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Database: UniProt
Entry: D8T8Z1_SELML
LinkDB: D8T8Z1_SELML
Original site: D8T8Z1_SELML 
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
//
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