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Database: UniProt
Entry: A0A3P9Q377_POERE
LinkDB: A0A3P9Q377_POERE
Original site: A0A3P9Q377_POERE 
ID   A0A3P9Q377_POERE        Unreviewed;       682 AA.
AC   A0A3P9Q377;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Caseinolytic mitochondrial matrix peptidase chaperone subunit B {ECO:0000313|Ensembl:ENSPREP00000028464.1};
GN   Name=CLPB {ECO:0000313|Ensembl:ENSPREP00000028464.1};
OS   Poecilia reticulata (Guppy) (Acanthophacelus reticulatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Poecilia.
OX   NCBI_TaxID=8081 {ECO:0000313|Ensembl:ENSPREP00000028464.1, ECO:0000313|Proteomes:UP000242638};
RN   [1] {ECO:0000313|Proteomes:UP000242638}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Guanapo {ECO:0000313|Proteomes:UP000242638};
RA   Kuenstner A., Dreyer C.;
RT   "The genomic landscape of the Guanapo guppy.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSPREP00000028464.1}
RP   IDENTIFICATION.
RC   STRAIN=Guanapo {ECO:0000313|Ensembl:ENSPREP00000028464.1};
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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DR   AlphaFoldDB; A0A3P9Q377; -.
DR   STRING; 8081.ENSPREP00000028464; -.
DR   Ensembl; ENSPRET00000028777.1; ENSPREP00000028464.1; ENSPREG00000019244.1.
DR   GeneTree; ENSGT00390000012961; -.
DR   OMA; AKERHMI; -.
DR   Proteomes; UP000242638; Unassembled WGS sequence.
DR   Bgee; ENSPREG00000019244; Expressed in head and 1 other cell type or tissue.
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; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
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; PF12796; Ank_2; 1.
DR   Pfam; PF10431; ClpB_D2-small; 1.
DR   PRINTS; PR00300; CLPPROTEASEA.
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; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 1.
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:UP000242638}.
FT   REPEAT          215..247
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   DOMAIN          563..654
FT                   /note="Clp ATPase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01086"
FT   REGION          663..682
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   682 AA;  76679 MW;  BC802BEEA98EE23C CRC64;
     MLSSVPTRLL TRRSRSLSPC GRVLQTSASG ATGQCFRETQ AETNRNPIVS TSRVSRRGIL
     SEETAVTSVN PSVQYHHLAP RWLSNLENRR SSWAALASRG RQNNQYWEDS RQSGGGASRA
     GLASAGVLSA AAVAFCLRKD SDNKGTHALS CRVLNTAHKY TEKFTNIVEI QLTAITGHTH
     SLLYDSLLEA ARTNNAQDVS RLIKEGVDPN HRHRLGWTAL MVAAMNRQHS AVKTLLEAGA
     DPNAGDDFNN VYDTSREKGI HSLEVLVSRE DEFSSRLSSR AGFRGCTALH YATLADDPLA
     VRMLLEAAYY TLISLNTPSY ISFSRREAEE RRRFPLERRL KEYIIGQEGA INTVASAIRR
     KENGWYDEEH PLVFLFLGSS GIGTFFLRHT HLSSTLGFIR MDMSEFQEKH EVAKFIGSPP
     GYIGHEEGGQ LTKLLKACPN AVVLFDEVDK AHPDVLTIML QLFDEGRLTD GKGKTIECKD
     AIFIMTSNVA SEDIAQHALQ LRQEAEEVSR RKLADKLEDV EKSDDIKISR QFKETVIQPI
     LKAHFRRDEF LGRINEIVYF LPFCYSELLQ LVSKELNFWA KKAKQRHDIT LQWDHLVLDL
     LAGGYNLHYG ARSIKHEVER RVVNQLAAAY EQELLPKGCT LRLSVQSEGQ EERSMPRLRL
     EVVGEDSSSR TLDIRPPLNP EH
//
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