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Database: UniProt
Entry: A0A401NSZ6_SCYTO
LinkDB: A0A401NSZ6_SCYTO
Original site: A0A401NSZ6_SCYTO 
ID   A0A401NSZ6_SCYTO        Unreviewed;       632 AA.
AC   A0A401NSZ6;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   RecName: Full=ClpX-type ZB domain-containing protein {ECO:0000259|PROSITE:PS51902};
GN   ORFNames=scyTo_0011693 {ECO:0000313|EMBL:GCB64006.1};
OS   Scyliorhinus torazame (Cloudy catshark).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC   Elasmobranchii; Galeomorphii; Galeoidea; Carcharhiniformes; Scyliorhinidae;
OC   Scyliorhinus.
OX   NCBI_TaxID=75743 {ECO:0000313|EMBL:GCB64006.1, ECO:0000313|Proteomes:UP000288216};
RN   [1] {ECO:0000313|EMBL:GCB64006.1, ECO:0000313|Proteomes:UP000288216}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=30297745; DOI=.1038/s41559-018-0673-5;
RA   Hara Y, Yamaguchi K, Onimaru K, Kadota M, Koyanagi M, Keeley SD, Tatsumi K,
RA   Tanaka K, Motone F, Kageyama Y, Nozu R, Adachi N, Nishimura O, Nakagawa R,
RA   Tanegashima C, Kiyatake I, Matsumoto R, Murakumo K, Nishida K, Terakita A,
RA   Kuratani S, Sato K, Hyodo S Kuraku.S.;
RT   "Shark genomes provide insights into elasmobranch evolution and the origin
RT   of vertebrates.";
RL   Nat. Ecol. Evol. 2:1761-1771(2018).
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:GCB64006.1}.
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DR   EMBL; BFAA01005411; GCB64006.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A401NSZ6; -.
DR   STRING; 75743.A0A401NSZ6; -.
DR   OMA; LDKTHLM; -.
DR   Proteomes; UP000288216; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd19497; RecA-like_ClpX; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR019489; Clp_ATPase_C.
DR   InterPro; IPR004487; Clp_protease_ATP-bd_su_ClpX.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR010603; Znf_CppX_C4.
DR   NCBIfam; TIGR00382; clpX; 1.
DR   PANTHER; PTHR48102:SF7; ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPX-LIKE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR48102; ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPX-LIKE, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF07724; AAA_2; 1.
DR   Pfam; PF10431; ClpB_D2-small; 1.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM01086; ClpB_D2-small; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51902; CLPX_ZB; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000288216};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          92..145
FT                   /note="ClpX-type ZB"
FT                   /evidence="ECO:0000259|PROSITE:PS51902"
FT   REGION          67..100
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          597..632
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        78..97
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        606..632
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   632 AA;  69273 MW;  A4361CAB1FEF3AA6 CRC64;
     MSCVVVMCTC SSAARLLRSS ITGLGFASAR FHFPLLAHSA SFETQGGRKI PCRTFCETIT
     LLASKEGGTK DTSGDSNKKS VSEGSTKRAS GSGGSGKGGN QLRCPKCGDP CTHVETFVSS
     TRFVKCEKCH HFFVVLSEAD SKKSLNKEPE SAAEAVKLAF QQKPPPPPKK IYSYLDKYVV
     GQSYAKKVLS VAVYNHYKRI YNNIPTSLRQ QTEVEKQASL TPRELEIRRR EDEYRFTKLL
     QIAGISPHGN ALGASMQQQA SQSIPQEKRG GEVLDSTHDD IKLEKSNILL LGPTGSGKTL
     LAQTLARCLE VPFAICDCTT LTQAGYVGED IESVVAKLLQ DANYNVDKAQ QGIVFLDEVD
     KIGSVPGIHQ LRDVGGEGVQ QGLLKLLEGT IVNVPEKNSR KLRGETVQVD TTNILFVASG
     AFNGLDRIIS RRKNEKYLGF GTPSNLGKGR RAAAAADLAN TSGDNNTVQE LEEKDRLLRH
     VEARDLIEFG MIPEFVGRLP VIVPLHSLNE DTLVRILTEP RNAVIPQYQA LFSMDKCDLN
     VSEDALRAIA RLALERKTGA RGLRSIMEKL LLEPMFEVPN SDIVAVEVDK DIVDGKKPPA
     YIRAPSKEPV EEEYDSGVED DRWHRQADAA NN
//
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