ID A0A3B3SII8_9TELE Unreviewed; 654 AA.
AC A0A3B3SII8;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Interferon-induced GTP-binding protein Mx3-like {ECO:0000313|Ensembl:ENSPKIP00000030569.1};
OS Paramormyrops kingsleyae.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000030569.1, ECO:0000313|Proteomes:UP000261540};
RN [1] {ECO:0000313|Ensembl:ENSPKIP00000030569.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
CC superfamily. Dynamin/Fzo/YdjA family. {ECO:0000256|RuleBase:RU003932}.
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DR AlphaFoldDB; A0A3B3SII8; -.
DR STRING; 1676925.ENSPKIP00000030569; -.
DR Ensembl; ENSPKIT00000011390.1; ENSPKIP00000030569.1; ENSPKIG00000011367.1.
DR GeneTree; ENSGT00940000155686; -.
DR OrthoDB; 1052588at2759; -.
DR Proteomes; UP000261540; Unplaced.
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; 1.20.120.1240; Dynamin, middle domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; DYNAMIN; 1.
DR PANTHER; PTHR11566:SF225; INTERFERON-INDUCED GTP-BINDING PROTEIN MXA-RELATED; 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; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00410; G_DYNAMIN_1; 1.
DR PROSITE; PS51718; G_DYNAMIN_2; 1.
DR PROSITE; PS51388; GED; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|RuleBase:RU003932};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU003932}.
FT DOMAIN 67..340
FT /note="Dynamin-type G"
FT /evidence="ECO:0000259|PROSITE:PS51718"
FT DOMAIN 566..654
FT /note="GED"
FT /evidence="ECO:0000259|PROSITE:PS51388"
FT REGION 7..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 594..621
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 654 AA; 73875 MW; 8EB14890F3378298 CRC64;
MELALLEESG SLSSALSDDL EPGELEETAA SPKPCGVTNI LNEHYEEKVR PCIDLIDSLR
SLGVEQDLAL PAIAVIGDQS SGKSSVLEAL SGVALPRGSG IVTRCPLELK MKKIKAEDNW
YGKIKYKSEE KEIKDPSEVE RFIRKAQDEI AGVGVGISQE LISLEISSPD VPDLTLIDLP
GIARVAVKGQ PENIGEQIKC LIKKFIAKQE TINLVVVPCN VDIATTEALK MAQEVDPHGE
RTLGILTKPD LVDKGTEETI VQIILNEVIH LAKGYMVVKC RGQKDITDRV SLTEALDKEK
FFFEGHSHFG VLYKEGYASI PHLAEKLTLE LVQHIEKSLP RLEDQIQRKI ADLEKELERY
GRGSPTDAAD RRMFLIDKVT EFTQATLNLA TGEELKHGNK ASLLSVLRVQ FEKWKKVLDE
SGLKFNQKIE SESSEYEKKY RGRELPGFVN YKTFEMIMKE QISQLEEPAV KKLKEISDIV
RRAFIQLSQE SLIGYPNLQK TAKTKIEVIK QSKDTAAESI LRTQFKMEMV VYTQDSTYGH
SLKKMKGEDG VGFGFKSQTF SERTTLQEMA MHIKSYYQVA SQRLADQIPL VVRYEILQEA
ARQLQREMIE LLQNKDNVDD LLKEDYDIGT KRKNLIFRLS RLKEAQRHLL FFSL
//
