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Database: UniProt
Entry: A0A151MC37_ALLMI
LinkDB: A0A151MC37_ALLMI
Original site: A0A151MC37_ALLMI 
ID   A0A151MC37_ALLMI        Unreviewed;      1110 AA.
AC   A0A151MC37;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN   Name=TRIM66 {ECO:0000313|EMBL:KYO22062.1};
GN   ORFNames=Y1Q_0000680 {ECO:0000313|EMBL:KYO22062.1};
OS   Alligator mississippiensis (American alligator).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC   Alligator.
OX   NCBI_TaxID=8496 {ECO:0000313|EMBL:KYO22062.1};
RN   [1] {ECO:0000313|EMBL:KYO22062.1, ECO:0000313|Proteomes:UP000050525}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KSC_2009_1 {ECO:0000313|EMBL:KYO22062.1};
RX   PubMed=22293439; DOI=10.1186/gb-2012-13-1-415;
RA   St John J.A., Braun E.L., Isberg S.R., Miles L.G., Chong A.Y., Gongora J.,
RA   Dalzell P., Moran C., Bed'hom B., Abzhanov A., Burgess S.C., Cooksey A.M.,
RA   Castoe T.A., Crawford N.G., Densmore L.D., Drew J.C., Edwards S.V.,
RA   Faircloth B.C., Fujita M.K., Greenwold M.J., Hoffmann F.G., Howard J.M.,
RA   Iguchi T., Janes D.E., Khan S.Y., Kohno S., de Koning A.J., Lance S.L.,
RA   McCarthy F.M., McCormack J.E., Merchant M.E., Peterson D.G., Pollock D.D.,
RA   Pourmand N., Raney B.J., Roessler K.A., Sanford J.R., Sawyer R.H.,
RA   Schmidt C.J., Triplett E.W., Tuberville T.D., Venegas-Anaya M.,
RA   Howard J.T., Jarvis E.D., Guillette L.J.Jr., Glenn T.C., Green R.E.,
RA   Ray D.A.;
RT   "Sequencing three crocodilian genomes to illuminate the evolution of
RT   archosaurs and amniotes.";
RL   Genome Biol. 13:415-415(2012).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC         [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC         cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC         EC=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KYO22062.1}.
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DR   EMBL; AKHW03006283; KYO22062.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A151MC37; -.
DR   Proteomes; UP000050525; Unassembled WGS sequence.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd19811; Bbox1_TRIM66; 1.
DR   CDD; cd19794; Bbox2_TRIM66-like; 1.
DR   CDD; cd05502; Bromo_tif1_like; 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; IPR037372; TRIM66_Bbox1_Znf.
DR   InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR   InterPro; IPR027370; Znf-RING_euk.
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; TRANSCRIPTION INTERMEDIARY FACTOR; 1.
DR   PANTHER; PTHR45915:SF7; TRIPARTITE MOTIF-CONTAINING PROTEIN 66; 1.
DR   Pfam; PF00439; Bromodomain; 1.
DR   Pfam; PF00628; PHD; 1.
DR   Pfam; PF00643; zf-B_box; 1.
DR   Pfam; PF13445; zf-RING_UBOX; 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}; Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000050525};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
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:PRU00024}.
FT   DOMAIN          88..142
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          165..211
FT                   /note="B box-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50119"
FT   DOMAIN          230..266
FT                   /note="B box-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50119"
FT   DOMAIN          897..944
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   DOMAIN          984..1056
FT                   /note="Bromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50014"
FT   REGION          1080..1110
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1080..1098
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1110 AA;  125105 MW;  7C30502ADD0E8D35 CRC64;
     MEREGNELSR DRLTRRRERN LARSRNAAVT KLICAGTTET VAMDEESQMI STGFSPAEAL
     LKWEGIISPL DIKLWTRKME SFDLLRNCLV CKWELKGRDP RLLPCLHSFC KDCLPDLIQG
     YRYTPTEKEI LYEGILSCPV CKQPCFAKDV AENYFLKDFP TANPAMARSC SVCKEKRPAH
     SLCTTCNKWL CSSCTEEHRH GKETGDHFLS VSLKSCSGTE GGASEFTLCC PMHSQEPLKL
     FCETCDVLTC RSCLLTEHKE HRFKHLEEAL QNQRVILENV TAKVEEKRTG IQVSAKQIED
     RLFEVKHLHK KVENQIKMAK MVVMNEINKR TNSLLEQLER ITSERKQKLE QQLQGIVVLN
     RQFEHVQNFI NWAVCSKNNI PFLFSKELIV FQIQRLLETN CSTDVGPPLK IRFTWDPSFW
     TKQLSNLGGL TLEGGHISHS DVLAYGSAQG LHTPLYHGHH SPAPQLEPIS NHSHQFPVPV
     QCPTPAQGQP SLQLNQTKQP QHVQQTIVGQ INYIVRQPAP VQQQIQDEVQ QRCEDSAELD
     GQKPVLPLDR NVMPPVLQPS SEEFIAGSHS PESTLQHPSL NPVRKRSASL SIVGFSNTLE
     MELSSTRLTR SADPQMQGVS AVTFGQSQSM PHASDIQPEP VPSYSLASDR AINDLSPGTT
     NNLATGDVLL GNAKYKLENE DFSTTSDPLG NDSATTSPST INELALPMQK MLEEPINLSV
     KKSQQCASPS TPINNAPCLL SASVKQLSNE KDFSNCEQEH FEMDVKNNQN ISTYAKELKI
     PYVRLERLKI CMSESGELPV FKLQPQKSEQ DGTFLLIIEC GTQSSSMAIK VNQDNPSEGK
     IHKLGGSENR KIPINPPSGQ VPSPFVDIRP VDHKLNNGIP STRKPPLPQE ISPIENEDFC
     AVCLNGGELL CCDHCPKVFH LSCHVPALLS FPVGEWVCTL CCNPLKPEVE YDCENTRYRR
     INKALHGLDD CDQKKCEKLV LFLFCSSLSL PFHEPVSPLA RHYYQIIKRP MDLSIIRRKL
     QKREKSHYSA PEQLVADVRL MFWNCAKFNY PDSEVAEAGQ CLEVFFEGKL KEIYPDKHFP
     LMQQEDSDSE EESEKTKRTM FQPSNSLPQV
//
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