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
//