ID F7WA64_SORMK Unreviewed; 802 AA.
AC F7WA64;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE SubName: Full=Putative dynamin-related protein {ECO:0000313|EMBL:CCC14127.1};
GN ORFNames=SMAC_08468 {ECO:0000313|EMBL:CCC14127.1};
OS Sordaria macrospora (strain ATCC MYA-333 / DSM 997 / K(L3346) / K-hell).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Sordaria.
OX NCBI_TaxID=771870 {ECO:0000313|EMBL:CCC14127.1, ECO:0000313|Proteomes:UP000001881};
RN [1] {ECO:0000313|EMBL:CCC14127.1, ECO:0000313|Proteomes:UP000001881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-333 / DSM 997 / K(L3346) / K-hell
RC {ECO:0000313|Proteomes:UP000001881};
RC TISSUE=Mycelium {ECO:0000313|EMBL:CCC14127.1};
RX PubMed=20386741; DOI=10.1371/journal.pgen.1000891;
RA Nowrousian M., Stajich J., Chu M., Engh I., Espagne E., Halliday K.,
RA Kamerewerd J., Kempken F., Knab B., Kuo H.C., Osiewacz H.D., Poeggeler S.,
RA Read N., Seiler S., Smith K., Zickler D., Kueck U., Freitag M.;
RT "De novo assembly of a 40 Mb eukaryotic genome from short sequence reads:
RT Sordaria macrospora, a model organism for fungal morphogenesis.";
RL PLoS Genet. 6:E1000891-E1000891(2010).
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:CCC14127.1}.
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DR EMBL; CABT02000058; CCC14127.1; -; Genomic_DNA.
DR RefSeq; XP_003346942.1; XM_003346894.1.
DR AlphaFoldDB; F7WA64; -.
DR STRING; 771870.F7WA64; -.
DR GeneID; 10804356; -.
DR KEGG; smp:SMAC_08468; -.
DR VEuPathDB; FungiDB:SMAC_08468; -.
DR eggNOG; KOG0446; Eukaryota.
DR HOGENOM; CLU_008964_5_0_1; -.
DR InParanoid; F7WA64; -.
DR OMA; KICHNCG; -.
DR OrthoDB; 1052588at2759; -.
DR Proteomes; UP000001881; 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:UP000001881}.
FT DOMAIN 27..314
FT /note="Dynamin-type G"
FT /evidence="ECO:0000259|PROSITE:PS51718"
FT DOMAIN 715..802
FT /note="GED"
FT /evidence="ECO:0000259|PROSITE:PS51388"
FT REGION 544..622
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 544..581
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 603..621
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 802 AA; 89201 MW; D2A56AA89B62CACA CRC64;
MAALGDDLLG VVNKLQDLVF NTIGNDSLDL PQIVVVGSQS AGKSSVLENI VGRDFLPRGS
GIVTRRPLIL QLINVPADDE TEDVTHPSYR NPNAAGRNEW AEFHHIPNRR FTDFGDVKRE
IENETARVAG TNKGINRQPI NLKIFSPHVL NLTLVDLPGL TKVPIGDQPT DIEKQTRNLI
SEYIAKPNSI VLAVSPANVD IVNSEALKLA RHVDPMGRRT IGVLTKVDLM DHGTNALDIL
SGRVYPLKLG WIGVVNRSQQ DIQGNKPMEE ALKSESDFFR HHPAYRNIST RCGTQFLART
LNTTLMAHIR ERLPDIKARL NTLMGQTQQE LASYGDMHFS GKEHRGSLIL QLMTRFASSF
IASIDGTSTE ISTKELCGGA RIYYIFNSVF GSSLESIDPT SNLTALDIRT AIRNSTGPRP
SLFVPEMAFD LLVKPQIKLL EPPSQRCVEL VYEELIKICH TCGSTELSRF PRMQAKLIEV
VSDLLRERLG PASNYVESLI SIQRAYINTN HPNFLGAAAA MSHVVSNKQE RERKRLIQEE
RERRERRRLK EHGANGTETP AEGEEEGTAL EKSDNVHARK MTGKSARSMS PAVRDNGPGS
IASALNGARS NSPSRFNGGQ GAGNAKESFL NYFFGKDGAI VPGPSHSGNI GRHVNQPMEP
TFSQSMRRPE EKQVRAPTQS TRVDDDMDYV SNVKGTELQS NDGEPAMTDR EAMEAELIRA
LISSYFNIVR ESIADQVPKA IMHLLVNHCK DVVQNRLVSE LYKETMFEEL LYEDDAVKKE
REKCERLLQT YREAAKIIGE VV
//
