ID W9X9T5_9EURO Unreviewed; 797 AA.
AC W9X9T5;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Dynamin GTPase {ECO:0000313|EMBL:EXJ76973.1};
GN ORFNames=A1O3_10130 {ECO:0000313|EMBL:EXJ76973.1};
OS Capronia epimyces CBS 606.96.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Capronia.
OX NCBI_TaxID=1182542 {ECO:0000313|EMBL:EXJ76973.1, ECO:0000313|Proteomes:UP000019478};
RN [1] {ECO:0000313|EMBL:EXJ76973.1, ECO:0000313|Proteomes:UP000019478}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 606.96 {ECO:0000313|EMBL:EXJ76973.1,
RC ECO:0000313|Proteomes:UP000019478};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Capronia epimyces CBS 606.96.";
RL Submitted (MAR-2013) 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:EXJ76973.1}.
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DR EMBL; AMGY01000011; EXJ76973.1; -; Genomic_DNA.
DR RefSeq; XP_007738411.1; XM_007740221.1.
DR AlphaFoldDB; W9X9T5; -.
DR STRING; 1182542.W9X9T5; -.
DR GeneID; 19174211; -.
DR eggNOG; KOG0446; Eukaryota.
DR HOGENOM; CLU_008964_5_0_1; -.
DR OrthoDB; 1052588at2759; -.
DR Proteomes; UP000019478; Unassembled WGS sequence.
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 GO; GO:0006996; P:organelle organization; IEA:UniProt.
DR CDD; cd08771; DLP_1; 1.
DR Gene3D; 1.20.120.1240; Dynamin, middle domain; 2.
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:UP000019478}.
FT DOMAIN 27..318
FT /note="Dynamin-type G"
FT /evidence="ECO:0000259|PROSITE:PS51718"
FT DOMAIN 710..797
FT /note="GED"
FT /evidence="ECO:0000259|PROSITE:PS51388"
FT REGION 534..609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 623..649
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 666..685
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 534..554
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 591..609
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 797 AA; 88429 MW; 9063203A6335211F CRC64;
MTTLGDDLLR TVNKLQDLVF NTIGNDSLDL PQIVVVGSQS SGKSSVLENI VGRDFLPRGS
GIVTRRPLIL QLINIPPDDE DGANDEDEVR IPHTAASVAE HGEWAEFHHI PGRKFRDFNQ
VRAEIENETA RIAGNNKGIN RQPINLKIFS PHVLNLTLVD LPGLTKVPIG DQPSDIEKQT
RTLISEYIAK PNSIVLAVSP ANVDIVNSEA LKLARHVDPL GRRTIGVLTK LDLMDHGTNA
LDILSGRVYP LKLGFIGVVN RSQQDIQTNK PMAEALKAEA EFFRHHPAYR NMATRCGTQY
LAKTLNTTLM AHIRDRLPDI KARLNTLMGQ TQQELASYGS KQFSGKEHRG SLILQLMTRF
ANSFISSIDG TSTEISTKEL CGGARIYYIF NSVFGNSLET IDPTHNLSVL DIRTAIRNST
GPRPSLFVPE LAFDLLVKPQ IKLLEIPSQR CVELVYEELI KICHTCGSQE LSRFPRLQGK
LIEVVSDLLR ERLGPSSHYV ESLISIQRAY INTNHPNFLG AAAAMSSVIA SKNEKDKRAA
QAEEKRKREK QRLKQIGLNG TATPDEEDAE QEDKATALPV RKHPAATRSM SPAVSRENGF
GSVSGATGTG GNTRDSFLNY FFGKDGGLPS GPPSGPPAAS APHRHPTQNI DASFSQSMRR
MERGSFTDRT PAFPPPMNDD YAPSEYGDSN SLFPEQSAEP VLTDREALET ELIRRLISSY
FNIVRETIAD QVPKAIMHLL VNHSRDEVQN RLVSELYKEE LFDELLYEDD GIKKEREKCE
RLLATYKEAA RIVGEVL
//
