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Database: UniProt
Entry: A0A0V1KT41_9BILA
LinkDB: A0A0V1KT41_9BILA
Original site: A0A0V1KT41_9BILA 
ID   A0A0V1KT41_9BILA        Unreviewed;      2437 AA.
AC   A0A0V1KT41;
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:KRZ50474.1};
GN   ORFNames=T02_14044 {ECO:0000313|EMBL:KRZ50474.1};
OS   Trichinella nativa.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=6335 {ECO:0000313|EMBL:KRZ50474.1, ECO:0000313|Proteomes:UP000054721};
RN   [1] {ECO:0000313|EMBL:KRZ50474.1, ECO:0000313|Proteomes:UP000054721}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS10 {ECO:0000313|EMBL:KRZ50474.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (MAY-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:KRZ50474.1}.
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DR   EMBL; JYDW01000263; KRZ50474.1; -; Genomic_DNA.
DR   Proteomes; UP000054721; Unassembled WGS sequence.
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};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU364024};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054721};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163,
KW   ECO:0000256|RuleBase:RU364024};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015,
KW   ECO:0000256|RuleBase:RU364024}.
FT   DOMAIN          572..618
FT                   /note="Cyclic nucleotide-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50042"
FT   DOMAIN          904..969
FT                   /note="Cyclic nucleotide-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50042"
FT   DOMAIN          1034..1153
FT                   /note="N-terminal Ras-GEF"
FT                   /evidence="ECO:0000259|PROSITE:PS50212"
FT   DOMAIN          1154..1225
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          1488..1600
FT                   /note="Ras-associating"
FT                   /evidence="ECO:0000259|PROSITE:PS50200"
FT   DOMAIN          1625..1854
FT                   /note="Ras-GEF"
FT                   /evidence="ECO:0000259|PROSITE:PS50009"
FT   REGION          763..859
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1292..1311
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1371..1406
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1939..1964
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2121..2164
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        766..781
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        789..804
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        813..828
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        832..859
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1389..1406
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2121..2155
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2437 AA;  269823 MW;  46572181B7670F7F CRC64;
     MAHMRRIVQQ YKRTATNFIV LTTVRNDYKG RIGPIMQKYI PKGKMNSTHK VPQTFLNYLS
     QLPSGILNKL YESAVACTGI YRYLPSVAQQ IVMRLSLVSS GTTIADIEGW MVDEKKDILH
     ESLKYLRQLH ILQECNLSSI ESVVLNRVFA KNLRLALLCK DTICFKTVTV DPKHQKSFAD
     LDSYASERWE SVLKYLALPS AQSEKSVSVE TKRVLQDSGL IQLCDSKMQL TSDGFQFILY
     DRRQQLWTYL LHYLAQLEKK GSPVHDCIML ILQACLGSHR AAYSTENLTE AALNFIQHLR
     EIGLVHQRKR SAGWFYYTPL ISVLTGLKSS SSSSKEGFLI VETNFRVYCY TDSVLDLAIV
     STFCEPLYRF PNLVACILNR ESVRRAFQVN ISAEQIIQYL FSNAHKNMQK QTPTIPSTVT
     DQIKLWEMER DRFKFDPGVM YSNFFSDTDY ITIRDYAKDL GVLLCEHEAN RALVVSADGH
     EQRIRKLSDN CSDRSNSATL EFCPTLILFY FFLVWGSLNF LSQSIACWLI DASDFLLRMA
     DTAVIEALRK PSKFRNLKEV QLVYFFLRRL DVFRGVDDQT LRTICQSARY EQFQQAGKFL
     YKKGQRSFCW YILLSGAVFC DGRIYLPVES FGKRVRFSEH CRISDCILLE SSEMIVIDYN
     STEPSVGSYP ESREQLPMAA TSLVVNRVPV ADGEPTTSST SSCSTSPSMC SSKVVLCRPI
     HQTTASTSFA ASFKKACTVG EQQSSSCSVD EVEISTVAEI PPNLLPNRRL SSSQQQQKHR
     HDGTLAMIRR SNSIRSSGSS SAGGRVSGFK PIAAIPSTSS TTMSDDDFSG LPEISVDSDD
     EDDDEAELEE EDEEEEEEGC CLYAESSFTG HLRDLVRECL EKLPTERTDD DIAILLDFVQ
     HMSSFASLPI YVKCELCRKM VFAVVDKAGT IVMKHGEQLD SWSVVINGEV EVVFPDGHRY
     EYHIGDCFGV QPTEQVQFHQ GEMRTLVDDC QFVLVAQADY VQIISKLSDS YTRQLDSAGQ
     VVCEKEKRAF ESRVGYVLTK AKPCKLISAL FEDRRDCVVD PHFVEDFLLT YRTFVDNPAE
     VLEKILACFS EPSKREKVAR LVLLWVNNHF GDFESNAEMT NLLEKFDKML EDEAMFNHQQ
     LLNIACSVKS RTRNVTYTRS NRDEVLHFSI LGGTEKNNGI YVVKVAAGSA AERVGLKRGD
     QIIEVNGHNF RNIARHRALE VLRGSTHLSM VVKSNLLGFK EMLVADQCDA GALLAPVLLQ
     QAVATSKDGS SRRRMSPVQP RRSLVQLHQL GGVDGLPMPS LRPPPRQQKH SLHLETQRAV
     MPALVHALAN TNTTTTTTSS RTLARLNHAG KESGGSGSRL GKLIKKLRQG SSSSALSLDA
     DDDDVDNDHV DGHEPRVDDG GRKCSKQKIR QTLDDCDATD EAVRRATLGR PTGAQSVSMP
     SGVPLLGRRL KHSRSNPDLS STANQPILPG GFGQMISQYY EPVRPQHPEH ILKVYRIDQT
     FKYLSVYKET SAQNVVQLAL QEFGMCNNNS GVGNDAVHNG SSSSSTTTTT TTANGDEWSL
     CEVTVTTDGL IKQRRLPAQM QNLAERISLN SRYYLKNNNC PLPLVPDELA PDLLKDAQAQ
     LGCLHASIVA AQLTLQDFAA FASIEPAEYV ANLFKLGGAP TRWPRLADFE QSVNRETFWV
     ATEVCKERNS IRRAKIVKKF IKIANHCRDF KNFNSMFAII SGLEKPCVRR LHNTWDKISS
     KYTKMLDNLQ SLLDPSRNMS KYRQHLADAS NDPPVIPLLP VLKKDLTFLH ECNPTWCDGG
     MVNFEKLRMV AKEIRFVTKL ASAPYELSSM FERSGNQAQL NDALLHMNTF EGGSSVATMK
     KQHVQHRVPL SRKKLYEQAL MVRRVKFYLT QFEPISDESV LDKLSLELEP VTVTSGGGGG
     GGAHSASTGN LGVVTVASAG KRSQPSPSLS SGSSMSVTSS DCSRRCNGPK FGVESPHAVQ
     KMLSLVDHSR VRASSNNTRA IGIGSPPTSP GAPLKAVRPA TAAVAHSLLY FGSNIHQHQQ
     QQHGRFNNHD LNTFAIPPPL SSVVPVDLTC ESSAVTSSIT PSRLHGSASA TSSTDSVISS
     HQSDLLPLSS SSSSYIPHAV SCDSTDSGHG SLDSPSMITG VGVASSSSSS SPPSQRQSYP
     PRPNTIALKA ASNSTTHYDL YSTTTTGVVV STKPFRSFEK AQQQQQQQQP QQNFRFTAPQ
     HENRASSSVA SSTFLKQSQP LSSSLTIGSR RLATTADQSQ SDTNNGATQV SRHLASVPVA
     AAVLKSPSKC STWKSFFLEN KTHKKLSHTE KSELVKHQTF FVSTVVINQR EPSFSLVIGT
     TSAPEVTSIF PESGTIENGP WQYFSSVAFV HAVNDDCIAG ATGVTGLVLK TVDIVVVCFA
     EGLPSTRSVN GVSGQSGMET VDESYQIFKV SASLTAA
//
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