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Database: UniProt
Entry: H0EUG0_GLAL7
LinkDB: H0EUG0_GLAL7
Original site: H0EUG0_GLAL7 
ID   H0EUG0_GLAL7            Unreviewed;      1544 AA.
AC   H0EUG0;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   22-FEB-2023, entry version 39.
DE   SubName: Full=Putative Hypoxia up-regulated protein 1 {ECO:0000313|EMBL:EHK97834.1};
GN   ORFNames=M7I_6417 {ECO:0000313|EMBL:EHK97834.1};
OS   Glarea lozoyensis (strain ATCC 74030 / MF5533).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Helotiaceae; Glarea.
OX   NCBI_TaxID=1104152 {ECO:0000313|EMBL:EHK97834.1, ECO:0000313|Proteomes:UP000005446};
RN   [1] {ECO:0000313|EMBL:EHK97834.1, ECO:0000313|Proteomes:UP000005446}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 74030 / MF5533 {ECO:0000313|Proteomes:UP000005446};
RX   PubMed=22302591; DOI=10.1128/EC.05302-11;
RA   Youssar L., Gruening B.A., Erxleben A., Guenther S., Huettel W.;
RT   "Genome sequence of the fungus Glarea lozoyensis: the first genome sequence
RT   of a species from the Helotiaceae family.";
RL   Eukaryot. Cell 11:250-250(2012).
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:EHK97834.1}.
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DR   EMBL; AGUE01000171; EHK97834.1; -; Genomic_DNA.
DR   HOGENOM; CLU_246670_0_0_1; -.
DR   InParanoid; H0EUG0; -.
DR   Proteomes; UP000005446; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   CDD; cd10230; HYOU1-like_NBD; 1.
DR   Gene3D; 1.20.1270.10; -; 1.
DR   Gene3D; 3.30.30.30; -; 1.
DR   Gene3D; 3.30.420.40; -; 2.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR029048; HSP70_C_sf.
DR   InterPro; IPR013126; Hsp_70_fam.
DR   PANTHER; PTHR45639; HSC70CB, ISOFORM G-RELATED; 1.
DR   PANTHER; PTHR45639:SF3; HYPOXIA UP-REGULATED PROTEIN 1; 1.
DR   Pfam; PF00012; HSP70; 1.
DR   PRINTS; PR00301; HEATSHOCK70.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR   SUPFAM; SSF100934; Heat shock protein 70kD (HSP70), C-terminal subdomain; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005446}.
FT   REGION          1118..1173
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1342..1390
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1446..1544
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1126..1150
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1153..1173
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1342..1358
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1446..1460
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1462..1476
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1506..1544
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1544 AA;  170262 MW;  434A91B76096C353 CRC64;
     MLDIMAVVLD IYSCLLSSHI PRLPGVIRCP LEIDTEVDGL MVLRGITFQL STLSFVVHGV
     EVGIKLSDDM ELAIQCEEVT IKLFRGIVVG DCFANLKGGE FEMTFGKVKA KNRRSLAESD
     TSSIKSPVEP KFFFNEEEEG KTVKMTEEMT NNHAPEDSSP KESLSLIKKM SPDNEEASGK
     YKRTVEFIQQ TNAIYEARQH IQGLNKEAIK RDQNSFGHDD LNGLRAAVCS YVHSTPSVPH
     PPQKSIKVTT LQNLMPPWLR RFLHRLPLLY RLLLNPISYF HPVKIESITA TASGKWIRYM
     LVENVLKDYS GSDDEIKGLK KKFAQWLIDA NFAVQLGNIT GIAQVPIISS YDIVTMLGFE
     DVMAYRTIPE TVELKQVLRL GGADARFVIP SFLLPHHDHL LPPLPTAEIK QELQAKVATA
     DGKPKELQAT HELEQALKDE ANVQISVHAR LPACFDQQLL DFIAALVKAT KIVEFDKVAA
     EETGDEEDDE ERKRGIKELG RAFTGSMKRT VKKAVVGGVV NDRWIASSLP NNTYNHGPSI
     AGPIEQTALV ANIFTLMHSL VKPGIPLEIV LTKDSRRKEA SAVVFKPAKN PKAGEFPERL
     YGSDALALAA RFPGDVYPNL KALLGLGADN SVVKEYASRH PALKLATDKT RGTVAFKSGA
     FTPEEEAWTI EEILAMELQS IQKNAEALAG RGSSVKDLVI TVPPFYTAEE RRAVELAADL
     AGLRVLELIS DGLAVGLNYA TSRQFKSAKD GGTPEHHMVF DMGAGSTKAT ILKFQGRTVK
     DVGKFNKTVQ EVQVLGVGWD RTLGGDALNA VIMDDMISQF VSSPAAKSVA PTVEAVKAHG
     RASAKLLKEA ERLRHVLSAN ANTQAGFEGL YEDIDFKYKI TRAEFEKLAE PHVARISVAI
     QKALDMANLE AKDLDSVILH GGAIRTPFVQ QELEKFLGSA DKVRTNVNSD ESAVFGAVFR
     GAGLSPSFRV KEIRALEAAV YPTGIKWTNI YDKPQHERLW EAKSLVGVER KYIFKNQKDF
     PIKFYQHVPS SENVSPGSAE KELLTLTTQN LTESLAHLKE KFSCSDGDIN LKLSTRLAVN
     NGQVEIVKLV LDCEVEESEG KAGAFDSVKN MLGFGKKDQA PLTDEEEAET VSSSATSSSS
     STSSYASASA SGKDAKKDAK SKDKDAKSKD KDAKPKIVKR FEIVPIKFTI EKNGLPQIPE
     TELTRMKSRL SAFADSDLSR RRREEALNQL EGYTYKVRDF LEKEDFIAAS TEEERSSLEA
     KSAAASEWIY GDGAHANRDE FKAKLKEMKD IVEPIQLRKT EAVARPEQLK LLQESLNQTQ
     SMIAGIKEQI ANDTKNHEAF TSSKLAASKA TPLPSSSTKE ADDFDGLEDE ATASATVEPE
     AEETMAPSTY VEADIVRPQS LYDEITVWLT KKLSEQEKLS ETADPVLLSK DLESRSKQLQ
     EVQVELIMKS MQQPFKSSRP PKSKKPSPKP KKTKSAKTKT TSTEAAEKTA AGDEQPMFQV
     GEDGKPIFKV GEDGKMPSEE EILEFIEKSK KENAGKAEGK HDEL
//
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