ID S7NTD6_MYOBR Unreviewed; 572 AA.
AC S7NTD6;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE RecName: Full=microtubule-severing ATPase {ECO:0000256|ARBA:ARBA00038871};
DE EC=5.6.1.1 {ECO:0000256|ARBA:ARBA00038871};
DE AltName: Full=60S ribosomal protein L21 {ECO:0000256|ARBA:ARBA00035327};
GN ORFNames=D623_10019013 {ECO:0000313|EMBL:EPQ20130.1};
OS Myotis brandtii (Brandt's bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=109478 {ECO:0000313|EMBL:EPQ20130.1, ECO:0000313|Proteomes:UP000052978};
RN [1] {ECO:0000313|Proteomes:UP000052978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23962925; DOI=10.1038/ncomms3212;
RA Seim I., Fang X., Xiong Z., Lobanov A.V., Huang Z., Ma S., Feng Y.,
RA Turanov A.A., Zhu Y., Lenz T.L., Gerashchenko M.V., Fan D., Hee Yim S.,
RA Yao X., Jordan D., Xiong Y., Ma Y., Lyapunov A.N., Chen G., Kulakova O.I.,
RA Sun Y., Lee S.G., Bronson R.T., Moskalev A.A., Sunyaev S.R., Zhang G.,
RA Krogh A., Wang J., Gladyshev V.N.;
RT "Genome analysis reveals insights into physiology and longevity of the
RT Brandt's bat Myotis brandtii.";
RL Nat. Commun. 4:2212-2212(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=n ATP + n H2O + a microtubule = n ADP + n phosphate + (n+1)
CC alpha/beta tubulin heterodimers.; EC=5.6.1.1;
CC Evidence={ECO:0000256|ARBA:ARBA00036378};
CC -!- SIMILARITY: Belongs to the AAA ATPase family.
CC {ECO:0000256|ARBA:ARBA00006914, ECO:0000256|RuleBase:RU003651}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL21 family.
CC {ECO:0000256|ARBA:ARBA00008427}.
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DR EMBL; KE164790; EPQ20130.1; -; Genomic_DNA.
DR AlphaFoldDB; S7NTD6; -.
DR eggNOG; KOG0740; Eukaryota.
DR Proteomes; UP000052978; Unassembled WGS sequence.
DR GO; GO:0031090; C:organelle membrane; IEA:UniProt.
DR GO; GO:0005840; C:ribosome; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006412; P:translation; IEA:InterPro.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 1.20.58.80; Phosphotransferase system, lactose/cellobiose-type IIA subunit; 1.
DR Gene3D; 2.30.30.70; Ribosomal protein L21; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR007330; MIT_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001147; Ribosomal_eL21.
DR InterPro; IPR036948; Ribosomal_eL21_sf.
DR InterPro; IPR015415; Spast_Vps4_C.
DR InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR PANTHER; PTHR23074; AAA DOMAIN-CONTAINING; 1.
DR PANTHER; PTHR23074:SF86; SPASTIN; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF01157; Ribosomal_L21e; 1.
DR Pfam; PF09336; Vps4_C; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00745; MIT; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50104; Translation proteins SH3-like domain; 1.
DR PROSITE; PS00674; AAA; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU003651};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU003651};
KW Reference proteome {ECO:0000313|Proteomes:UP000052978}.
FT DOMAIN 105..174
FT /note="MIT"
FT /evidence="ECO:0000259|SMART:SM00745"
FT DOMAIN 354..466
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 195..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..209
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..236
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..285
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 572 AA; 63814 MW; 3774284F0EEE47E5 CRC64;
MTNTKGKRRG TRYMHFRKHG VVPLATYMRI YKKGDIVDIK GMGTVQKGMP QKCYHGKTES
VYNVTQHAVG IIVNKQVKGK VLAKRILHIE HIKHSMSRHS FLKRVKENDQ KKKEAKEKAG
QKEQAMEWYK KGIEELEKGI AVIVTGQGEQ CERARRLQAK MMTNLVMAKD RLQLLEKLQP
VLQFSKSQTD VYNDSTNLTC RNGQLQSESG AVPKRKDPLT HPSNSLPRSK TVMKAGSTGL
SGHHRAPSCS GLSMVSGVRQ GPGPATATHK STPKTNRTNK PSTPTTAARK KKDLKNFRNV
DSNLANLIMN EIVDNGTAVK FDDVAGQELA KQALQEIVIL PSLRPELFTG LRAPARGLLL
FGPPGNGKTM LVGEGEKLVR ALFAVARELQ PSIIFIDEVD SLLCERREGE HDASRCLKTE
FLIEFDGVQS AGDERVLVMG ATNRPQELDE AVLRRFTKRV YVSLPNEETR RLLLKNLLCK
QGSPLTQKEL AQLARMTDGY SGSDLTALAK DAALGPIREL KPEQVKNMSA NEMRNIRLSD
FTESLKKIKR SVGPQTLEAY IRWNKDFGDT TV
//