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Database: UniProt
Entry: A0A094KYD5_ANTCR
LinkDB: A0A094KYD5_ANTCR
Original site: A0A094KYD5_ANTCR 
ID   A0A094KYD5_ANTCR        Unreviewed;       539 AA.
AC   A0A094KYD5;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   SubName: Full=Tripartite motif-containing protein 55 {ECO:0000313|EMBL:KFZ63600.1};
GN   ORFNames=N321_13453 {ECO:0000313|EMBL:KFZ63600.1};
OS   Antrostomus carolinensis (Chuck-will's-widow) (Caprimulgus carolinensis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Caprimulgimorphae; Caprimulgiformes;
OC   Caprimulgidae; Antrostomus.
OX   NCBI_TaxID=279965 {ECO:0000313|EMBL:KFZ63600.1, ECO:0000313|Proteomes:UP000053620};
RN   [1] {ECO:0000313|EMBL:KFZ63600.1, ECO:0000313|Proteomes:UP000053620}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N321 {ECO:0000313|EMBL:KFZ63600.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KL358232; KFZ63600.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A094KYD5; -.
DR   Proteomes; UP000053620; Unassembled WGS sequence.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd19832; Bbox2_MuRF2_C-II; 1.
DR   CDD; cd16760; RING-HC_MuRF2; 1.
DR   Gene3D; 1.20.5.170; -; 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; IPR017903; COS_domain.
DR   InterPro; IPR027370; Znf-RING_euk.
DR   InterPro; IPR000315; Znf_B-box.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR24103; E3 UBIQUITIN-PROTEIN LIGASE TRIM; 1.
DR   PANTHER; PTHR24103:SF640; TRIPARTITE MOTIF-CONTAINING PROTEIN 55; 1.
DR   Pfam; PF00643; zf-B_box; 1.
DR   Pfam; PF13445; zf-RING_UBOX; 1.
DR   SMART; SM00336; BBOX; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF57845; B-box zinc-binding domain; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS51262; COS; 1.
DR   PROSITE; PS50119; ZF_BBOX; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053620};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00024}.
FT   DOMAIN          26..82
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          119..161
FT                   /note="B box-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50119"
FT   DOMAIN          269..327
FT                   /note="COS"
FT                   /evidence="ECO:0000259|PROSITE:PS51262"
FT   REGION          325..525
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          190..239
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        328..365
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        379..397
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        406..426
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        439..455
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        488..505
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   539 AA;  60056 MW;  1E7611113C91B0C7 CRC64;
     MSTSLNYKSF SKEQQTMDNL EKQLICPICL EMFTKPVVIL PCQHNLCRKC ASDIFQASNP
     YLPTRGGTTV ASGGRFRCPS CRHEVVLDRH GVYGLQRNLL VENIIDIYKQ ESTRPERKCD
     QPMCEEHEDE RINIYCLNCE MPTCSLCKVF GAHKDCQVAP LTNVYQRQKS ELSDGIAVLV
     GSNDRVQGIV TQLEETCKTV EECCRRQKEQ LCEKFDYLYS ILEERKNEMT QIITRTQEEK
     LEHVRSLMKK YADHLEAVSK LVESGIQFME EPEMAVFLQN AKTLLQKITE ASKGFEMEKI
     EDGYENMNQF TVNLSREEKI IREIDFDREE EGAEEEEEAV DGEDLDEVRT ESSGEEEEEE
     VEEEGAERAS QPPQQDPEPQ STAGEPPAEP TPVPLPAAPA GQVSDEVVTP SGSQQTPESD
     TQVPATAETI DPLFYPSWYK AQSRQSSSPS STPVSGLGKV GPPVSLETSA KKAEAPAAAA
     IEESAPGSGK ESNATAATSK VSSTEVPPEG LEETPMSNER GDEPARHVFS FSWLNSLNE
//
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