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Database: UniProt
Entry: A0A1S3BZF7_CUCME
LinkDB: A0A1S3BZF7_CUCME
Original site: A0A1S3BZF7_CUCME 
ID   A0A1S3BZF7_CUCME        Unreviewed;       822 AA.
AC   A0A1S3BZF7;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Dynamin-related protein 3A-like {ECO:0000313|RefSeq:XP_008454460.1};
GN   Name=LOC103494859 {ECO:0000313|RefSeq:XP_008454460.1};
OS   Cucumis melo (Muskmelon).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Cucumis.
OX   NCBI_TaxID=3656 {ECO:0000313|Proteomes:UP000089565, ECO:0000313|RefSeq:XP_008454460.1};
RN   [1] {ECO:0000313|Proteomes:UP000089565}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. DHL92 {ECO:0000313|Proteomes:UP000089565};
RX   PubMed=22753475; DOI=10.1073/pnas.1205415109;
RA   Garcia-Mas J., Benjak A., Sanseverino W., Bourgeois M., Mir G.,
RA   Gonzalez V.M., Henaff E., Camara F., Cozzuto L., Lowy E., Alioto T.,
RA   Capella-Gutierrez S., Blanca J., Canizares J., Ziarsolo P.,
RA   Gonzalez-Ibeas D., Rodriguez-Moreno L., Droege M., Du L.,
RA   Alvarez-Tejado M., Lorente-Galdos B., Mele M., Yang L., Weng Y.,
RA   Navarro A., Marques-Bonet T., Aranda M.A., Nuez F., Pico B., Gabaldon T.,
RA   Roma G., Guigo R., Casacuberta J.M., Arus P., Puigdomenech P.;
RT   "The genome of melon (Cucumis melo L.).";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:11872-11877(2012).
RN   [2] {ECO:0000313|RefSeq:XP_008454460.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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   RefSeq; XP_008454460.1; XM_008456238.2.
DR   AlphaFoldDB; A0A1S3BZF7; -.
DR   GeneID; 103494859; -.
DR   KEGG; cmo:103494859; -.
DR   eggNOG; KOG0446; Eukaryota.
DR   InParanoid; A0A1S3BZF7; -.
DR   OrthoDB; 447862at2759; -.
DR   Proteomes; UP000089565; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:UniProt.
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:SF21; DYNAMIN-1-LIKE PROTEIN; 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   GTP-binding {ECO:0000256|RuleBase:RU003932};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU003932};
KW   Reference proteome {ECO:0000313|Proteomes:UP000089565}.
FT   DOMAIN          44..312
FT                   /note="Dynamin-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51718"
FT   DOMAIN          654..745
FT                   /note="GED"
FT                   /evidence="ECO:0000259|PROSITE:PS51388"
FT   REGION          532..594
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          741..822
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        538..557
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        741..755
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        763..812
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   822 AA;  90569 MW;  4D4EA42F11F30663 CRC64;
     MADDPVAPSM PSVSSSSAAP LGSSVIPIVN KLQDIFAQLG SQSTIELPQV AVVGSQSSGK
     SSVLEALVGR DFLPRGSGIC TRRPLVLQLL QTNTDKEYGE FLHLPGKKFY DFSEIRREIQ
     SETEREVGGN KGVSDKQIRL KIFSPNVLDI TLVDLPGITK VPVGDQPSDI EARIRTMIMS
     YIKVPSCLIL AVTPANSDLA NSDALQIAGN ADPDGVRTIG VITKLDIMDR GTDARNLLLG
     KVIPLRLGYV GVVNRSQEDI LLNRSIKDAL VDEEKFFRTH PVYNGLADRC GIAQLAKKLN
     QVLVQHIKAV FPGLKSRISA ALVSVAKEHA SYGEITESKA GQGALLLNIL SKYCEAFCSM
     VEGKNEKSTN KLLGGARIHY IFQSIYVKSL EEVDPCEDLT DDDIRTAIQN ATGPKSAVFV
     PDVPFEVLIR RQIIRLLDPS LQCARFIYDE LVEISHRCLT NELQRFPVLR KRIDEVIGNF
     LREGLEPSET IIGHLINIEM GYINTSHPNF IGGSKAVEMA LQQVKSSRVP STVPRLKDGV
     VEPDKAPPSE KTSKSRAFLA RHSNGFLTEK GARPSGDGEK VAPPGATANN SSWGISSIFG
     GSDNRTSAKE SSTSKPYNEH VLNTEQSFSM IHLREPPLVL RPSGGCTEQE AIEIAVIKLL
     LRSYYDIVRN NIKDLVPKSI MHFLVNHTKQ EMHNVFIKKL YRENLFEEML QEPDEVAMKR
     KHTRETLRVL QQAFRTLDEL PLEAESVERG DDPTGLPRMH GMPTSSMYST TSSNDSFSPS
     PKNPKPRKSS YSGELQVPVY GNSDSNGNGR SFMPSLYPKL DL
//
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