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Database: UniProt
Entry: A0A0V1BM63_TRISP
LinkDB: A0A0V1BM63_TRISP
Original site: A0A0V1BM63_TRISP 
ID   A0A0V1BM63_TRISP        Unreviewed;       891 AA.
AC   A0A0V1BM63;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=dynamin GTPase {ECO:0000256|ARBA:ARBA00011980};
DE            EC=3.6.5.5 {ECO:0000256|ARBA:ARBA00011980};
GN   Name=dyn-1 {ECO:0000313|EMBL:KRY38054.1};
GN   ORFNames=T01_11757 {ECO:0000313|EMBL:KRY38054.1};
OS   Trichinella spiralis (Trichina worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=6334 {ECO:0000313|EMBL:KRY38054.1, ECO:0000313|Proteomes:UP000054776};
RN   [1] {ECO:0000313|EMBL:KRY38054.1, ECO:0000313|Proteomes:UP000054776}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS3 {ECO:0000313|EMBL:KRY38054.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
CC       superfamily. Dynamin/Fzo/YdjA family. {ECO:0000256|RuleBase:RU003932}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KRY38054.1}.
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DR   EMBL; JYDH01000028; KRY38054.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V1BM63; -.
DR   STRING; 6334.A0A0V1BM63; -.
DR   eggNOG; KOG0446; Eukaryota.
DR   InParanoid; A0A0V1BM63; -.
DR   Proteomes; UP000054776; Unassembled WGS sequence.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR   CDD; cd08771; DLP_1; 1.
DR   CDD; cd01256; PH_dynamin; 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   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 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   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   PANTHER; PTHR11566; DYNAMIN; 1.
DR   PANTHER; PTHR11566:SF212; DYNAMIN; 1.
DR   Pfam; PF01031; Dynamin_M; 1.
DR   Pfam; PF00350; Dynamin_N; 1.
DR   Pfam; PF02212; GED; 1.
DR   Pfam; PF00169; PH; 1.
DR   PRINTS; PR00195; DYNAMIN.
DR   SMART; SM00053; DYNc; 1.
DR   SMART; SM00302; GED; 1.
DR   SMART; SM00233; PH; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   PROSITE; PS00410; G_DYNAMIN_1; 1.
DR   PROSITE; PS51718; G_DYNAMIN_2; 1.
DR   PROSITE; PS51388; GED; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   3: Inferred from homology;
KW   Endocytosis {ECO:0000256|ARBA:ARBA00022583};
KW   GTP-binding {ECO:0000256|RuleBase:RU003932};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW   Motor protein {ECO:0000256|ARBA:ARBA00023175};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU003932};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054776}.
FT   DOMAIN          30..297
FT                   /note="Dynamin-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51718"
FT   DOMAIN          519..625
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          653..744
FT                   /note="GED"
FT                   /evidence="ECO:0000259|PROSITE:PS51388"
FT   REGION          629..650
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          742..793
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        631..647
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        742..765
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   891 AA;  100530 MW;  E74B48EE7EAFDB55 CRC64;
     MAWINQGMQQ LIPLVNQLQD AFNKLGVSLA LDLPQIAVVG GQSAGKSSVL EAFVGKDFLP
     RGSGIVTRRP LVLQLIHDRS VEYGEFLHKK GQKYGDFELI RAEIEAETER VTGSNKGISP
     VPINLRIYSP NVLNLTLIDL PGLTKVPVGD QPHDIETQIR DMILTYVTRE NCLILAVTSA
     NTDLATSDAL KLAKEVDPAG QRTIGVITKL DLMDEGTDAR EILENRLLPL RRGYIGVVNR
     SQKDIDGRKD IRSALEAERR FFLSHPSYRH MADRMGTTYL QKVLNQQLTN HIRDTLPALR
     DRLQRQLLIL EKDVSEYKNF RPDDPSRKTK AMLQMVQQFC ADFEKSIEGS SGKDVSVNEL
     SGGAKINRLF HERFPFEIVK MEIDEKELRK EIAYAIRNIH GIRVGLFTPD MAFEAIVKKQ
     ISRLKEPSLK CVDLVVTELG NVIRMCAEMM SRYPRLMEEV ERIVTTHLRD REQKCKDQLI
     LLVEYELAYM NTNHEDFIGF ANAEAKASAV QRQKKLGNQV IRKGWLTIHN VSFIKGGSRD
     FWFVLSSDNL SWYKDDEEKE KKYMLPLDGL KLRDIEAGFM SRTHKFALFY PDNKNVYKDY
     RQLELSAITP DEVDAWKASF LRAGVYPEKE STAGAEERQE DNSSMDPQLE RQVETIRNLV
     DSYMRIVTKT IRDLVPKAIM HLMIHNTNDF IHHELLAHLY QSGDQDSMME ESEAESQRRE
     EMLRMYHACK EALRIIGDVS LNTTPSTISS TSNGGGSSSH DWLKNDNQII PPRPVVNGPP
     SPNLPRPASG AALRPAPMPV GVQASSVPTV GGGGAGIQIP KIPSRPAPTL NQMGAGSLPP
     PLIPQYYSPL ASKVIIAICQ KYGQIVWQLY PPYNKPAPKI PDRPAVTHRH Y
//
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