UniProt: U3JYN5

Database: UniProt
Entry: U3JYN5_FICAL

LinkDB:  U3JYN5_FICAL 
Original site:  U3JYN5_FICAL

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Ontology (30)   
   GO (30)   
Gene (4)   
   NCBI-Gene (1)   
   ENSEMBL-UP (3)   
Protein sequence (6)   
   RefSeq(pep) (6)   
Protein domain (12)   
   InterPro (6)   
   Pfam (2)   
   PROSITE (2)   
   SMART (2)   
Literature (1)   
   PubMed (1)   
All databases (53)   

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ID   U3JYN5_FICAL            Unreviewed;      1484 AA.
AC   U3JYN5;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   SubName: Full=ERCC excision repair 6, chromatin remodeling factor {ECO:0000313|Ensembl:ENSFALP00000007889.1};
GN   Name=ERCC6 {ECO:0000313|Ensembl:ENSFALP00000007889.1};
OS   Ficedula albicollis (Collared flycatcher) (Muscicapa albicollis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Muscicapidae; Ficedula.
OX   NCBI_TaxID=59894 {ECO:0000313|Ensembl:ENSFALP00000007889.1, ECO:0000313|Proteomes:UP000016665};
RN   [1] {ECO:0000313|Ensembl:ENSFALP00000007889.1, ECO:0000313|Proteomes:UP000016665}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23103876; DOI=10.1038/nature11584;
RA   Ellegren H., Smeds L., Burri R., Olason P.I., Backstrom N., Kawakami T.,
RA   Kunstner A., Makinen H., Nadachowska-Brzyska K., Qvarnstrom A., Uebbing S.,
RA   Wolf J.B.;
RT   "The genomic landscape of species divergence in Ficedula flycatchers.";
RL   Nature 491:756-760(2012).
RN   [2] {ECO:0000313|Ensembl:ENSFALP00000007889.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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DR   RefSeq; XP_005048418.1; XM_005048361.2.
DR   RefSeq; XP_005048419.1; XM_005048362.2.
DR   RefSeq; XP_005048420.1; XM_005048363.2.
DR   RefSeq; XP_005048421.1; XM_005048364.2.
DR   RefSeq; XP_016154973.1; XM_016299487.1.
DR   RefSeq; XP_016154974.1; XM_016299488.1.
DR   STRING; 59894.ENSFALP00000007889; -.
DR   Ensembl; ENSFALT00000007922.2; ENSFALP00000007889.1; ENSFALG00000007563.2.
DR   GeneID; 101819888; -.
DR   eggNOG; KOG0387; Eukaryota.
DR   GeneTree; ENSGT00940000158057; -.
DR   HOGENOM; CLU_000315_7_2_1; -.
DR   OMA; VKHDAIM; -.
DR   OrthoDB; 5488252at2759; -.
DR   Proteomes; UP000016665; Chromosome 6.
DR   GO; GO:0110016; C:B-WICH complex; IEA:Ensembl.
DR   GO; GO:0090734; C:site of DNA damage; IEA:Ensembl.
DR   GO; GO:0008023; C:transcription elongation factor complex; IEA:Ensembl.
DR   GO; GO:0005524; F:ATP binding; IEA:Ensembl.
DR   GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:Ensembl.
DR   GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR   GO; GO:0003677; F:DNA binding; IEA:Ensembl.
DR   GO; GO:0030296; F:protein tyrosine kinase activator activity; IEA:Ensembl.
DR   GO; GO:0006284; P:base-excision repair; IEA:Ensembl.
DR   GO; GO:0000077; P:DNA damage checkpoint signaling; IEA:Ensembl.
DR   GO; GO:0097680; P:double-strand break repair via classical nonhomologous end joining; IEA:Ensembl.
DR   GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IEA:Ensembl.
DR   GO; GO:0007254; P:JNK cascade; IEA:Ensembl.
DR   GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl.
DR   GO; GO:2001033; P:negative regulation of double-strand break repair via nonhomologous end joining; IEA:Ensembl.
DR   GO; GO:0031175; P:neuron projection development; IEA:Ensembl.
DR   GO; GO:0045494; P:photoreceptor cell maintenance; IEA:Ensembl.
DR   GO; GO:0032786; P:positive regulation of DNA-templated transcription, elongation; IEA:Ensembl.
DR   GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; IEA:Ensembl.
DR   GO; GO:0045945; P:positive regulation of transcription by RNA polymerase III; IEA:Ensembl.
DR   GO; GO:0060261; P:positive regulation of transcription initiation by RNA polymerase II; IEA:Ensembl.
DR   GO; GO:0006290; P:pyrimidine dimer repair; IEA:Ensembl.
DR   GO; GO:0010332; P:response to gamma radiation; IEA:Ensembl.
DR   GO; GO:0000303; P:response to superoxide; IEA:Ensembl.
DR   GO; GO:0009636; P:response to toxic substance; IEA:Ensembl.
DR   GO; GO:0010224; P:response to UV-B; IEA:Ensembl.
DR   GO; GO:0010165; P:response to X-ray; IEA:Ensembl.
DR   GO; GO:0000012; P:single strand break repair; IEA:Ensembl.
DR   GO; GO:0006362; P:transcription elongation by RNA polymerase I; IEA:Ensembl.
DR   GO; GO:0006283; P:transcription-coupled nucleotide-excision repair; IEA:Ensembl.
DR   CDD; cd21397; cc_ERCC-6_N; 1.
DR   CDD; cd22254; CSB_WHD; 1.
DR   CDD; cd18000; DEXHc_ERCC6; 1.
DR   CDD; cd18793; SF2_C_SNF; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR049730; SNF2/RAD54-like_C.
DR   InterPro; IPR000330; SNF2_N.
DR   PANTHER; PTHR45629:SF7; DNA EXCISION REPAIR PROTEIN ERCC-6-RELATED; 1.
DR   PANTHER; PTHR45629; SNF2/RAD54 FAMILY MEMBER; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00176; SNF2-rel_dom; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016665}.
FT   DOMAIN          514..690
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          839..998
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          283..404
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          423..446
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1138..1235
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1328..1375
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1391..1410
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          167..194
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        337..370
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        371..398
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1149..1164
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1166..1195
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1210..1235
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1336..1355
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1356..1375
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1484 AA;  168089 MW;  2ABFCE90C174CC2A CRC64;
     MPTHKSLLPD SAQEQESATT SSNDCLHNDE NSGTEQENGI CDNGVGNSVG IPNSDCQAST
     SMAVPLEAPR RTHPLLQINR QQIQSVSCSA HAAELKDLGV DVYDQDVLEQ GVLQQVDNAI
     NEANKAAKIA NASKEYESVL EDLRSCTTSL RHINKIIEEL SPQAADNKNV NRKLDSVKRQ
     KYNKEQQLKK IKAKQKRLQG ILGLTEFADE ANEIEYEEDE EPGPSSLGSM LMPAQETEWA
     ELIRTGQMTP FGTKIPQKPE RKARQLRLNE ASDFEKYLAD QAKLSSERRK LSRHRGAKKK
     AQAKNVQCVA PAAATKEKSG KALSKTDKRL KKHLRELQKH ALQIHSKARI PKEKKYPEAK
     KFRHEQEDDS GESEYVPDEE LFDPEAAEEE EQSSSLDEND SDYELKSLSR KRKHLVKKGF
     KEDENDADFV PSSEEEEHTP GKHKVRRWRD DGDVDYYKQR LRKWQKERLK DKEHQTAEEL
     SEESDVEFEE GFKVPGFLFK KLFKYQQTGV RWLWELHCQQ AGGILGDEMG LGKTIQIIAF
     LAGLSYSNMR TRGSNYRYQG LGPTVIVCPA TVLHQWVKEF HTWWPPFRVA VLHETGSYTK
     SKVKLIHEIA SCHGILITSY SYIRLMQDNI HTYDWHYVIL DEGHKIRNPN AAVTLACKQF
     RTPHRIILSG SPMQNNLKEL WSLFDFIFPG KLGTLPVFME QFSVPITMGG YCNASPVQVK
     TAYKCACVLR DTINPYLLRR MKADVKMSLS LPDKNEQVLF CRLTEEQRQI YQNYINSKEV
     YQILNGDMQI LLGLSTLRKI CNHPDFVADS PRILKSVPDA EVEDPNQFGY WKRSGKMIVV
     ESLLKIWHKQ GHRVLFFTQS RQMMQILEVF VRYRNYSYLR MDGTTAVASR QPLVTKYNED
     KSIFLFLLTT RVGGIGVNLV GADRVIIYDP DWNPSVDTQA RERAWRIGQK KEVTVYRLLT
     AGTIEEKIYH RQIFKQFLTN RVLKDPKQNR FFKSNDLYEL FTLNSPDVSQ GTETSAIFAG
     TGSDVQVPKP PDKRDIHIAE NSSHKKIKSS NSYSTTHMKD SSFKAIETNE ETKGNLEAFN
     QNSYAKDNAQ AATDTNSLNK SKEECLEDDD KCLSQSMPCS AGSSENAERL TAVVAGEGHG
     AAPADARTDL SPTSDTTGSW EKQGAKTEDG QFDNNHSKCI SKTKHKVDML SHDSHKDKSK
     KKHHKDAKFE GKRIPHLVKQ KQFRRENSEE QDSKKNDDYV LQKLFKKSGV HSVMKHDAIM
     DASNADHVLE EAEASRVAQD ALRALRLSRQ QCLGAASGVP TWTGTSGLSG APSGIKSRFG
     QKRNSMLLSS HSTCASPAKK HKDGDTIKKQ NIKKCSSSEH FNGKSGESSS SALDSSSLLA
     RMRARNHLVL PQQTRSEGDE NHQPAPAPVQ GSTEYDELLV DLRNFLAFQA RVDGEASTRE
     LLQEFESKLP AEHSCVFREL LRNICTFHRS PSGEGVWRLK PEFR
//

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