ID G1PGM1_MYOLU Unreviewed; 633 AA.
AC G1PGM1;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE SubName: Full=Tripartite motif containing 25 {ECO:0000313|Ensembl:ENSMLUP00000009789.2};
GN Name=TRIM25 {ECO:0000313|Ensembl:ENSMLUP00000009789.2};
OS Myotis lucifugus (Little brown bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000009789.2, ECO:0000313|Proteomes:UP000001074};
RN [1] {ECO:0000313|Ensembl:ENSMLUP00000009789.2, ECO:0000313|Proteomes:UP000001074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSMLUP00000009789.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR EMBL; AAPE02030735; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAPE02030736; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; G1PGM1; -.
DR STRING; 59463.ENSMLUP00000009789; -.
DR Ensembl; ENSMLUT00000010738.2; ENSMLUP00000009789.2; ENSMLUG00000010740.2.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000160741; -.
DR HOGENOM; CLU_013137_0_2_1; -.
DR InParanoid; G1PGM1; -.
DR OMA; KRGVHYW; -.
DR TreeFam; TF351086; -.
DR Proteomes; UP000001074; Unassembled WGS sequence.
DR GO; GO:0010494; C:cytoplasmic stress granule; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0016604; C:nuclear body; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0039552; F:RIG-I binding; IEA:Ensembl.
DR GO; GO:0003713; F:transcription coactivator activity; IEA:Ensembl.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:Ensembl.
DR GO; GO:0140374; P:antiviral innate immune response; IEA:Ensembl.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
DR GO; GO:0002753; P:cytoplasmic pattern recognition receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0036503; P:ERAD pathway; IEA:Ensembl.
DR GO; GO:0046597; P:negative regulation of viral entry into host cell; IEA:Ensembl.
DR GO; GO:0043123; P:positive regulation of canonical NF-kappaB signal transduction; IEA:Ensembl.
DR GO; GO:0070936; P:protein K48-linked ubiquitination; IEA:Ensembl.
DR GO; GO:0006513; P:protein monoubiquitination; IEA:Ensembl.
DR GO; GO:0032880; P:regulation of protein localization; IEA:Ensembl.
DR GO; GO:0043627; P:response to estrogen; IEA:Ensembl.
DR GO; GO:0006979; P:response to oxidative stress; IEA:Ensembl.
DR GO; GO:0044790; P:suppression of viral release by host; IEA:Ensembl.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:Ensembl.
DR GO; GO:0019076; P:viral release from host cell; IEA:Ensembl.
DR CDD; cd19842; Bbox1_TRIM25-like_C-IV; 1.
DR CDD; cd19776; Bbox2_TRIM25_C-IV; 1.
DR CDD; cd16597; RING-HC_TRIM25_C-IV; 1.
DR Gene3D; 2.60.120.920; -; 1.
DR Gene3D; 4.10.830.40; -; 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; IPR001870; B30.2/SPRY.
DR InterPro; IPR043136; B30.2/SPRY_sf.
DR InterPro; IPR003879; Butyrophylin_SPRY.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR006574; PRY.
DR InterPro; IPR003877; SPRY_dom.
DR InterPro; IPR027370; Znf-RING_euk.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR25465; B-BOX DOMAIN CONTAINING; 1.
DR PANTHER; PTHR25465:SF40; E3 UBIQUITIN_ISG15 LIGASE TRIM25; 1.
DR Pfam; PF13765; PRY; 1.
DR Pfam; PF00622; SPRY; 1.
DR Pfam; PF13445; zf-RING_UBOX; 1.
DR PRINTS; PR01407; BUTYPHLNCDUF.
DR SMART; SM00589; PRY; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00449; SPRY; 1.
DR SUPFAM; SSF57845; B-box zinc-binding domain; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50188; B302_SPRY; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Immunity {ECO:0000256|ARBA:ARBA00022859};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000001074};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 13..54
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 442..633
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000259|PROSITE:PS50188"
FT REGION 352..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 217..301
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 380..394
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 633 AA; 70801 MW; 56904C85F3A72973 CRC64;
LSEYMSLAEE LTCSICLELF KVPVTTPCGH NFCGSCLDET WTVQGAPFQC PQCRTEYPAR
PQLRKNTVLC TVVEQFAQAE LARATAPDDW TPPSRAAAPS PTGQVACDHC LKAAAIKTCL
VCMASFCQEH LRPHFDSPAF RDHPLQPPVQ DLFRRKCPQH NRLRDLFCPE HSECICHICL
VEHKTCSPVP LSQASADLED KLKYKLTVMY GQINGAARAL EDVRARQKDV REAAQKKMEQ
LRQEYLEMKA LIDASEASST RKIKEEEKRV SSKFDNIYQI LLKKKAEMQT VKEEIEAALT
KGGEFEFLEK AAQLQAVSTK PVYVPKVELN HELIKGVSQS TADLKTELKR CLRKPEEPLT
SGTGEPAEHA TAPTPKPTRP VKKVPKEEKK PKKVPPAAAA VSPNKLPTFG SSEQLGDLKQ
AGFEAAAKPT PVQPNSVSLK AKVLENFLAK SRPELLAYAV KVILDYNTAY SKVALSENYT
VASVAETHQS YRPHPQRFTY CSQVLGLHCY KKGIHYWEVE LQKNNFCGMG ICYGSMARQG
PESRLGRNNA SWCVEWFNNK ISAWHNNVEK ILPTTKATRV GVLLNCDHGF VIFFAVALDR
IHVMYKYKED FTEALYPAFW VFSTGATLSI CSA
//
