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Database: UniProt
Entry: S4R9A3_PETMA
LinkDB: S4R9A3_PETMA
Original site: S4R9A3_PETMA 
ID   S4R9A3_PETMA            Unreviewed;       352 AA.
AC   S4R9A3;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   RecName: Full=Tripartite motif-containing protein 54 {ECO:0000256|ARBA:ARBA00014725};
OS   Petromyzon marinus (Sea lamprey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Cyclostomata;
OC   Hyperoartia; Petromyzontiformes; Petromyzontidae; Petromyzon.
OX   NCBI_TaxID=7757 {ECO:0000313|Ensembl:ENSPMAP00000001784.1, ECO:0000313|Proteomes:UP000245300};
RN   [1] {ECO:0000313|Ensembl:ENSPMAP00000001784.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: May bind and stabilize microtubules during myotubes
CC       formation. {ECO:0000256|ARBA:ARBA00003888}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, Z line
CC       {ECO:0000256|ARBA:ARBA00004216}.
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DR   AlphaFoldDB; S4R9A3; -.
DR   STRING; 7757.ENSPMAP00000001784; -.
DR   Ensembl; ENSPMAT00000001793.1; ENSPMAP00000001784.1; ENSPMAG00000001617.1.
DR   GeneTree; ENSGT00940000156529; -.
DR   HOGENOM; CLU_013137_5_1_1; -.
DR   OMA; LMTEVYY; -.
DR   Proteomes; UP000245300; Unplaced.
DR   GO; GO:0030018; C:Z disc; IEA:UniProtKB-SubCell.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd19833; Bbox2_MuRF3_C-II; 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; IPR033492; Trim54_Bbox2_Zfn.
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   PANTHER; PTHR24099; E3 UBIQUITIN-PROTEIN LIGASE TRIM36-RELATED; 1.
DR   PANTHER; PTHR24099:SF32; TRIPARTITE MOTIF CONTAINING 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; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245300};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00024}.
FT   DOMAIN          22..46
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          115..157
FT                   /note="B box-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50119"
FT   DOMAIN          265..323
FT                   /note="COS"
FT                   /evidence="ECO:0000259|PROSITE:PS51262"
FT   REGION          318..352
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        325..352
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   352 AA;  39679 MW;  4E9D14B305A364C0 CRC64;
     MEYSSLLKPT ENLENLERQL MCPICLEVFS KPVVILPCQH NLCRKCANDV FQAANPFMVT
     RGNTVTSGGR FRGPLKTHRV IIDFFNTTNI QQLSRVNSAL CLSRAVENHR PVKKVDHPMC
     VEHAEEKINI FCLTCSMPTC SLCKVFGAHK DCQVAPLGSV YKSHKNDLSD SISRLVASND
     RVQLMISEME HSCKVIDENS RVQKQMLCEQ FDGVYAALEE RKQEMLMVIS QEQEDKNQHV
     RDLIKQYNEH LQSASKLVET AFQAMEEPEA AAFLQSASAL QKSVVDATKG SDMPKMEMGY
     ENMNHFLVDL DNVQEAVRGI DFGKDAEDED EEEDEEGEEV AESEEGNSDS SD
//
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