ID A0A3N2PY20_9PEZI Unreviewed; 963 AA.
AC A0A3N2PY20;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Paraplegin {ECO:0000313|EMBL:ROT39245.1};
GN ORFNames=SODALDRAFT_294602 {ECO:0000313|EMBL:ROT39245.1};
OS Sodiomyces alkalinus F11.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Sodiomyces.
OX NCBI_TaxID=1314773 {ECO:0000313|EMBL:ROT39245.1, ECO:0000313|Proteomes:UP000272025};
RN [1] {ECO:0000313|EMBL:ROT39245.1, ECO:0000313|Proteomes:UP000272025}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F11 {ECO:0000313|EMBL:ROT39245.1,
RC ECO:0000313|Proteomes:UP000272025};
RX PubMed=30368956; DOI=10.1111/mec.14912;
RA Grum-Grzhimaylo A.A., Falkoski D.L., van den Heuvel J.,
RA Valero-Jimenez C.A., Min B., Choi I.G., Lipzen A., Daum C.G., Aanen D.K.,
RA Tsang A., Henrissat B., Bilanenko E.N., de Vries R.P., van Kan J.A.L.,
RA Grigoriev I.V., Debets A.J.M.;
RT "The obligate alkalophilic soda-lake fungus Sodiomyces alkalinus has
RT shifted to a protein diet.";
RL Mol. Ecol. 27:4808-4819(2018).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ML119054; ROT39245.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N2PY20; -.
DR STRING; 1314773.A0A3N2PY20; -.
DR OrthoDB; 9585at2759; -.
DR Proteomes; UP000272025; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
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: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; ATP-DEPENDENT PROTEASE; 1.
DR PANTHER; PTHR43655:SF2; SD01613P; 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 Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000272025}.
FT DOMAIN 493..634
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 38..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 206..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 905..963
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..245
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 930..944
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 963 AA; 106071 MW; 046A9B52014F4AD3 CRC64;
MARILRQSAQ LARIARQSQQ LALGRSLSST SRLARLAPLT ARHLPQSPSR SSPSSLRFYS
TEDPNKNKPS DEKESSSNNS SSSSKNNNNN NNNSVPEESS DGQTELEKTR KEFPLPDGWV
HFTEEELERF RQFGALKGLP QFMKDDLNRT VNAIRVVGAP DELRELARRH PNGNLTIGEM
GRVIRILTKM TKRLAEYEVT MHRRALGRDK DAVKSKEQDP QGAKEPRPEE QEQEKEERHE
EQTKKAGGPA AGQAGGAGSG KGGDGKNKGG KESGGPQDGG NPFGKKWFLG RFSTGDLIMA
AVVWALIIPY AEATFFGQSK EITWQEVHKD FLSKGLVKKL TVYNTGKVRV ELHQDAPSAG
GLDPNVQYFF SIGSVDSFQK QLEEAQNQLG IPLQDRIPVN YATEGGMWPI IMAFGPTLLL
VGLLMYTTRS LGGRGGNQMF GFGKSKAKMF NHESAVKVKF SDVAGMDEAK AEIMEFVSFL
KTPERFERLG AKIPRGAILS GPPGTGKTLL AKATAGESGV PFFSVSGSEF VEMFVGVGSS
RVRDLFASAR KNAPCIIFID EIDAIGRSRQ DGSRPGGSND ERESTLNQIL TEMDGFNTSE
QIVVLAGTNR ADILDQALLR PGRFDRHIYI DRPTMKGRQD IFKVHLKKIV TKEDQEHLVG
RLSTLTPGFS GADIANVVNE AALAAARVNA ESVELIHFEQ AIERVIGGLE RKSLVLKPQE
KRTVAYHEAG HAICGWYFEN ADPLLKVSII PRGKGALGYA QYLPSGDAYL MTVEQLMDRM
AMTLGGRISE ELHFPTVTTG ASDDFRKVTQ MARKMVTEWG MSDKVGPMHF SEDPHQLQKP
FSETTAQAID AEVRRIVDQA YAQCRELLLA KKHEVGLVAE ELLKKEMLTR DDMVRLLGKR
PFPDHQDFEK YFGGEDGLKK PDGSGGQGQK SAPPPPPAED AGSPPKEQPS PAFKEVRGRD
ELR
//
