ID A0A3Q1HHA1_ANATE Unreviewed; 1136 AA.
AC A0A3Q1HHA1;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Tripartite motif containing 33 {ECO:0000313|Ensembl:ENSATEP00000006775.2};
OS Anabas testudineus (Climbing perch) (Anthias testudineus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Anabantiformes; Anabantoidei; Anabantidae; Anabas.
OX NCBI_TaxID=64144 {ECO:0000313|Ensembl:ENSATEP00000006775.2, ECO:0000313|Proteomes:UP000265040};
RN [1] {ECO:0000313|Ensembl:ENSATEP00000006775.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR AlphaFoldDB; A0A3Q1HHA1; -.
DR STRING; 64144.ENSATEP00000006775; -.
DR Ensembl; ENSATET00000006888.2; ENSATEP00000006775.2; ENSATEG00000004717.2.
DR GeneTree; ENSGT00940000156361; -.
DR InParanoid; A0A3Q1HHA1; -.
DR OrthoDB; 56754at2759; -.
DR Proteomes; UP000265040; Unplaced.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd16766; RING-HC_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); 2.
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; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
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 SMART; SM00184; RING; 2.
DR SUPFAM; SSF57845; B-box zinc-binding domain; 1.
DR SUPFAM; SSF47370; Bromodomain; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF57850; RING/U-box; 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.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW ProRule:PRU00035}; Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000265040};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00024}.
FT DOMAIN 149..209
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 236..283
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT DOMAIN 293..334
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT DOMAIN 898..945
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 972..1052
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 1..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 116..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 504..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 544..636
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 654..694
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 749..834
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 858..895
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1088..1136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 363..412
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 13..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..49
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..138
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 544..586
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 749..794
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 866..882
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1116..1136
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1136 AA; 123805 MW; CD8762F799A12C51 CRC64;
MADNKGDEDM EPSTNSDSVP SVQDNKQPET KDAVIIIEAN RKDGEETESN DNGNEVSTLG
GDVSSSSSSG GGGGGGGAVA AGGEANGNVS AANAVSPAGT SSTNTEQTVA ETLTAGDAPA
AGPTTETSPP PSAPGSTPVP APINLLDTCA VCKQSLQSRD CEPKLLPCLH SFCLKCIPQP
DRQISVQVPG PHGQTDTHIV NVMRCSVCHQ DYKQSDIVDN YFVKDTTEAT STSDEKTAQV
CTSCEDNAGT IGFCVECGEW LCKTCVEAHQ RVKITKDHKI RTKEDADAVG TGQRPVFCPI
HKQEPLKLFC ETCDTLTCRD CQLLEHKEHR YQFLEEAFQN QKGIIETTMA KLQEKKNYVH
YSVSQVQSRL KELNETHRKV EHEIKIAVFT LINEINKKGK SLLQQLESVT KERSMRLVAQ
HKDTTQLAQQ IHHVLNFCQW AITTGSSTAL LYSKRLILFQ LRQLFKARLE PAPQANGVVR
FFCDPTFWAK NVVNLGSLVI EKPPPSAQPP TVMVGGPPLS PGQGHPGKHP GQINLAQLRL
QHMQQAAYAQ QKQQQQQQQQ QHQQQIQQQM RIASQMSQQH PRQAGPPMVQ QQPPRLISMQ
PLPRGPGGMN GGPGPPMYTS SHHMRLPGPP QGRMPTAQPR LNGQQYSPMM QPQLQRQHSN
PGHAGPFPVA SLHNANPTSP TSASMAGAHA HRGPASPIIG PIELIPSVTN PENLPSLPEI
PPIQLEDAGS SNLGHLLSRY ITASTQHQLG SVDMNPSPGL STHSPGSSGL SNAHTPARPS
STSSTGSRGS GTAVEQVRVK QEPGTEDSYS CPASSLKTEH GKDAGRSACM MSSPENSPLP
VLGVVSTGQD ALKALGERIK TEPKSETPCS GLNGSNAKEK GASAGTGNPG GKEDDPNEDW
CAVCINGGDL LCCDRCPKVF HMKCHVPTIK IFPKGDFLCT FCRSLASPEI EYCDDSKIKG
DQGLSPEDQR RCERLLLYIF CHELSVGFRE PVPSSVPNYY KIIKQPMDLK KVKKKLQLRS
SHHYQSTQDF VSDMRLVFKN CAKYNEMSRI IQVYDEEKQI NTQVGSEMAI SGKAVSLYFE
EKLQEMFPGQ SFPEAPEPKS PSEKEKEDDD TDDSEEDFIQ PRRKRLKTDE KVLHIK
//
