ID W6QCC5_PENRF Unreviewed; 917 AA.
AC W6QCC5;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Protein msp1, mitochondrial {ECO:0000313|EMBL:CDM34130.1};
GN Name=msp1 {ECO:0000313|EMBL:CDM34130.1};
GN ORFNames=PROQFM164_S03g000854 {ECO:0000313|EMBL:CDM34130.1};
OS Penicillium roqueforti (strain FM164).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1365484 {ECO:0000313|EMBL:CDM34130.1};
RN [1] {ECO:0000313|EMBL:CDM34130.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FM164 {ECO:0000313|EMBL:CDM34130.1};
RX PubMed=24407037; DOI=10.1038/ncomms3876;
RA Cheeseman K., Ropars J., Renault P., Dupont J., Gouzy J., Branca A.,
RA Abraham A.L., Ceppi M., Conseiller E., Debuchy R., Malagnac F., Goarin A.,
RA Silar P., Lacoste S., Sallet E., Bensimon A., Giraud T., Brygoo Y.;
RT "Multiple recent horizontal transfers of a large genomic region in cheese
RT making fungi.";
RL Nat. Commun. 5:2876-2876(2014).
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; HG792017; CDM34130.1; -; Genomic_DNA.
DR AlphaFoldDB; W6QCC5; -.
DR STRING; 1365484.W6QCC5; -.
DR OMA; PLKMGYV; -.
DR OrthoDB; 1052588at2759; -.
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}.
FT DOMAIN 238..511
FT /note="Dynamin-type G"
FT /evidence="ECO:0000259|PROSITE:PS51718"
FT DOMAIN 803..896
FT /note="GED"
FT /evidence="ECO:0000259|PROSITE:PS51388"
FT REGION 158..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 896..917
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 917 AA; 101133 MW; 0690BFDAA97BFFDD CRC64;
MSGRILSHRL GPLLRNGQLA RHIHNAGSRT GGLLRADGGA ALRGRAWPVG ANAIHNVPAV
RSISFARMLP KLALKLFRIP AMFGGATIAG LAYFQYQATQ AGNYVMDVFR QASDTAGNTA
STLFQGLQGM ADQTQRGWNK TTGNIEMPDW LQKVLRFDEE SESRNGDSSG GGGKEPKQSR
AGTAAAAAAT TAAFGYAQSG EGDLRPERDV AEDDQMMLLT RKMIEIRNIL QTIGQSGTLT
LPSIVVIGSQ SSGKSSVLEA IVGHEFLPKG SNMVTRRPIE LTLVNTPNAQ AEYGEFPALG
LGKITDFSQV QRTLTDLNLA VPEKDCVTDD PIQLTIYSPN VPDLSLIDLP GYIQVAGRDQ
PPELKQKIVD LCDRYIQPPN VILAISAADV DLANSTALRA SRRVDPRGER TIGVITKMDL
VSPERGHDVL SDKKYPLRLG YVGVVTRIPQ TTALFSRGPG NITSAILKNE HAYFSAHQNE
FGPHSDVSVG VSTLRKTLMQ VLEQTMSSSL SGTRDAISQE LEETTYEFKV QYNDRPLSAE
SHLAESLDAF KHSFKAFAES FGRPQVREML KAELDQRVMD ILAQRYWNKP VEDLDPPLLE
LDPLKDLPKA DAESLYWHRK LDASTSSLTK LGIGRLATTV VANALNNHVD SLLASSTFAS
HPGARKQITD ACTGILNDKF FSTSDQVENC IKPYKFEIEI EDPEWAKGRD NAGKVLKEEL
KSCESALKHV EDTVGKRKLQ DVVAFIDRVR KGEVVLEGNG EGGAGGFSAA LLARGREGLF
LRDRADLIKM RLLAVRSKQC ATQKNKYYCP EVFLDVVADK LTSTAVLFLN VELLSEFYYN
FPRELDSRLG RQLSDAEVER FAREDPRIRR HLDIIRKKEL LELALQKIEG IRQLDGRARK
SDRTPPGKEP RGRWNLF
//