ID A0A0V0Z9T2_9BILA Unreviewed; 963 AA.
AC A0A0V0Z9T2;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 22-FEB-2023, entry version 22.
DE RecName: Full=Dynamin-like 120 kDa protein, mitochondrial {ECO:0000256|ARBA:ARBA00018307};
DE EC=3.6.5.5 {ECO:0000256|ARBA:ARBA00011980};
GN Name=opa1 {ECO:0000313|EMBL:KRY09117.1};
GN ORFNames=T12_2086 {ECO:0000313|EMBL:KRY09117.1};
OS Trichinella patagoniensis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=990121 {ECO:0000313|EMBL:KRY09117.1, ECO:0000313|Proteomes:UP000054783};
RN [1] {ECO:0000313|EMBL:KRY09117.1, ECO:0000313|Proteomes:UP000054783}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS2496 {ECO:0000313|EMBL:KRY09117.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.5;
CC Evidence={ECO:0000256|ARBA:ARBA00001837};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}. Mitochondrion
CC inner membrane {ECO:0000256|ARBA:ARBA00004434}; Single-pass membrane
CC protein {ECO:0000256|ARBA:ARBA00004434}. Mitochondrion membrane
CC {ECO:0000256|ARBA:ARBA00004325}.
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:KRY09117.1}.
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DR EMBL; JYDQ01000290; KRY09117.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0Z9T2; -.
DR Proteomes; UP000054783; Unassembled WGS sequence.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
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; IPR045063; Dynamin_N.
DR InterPro; IPR030381; G_DYNAMIN_dom.
DR InterPro; IPR045817; OPA1_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11566; DYNAMIN; 1.
DR PANTHER; PTHR11566:SF67; DYNAMIN-LIKE 120 KDA PROTEIN, MITOCHONDRIAL; 1.
DR Pfam; PF00350; Dynamin_N; 1.
DR Pfam; PF19434; OPA1_C; 1.
DR PRINTS; PR00195; DYNAMIN.
DR SMART; SM00053; DYNc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51718; G_DYNAMIN_2; 1.
PE 4: Predicted;
KW Apoptosis {ECO:0000256|ARBA:ARBA00022703};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792};
KW Reference proteome {ECO:0000313|Proteomes:UP000054783};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..963
FT /note="Dynamin-like 120 kDa protein, mitochondrial"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006873532"
FT DOMAIN 271..547
FT /note="Dynamin-type G"
FT /evidence="ECO:0000259|PROSITE:PS51718"
FT COILED 205..239
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 963 AA; 110522 MW; 345FF74F2375764F CRC64;
MRRIYCLFMR HVFLVSALRK SSPCFNVSSS RRGYVICRHS SLNRQVFEIM SLLKVNVPLS
VAPYGIRNFS LITRLVKGIM HIRYVVIGTI VGGGLTLSQH VQSWMDKLPD LSWINMDSTL
VAQLKDSFRT VADTVTTQKM LLYKKMEDTG WLPKQVKRDL LEWFEDKKTV LTDTPLLSLI
TDPAVFVYAE ESPSDEAKEA HERGRNDTLQ TEMKFQEKIE QLEKENAELR RVLQSQSGKD
VKLRKGNESL IDMYSSVLDL LIDYDSSYST QDHLPRVVVV GDQSSGKTSV LEMIAQARIF
PRGSGEMMTR APVKVTLSDG PYHIAQFRDS QREFDLTSEK ELAELRREIE LRMLNSVKGG
KTVSNEVIGL SVKGPGLPRM VLVDLPGVIS TVTTGMAADT KEDILKICKT YLENPNAIIL
CIQDGSVDAE RSNVTELVSS VDPAGKRTIL VLTKVDLAEE NLTNPDMIKK ILQGELFPMK
ALGYFAVVTG KGNSGDSIDV IRNYEESFFA KSQLFQGSIL PPSQLTTKNM SLAVSKCFWK
MVKESIGQQA DSFKAVRFNL ETEWKNRFPK LRDIDRDELY ARAKTEILDE LVQLNATSTA
EWETALREKL WETMSSYVFE NILISAFVGD KPHTFNTTVD IKLKHWADTQ LPRKCVEAGW
AVLREQFTRL NVSKKHQPED GWSSCYKPLK EAVIEKALNS HTWNKRALES LRIIQQNALE
DRTVPSKACW KDAILFMEDK IKLRLKELEK HSLHDSKTAR WFRWSSPSED ELKIQAIADH
LKPLLHNISS RNPFIDSDEM IMIRRNVRNS GFEVGEDEVR ETWHQLYRVW FLRKSLLTAN
ECQSMFLHHQ KGFDEVGDCS SVVLFWRVQR MLHITANALR QQIVSTEVRY LEKEIKEMLN
EWSHDSQMKR QYLQGAQVEL AEKLKQVRVI QEKIEDFIAM LNNESKRSTH CKGCYCIKFP
VKY
//
