ID D8T8Z1_SELML Unreviewed; 984 AA.
AC D8T8Z1;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=AAA+ ATPase domain-containing protein {ECO:0000259|SMART:SM00382};
GN ORFNames=SELMODRAFT_430300 {ECO:0000313|EMBL:EFJ06878.1};
OS Selaginella moellendorffii (Spikemoss).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Lycopodiopsida; Selaginellales; Selaginellaceae; Selaginella.
OX NCBI_TaxID=88036 {ECO:0000313|Proteomes:UP000001514};
RN [1] {ECO:0000313|EMBL:EFJ06878.1, ECO:0000313|Proteomes:UP000001514}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551031; DOI=10.1126/science.1203810;
RA Banks J.A., Nishiyama T., Hasebe M., Bowman J.L., Gribskov M.,
RA dePamphilis C., Albert V.A., Aono N., Aoyama T., Ambrose B.A., Ashton N.W.,
RA Axtell M.J., Barker E., Barker M.S., Bennetzen J.L., Bonawitz N.D.,
RA Chapple C., Cheng C., Correa L.G., Dacre M., DeBarry J., Dreyer I.,
RA Elias M., Engstrom E.M., Estelle M., Feng L., Finet C., Floyd S.K.,
RA Frommer W.B., Fujita T., Gramzow L., Gutensohn M., Harholt J., Hattori M.,
RA Heyl A., Hirai T., Hiwatashi Y., Ishikawa M., Iwata M., Karol K.G.,
RA Koehler B., Kolukisaoglu U., Kubo M., Kurata T., Lalonde S., Li K., Li Y.,
RA Litt A., Lyons E., Manning G., Maruyama T., Michael T.P., Mikami K.,
RA Miyazaki S., Morinaga S., Murata T., Mueller-Roeber B., Nelson D.R.,
RA Obara M., Oguri Y., Olmstead R.G., Onodera N., Petersen B.L., Pils B.,
RA Prigge M., Rensing S.A., Riano-Pachon D.M., Roberts A.W., Sato Y.,
RA Scheller H.V., Schulz B., Schulz C., Shakirov E.V., Shibagaki N.,
RA Shinohara N., Shippen D.E., Soerensen I., Sotooka R., Sugimoto N.,
RA Sugita M., Sumikawa N., Tanurdzic M., Theissen G., Ulvskov P., Wakazuki S.,
RA Weng J.K., Willats W.W., Wipf D., Wolf P.G., Yang L., Zimmer A.D., Zhu Q.,
RA Mitros T., Hellsten U., Loque D., Otillar R., Salamov A., Schmutz J.,
RA Shapiro H., Lindquist E., Lucas S., Rokhsar D., Grigoriev I.V.;
RT "The Selaginella genome identifies genetic changes associated with the
RT evolution of vascular plants.";
RL Science 332:960-963(2011).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: In the C-terminal section; belongs to the peptidase M41
CC family. {ECO:0000256|ARBA:ARBA00010044}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the AAA ATPase
CC family. {ECO:0000256|ARBA:ARBA00010550}.
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DR EMBL; GL377692; EFJ06878.1; -; Genomic_DNA.
DR RefSeq; XP_002992029.1; XM_002991983.1.
DR AlphaFoldDB; D8T8Z1; -.
DR STRING; 88036.D8T8Z1; -.
DR MEROPS; M41.A06; -.
DR EnsemblPlants; EFJ06878; EFJ06878; SELMODRAFT_430300.
DR Gramene; EFJ06878; EFJ06878; SELMODRAFT_430300.
DR KEGG; smo:SELMODRAFT_430300; -.
DR eggNOG; KOG0731; Eukaryota.
DR HOGENOM; CLU_000688_16_0_1; -.
DR InParanoid; D8T8Z1; -.
DR OMA; WRKTMPK; -.
DR Proteomes; UP000001514; Unassembled WGS sequence.
DR GO; GO:0005745; C:m-AAA complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR GO; GO:0034982; P:mitochondrial protein processing; IBA:GO_Central.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.20.58.760; Peptidase M41; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000642; Peptidase_M41.
DR InterPro; IPR037219; Peptidase_M41-like.
DR PANTHER; PTHR43655; ATP-DEPENDENT PROTEASE; 1.
DR PANTHER; PTHR43655:SF19; ATP-DEPENDENT ZINC METALLOPROTEASE FTSH 12, CHLOROPLASTIC; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF01434; Peptidase_M41; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF140990; FtsH protease domain-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000001514};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 159..180
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 509..644
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 48..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 984 AA; 112077 MW; C46418A316742188 CRC64;
MQALGYGASH SRASPRFHLP APVLGRPCGT DFVDRSFGSD VQRINAGSRS RFRARPSAQL
SSDDQSVPEG SSNRRLRAAL SRYYRNFVQD LKAEAGVDVE NIKEVVTARY KELRENASHV
FDRAASTAQD ARGRLEVARN EGDELLEDFR LKKLDAQHIG ALVLYLLLVI GSFRGLYVAA
TTPRLSKREA KELTEAYLEA TIPEPTLENV RKLEKFQWRE NMPGGVRVRK HLLQPDGSYR
HDPSFVGEHA WDDDSNEAAA AQELNKGAED TGTNEKLTWR ERLTKLEDML EKESIKEDTD
ALTSKYVVLL DSEEMAKDIA EKKEEPVIPP QYGRGFWAAR RWWKYRPKMP YFDFFEKVER
MEVQSAVFSQ DRTRLFVTMK EGFPSEFVVD APADPYLNDA LQRFQVEVDT IPESGLRNIL
RAYAILLPCF FIALKLDNTI FNIRRNASEK IVDLIKMKSS SIVLPEQAEE AGFPSFDDVI
VSHTVWRVVE EIGNYLSDPM RYYDKFCFIP RGILIHGPPG TGKTHIARAM ARELQLPFIF
ASGSEFGDSE IPGPKKVSQA PSIVFIDEID ALAGKQVDED PRRLKTFKQL IKELDGLEID
TEVHRFAPRQ AFILICATNR RDDLHEAFLQ RQRIDREIHV GLPKEAERLR IFKVHTAKYK
LADDVDFEKV VYRTRGFSGA DLKNFANEIF VYAKQKGRAY IQQSDLLDVL EKQLFEGIGM
TVTQEQQKES ELKVKAETKR LLAAHEAGHV LLAHLFPRFD WHAFTHLLPG GAESSLSVFY
PSEDMLEYGG TIGYFEAQMI VAHGGRGAEI LLLGDNITDG WTDDLEKISA LARECAVHPE
NRNLGLLQVA RKPLPPRPRP RPEELYPMTW NHPRSIVIPM TLEVSELVGR EIQMFIDDTE
KMAMKALQNN RHILERLARE LELNIKMTGD EIKDIVHSMN PVLLPDIGGP PDFSKAVPID
PTPEEIRDGY YRDLDVYADR LHRC
//