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Database: UniProt
Entry: A0A0V0S0H4_9BILA
LinkDB: A0A0V0S0H4_9BILA
Original site: A0A0V0S0H4_9BILA 
ID   A0A0V0S0H4_9BILA        Unreviewed;      2547 AA.
AC   A0A0V0S0H4;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   RecName: Full=General transcription factor IIH subunit 4 {ECO:0000256|RuleBase:RU364024};
GN   Name=pxf-1 {ECO:0000313|EMBL:KRX20269.1};
GN   ORFNames=T07_3783 {ECO:0000313|EMBL:KRX20269.1};
OS   Trichinella nelsoni.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=6336 {ECO:0000313|EMBL:KRX20269.1, ECO:0000313|Proteomes:UP000054630};
RN   [1] {ECO:0000313|EMBL:KRX20269.1, ECO:0000313|Proteomes:UP000054630}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS37 {ECO:0000313|EMBL:KRX20269.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Component of the general transcription and DNA repair factor
CC       IIH (TFIIH) core complex which is involved in general and
CC       transcription-coupled nucleotide excision repair (NER) of damaged DNA.
CC       {ECO:0000256|RuleBase:RU364024}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC       ECO:0000256|RuleBase:RU364024}.
CC   -!- SIMILARITY: Belongs to the TFB2 family. {ECO:0000256|ARBA:ARBA00007132,
CC       ECO:0000256|RuleBase:RU364024}.
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:KRX20269.1}.
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DR   EMBL; JYDL01000051; KRX20269.1; -; Genomic_DNA.
DR   STRING; 6336.A0A0V0S0H4; -.
DR   Proteomes; UP000054630; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000439; C:transcription factor TFIIH core complex; IEA:InterPro.
DR   GO; GO:0001671; F:ATPase activator activity; IEA:InterPro.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0006289; P:nucleotide-excision repair; IEA:InterPro.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR   CDD; cd00038; CAP_ED; 2.
DR   CDD; cd00992; PDZ_signaling; 1.
DR   CDD; cd01785; RA_PDZ-GEF1; 1.
DR   CDD; cd00155; RasGEF; 1.
DR   CDD; cd06224; REM; 1.
DR   Gene3D; 2.30.42.10; -; 1.
DR   Gene3D; 3.30.70.2610; -; 1.
DR   Gene3D; 2.60.120.10; Jelly Rolls; 2.
DR   Gene3D; 1.10.840.10; Ras guanine-nucleotide exchange factors catalytic domain; 1.
DR   Gene3D; 1.20.870.10; Son of sevenless (SoS) protein Chain: S domain 1; 1.
DR   InterPro; IPR000595; cNMP-bd_dom.
DR   InterPro; IPR018490; cNMP-bd_dom_sf.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR000159; RA_dom.
DR   InterPro; IPR000651; Ras-like_Gua-exchang_fac_N.
DR   InterPro; IPR023578; Ras_GEF_dom_sf.
DR   InterPro; IPR001895; RASGEF_cat_dom.
DR   InterPro; IPR036964; RASGEF_cat_dom_sf.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR040662; Tfb2_C.
DR   InterPro; IPR004598; TFIIH_p52/Tfb2.
DR   NCBIfam; TIGR00625; tfb2; 1.
DR   PANTHER; PTHR13152:SF0; GENERAL TRANSCRIPTION FACTOR IIH SUBUNIT 4; 1.
DR   PANTHER; PTHR13152; TFIIH, POLYPEPTIDE 4; 1.
DR   Pfam; PF00595; PDZ; 1.
DR   Pfam; PF00617; RasGEF; 1.
DR   Pfam; PF00618; RasGEF_N; 1.
DR   Pfam; PF03849; Tfb2; 1.
DR   Pfam; PF18307; Tfb2_C; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SMART; SM00314; RA; 1.
DR   SMART; SM00147; RasGEF; 1.
DR   SMART; SM00229; RasGEFN; 1.
DR   SUPFAM; SSF51206; cAMP-binding domain-like; 2.
DR   SUPFAM; SSF50156; PDZ domain-like; 1.
DR   SUPFAM; SSF48366; Ras GEF; 1.
DR   PROSITE; PS50042; CNMP_BINDING_3; 2.
DR   PROSITE; PS50106; PDZ; 1.
DR   PROSITE; PS50200; RA; 1.
DR   PROSITE; PS50009; RASGEF_CAT; 1.
DR   PROSITE; PS50212; RASGEF_NTER; 1.
PE   3: Inferred from homology;
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|RuleBase:RU364024};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|RuleBase:RU364024};
KW   Guanine-nucleotide releasing factor {ECO:0000256|ARBA:ARBA00022658,
KW   ECO:0000256|PROSITE-ProRule:PRU00168}; Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU364024};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054630};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163,
KW   ECO:0000256|RuleBase:RU364024};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015,
KW   ECO:0000256|RuleBase:RU364024}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        633..659
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        719..737
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          683..729
FT                   /note="Cyclic nucleotide-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50042"
FT   DOMAIN          1018..1083
FT                   /note="Cyclic nucleotide-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50042"
FT   DOMAIN          1148..1267
FT                   /note="N-terminal Ras-GEF"
FT                   /evidence="ECO:0000259|PROSITE:PS50212"
FT   DOMAIN          1268..1339
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          1600..1711
FT                   /note="Ras-associating"
FT                   /evidence="ECO:0000259|PROSITE:PS50200"
FT   DOMAIN          1736..1965
FT                   /note="Ras-GEF"
FT                   /evidence="ECO:0000259|PROSITE:PS50009"
FT   REGION          874..973
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1486..1529
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2049..2071
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2231..2274
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        874..895
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        902..917
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        926..941
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        945..973
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1494..1529
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2547 AA;  282246 MW;  222485A7573A9DEA CRC64;
     MRRIVQQYKR TATNFIVLTT VRNDYKGRIG PILQKYIPKG KMNSTHKVPQ TFLNYLSQLP
     SGILNKLYES AVACTGIYRY LPSVAQQIVM RLSLVSSGTT IADIEGWMVD EKKDILHESL
     KYLRQLHILQ ECNLSSIESV VLNRVFAKNL RLALLCNDAI CFKTVAVDPK HQKSFADLDS
     YASERWESVL KYLALPSAQS EKSVSVETKR VLQDSGLIQL CDSKMQLTSD GFQFILYDRR
     QQLWTYLLHY LAQLEKKGSP VHDCIMLILQ ACLGSHRAAY STENLTEAAL NFIQHLREIG
     LVHQRKRSAG WFYYTPLISV LTGLKSSSSS SKEGFLIVET NFRVYCYTDS VLDLAIVSTF
     CEPLFPNLVA CILNRESVRR AFQVNISAEQ IIQYLFSNAH KNMQKQTPTI PSTVTDQIKL
     WEMERDRFKF DPGVMYSNFV SDTDYITIRD YAKDLGVLLC EHEANRALVV SADGHEQSNQ
     FLTLFTSDSK KHTINLVSFS EVKNDQLKQH GEKSTHYSSV SLRFFISSLS VACKSSSYQR
     IRKLSDNCSD RSNSVSVVNT TSQSIACWLI DASDFLQRMA DTAVIEALRK PSKFRNLKLV
     CSVGYGERGW GRVAANWSNK FCPLFAPMLS VKLVVLFLSY LLLLLLFLSM MIMVGTFVCP
     DTWGGEKKNE VQLVYFFLRR LDVFRGVDDQ TLKTICQSAR YEQYQQAGKF LYKKGQRSFC
     WYILLSGAVF CDGRMYLPVE SFGKRVRFSE HYRISGCILL ESSEMIVIDY NSTEPSVGSY
     PESREQLPMA ATSLVVNRVP VADGEPTTSS TSSCSTSPSM CSSKVVHCRP IHQTTASTSF
     AASFKKACTV GEQQSSSCSV DEVEINTAAE IPSNLLPNRR LSSSQQQQQQ QHRHGGTLAM
     IRRSNSIRSS GSSSAGGRVS GFKPIAAIPS TSSTTMSDDD FSGLPEISVD SDDSDEAELE
     EEDEEEEEEE EEGCCLYAES SFTGHLRDLV RECLEKLPTE RTDDDIAILL DFVQHMSSFA
     SLPIYVKCEL CRKMVFAVVD KAGTIVMKHG EQIDSWSVVV NGEAEVVFPD GHRYEYHIGD
     CFGVQPTEQV QFHQGEMRTL VDDCQFVLVA QADYVQIISK LSDSYTRQLD SAGQVVCEKE
     KRAFESRVGY VLTKAKPCKL ISALFEDRRD CVVDPHFVED FLLTYRTFVD NPAEVLEKIL
     ACFSEPSKRE KVARLVLLWV NNHFGDFESN AEMTNLLEKF DKMLEDEAMF NHQQLLNIAC
     SVKSRTRNVT YTRSNRDEVL HFSILGGTEK NNGIYVVKVA AGSAAERVGL KRGDQIIEVN
     GHNFRNIARH RALEVLRGST HLSMVVKSNL LGFKEMLVAD QCDAGALLAP VLLQQAVATS
     KDGSSRRRMS PVQPRRSLVQ LHQLGGVDGL PMPSLRPPPR QHKHSLHLET QRAVMPALVH
     SLANTNINTT TTTSSRTLAR LNHAGKESGG SGSRLGKLIK KLRQGSSSSA LSLDADDDND
     HVDGHEPRVD DGGRKCSKQK TRQTLDDCDA TDEAVRRATL GRPTGAQSVS MPSGVPLLGR
     RLKHSRSNPD LSSTANQPIL PGGFGQMISQ YYEPVRPQHP EHILKVYRID QTFKYLSVYK
     ETSAQNVVQL ALQEFGMCNN SGVGNDAVHS SSSSSSTSTI TTTANGGEWS LCEVTVTADG
     LIKQRRLPAQ MQNLAERISL NSRYYLKNNN CPLPLVPDEL APDLLKDAQA QLGCLHASIV
     AAQLTLQDFA TFASIEPAEY VANLFKLGVA PTRWPRLADF EQSVNRETFW VATEVCKERN
     SIRRAKIVKK FIKIANHCRD FKNFNSMFAI ISGLEKPCVR RLHNTWDKIS SKYTKMLDNL
     QSLLDPSRNM SKYRQHLAEA SNDPPVIPLL PVLKKDLTFL HECNPTWCDG GMVNFEKLRM
     VAKEIRFVTK LASAPYELSS MFERSGNQAQ LNDALLHMNT FEGGSSVATM KKQHVQHRVP
     LSRKKLYEQA LMVRRVKFYL TQFEPISDES VLDKLSLELE PVTVTSGGGG GGAHSTSTGN
     LGVVTVASAG KRSQPSPSLS SGSSMSVTSS DCSRRCNGPK FGVESPHAVQ KMLSLVDHSR
     VRASSNNTRA IGIGSPPTSP GAPLKAARPA TAAVAHSLLY FGSNIHQHQQ QHHGRFNNHD
     LNTFAIPPPL SSVVPVDLTC ESSAVTSSIT PSRLHGSASA TSSTDSVISS HQSDLLPLSS
     SSSSYIPHAV SCDSTDSGHG SLDSPSMITG VGVASSSSSS SPPSQRQSYP PRPNTITLKA
     ASNSTTHYDL YSTTTTGVVV STKPFRSFEK AQQQQQQQQP QQNFRFTAPQ HENRASSSVA
     SSTFLKQSQP LSATLTIGSR RLATTADQSQ SDTNNGATQV SRAYVRMNVV VTFGECSSCS
     SSFEKFMYIC IFQAKCSTWK SFFLENKTQN KKKLCHTEKS ELVKHQTFFV STVVINQREP
     SVSLVIGTTS APEVTSIFPE SGSIENGPRQ YFSSVAFVHE VNVPCSAGVT GLVLKTVDIV
     VVCFAEGLPS TKSVNGATLK ASGKCFR
//
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