ID A6R2J5_AJECN Unreviewed; 1669 AA.
AC A6R2J5;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE RecName: Full=GPI inositol-deacylase {ECO:0000256|ARBA:ARBA00015856, ECO:0000256|RuleBase:RU365011};
DE EC=3.1.-.- {ECO:0000256|RuleBase:RU365011};
GN ORFNames=HCAG_03853 {ECO:0000313|EMBL:EDN07322.1};
OS Ajellomyces capsulatus (strain NAm1 / WU24) (Darling's disease fungus)
OS (Histoplasma capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX NCBI_TaxID=2059318 {ECO:0000313|EMBL:EDN07322.1, ECO:0000313|Proteomes:UP000009297};
RN [1] {ECO:0000313|Proteomes:UP000009297}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NAm1 / WU24 {ECO:0000313|Proteomes:UP000009297};
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(2009).
CC -!- FUNCTION: Involved in inositol deacylation of GPI-anchored proteins
CC which plays important roles in the quality control and ER-associated
CC degradation of GPI-anchored proteins. {ECO:0000256|ARBA:ARBA00003496,
CC ECO:0000256|RuleBase:RU365011}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004477}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the GPI inositol-deacylase family.
CC {ECO:0000256|ARBA:ARBA00006931, ECO:0000256|RuleBase:RU365011}.
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DR EMBL; CH476657; EDN07322.1; -; Genomic_DNA.
DR STRING; 339724.A6R2J5; -.
DR VEuPathDB; FungiDB:HCAG_03853; -.
DR HOGENOM; CLU_002999_0_0_1; -.
DR OMA; IHDTTDW; -.
DR OrthoDB; 5477082at2759; -.
DR Proteomes; UP000009297; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR CDD; cd18799; SF2_C_EcoAI-like; 1.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR006935; Helicase/UvrB_N.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR012908; PGAP1-like.
DR InterPro; IPR039529; PGAP1/BST1.
DR PANTHER; PTHR15495:SF7; GPI INOSITOL-DEACYLASE; 1.
DR PANTHER; PTHR15495; NEGATIVE REGULATOR OF VESICLE FORMATION-RELATED; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07819; PGAP1; 1.
DR Pfam; PF04851; ResIII; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022806};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW ECO:0000256|RuleBase:RU365011}; Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU365011};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU365011};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022806};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927,
KW ECO:0000256|RuleBase:RU365011};
KW Reference proteome {ECO:0000313|Proteomes:UP000009297};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU365011};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU365011};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU365011}.
FT TRANSMEM 1365..1383
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 1415..1446
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 1483..1509
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 1529..1554
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 1566..1585
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 1597..1617
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT DOMAIN 65..223
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 278..445
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 624..665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1669 AA; 185986 MW; BEC71FA9869FE7F4 CRC64;
MRWLTKCIRE FKCAATYGNS ILSHRLISSA VAVAATPTKS HSPGSSLSDF HLRSYQEECI
QSVLSYLEKG HKRLGVSLAT GSGKTLIDRI PPRDEVANRT LIIVHRKELV EQAAKHCMLA
YPGKTIEIEM GKSHATGTAE ITIASIRSLL SKGRIEKFDP ERYKLILVDE AHHIVAPSYK
EVLGYFGLNE VSDGSPALVG VSATFSRFDG LKLGAAIDHI VYHKDYIDMI GEKWLADAVF
TTVNSRADLS KVSNGPNGDF QTGQLSAAVN TDTVNDITVR AWLSRASERK STLVFGVNIE
HVRCLTEAFR RFGVDARYIT SQTPKDIRTD ELEAFRNQEY PVLVNCGLFT EGTDIPNIDC
VLLARPTRSK NLLIQMIGRG LRLYPGKKNC HIIDMVASLG TGITSTPTLF GLHPDEGLDE
AKMEDIEKLK NRESYSFKSK LKFSAISADK VAVDFTDYDS VHDLLRDTSG ERHIRSLSQN
AWVSVAPDRY VLNAPPGRIT IIKDDSAKWQ PWRKKYASLG QVAFLNKHLP FDSQIKPREI
TKGDAADMIT KVKHGAMGQF KNIVAIKRRL GREKAKESEL EELRSREEVK SHTYLDAAPA
RRHGPEINND TGYLFVPQLN QQQATDLSSG EEANPSAFST RGFAGDTRQT TPSNSTNRQE
NAMSFESRIF SPITNNSMEG HKLRRSRPRI LWSCSLLTIS LTVLSAISLY GIIHSYMTRQ
IDPQGCKTPR MMPTYIQLIG FDTEHTRFAS KYRLYLYRER TVDKYSEQDI GVGGVPVLFL
PGNAGSYRQG RSLASEASLY FQDAISNDQE KLNAGTRSLD FFMADFNEDM AAFHGQTLLD
QAEYVNEALA YILSLYHDPT RPGRDLNLPD PSSVILIGHS MGGIVARTVL TMSNYQANSV
NTIITMSTPH ARPPVSFDRD VVRTYKQIND YWREAYSQRW ANNNPLWHVT LISIAGGGGD
SIVPSDYTSL SSLVPETHGF TVFTSTIPNV WTGMDHLSIA WCDSFRKVII RSLFDLVDVR
RSSQTKQRAE RMSVFKKWYL TGMEAISERS LPQKDPSTLL TLEDNTNSIL PQGQRLVLRA
FGSRQLPEAH LLPIPPQGAS GKKFTLLTDQ LLDSPGGNGK LEVLFCSVFP LRAGHSAPLL
SSNMDLSGGS AGSTRLACKS AMEDAINLPA STRSSKFAFD DALPFSYLQY NLEDLMEHQF
VAVIDKAAKR SSGWLVAEFS DSSDALIQTK VGLGRLLATG LDIRLPAERP MLTEVKIPAL
HSSLLAYKLR VGKQPCGEHA ELFTPLLRQY ISEPHESKYF VNVKEADINL HGVAPYMPPH
LRDRSAMRGI SFQLWSDPSC NASTELSLRV DIVGSMGKLA MRYRTVFAAL PLLVTALVLR
KQFQIHDTTD WRSNSTESAI DFTRNDLLLG SQDSFFWFLV PLFGLISIGL CVVVNHVVMA
LIYGLATIRS VLVSRRGYIK HDDPRPAAIY PSLSSRQRII NSAVLLCFVA TVIPYQFAYL
VACLVQLATC VQTLQYARES YNFYNYVHSI FILMLWILPV NVPVFAVWVH NLAVHWWTPF
SSHHNVLSIM PFILLVETLT NGHMIPRITS RLRHVTSALF IILAGYAALY GVTYAYLLHH
IANIVTAWLV GVHFASSGFS LRSLNQAFEG SSFGEDGPPG TNGNIKKLP
//
