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Database: UniProt
Entry: A0A158NN27_ATTCE
LinkDB: A0A158NN27_ATTCE
Original site: A0A158NN27_ATTCE 
ID   A0A158NN27_ATTCE        Unreviewed;       976 AA.
AC   A0A158NN27;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 31.
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=105622112 {ECO:0000313|EnsemblMetazoa:XP_012058935.1};
OS   Atta cephalotes (Leafcutter ant).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Myrmicinae; Atta.
OX   NCBI_TaxID=12957 {ECO:0000313|EnsemblMetazoa:XP_012058935.1, ECO:0000313|Proteomes:UP000005205};
RN   [1] {ECO:0000313|Proteomes:UP000005205}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21347285; DOI=10.1371/journal.pgen.1002007;
RA   Suen G., Teiling C., Li L., Holt C., Abouheif E., Bornberg-Bauer E.,
RA   Bouffard P., Caldera E.J., Cash E., Cavanaugh A., Denas O., Elhaik E.,
RA   Fave M.J., Gadau J., Gibson J.D., Graur D., Grubbs K.J., Hagen D.E.,
RA   Harkins T.T., Helmkampf M., Hu H., Johnson B.R., Kim J., Marsh S.E.,
RA   Moeller J.A., Munoz-Torres M.C., Murphy M.C., Naughton M.C., Nigam S.,
RA   Overson R., Rajakumar R., Reese J.T., Scott J.J., Smith C.R., Tao S.,
RA   Tsutsui N.D., Viljakainen L., Wissler L., Yandell M.D., Zimmer F.,
RA   Taylor J., Slater S.C., Clifton S.W., Warren W.C., Elsik C.G., Smith C.D.,
RA   Weinstock G.M., Gerardo N.M., Currie C.R.;
RT   "The genome sequence of the leaf-cutter ant Atta cephalotes reveals
RT   insights into its obligate symbiotic lifestyle.";
RL   PLoS Genet. 7:e1002007-e1002007(2011).
RN   [2] {ECO:0000313|EnsemblMetazoa:XP_012058935.1}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (APR-2016) to UniProtKB.
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}.
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DR   EMBL; ADTU01020949; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_012058935.1; XM_012203545.1.
DR   AlphaFoldDB; A0A158NN27; -.
DR   EnsemblMetazoa; XM_012203545.1; XP_012058935.1; LOC105622112.
DR   GeneID; 105622112; -.
DR   OrthoDB; 48011at2759; -.
DR   Proteomes; UP000005205; 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:UP000005205};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          301..577
FT                   /note="Dynamin-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51718"
FT   COILED          217..269
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          912..975
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   976 AA;  113933 MW;  8530FE6838C1E7B0 CRC64;
     MEQIICGKFG HSILLVSKTS RYPITIITTR KLSGKFSRHC KPLLASPQLR YFANPYRGYA
     MVIAKILRGA LKIRYLLLGS AVGGGITLQK KYEQWREGLP DLEWLENLMP NEKQWQDFRK
     SLMTIRSNVA DKIEIDPRIK EFGVIKYREY RTWFDQRLDD AIKAAESHQN SYQENNSMQS
     AFDIISMIAK QSYSETKEQL SKNVVAFARP LASDNNTEEE RKKAQSSQQR MDAMQDELMQ
     IQLKYQREIE RLERENKELR KQILLRGNQK FTNKKIKKSL IDMYSDVLDE LSDYDSAYST
     ADHLPRVVVV GDQSSGKTSV LEMIAQARIF PRGGGEMMTR APVKVTLSEG PYHIAQFKDS
     SREFDLTKES ELTELRREVE LRMKNSVKNG KTVSPDVISM TVKGPGLQRM VLVDLPGIIS
     TVTVDMAEDT REAIRQMSQQ YMSNPNAIIL CIQDGSVDAE RSNVTDLVAQ MDPSGKRTIF
     VLTKVDMAEE NLTNPERLRK ILSGKLFPMK ALGYFAVVTG RGRQDDSIQT IKDYEEKFFR
     NSKLFKDGLA MSGQVTTKNL SLAVAECFWK MVRETVEQQA DAFKATRFNL ETEWKNNFPR
     LRELDRDELF EKARGEILDE IVNLSQVSPR HWEEVLMSRN WDKVSMHVFE NIYLPAAQSG
     SPNTFNTTVD IKLRHWTEQQ LPARSVESGW ECLQQEFQNF MSQARLSPDH DDIFDNLKNA
     VVNEAMRRHS WEEKASEMLR VIQLNILEDR SVNDKREWDQ AVRFLETSVK EKLQSTEQIL
     HNMLGPNRKE RWMYWQNQSE EQQKRTAVKN ELDKILYADK KHAPTLTHDE LTAVRKNLQR
     NGLEVDNEFI RETWHPVYRR FFLQQSLARA YDCRKGYYLY HTGHENEMEC NDVVLFWRIQ
     QMLKVTSNAL RQQIMNREAR RLDKEIKEVL EDYSQDNEIK EKLLTGRRVT LAEELKRVRQ
     IQEKLEEFIQ ALNKEK
//
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