ID A0A1Q2YHX8_9ASCO Unreviewed; 791 AA.
AC A0A1Q2YHX8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:GAV29115.1};
GN ORFNames=PMKS-002595 {ECO:0000313|EMBL:GAV29115.1};
OS Pichia membranifaciens.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Pichiaceae; Pichia.
OX NCBI_TaxID=4926 {ECO:0000313|EMBL:GAV29115.1, ECO:0000313|Proteomes:UP000186136};
RN [1] {ECO:0000313|EMBL:GAV29115.1, ECO:0000313|Proteomes:UP000186136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KS47-1 {ECO:0000313|EMBL:GAV29115.1,
RC ECO:0000313|Proteomes:UP000186136};
RA Konishi M., Ishida M., Arakawa T., Kato Y., Horiuchi J.;
RT "Whole genome shotgun sequence of Pichia membranifaciens KS47-1.";
RL Submitted (AUG-2016) 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:GAV29115.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BDGI01000102; GAV29115.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q2YHX8; -.
DR Proteomes; UP000186136; 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:UP000186136}.
FT DOMAIN 25..338
FT /note="Dynamin-type G"
FT /evidence="ECO:0000259|PROSITE:PS51718"
FT DOMAIN 704..791
FT /note="GED"
FT /evidence="ECO:0000259|PROSITE:PS51388"
FT REGION 89..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 551..631
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..114
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 551..576
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 589..628
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 791 AA; 88586 MW; 7E220C99F3A6E422 CRC64;
MAALQELIPV VNKLQDIVTN TSLTDLDLPL LTVIGSQSAG KSSVLENIVG KDFLPRGTGI
VTRRPLILQL IHLDDDDPLL SRADYVADEP NDPSEMTLEQ HLRNQSSSTE INGEAGGHTP
PAEWGEFLHI PGKRFYNFDN IRKEIENETS RIAGKNKGIS RIPINLKIYS PNVLNLTLVD
LPGLTKIPIA DQPVDIERQI RNLILEYISK PNSIILAVTP ANQDLVNSEA LKLARQVDPQ
GKRTIGILSK LDLMDHGTNA LDILTGKVYP LKLGFIGVVN RSQQDIMSRK SLNDSLAAEM
EFFNSHPAYK TISARCGTAY LAKVLNKTLM NHIRERLPDI KAKLNTLMGQ TEQELASYGN
LNVVSKENRS GLILQMMNKF ATSFMNSIEG NSSEISTKEL CGGARIYYIY NEVLGNSLMS
INPLQNLTVI DIRTAIRNST GPRPSLFVPE LAFDLLVKPQ IQLLEGPSHR CVELVYEELM
KICHNCGSQE LARYPKLHAK LIEVVSDLLR ERLGPTTKYV ESLIEINRAY INTNHPNFVG
AATAMASVVE ERQKQKEHER DHEKHLLLKR EENATAPTKA AKAAASTAAA NAENGSVSAN
SKDHSAKANN KPESSVLDAI SSSSHSLTSE SKPEKENFLN FFFGKKEEVQ GKVEHTKIAP
FSYPTETESS NLQFHLPMED SIQHQMDQFH LNEEQLSERE QLECELIRRL IASYFAIVRE
TIRDQVPKAI MCLLVNYTKE SVQNQLVQKL YKESLFEDLL YEDEALIQER EKCEKLLDTY
RQAATVISEV M
//
