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Database: UniProt
Entry: A0A3Q2ZUV0_KRYMA
LinkDB: A0A3Q2ZUV0_KRYMA
Original site: A0A3Q2ZUV0_KRYMA 
ID   A0A3Q2ZUV0_KRYMA        Unreviewed;       677 AA.
AC   A0A3Q2ZUV0;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=Caseinolytic mitochondrial matrix peptidase chaperone subunit B {ECO:0000313|Ensembl:ENSKMAP00000002064.1};
GN   Name=CLPB {ECO:0000313|Ensembl:ENSKMAP00000002064.1};
OS   Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX   NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000002064.1, ECO:0000313|Proteomes:UP000264800};
RN   [1] {ECO:0000313|Ensembl:ENSKMAP00000002064.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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DR   RefSeq; XP_017279422.1; XM_017423933.1.
DR   AlphaFoldDB; A0A3Q2ZUV0; -.
DR   STRING; 37003.ENSKMAP00000002064; -.
DR   Ensembl; ENSKMAT00000002112.1; ENSKMAP00000002064.1; ENSKMAG00000001615.1.
DR   GeneID; 108240452; -.
DR   KEGG; kmr:108240452; -.
DR   CTD; 81570; -.
DR   GeneTree; ENSGT00390000012961; -.
DR   OMA; AKERHMI; -.
DR   OrthoDB; 35211at2759; -.
DR   Proteomes; UP000264800; Unplaced.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   CDD; cd19499; RecA-like_ClpB_Hsp104-like; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 2.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR019489; Clp_ATPase_C.
DR   InterPro; IPR001270; ClpA/B.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR   PANTHER; PTHR11638:SF93; CASEINOLYTIC PEPTIDASE B PROTEIN HOMOLOG; 1.
DR   Pfam; PF07724; AAA_2; 1.
DR   Pfam; PF00023; Ank; 1.
DR   Pfam; PF12796; Ank_2; 1.
DR   Pfam; PF10431; ClpB_D2-small; 1.
DR   PRINTS; PR00300; CLPPROTEASEA.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM00248; ANK; 3.
DR   SMART; SM01086; ClpB_D2-small; 1.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 2.
DR   PROSITE; PS50088; ANK_REPEAT; 2.
PE   4: Predicted;
KW   ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000264800}.
FT   REPEAT          183..215
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          252..284
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   DOMAIN          360..504
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          558..648
FT                   /note="Clp ATPase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01086"
FT   REGION          1..74
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          100..127
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   677 AA;  75340 MW;  94E8203F91C11183 CRC64;
     MLSSVPTRLL TRRSRSLSPC SRVLQTSAGG ATRSQGVRET PAAETNRNPI VSTSRVSRRG
     ILSEETSGSG ANPSVQYHHL APRWLSNLEN RRSSWAALAS RGRHNNQYWE ESGRGEGRGA
     GGGGGRAGVA SAGVLSAAAV AFCLRKDSDN KGDALLEAAR TNNSQDVTRL IKEGVDPNHR
     HRLGWTALMV AAMNRQHSAV KVLLEAGADP NAGDDFNNVY DTSREKGIHS LEVLVSREDE
     FSSRLSSRAG FRGCTALHYA TLADDPHAVR MLLEAGANPL QTNGLGHAPR TYAKEGEVSA
     ALQEWEGKFK ELQARREAEE RRRFPLERRL KEHIIGQEGA INTVASAIRR KENGWYDEEH
     PLVFLFLGSS GIGKTELAKQ VARYMHKDVK KGFIRMDMSE FQEKHEVAKF IGSPPGYVGH
     EEGGQLTKLL RACPNAVVLF DEVDKAHPDV LTIMLQLFDE GRLTDGKGKT IECKDAIFIM
     TSNVASEDIA QHALQLRQEA EEISRRKLAD NLEDVQKSDD VKISRQFKET VIQPILKAHF
     RRDEFLGRIN EIVYFLPFCH SELLQLVSKE LNFWAKKAKQ RHNITLQWDR PVLDLLAGGY
     NLHYGARSIK HEVERRVVNQ LAAAYEQELL PKGCTLRLSV HSEGQEEHGA PSLRLEVLGE
     DSSSRTLDIR PPLNPEH
//
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