ID A0A0B7N689_9FUNG Unreviewed; 913 AA.
AC A0A0B7N689;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Dynamin-type G domain-containing protein {ECO:0008006|Google:ProtNLM};
GN Name=PARPA_04789.1 scaffold 15639 {ECO:0000313|EMBL:CEP10990.1};
OS Parasitella parasitica.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Parasitella.
OX NCBI_TaxID=35722 {ECO:0000313|EMBL:CEP10990.1, ECO:0000313|Proteomes:UP000054107};
RN [1] {ECO:0000313|EMBL:CEP10990.1, ECO:0000313|Proteomes:UP000054107}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 412.66 {ECO:0000313|EMBL:CEP10990.1,
RC ECO:0000313|Proteomes:UP000054107};
RA Ellenberger Sabrina;
RL Submitted (SEP-2014) 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}.
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DR EMBL; LN725615; CEP10990.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B7N689; -.
DR STRING; 35722.A0A0B7N689; -.
DR OrthoDB; 1052588at2759; -.
DR Proteomes; UP000054107; Unassembled WGS sequence.
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; 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; IPR020850; GED_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11566; DYNAMIN; 1.
DR PANTHER; PTHR11566:SF237; INTERFERON-INDUCED GTP-BINDING PROTEIN MX; 1.
DR Pfam; PF01031; Dynamin_M; 1.
DR Pfam; PF00350; Dynamin_N; 1.
DR PRINTS; PR00195; DYNAMIN.
DR SMART; SM00053; DYNc; 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:UP000054107}.
FT DOMAIN 252..518
FT /note="Dynamin-type G"
FT /evidence="ECO:0000259|PROSITE:PS51718"
FT DOMAIN 807..900
FT /note="GED"
FT /evidence="ECO:0000259|PROSITE:PS51388"
FT REGION 141..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 188..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..220
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 913 AA; 103557 MW; EB5AAF15495A2564 CRC64;
MASRPRVALH RLHNTPVRQI PPSLLFRSAR ARTYHGTAPL ALQPQARAIS LWSLANSALK
TVRMPFLVAG TTITTASIAS NTFLDTANRS KEFVQDNIQS IKSALRKAQT AVESMDLSIP
EMHLRLPQSV RNLLLSKTSK KIEESKVVNH HKSTNGQSGS GGGEGGNNGG EDSAAAAATV
AAAAGFSLYS DKDNEDKEEE SDDEHDPLEK NRAKKRKKND YGISAQDEQL MMLTKKLIEI
RSILMSIDHN ETLKLPSIVV IGSQSSGKSS VLEAIVGHEF LPKGSNMVTR RPIELTLIHT
PNQEEEYGEF PDLGLGKIFD FKKIQKTLVD LNMAVSESEC VSDKPIELRV YSPNVPDLTL
IDLPGYIQIS NRNQPETLKN KIEDLCEKYI RGPNIILAVC SANVDLANSP ALKASRKWDP
LGLRTIGVIT KMDLVSPQVG AAILRNTDYP LHLGYIGVVC KAPENMANGN MTRALVKSEE
SFFRSHLIFN QRDIQVGTST LRHKLMNVLE QSMGKSLYSI VDAVQRELEE ARYQFKVQYN
DRRVTAESYV AETMDCLKHD FKDFANNFGK PQVRHEVRTM LEQRVLDICA EQYWCDPKIA
ELPKASSEDI YWLYKVDFAS AALTKSGIGR STTQLVVDVL MNNMERLANA ESFSCHPETR
KQIMKFTSEI LRTKFLATSD QVENTIKPYK FEVEVNDSEW NDGVKRSIIL LEKELEMCDE
MANSIKNSVG KKKLNSAINY VLDKEKEETK RQERVQQNDV EEEEEEVKSF YNPKLLEKAK
DAIYLRDRAI ILKYRIAALK SRQCKSSENK QYCPEAFLNV IAEKLTYTAV MFIQVELLNE
FFFQFPREVD NRLVYEMDRR QIQQFARENP PIQKHLELQE RKMKLEEVMD KLNYLVKRQA
DRANSAKFTA NSY
//