ID A0A2K5JXT0_COLAP Unreviewed; 791 AA.
AC A0A2K5JXT0;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=AAA+ ATPase domain-containing protein {ECO:0000259|SMART:SM00382};
OS Colobus angolensis palliatus (Peters' Angolan colobus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Colobus.
OX NCBI_TaxID=336983 {ECO:0000313|Ensembl:ENSCANP00000033607.1, ECO:0000313|Proteomes:UP000233080};
RN [1] {ECO:0000313|Ensembl:ENSCANP00000033607.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: In the C-terminal section; belongs to the peptidase M41
CC family. {ECO:0000256|ARBA:ARBA00010044}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the AAA ATPase
CC family. {ECO:0000256|ARBA:ARBA00010550}.
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DR AlphaFoldDB; A0A2K5JXT0; -.
DR STRING; 336983.ENSCANP00000033607; -.
DR Ensembl; ENSCANT00000056834.1; ENSCANP00000033607.1; ENSCANG00000040423.1.
DR Proteomes; UP000233080; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016043; P:cellular component organization; IEA:UniProt.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd19501; RecA-like_FtsH; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 3.40.1690.20; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.20.58.760; Peptidase M41; 1.
DR HAMAP; MF_01458; FtsH; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR005936; FtsH.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011546; Pept_M41_FtsH_extracell.
DR InterPro; IPR000642; Peptidase_M41.
DR InterPro; IPR037219; Peptidase_M41-like.
DR NCBIfam; TIGR01241; FtsH_fam; 1.
DR PANTHER; PTHR43655:SF9; AFG3-LIKE PROTEIN 2; 1.
DR PANTHER; PTHR43655; ATP-DEPENDENT PROTEASE; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF06480; FtsH_ext; 1.
DR Pfam; PF01434; Peptidase_M41; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF140990; FtsH protease domain-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00674; AAA; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000233080};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 140..157
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 247..265
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 334..473
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 69..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 753..791
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..95
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 765..791
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 791 AA; 87874 MW; A2C15BC0752DC0F8 CRC64;
MTFFPMCLCL GVGTGSDFPL DTPLLDSTWA GLYRFVTTQT KASRNSLLTD VIAAYQRFCS
RPPKGFEKYF PNGKNGEKAS EPKEVMGEKK ESKPAATTRS SGGGGGGGGG KRGGKKDDSH
WWSRFQKGDF PWDDKDFRMF FLWTSLFWGG VMFYFLLKRS GREITWKDFV NNYLSKGVVD
RLEVVNKRFV RVTFTPGKTP VDGQYVWFNI GSVDTFERNL ETLQQELGIE GENRVPVVYI
AESDGSFLLS MLPTVLIIAF LLYTIRRGPA GIGRTGRGMG GLFSVGETTA KVLKDEIDVK
FKDVAGCEEA KLEIMEFVNF LKNPKQYQDL GAKIPKGAIL TGPPGTGKTL LAKATAGEAN
VPFITVSGSE FLEMFVGVGP ARVRDLFALA RKNAPCILFI DEIDAVGRKR GRGNFGGQSE
QENTLNQLLV EMDGFNTTTN VVILAGTNRP DILDPALLRP GRFDRQIFIG PPDIKGRASI
FKVHLRPLKL DSTLEKDKLA RKLASLTPGF SGADVANVCN EAALIAARHL SDSINQKHFE
QAIERVIGGL EKKTQVLQPE EKKTVAYHEA GHAVAGWYLE HADPLLKVSI IPRGKGLGYA
QYLPKEQYLY TKEQLLDRMC MTLGGRVSEE IFFGRITTGA QDDLRKVTQS AYAQIVQFGM
NEKVGQISFD LPRQGDMVLE KPYSEATARL IDDEVRILIH DAYKRTVALL TEKKADVEKV
ALLLLEKEVL DKNDMVELLG PRPFAEKSTY EEFVEGTGSL DEDTSLPEGL KDWNKEREKE
KEEPPGEKVA N
//
