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Database: UniProt
Entry: A0A369GJH9_9HYPO
LinkDB: A0A369GJH9_9HYPO
Original site: A0A369GJH9_9HYPO 
ID   A0A369GJH9_9HYPO        Unreviewed;       479 AA.
AC   A0A369GJH9;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   03-MAY-2023, entry version 18.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:RDA82992.1};
GN   ORFNames=CP532_2418 {ECO:0000313|EMBL:RDA82992.1};
OS   Ophiocordyceps camponoti-leonardi (nom. inval.).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Ophiocordyceps.
OX   NCBI_TaxID=2039875 {ECO:0000313|EMBL:RDA82992.1, ECO:0000313|Proteomes:UP000252748};
RN   [1] {ECO:0000313|EMBL:RDA82992.1, ECO:0000313|Proteomes:UP000252748}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BCC 80369 {ECO:0000313|EMBL:RDA82992.1,
RC   ECO:0000313|Proteomes:UP000252748};
RA   Kobmoo N., Wichadakul D., Arnamnart N., Rodriguez De La Vega R.C.,
RA   Luangsa-Ard J.-J., Giraud T.;
RT   "A genome scan of diversifying selection in the zombie-ant fungus
RT   Ophiocordyceps unilateralis complex supports a role of enterotoxins in
RT   coevolution and host-specificity.";
RL   Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Recruits TFIIH to the initiation complex and stimulates the
CC       RNA polymerase II C-terminal domain kinase and DNA-dependent ATPase
CC       activities of TFIIH. Both TFIIH and TFIIE are required for promoter
CC       clearance by RNA polymerase. {ECO:0000256|ARBA:ARBA00025581}.
CC   -!- SIMILARITY: Belongs to the cytochrome b5 family.
CC       {ECO:0000256|RuleBase:RU362121}.
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:RDA82992.1}.
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DR   EMBL; PDHP01000225; RDA82992.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A369GJH9; -.
DR   STRING; 2039875.A0A369GJH9; -.
DR   Proteomes; UP000252748; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005673; C:transcription factor TFIIE complex; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0020037; F:heme binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006367; P:transcription initiation at RNA polymerase II promoter; IEA:InterPro.
DR   CDD; cd07977; TFIIE_beta_winged_helix; 1.
DR   Gene3D; 3.10.120.10; Cytochrome b5-like heme/steroid binding domain; 1.
DR   InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd.
DR   InterPro; IPR036400; Cyt_B5-like_heme/steroid_sf.
DR   InterPro; IPR018506; Cyt_B5_heme-BS.
DR   InterPro; IPR040501; TFA2_Winged_2.
DR   InterPro; IPR016656; TFIIE-bsu.
DR   InterPro; IPR003166; TFIIE_bsu_DNA-bd.
DR   PANTHER; PTHR12716:SF8; TRANSCRIPTION INITIATION FACTOR IIE SUBUNIT BETA; 1.
DR   PANTHER; PTHR12716; TRANSCRIPTION INITIATION FACTOR IIE, BETA SUBUNIT; 1.
DR   Pfam; PF00173; Cyt-b5; 1.
DR   Pfam; PF18121; TFA2_Winged_2; 1.
DR   Pfam; PF02186; TFIIE_beta; 1.
DR   PRINTS; PR00363; CYTOCHROMEB5.
DR   SMART; SM01117; Cyt-b5; 1.
DR   SUPFAM; SSF55856; Cytochrome b5-like heme/steroid binding domain; 1.
DR   PROSITE; PS00191; CYTOCHROME_B5_1; 1.
DR   PROSITE; PS50255; CYTOCHROME_B5_2; 1.
DR   PROSITE; PS51351; TFIIE_BETA_C; 1.
PE   3: Inferred from homology;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|RuleBase:RU362121};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU362121};
KW   Membrane {ECO:0000256|RuleBase:RU362121};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU362121}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000252748};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW   Transmembrane {ECO:0000256|RuleBase:RU362121};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU362121}.
FT   TRANSMEM        107..126
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362121"
FT   DOMAIN          2..78
FT                   /note="Cytochrome b5 heme-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50255"
FT   DOMAIN          248..333
FT                   /note="TFIIE beta"
FT                   /evidence="ECO:0000259|PROSITE:PS51351"
FT   REGION          77..102
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          209..250
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          427..461
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        87..102
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        209..229
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   479 AA;  52175 MW;  4653EFF70278479C CRC64;
     MSEGLTYQDV AEHNTKKDLY LVIHDKVYDC AQFVDEHPGG EEVMLDVAGQ DATEAFEDVG
     HSDEARETLD KLLVGKLKRQ PGDPAPHAAP QSSSTSGSSS DQNGLGMGLY VILLIGSALG
     YLAYYYPCAL SASLGRQPPS LVSPDPVVEI VSSNPFPPFD RLLFAMSSYL EKQSSAFRGT
     LASAASKLSN AKAAAANASS SSSMLKTATT AASLAPPSPS PSAASDSATP SGKRKRETGP
     EVPFSQPQLT GYGSEVKTQM TFAVDYLKKK GDQKTMTDII NHLSLRSYPE EHKRELAEGL
     RGHPRIDWRP DGSLTEQTWR TGTYAHRPII PGVRDGTSLL AFLQRKTDAS GVAVKDLKDG
     WPDCEETLAS LEKQHKVLVV RTKKDNFPRH VWPDDASLKH VVQPEFQARW HAVPLPSLED
     MHRKLVSVGQ KPTSEDPRKL AQALGSKPKA QKKKAGKKVG KATNVHMAHL MQDYSNLRR
//
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