPAG GTLRLNQAAL AHASGRHLRL LPQQRYLRVE
     RAEVSALERK RNILCCLITR ILKVEKQLHI DNLVFRVIDA CQKGELGPGL QFLSFCCHSV
     DVLSCVLHLL NQGYLRRQEE RPHVLEYISA EPVTPPGGQA QMAFQSRPPE FLMAVLQVPR
     GHTLSPEEAK LLMNQTVQQV QDVLSIPDDV ARHLLMHCRW NVDFLIQCYM ENRETLLISS
     GLQVQDAQPP PSPGTHCPVC VNQLCPTEKP PTLCCMHYCC KPCWSEYLTT RIEQNMVVNC
     TCPISDCHAQ PTTAFICSIV SSEEIIAKYE KALLRGYVEC CSNLTWCTNP QGCDQILLKD
     GFGYGAACSK CSWISCFNCN FPEAHYPASC SHMSQWVDDD GYYEGMTSEA QSKHLAKLIS
     KHCPSCQAQI EKNEGCLHMT CAKCNHGFCW RCLKPWRPTH KDYYNCSAMV SKAAWQEKRF
     QDYNERCTFH HHAREFAMNL RNSIFSIREM PKIRTLTFVL DACKVLEQAR KVLAYSCVYS
     YYNQDTESMD IVKEQTESLE LHTNALQILL EETLLQYQDL ASSLQLLKAE HFKAGLELVH
     QIKERLFAIL WHSTQDFHVG LQTSSDPDQR KVKLSNVPAS GPACVG
//
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