ID M4ADZ1_XIPMA Unreviewed; 1297 AA.
AC M4ADZ1;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 2.
DT 27-MAR-2024, entry version 73.
DE SubName: Full=E3 ubiquitin-protein ligase TRIM33 {ECO:0000313|Ensembl:ENSXMAP00000012685.2};
OS Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Xiphophorus.
OX NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000012685.2, ECO:0000313|Proteomes:UP000002852};
RN [1] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA Walter R., Schartl M., Warren W.;
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX PubMed=23542700; DOI=10.1038/ng.2604;
RA Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA Postlethwait J.H., Warren W.C.;
RT "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT evolutionary adaptation and several complex traits.";
RL Nat. Genet. 45:567-572(2013).
RN [3] {ECO:0000313|Ensembl:ENSXMAP00000012685.2}
RP IDENTIFICATION.
RC STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000012685.2};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR STRING; 8083.ENSXMAP00000012685; -.
DR Ensembl; ENSXMAT00000012701.2; ENSXMAP00000012685.2; ENSXMAG00000012634.2.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000156361; -.
DR HOGENOM; CLU_005817_0_1_1; -.
DR InParanoid; M4ADZ1; -.
DR OMA; ICQNCVM; -.
DR Proteomes; UP000002852; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; IPR018359; Bromodomain_CS.
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; PS00633; BROMODOMAIN_1; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000002852};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00024}.
FT TRANSMEM 12..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 46..72
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 256..316
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 343..390
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT DOMAIN 404..445
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT DOMAIN 1058..1105
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1133..1213
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 104..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 193..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 620..642
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 655..708
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 722..757
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 807..828
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 882..1054
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1249..1297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 474..523
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 120..135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..158
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..212
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 655..701
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 882..932
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 944..968
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1004..1040
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1277..1297
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1297 AA; 142697 MW; D983EC0DA1ADAF15 CRC64;
MKKLISKCHP ASHFLFFFFF FFFFFFTTNS FYVFALHQTI SDSRWLYFLI TISFSFSFFP
PVTTFVSLLS CFARRHNLRR HACSRFENFT QDVQRFVRGR KMADNKGEEE MEPSANADPV
PSGQAETQSS TESEDKGIAT ETDSKGDAET ESPKDANEEL NASSEGVDDS IDGAAEATAT
PAAAAVVAAG EAGGNASNAA SPTETSNGNS EPPAVDAVPA ADAPVSGNTS ETSPAPTAPA
AAATPVSTPI NLLDTCAVCK QSLQTRDCEP KLLPCLHSFC LKCIPQPDRQ ISVQVPGPHG
QTDTHIVNVM RCSVCHQDYK QSDIIDNYFV KDTTEATSTS DEKAAQVCTS CEDNAGTVGF
CVECGEWLCK TCVEAHQRVK ITKDHKIRTK EDADAASDSV TTGQRPVFCP IHRQEPLKLF
CETCDTLTCR DCQLLEHKEH RYQFLEEAFQ NHKGIIEANM AKLQEKKNYV HYSVSQLQNR
LKELGETHRK VEHEIKIAVF TLINEINKKG KALLQQLESV NKERSLRLMG QHKDTTQLAQ
QIHHVLNFCN WAITSGSSTA LLYSKRPIMY QLRQLFKARL EPAPQSNGVV RFFCDPTFWA
KNVVNLGNLV IEKPPPVPQP PGVMVGGPAI SPGQSHPGKH PGQINLAQLR LQHMQQAAYA
QQKHQQHQQQ QQQQQQQQQQ QIQQQMRLAS QMSQQHPRPG GPPLVQQQPP RLISMQQLQR
TGAINGGTNP SMYPSSHHMR LAGPPQGRMP TAQPRHNGQQ YAPMMQPQLQ RQMSLESEMS
HQRFRFLLQS GHSNPGHAGP FPVASLHNAS PTSPTSASMA GAHAHRGPAS PIIGPIELIP
SVTNPENLPC LPEIPPIQLE DAGSSNLGYL LSRCISASQQ HQLGSTDMNP SPGLSTLSPG
SSGLSNAHTP ARPSSTSSTG SRGSSSSAGR AGTGGGSAAE QLKVKKEPCT EDDYSCSSSV
KTERGKDAGR SACMMSSPES SPLGVPSAGP DAYRDVGERV KTEPMSETSC SGLNGTSSST
NTTTSQTGSA LTNGSVVKRS GSHDAAQGGG GKDDDPNEDW CAVCINGGDL LCCDRCPKVF
HMKCHVPTIK IFPQGEFLCT FCRSIADPEI EYCDESKRIK GDQSLSPEDQ RRCERLLLYI
FCHELSMGFR EPVASSVPNY YKIIKQPMDL KKVKKKLQLR SSQYYKTTQE FVNDMRLIFK
NCAKYNEMSR IIQVYDEEKE INTQAGSEMA ISGKAVSLYF EEKLQDIFPD QHFPDSPDPA
SSDEKEREDV DTEDSEEDFV QPRRKRLKTD DKLVHIK
//
