ID H3AWI9_LATCH Unreviewed; 1771 AA.
AC H3AWI9;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE SubName: Full=RB binding protein 6, ubiquitin ligase {ECO:0000313|Ensembl:ENSLACP00000014010.1};
GN Name=RBBP6 {ECO:0000313|Ensembl:ENSLACP00000014010.1};
OS Latimeria chalumnae (Coelacanth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Coelacanthiformes; Coelacanthidae; Latimeria.
OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000014010.1, ECO:0000313|Proteomes:UP000008672};
RN [1] {ECO:0000313|Proteomes:UP000008672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT "The draft genome of Latimeria chalumnae.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLACP00000014010.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR EMBL; AFYH01093523; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01093524; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01093525; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_014345418.1; XM_014489932.1.
DR Ensembl; ENSLACT00000014109.1; ENSLACP00000014010.1; ENSLACG00000012333.1.
DR GeneID; 102350973; -.
DR CTD; 5930; -.
DR GeneTree; ENSGT00940000157561; -.
DR HOGENOM; CLU_239162_0_0_1; -.
DR OrthoDB; 150979at2759; -.
DR Proteomes; UP000008672; Unassembled WGS sequence.
DR Bgee; ENSLACG00000012333; Expressed in muscle tissue and 6 other cell types or tissues.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:InterPro.
DR CDD; cd16620; vRING-HC-C4C4_RBBP6; 1.
DR Gene3D; 4.10.60.10; Zinc finger, CCHC-type; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR014891; DWNN_domain.
DR InterPro; IPR003613; Ubox_domain.
DR InterPro; IPR025829; Zn_knuckle_CX2CX3GHX4C.
DR InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR15439:SF29; CELL DIVISION CYCLE AND APOPTOSIS REGULATOR PROTEIN 1-RELATED; 1.
DR PANTHER; PTHR15439; RETINOBLASTOMA-BINDING PROTEIN 6; 1.
DR Pfam; PF08783; DWNN; 1.
DR Pfam; PF04564; U-box; 1.
DR Pfam; PF13696; zf-CCHC_2; 1.
DR SMART; SM01180; DWNN; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00343; ZnF_C2HC; 1.
DR SUPFAM; SSF57756; Retrovirus zinc finger-like domains; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51282; DWNN; 1.
DR PROSITE; PS51698; U_BOX; 1.
DR PROSITE; PS50158; ZF_CCHC; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000008672};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00047}.
FT DOMAIN 4..76
FT /note="DWNN"
FT /evidence="ECO:0000259|PROSITE:PS51282"
FT DOMAIN 160..174
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT DOMAIN 251..328
FT /note="U-box"
FT /evidence="ECO:0000259|PROSITE:PS51698"
FT DOMAIN 258..299
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 325..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 486..541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 602..784
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 825..1235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1249..1271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1304..1771
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..348
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 486..536
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 622..668
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 669..717
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 718..755
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 768..784
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 829..857
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 858..872
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 889..914
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 966..1180
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1219..1235
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1335..1353
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1362..1377
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1378..1595
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1628..1654
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1657..1700
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1707..1728
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1771 AA; 197993 MW; C204EF515DCEE6B7 CRC64;
MSCVHYKFSS KLNYDTVTFD GLHISLCDLK KQIMGREKLK AADCDLQITN AQTKEEYTDD
NALIPKNSSV IIRRIPIGGV KTASKTFIGR TEPVSGTSKA IEDSSASISL AQLTKTANLA
EANASEEDKI KAMMSQSGHE YDPINYMKKP LGPPPPSYTC FRCGKPGHYI KNCPTNGDKN
FEAVPRIKKS TGIPRSFMRE VDDPNMKGAM LTNTGKYAIP TIDAEAYALG KKEKPPFLPE
EPSSSSEDED PIPDELLCLI CKDIMNDAVV IPCCGNSYCD ECIRTALLES EEHTCPTCHQ
TDVSPDALIA NKFLRQAVNN FKNETGYTKR LRKPTQPHQS QQARQPPQRI LQPVGRPTLS
RQQDPLMVAA PAPLVTTVNT PTPVPAVPPV TSTVQMNQPS AVVQSTDIPI APASQETGKY
KGGDLNEPSA KVAVTVVTLA AAAPPPPVAA ATTAGITTAH PPLLATIATE QKGYQVPVLG
HPTSQGHTIP ITGPPMRSST IRTGSSRPGW EATSTRTRQQ PNDRTPRTQT ATTLPVPTPV
YVPPPTLYPP PPHSLPVPPG VPPPQFPPQF PPGQPPATGY TVPPPGFPPA PTSITSWVPA
GTQATQTSAV TSLAQAPPLS REEFYREQRR LKEEEKKKSK LDEFTNDFAK ELMEYRKIQK
ERRRSFSRSK SPFSGSSYSG SSYSYSKSRS RSSRSRSYSR SFSRSRSRSY SRSPTYSRRG
RGKSRSYRSR SRSHGYRHSR SRSPPYRKYR SRSKSPAYRG HSPTKRNAPQ GDGEREHINR
YRDIPTYDMK AYGCGRSVDL RDPYERERYR EWERNYREWY EYYRGYTNAT QPKPRTPTNR
ENYTPERYGP TVSRRENSSY IRGRREDYSG GQSHRGRTIG GNYPDKFSAR DSRGVKDPRR
SKEKEAEIAS GEGKGNKHKK HRKKKKGDEN EGPPTADSAD VGKKPREPVG NDGKGDSLFT
APNRDDATPV RDEPMENDSV SYKPVSDKDR KDKPKAKGEK VKRKAEGSDS KKESGMKSIK
VSQEKFEVDR EKSPRSEPPA KKLKEDVHQK VETSKPYLSQ KEEKGLHTRK VYLKVVKEQT
DAKGVKEEKV KKEHVKEVKQ EKVLNKEDKP KKSNEKVSKT TEVKSEKRKR KAEEKGVEKD
LETPSVKALK AESAEELKQS KTKAESDLEK NTEAPLEKAG EDRSIPVTAP VKKIKLNRET
GKKIASGEGV SAGDEPADKP ETNNGKVKQE KVKKMRRKII AEGSSSTLVD YTSTSSTGGS
PVRKTEEKHD IKRTVIKTME EYNNDNTAPA EDVIIMVQVP QSKWDKDEFD SEEDDKASSA
PSSVVAKPPT VVKNLAVKAS NSVKQNEIET VPSEKMQKSA KDSSYEGAQL ESKATKSSVP
SEKGKPKERE HLGPDKDALE KKKGLVQQEK DKNAERAIDA KNTQPPSKDR PCDKHDAGSR
GSSLKDFGMS NDRKAEHESG KDNYSSKRKD EISRRRESPH RNKEPVLGQR SREREAYEEI
SKRTDSKRSS YSPTRERKPY TDHKVLSDAK HNAGEYKSDK TSSKEKEKYV APEIRNKDRD
LTGHRSSSRT QSPDTKNERD RSAGQSEREY GKSKPLLSRS SRLSSDLTRE TDEAAFVPDY
NESDSESNLS VKNDEHTGKS LKDSRDKGDR VKESKGLLLS PQQSLNRSHS QSSQSVSHSR
SQSPLESQPR SRSSSATSAE SQDSKKKKKK KDKKKHKKHK KHKKHKKHTG NESESEKGQK
HKHKKKKSKK NKEKEKEKNK DDQKLKSSVS V
//
