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Database: UniProt
Entry: A0A176VZ33_MARPO
LinkDB: A0A176VZ33_MARPO
Original site: A0A176VZ33_MARPO 
ID   A0A176VZ33_MARPO        Unreviewed;       913 AA.
AC   A0A176VZ33;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Clp R domain-containing protein {ECO:0000259|PROSITE:PS51903};
GN   ORFNames=AXG93_4368s1120 {ECO:0000313|EMBL:OAE25653.1};
OS   Marchantia polymorpha subsp. ruderalis.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC   Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX   NCBI_TaxID=1480154 {ECO:0000313|EMBL:OAE25653.1, ECO:0000313|Proteomes:UP000077202};
RN   [1] {ECO:0000313|EMBL:OAE25653.1, ECO:0000313|Proteomes:UP000077202}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Tak-1 and cv. Tak-2 {ECO:0000313|Proteomes:UP000077202};
RC   TISSUE=Whole gametophyte {ECO:0000313|EMBL:OAE25653.1};
RA   Honkanen S., Jones V.A., Morieri G., Champion C., Hetherington A.J.,
RA   Kelly S., Saint-Marcoux D., Proust H., Prescott H., Dolan L.;
RT   "Mechanisms controlling the formation of the plant cell surface in tip-
RT   growing cells are functionally conserved among land plants.";
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC       {ECO:0000256|RuleBase:RU004432}.
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:OAE25653.1}.
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DR   EMBL; LVLJ01002295; OAE25653.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A176VZ33; -.
DR   OrthoDB; 35211at2759; -.
DR   Proteomes; UP000077202; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   CDD; cd00009; AAA; 1.
DR   CDD; cd19499; RecA-like_ClpB_Hsp104-like; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 1.10.1780.10; Clp, N-terminal domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR019489; Clp_ATPase_C.
DR   InterPro; IPR036628; Clp_N_dom_sf.
DR   InterPro; IPR004176; Clp_R_dom.
DR   InterPro; IPR001270; ClpA/B.
DR   InterPro; IPR018368; ClpA/B_CS1.
DR   InterPro; IPR028299; ClpA/B_CS2.
DR   InterPro; IPR041546; ClpA/ClpB_AAA_lid.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR   PANTHER; PTHR11638:SF190; CLP R DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF07724; AAA_2; 1.
DR   Pfam; PF17871; AAA_lid_9; 1.
DR   Pfam; PF02861; Clp_N; 2.
DR   Pfam; PF10431; ClpB_D2-small; 1.
DR   PRINTS; PR00300; CLPPROTEASEA.
DR   SMART; SM00382; AAA; 2.
DR   SMART; SM01086; ClpB_D2-small; 1.
DR   SUPFAM; SSF81923; Double Clp-N motif; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS51903; CLP_R; 1.
DR   PROSITE; PS00870; CLPAB_1; 1.
DR   PROSITE; PS00871; CLPAB_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004432};
KW   Chaperone {ECO:0000256|RuleBase:RU004432};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077202};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          3..147
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          413..500
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   913 AA;  101218 MW;  A47C9170612CD073 CRC64;
     MNPERFTHKT NEALAAGQEI AINAGHAQYT PLHLAVALLQ DPDGLFSQAV SAARGDGAVS
     SVERAFNQAL KKIPSQSPAP DEVPANSALV KCIRKAQSLQ KKRGDSHLSI DQIILAVLDD
     SQISDCLQEA GVQAAKVKQE LEKVRGGEGK KVDNATGDTN FQALKKYGRD LVEQAGKLDP
     VIGRDEEIRR VIRVLSRRTK NNPVLIGEPG VGKTAVVEGL AQRVVRGDVP SNLLDVRLIA
     LDMGALIAGA KYRGEFEERL KAVLKEVEDA DGKVILFIDE IHLVLGAGRT EGSMDAANLL
     KPMLARGQLR CIGATTLDEY RSYVEKDAAF ERRFQQVFVP EPSVPDTISI LRGLKEKYEG
     HHGVRILDKS LVVAAQLSSR YITGRHLPDK AIDLVDEACA NVRVQLDSQP EEVDALERRR
     IQLEVELHAL EKEKDKSSKA RLVEVKQELD DLNEKLRPLK MKYQREKGRV DESRRLKQKR
     EEILRSIQDA ERRMDLARVA DLKYGALQEI EESIAHLDAD IGDNNMLTET VAPDQIAEVV
     SRWTGIPVSR LGQNDKARLL GLADRLHLRV VGQDEAVQAV AEAVLRSRAG LGRPQQPTGS
     FLFLGPTGVG KTELAKALAE QLFDDENQLV RIDMSEYMEQ HSVARLIGAP PGYVGYDKGG
     QLTEAVRRRP YSVILFDEIE KAHPSVFNTL LQLLDDGRLT DGQGRTVNFN NTVIILTSNL
     GAEHLLAGLS GEQTMTVAKD QVLQEVRRHF RPELLNRLDE MVVFSPLSHE QLRKVCRIQM
     KDVAMRLAER GVALAVTDAA LDLVLTEAYN PIYGARPLRR WLEKKVVTQL SIMLINDEID
     ENSTVYIDCK PGARVLTYRV EKNGGFVNSE TGAKADVLIS VPAPKINSSP HHQVKKMKIE
     EPMMDDDDDE MAD
//
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