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Database: UniProt
Entry: A0A091FVP2_9AVES
LinkDB: A0A091FVP2_9AVES
Original site: A0A091FVP2_9AVES 
ID   A0A091FVP2_9AVES        Unreviewed;      1143 AA.
AC   A0A091FVP2;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Transcription termination factor 2 {ECO:0000313|EMBL:KFO73259.1};
DE   Flags: Fragment;
GN   ORFNames=N303_06871 {ECO:0000313|EMBL:KFO73259.1};
OS   Cuculus canorus (common cuckoo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Cuculiformes; Cuculidae; Cuculus.
OX   NCBI_TaxID=55661 {ECO:0000313|EMBL:KFO73259.1, ECO:0000313|Proteomes:UP000053760};
RN   [1] {ECO:0000313|EMBL:KFO73259.1, ECO:0000313|Proteomes:UP000053760}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N303 {ECO:0000313|EMBL:KFO73259.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KL447417; KFO73259.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091FVP2; -.
DR   STRING; 55661.A0A091FVP2; -.
DR   Proteomes; UP000053760; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProt.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   CDD; cd18072; DEXHc_TTF2; 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; IPR002464; DNA/RNA_helicase_DEAH_CS.
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; PTHR45626:SF54; TRANSCRIPTION TERMINATION FACTOR 2; 1.
DR   PANTHER; PTHR45626; TRANSCRIPTION TERMINATION FACTOR 2-RELATED; 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; PS00690; DEAH_ATP_HELICASE; 1.
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   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053760}.
FT   DOMAIN          559..764
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          972..1138
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          137..269
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          425..473
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        138..178
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        191..216
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        247..269
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        452..473
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFO73259.1"
FT   NON_TER         1143
FT                   /evidence="ECO:0000313|EMBL:KFO73259.1"
SQ   SEQUENCE   1143 AA;  125807 MW;  22567ABA7344821E CRC64;
     GSPCLLKTGV RGGPNQGRSF YVCGVRSPAP CGFVLPAPIP ASHCLIHEGC MVELQVLIQH
     QGKDEYQLLY RCTKGYSNGK TWCGSIPWQD PKATKVSKAL ESQHNIAPVF NPSGQRNPFK
     VIDKNCDPSC WKQIKQGNGE ESRAKGVKAE KASMLASHKE KKSIPASSIE KEPLEGLKTK
     NKQSTGNKTD KNTLWEKEKY GGSGRESKKS SESVEKEPGG SSKLFPLSLG KQSASTKPVE
     DKQLGGKSLN SCEDKETRKK EYIGGKNGEM KLMSKEDMIS PAAGKDAFQH PAQKGGGVAA
     PSRTQIRPEL GQAAGAVSGR DTDGVGFVYT SSGKSEPEES VEDLQSREIL AGKSGTSLPG
     AAASHHVEGL QDPKALYNHL VVQLRQKKSV LATVNTQRLP DKGERLRKQV QDLEAALSAF
     NISTAGEHST SSDYHEESLP TQLDRPGGTK LITPQLLQNP TSGTSSYSHS HTSAATTLGS
     SEYGSSHGFG MNSGVQNLYG GRMTEDRIRA VHSATSEAIN HLHKSLESCP TEQTTAEDPS
     GLKVPLLPHQ KQALAWLLWR ESQRPCGGIL ADDMGLGKTL TMIALILTQK QLNTEKRKEE
     KLEIWLSKND SAVIPSHSTL IICPASLIHH WKKEIDRRVS YGKLRVCLYH GSNREKHAEV
     LTGYDIVVTT YSLLSKEVPT SKEEGEVPAE DHDVRSGSSP CSPLLRIAWA RIILDEAHNI
     KNPKIQTSIA VCKLRASARW AVTGTPIQNN LLDMYSLLRF LRCSPFDEYK VWKYQVDNNT
     KKGGERLSLL TRSLLLRRTK DQLDSAGKPL VALPQRSTQL HQLKLSPEEQ SVYNVLFARS
     RSTLQSYLQR QEQKNEGREY AGGNPFERVA QDFGINQKEF LAGSQSAPQV SSTVHVLSML
     LRLRQCCCHL SLLKVALDQT NLHSEGLTLS IEEQLSALTL TELQTPDYKS TVYLSGTAFK
     TDLFEITRES TKIAHLLAEL KTIQSHSEPQ KSVVVSQWTS MLKVVSVHLQ RLGLKYATVD
     GSVNPKQRMD VVEEFNNNPR GPQVLLVSLL AGGVGLNLTG GNHLFLLDMH WNPALEDQAC
     DRIYRVGQQK DVVIHRFVCE GTVEEKILQL QRSKKVLAQQ VLSGKGETFT KLTLDDLKNL
     FGI
//
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