ID A0A091GNA8_9AVES Unreviewed; 917 AA.
AC A0A091GNA8;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 22-FEB-2023, entry version 40.
DE SubName: Full=E3 ubiquitin-protein ligase TRIM33 {ECO:0000313|EMBL:KFO82679.1};
DE Flags: Fragment;
GN ORFNames=N303_11084 {ECO:0000313|EMBL:KFO82679.1};
OS Cuculus canorus (common cuckoo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Cuculiformes; Cuculidae; Cuculus.
OX NCBI_TaxID=55661 {ECO:0000313|EMBL:KFO82679.1, ECO:0000313|Proteomes:UP000053760};
RN [1] {ECO:0000313|EMBL:KFO82679.1, ECO:0000313|Proteomes:UP000053760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N303 {ECO:0000313|EMBL:KFO82679.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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; KL448316; KFO82679.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091GNA8; -.
DR STRING; 55661.A0A091GNA8; -.
DR Proteomes; UP000053760; Unassembled WGS sequence.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd19847; Bbox1_TIF1g_C-VI; 1.
DR CDD; cd05502; Bromo_tif1_like; 1.
DR CDD; cd15624; PHD_TIF1gamma; 1.
DR Gene3D; 1.20.920.10; Bromodomain-like; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR003649; Bbox_C.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR000315; Znf_B-box.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45915:SF3; E3 UBIQUITIN-PROTEIN LIGASE TRIM33; 1.
DR PANTHER; PTHR45915; TRANSCRIPTION INTERMEDIARY FACTOR; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00502; BBC; 1.
DR SMART; SM00336; BBOX; 2.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF57845; B-box zinc-binding domain; 1.
DR SUPFAM; SSF47370; Bromodomain; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS50119; ZF_BBOX; 2.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 4: Predicted;
KW Bromodomain {ECO:0000256|PROSITE-ProRule:PRU00035};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000053760};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00024}.
FT DOMAIN 40..87
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT DOMAIN 100..141
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT DOMAIN 699..746
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 786..858
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 522..598
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 879..917
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 138..190
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 522..589
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 901..917
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFO82679.1"
FT NON_TER 917
FT /evidence="ECO:0000313|EMBL:KFO82679.1"
SQ SEQUENCE 917 AA; 102478 MW; D642273FAAAD67D2 CRC64;
CPAVGVIRCP VCRQECREID LVDNYFVKDT SETPSSSDEK SEQVCTSCED NASAVGFCVE
CGEWLCKTCI EAHQRVKFTK DHLIRKKEDV SSEAVGASGQ RPVFCPVHKQ EQLKLFCETC
DRLTCRDCQL LEHKEHRYQF LEEAFQNQKG AIENLLAKLL EKKNYVNFAA AQVQNRIKEV
NETNKRVEQE IKVAIFTLIN EINKKGKSLL QHLESVTKER QMKLIQQQND ITGLSRQVKH
VMNFTNWAIA SGSSTALLYS KRLITFQLRH ILKARCDPVP AANGAIRFHC DPTFWAKNVV
NLGNLVIENK PAPSYTPNVV VGQTPPGTNH VSKTPGQINL AQLRLQHMQQ QVYAQKHQQL
QQMRMGQPSG SVPRQTSQQV LQQQPPRLIS MQTMQRGNMN CGAFQAHQMR MAQNAARIPG
IPRHNGPQYS MMQPHLQRQV YPVYTLHLCH FVSVHNTTIN PTSPTTATMA SANRGPTSPS
VAAIELIPSV TNPENLPSLP DIPPIQVNAG SNSLDNLLSR YITGSHLPPQ PTSTMNPSPG
PSALSPGSSG LSNSHTPVRP PSTSSTGSRG SCGSSGRTAE KTGVNFKSDQ VKVKQEPGTE
EEICSFSGTV KQEKTEDGRR SACMVNLTPP LSTNLHLESE LEALGSLENH VKTEPADLSE
SCKQSGHSLV NGKSPVRSLM HRSARIGGEG NNKDDDPNED WCAVCQNGGD LLCCEKCPKV
FHLTCHVPTL LSFPSGEWIC TFCRDLSKPE VEYDCDNSQH SKKGKTAQGL SPVDQRKCER
LLLYLYCHEL SIEFQEPVPA SIPNYYKIIK KPMDLSTVKK KLQKKHSQHY QTPEDFVADV
RLIFKNCERF NEADSEVAQA GKAVALYFED KLTEIYPDRT FQPLPEFEQE EDDGEITEDS
DEDFIQPRRK RLKSDER
//