ID A0A093HL46_STRCA Unreviewed; 980 AA.
AC A0A093HL46;
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=E3 ubiquitin-protein ligase TRIM37 {ECO:0000313|EMBL:KFV80175.1};
DE Flags: Fragment;
GN ORFNames=N308_07031 {ECO:0000313|EMBL:KFV80175.1};
OS Struthio camelus australis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Palaeognathae; Struthioniformes; Struthionidae;
OC Struthio.
OX NCBI_TaxID=441894 {ECO:0000313|EMBL:KFV80175.1, ECO:0000313|Proteomes:UP000053584};
RN [1] {ECO:0000313|EMBL:KFV80175.1, ECO:0000313|Proteomes:UP000053584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N308 {ECO:0000313|EMBL:KFV80175.1};
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; KL206227; KFV80175.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093HL46; -.
DR STRING; 441894.ENSSCUP00000008058; -.
DR Proteomes; UP000053584; Unassembled WGS sequence.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:InterPro.
DR CDD; cd19779; Bbox2_TRIM37_C-VIII; 1.
DR CDD; cd03773; MATH_TRIM37; 1.
DR CDD; cd16619; mRING-HC-C4C4_TRIM37_C-VIII; 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; IPR003649; Bbox_C.
DR InterPro; IPR002083; MATH/TRAF_dom.
DR InterPro; IPR008974; TRAF-like.
DR InterPro; IPR037299; TRIM37_MATH.
DR InterPro; IPR000315; Znf_B-box.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR36754; E3 UBIQUITIN-PROTEIN LIGASE TRIM37; 1.
DR PANTHER; PTHR36754:SF2; E3 UBIQUITIN-PROTEIN LIGASE TRIM37; 1.
DR Pfam; PF00917; MATH; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR SMART; SM00502; BBC; 1.
DR SMART; SM00336; BBOX; 1.
DR SMART; SM00061; MATH; 1.
DR SUPFAM; SSF57845; B-box zinc-binding domain; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF49599; TRAF domain-like; 1.
DR PROSITE; PS50144; MATH; 1.
DR PROSITE; PS50119; ZF_BBOX; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000053584};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00024}.
FT DOMAIN 10..50
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 85..127
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT DOMAIN 271..398
FT /note="MATH"
FT /evidence="ECO:0000259|PROSITE:PS50144"
FT REGION 442..555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 573..606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 755..845
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 857..879
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 918..946
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 959..980
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 128..169
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 442..458
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..521
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 523..539
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 540..555
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 584..606
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 755..769
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 790..819
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFV80175.1"
FT NON_TER 980
FT /evidence="ECO:0000313|EMBL:KFV80175.1"
SQ SEQUENCE 980 AA; 108631 MW; BA9209CF83099382 CRC64;
LQSIAEVFRC FICMEKLRDA RLCPHCSKLC CFSCIRRWLT EQRAQCPHCR APLQLRELVN
CRWAEEVTQQ LDTLQLCNLT KHEENEKDKC ENHHEKLSVF CWTCKKCICH QCALWGGMHG
GHTFKPLAEI YEQHVTKVNE EVAKLRRRLM ELISLVQEVE RNVEAVRSAK DERVREIRNA
VEMMIARLDT QLKNKLITLM GQKTSLTQET ELLESLLQEV EHQLRSCSKS ELISKSSEIL
MMFQQVHRKP MASFVTTPVP PDFTSELVPA YDSTTFVLEN FSTLRQRADP VYSPPLQVSG
LCWRLKVYPD GNGVVRGYYL SVFLELSAGL PETSKYEYRV EMVHQSTNDP AKNIIREFAS
DFEVGECWGY NRFFRLDLLA NEGYLNRQND TVILRFQVRS PTFFQKCRDQ HWYIAQLEAA
QTSYIQQINN LKERLAIELS RTQKSRGISP PDTHLSPQND DGPETRSKKP GQSAEVLLEN
VAAPGVRDSK EDDEEKIQHE DFNHELSDGD LDVDLAGEDE INHLDGSSSS ASSTATSNTE
ENDIDEETMS GENDVEYSNN MELEEGDLME DAAAAAAATP GASGTSHGYA NANGRSSRRG
GSTLGSAASS SLLDIDPLIL IHLLDLKDRN GMENLWGLQP RPPASLLQNR ASSYSLKDRD
QRRHQAMWRV PPDLKMLKRL KTQVAEVRSK MSDVKNQLSE VRSSNNAGTC DGQPSFFSVD
QGALAACGTE SCSKLQEIGM ELLTKSSVTS CYIRNPASKK SNSPKPIRSG AAGSLSLRRA
MDCGDGNLRS KGDGQTSEGG IGSSKSSSRH NSPRPLTGSN VSEALPKPEE RPCEGLDSDM
GTSGLNGLAA LEKTRKAGAL GSNSKGRHTE ETQSADLENN LETGELQGML SEGASAAAEE
AGICQKHVLH LLPGMSSDSD IECDTENEEQ EDATSTSEGF NHAFSVQSSS EALERCAVFP
EGDQAGSDDL SFVTGEDSTR
//
