ID E5R042_ARTGP Unreviewed; 906 AA.
AC E5R042;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Paraplegin {ECO:0000313|EMBL:EFQ97453.1};
GN ORFNames=MGYG_00494 {ECO:0000313|EMBL:EFQ97453.1};
OS Arthroderma gypseum (strain ATCC MYA-4604 / CBS 118893) (Microsporum
OS gypseum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Nannizzia.
OX NCBI_TaxID=535722 {ECO:0000313|Proteomes:UP000002669};
RN [1] {ECO:0000313|Proteomes:UP000002669}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4604 / CBS 118893 {ECO:0000313|Proteomes:UP000002669};
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
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 EMBL; DS989822; EFQ97453.1; -; Genomic_DNA.
DR RefSeq; XP_003176405.1; XM_003176357.1.
DR AlphaFoldDB; E5R042; -.
DR STRING; 535722.E5R042; -.
DR MEROPS; M41.003; -.
DR GeneID; 10031722; -.
DR VEuPathDB; FungiDB:MGYG_00494; -.
DR eggNOG; KOG0731; Eukaryota.
DR HOGENOM; CLU_000688_23_4_1; -.
DR InParanoid; E5R042; -.
DR OMA; ARQKGNF; -.
DR OrthoDB; 9585at2759; -.
DR Proteomes; UP000002669; 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:UP000002669}.
FT DOMAIN 450..590
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 51..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 174..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 862..906
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..83
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..233
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 906 AA; 100188 MW; 2A0B4C5A20ED12BB CRC64;
MATLLRRPGG LAQYSRRAAG YTAFSRTPFS ASLPQSRLSA FIVANRSRLY ATSSTGGSEP
PKDKKNGEND IGKHAERPSH GQSGESEGSE PKYALNAEQR EEFDKIVDQL KVSLPKSQAK
LIETAAEVIK REGLPEEVKN ALEEVRESKH ISLSNAAKLV RVLNKHSVKL ASSVNEEYSK
NSPEAQRKEN EASKEEKPKD ESKEGPKQES KEESSNKSEQ QRQRKDDKDQ PKGPQFKIMD
FKFDAGNFLV AAFISYYVYR SVFPGESSRD ITWQEFRNTF FDKGLVEKLT VVNRSKVRVE
LDRDAVAKLY PESPATNLNF HYYFTIGSVE AFERRLDDAH RELNIPSSER IPVAYADEVP
WLATLLSFGP TLLLIGSFFW LSRRAGGAGG GGQSGIFGIG KSRARKFNHE TDVKTKFADV
AGMDEAKVEI MEFVSFLKKP EQFQRLGAKI PRGAILSGPP GTGKTLLAKA TAGESAVPFY
SVSGSEFVEM FVGVGPSRVR DLFATARKNT PCIIFIDEID AIGKSRSKSN FGGGNDERES
TLNQILTEMD GFNTSEQVVV LAGTNRPDVL DKALMRPGRF DRHIAIDKPT MDGRKQIFGV
HLKKIVTKED IEYLKGRLAA LTPGFSGADI ANCVNEAALV AARMHADHVV MSHFEHAIER
VVGGLEKKSL GLSPEEKRTV AYHEAGHAIC GWYFKYADPL LKVSIIARGQ GALGYAQYLP
AQGDTYLMNV HQLMDRMAMT LGGRVSEELH FDTVTSGASD DFNKVTRLAT AMVTKFGMSP
KIGTIYFEED QQQLHKPFSE ETARNIDMEV RRLVDEAYKQ CRDLLTEKKA EVGIVAEELL
SKEVLSRDDM IRLLGKRPYP ESGEFAKYFD GTGGKIQPPP PAEAPADTSE VGHAEAKGNN
PPSPST
//
