ID   MX_EPICO                Reviewed;         626 AA.
AC   Q6PW23;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 58.
DE   RecName: Full=Interferon-induced GTP-binding protein Mx;
DE   AltName: Full=Interferon-inducible Mx protein;
GN   Name=mx;
OS   Epinephelus coioides (Orange-spotted grouper) (Epinephelus nebulosus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Perciformes; Serranoidei; Serranidae; Epinephelinae;
OC   Epinephelini; Epinephelus.
OX   NCBI_TaxID=94232;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=15967681; DOI=10.1016/j.fsi.2005.04.001;
RA   Chen Y.-M., Su Y.-L., Lin J.-H., Yang H.-L., Chen T.-Y.;
RT   "Cloning of an orange-spotted grouper (Epinephelus coioides) Mx cDNA and
RT   characterisation of its expression in response to nodavirus.";
RL   Fish Shellfish Immunol. 20:58-71(2006).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- INDUCTION: By interferons.
CC   -!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
CC       superfamily. Dynamin/Fzo/YdjA family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01055}.
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DR   EMBL; AY574372; AAS82739.1; -; mRNA.
DR   AlphaFoldDB; Q6PW23; -.
DR   SMR; Q6PW23; -.
DR   PRIDE; Q6PW23; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   CDD; cd08771; DLP_1; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR022812; Dynamin.
DR   InterPro; IPR001401; Dynamin_GTPase.
DR   InterPro; IPR019762; Dynamin_GTPase_CS.
DR   InterPro; IPR045063; Dynamin_N.
DR   InterPro; IPR000375; Dynamin_stalk.
DR   InterPro; IPR030381; G_DYNAMIN_dom.
DR   InterPro; IPR003130; GED.
DR   InterPro; IPR020850; GED_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR11566; PTHR11566; 1.
DR   Pfam; PF01031; Dynamin_M; 1.
DR   Pfam; PF00350; Dynamin_N; 1.
DR   Pfam; PF02212; GED; 1.
DR   PRINTS; PR00195; DYNAMIN.
DR   SMART; SM00053; DYNc; 1.
DR   SMART; SM00302; GED; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00410; G_DYNAMIN_1; 1.
DR   PROSITE; PS51718; G_DYNAMIN_2; 1.
DR   PROSITE; PS51388; GED; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; GTP-binding; Nucleotide-binding.
FT   CHAIN           1..626
FT                   /note="Interferon-induced GTP-binding protein Mx"
FT                   /id="PRO_0000292872"
FT   DOMAIN          30..303
FT                   /note="Dynamin-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT   DOMAIN          540..626
FT                   /note="GED"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00720"
FT   REGION          40..47
FT                   /note="G1 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT   REGION          65..67
FT                   /note="G2 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT   REGION          141..144
FT                   /note="G3 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT   REGION          210..213
FT                   /note="G4 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT   REGION          242..245
FT                   /note="G5 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT   BINDING         40..47
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
FT   BINDING         141..145
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
FT   BINDING         210..213
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   626 AA;  71322 MW;  3416AB1FE6974547 CRC64;
     MNTLNQQYEE KVRPCIDLID SLRSLGVEKD LALPAIAVIG DQSSGKSSVL EALSGVALPR
     GSGIVTRCPL ELKMKRKKEG EEWYGKISYR GCEKELEDPS DVENKIREAQ DEMAGVGVGI
     SDDLISLEIA SPDVPDLTLI DLPGIARVAV KGQPEDIGKQ IKGLIQRFIT RQETISLVVV
     PCNVDIATTE ALKMAQEVDP DGERTLGILT KPDLVDKGTE ETVVEIVHNE VIHLKKGYMI
     VRCRGQKEIT EKVSLTEALE SEKAFFRDHV HFHTLYNEGQ ATVPKLAEKL TLELVHHIER
     SLPRLEEQIE DKLEQTQAEL ERYGSGPPSD ATEKLFFLID KVTAFTQDAI SLTTGEDLKC
     GDKLNVFSAL RREFARWNAH LDLSGEKFNK RIEKEVENYE EKYRGRELPG FINYKTFEVM
     VKEQIKQLEE PAVKRLKEIG DTVRKAFIQL AHSSFIGFPN LIKTAKAKIE AIKQEKESTA
     ESMLRTQFKM ELIVYTQDRT YSNSLSDRKR EEDEEEDTRK GPVFAKQRSI VYRMDNHATL
     QELMLHIKSY YKIASQRLAD QIPLVIRYQM LQESAAQLQR EMLQMLQDKE NMDFLLKEDC
     DIGSKRAGLQ SRLKRLMKAR AYLVEF