TEB_ARATH
ID TEB_ARATH Reviewed; 2154 AA.
AC Q588V7; O65531;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Helicase and polymerase-containing protein TEBICHI;
DE EC=3.6.4.-;
GN Name=TEB; OrderedLocusNames=At4g32700; ORFNames=F4D11.100;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE
RP SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=16517762; DOI=10.1105/tpc.105.036798;
RA Inagaki S., Suzuki T., Ohto M., Urawa H., Horiuchi T., Nakamura K.,
RA Morikami A.;
RT "Arabidopsis TEBICHI, with helicase and DNA polymerase domains, is required
RT for regulated cell division and differentiation in meristems.";
RL Plant Cell 18:879-892(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19696887; DOI=10.1371/journal.pgen.1000613;
RA Inagaki S., Nakamura K., Morikami A.;
RT "A link among DNA replication, recombination, and gene expression revealed
RT by genetic and genomic analysis of TEBICHI gene of Arabidopsis thaliana.";
RL PLoS Genet. 5:E1000613-E1000613(2009).
RN [5]
RP GENE FAMILY.
RX PubMed=24265739; DOI=10.1371/journal.pone.0078982;
RA Xu R., Zhang S., Huang J., Zheng C.;
RT "Genome-wide comparative in silico analysis of the RNA helicase gene family
RT in Zea mays and Glycine max: a comparison with Arabidopsis and Oryza
RT sativa.";
RL PLoS ONE 8:E78982-E78982(2013).
CC -!- FUNCTION: Required for regulated cell division and differentiation in
CC meristems and embryos, thus modulating adaxial-abaxial polarity.
CC Regulates the progression of cell cycle and DNA replication (e.g. G2/M
CC progression and intrachromosomal recombination) and the expression of
CC genes during development, especially genes nearby the Helitron
CC transposons. {ECO:0000269|PubMed:16517762,
CC ECO:0000269|PubMed:19696887}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in flower buds and flowers, and,
CC to a lower extent, in leaves, stems, seedlings, roots and siliques.
CC {ECO:0000269|PubMed:16517762}.
CC -!- DISRUPTION PHENOTYPE: Morphological defects including short roots,
CC abnormal phyllotaxy with defects in adaxial-abaxial polarity of leaves,
CC highly serrated and asymmetric leaves, and fasciation, as well as
CC defective patterns of cell division and differentiation in meristems
CC and during embryogenesis. Constitutively activated DNA damage responses
CC associated with a defect in G2/M cell cycle progression, but no
CC activation of transcriptionally silenced genes. Hypersensitive to DNA-
CC damaging agents such as the DNA cross-linking agent mitomycin C (MMC)
CC and the DNA-alkylating agent methyl-methane sulfonate (MMS). Reduced
CC frequency of intrachromosomal homologous recombination.
CC {ECO:0000269|PubMed:16517762, ECO:0000269|PubMed:19696887}.
CC -!- MISCELLANEOUS: 'Tebichi' means the 'cloven hoof of a pig' in the
CC regional dialect of the southernmost area of Japan.
CC {ECO:0000305|PubMed:16517762}.
CC -!- SIMILARITY: Belongs to the helicase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA18591.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB79987.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB192295; BAD93700.1; -; mRNA.
DR EMBL; AL022537; CAA18591.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161581; CAB79987.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE86105.1; -; Genomic_DNA.
DR PIR; T04456; T04456.
DR RefSeq; NP_001078482.1; NM_001085013.2.
DR AlphaFoldDB; Q588V7; -.
DR SMR; Q588V7; -.
DR STRING; 3702.AT4G32700.2; -.
DR iPTMnet; Q588V7; -.
DR PaxDb; Q588V7; -.
DR PRIDE; Q588V7; -.
DR ProteomicsDB; 234254; -.
DR EnsemblPlants; AT4G32700.2; AT4G32700.2; AT4G32700.
DR GeneID; 829406; -.
DR Gramene; AT4G32700.2; AT4G32700.2; AT4G32700.
DR KEGG; ath:AT4G32700; -.
DR Araport; AT4G32700; -.
DR TAIR; locus:2125677; AT4G32700.
DR eggNOG; KOG0950; Eukaryota.
DR HOGENOM; CLU_000818_2_0_1; -.
DR InParanoid; Q588V7; -.
DR OMA; NVSFCAE; -.
DR OrthoDB; 179246at2759; -.
DR PhylomeDB; Q588V7; -.
DR PRO; PR:Q588V7; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q588V7; baseline and differential.
DR Genevisible; Q588V7; AT.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IBA:GO_Central.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IMP:UniProtKB.
DR GO; GO:0006261; P:DNA-templated DNA replication; IEA:InterPro.
DR GO; GO:0006302; P:double-strand break repair; IBA:GO_Central.
DR GO; GO:1990067; P:intrachromosomal DNA recombination; IMP:UniProtKB.
DR GO; GO:0009933; P:meristem structural organization; IMP:UniProtKB.
DR GO; GO:0009640; P:photomorphogenesis; IMP:TAIR.
DR GO; GO:2000011; P:regulation of adaxial/abaxial pattern formation; IMP:UniProtKB.
DR GO; GO:1902749; P:regulation of cell cycle G2/M phase transition; IMP:UniProtKB.
DR GO; GO:0010468; P:regulation of gene expression; IGI:UniProtKB.
DR Gene3D; 3.30.420.10; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR001098; DNA-dir_DNA_pol_A_palm_dom.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR002298; DNA_polymerase_A.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR036397; RNaseH_sf.
DR PANTHER; PTHR10133; PTHR10133; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00476; DNA_pol_A; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR PRINTS; PR00868; DNAPOLI.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00482; POLAc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cell cycle; Cell division; Developmental protein; Helicase;
KW Hydrolase; Leucine-rich repeat; Nucleotide-binding; Reference proteome;
KW Repeat.
FT CHAIN 1..2154
FT /note="Helicase and polymerase-containing protein TEBICHI"
FT /id="PRO_0000429827"
FT DOMAIN 525..717
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 757..949
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REPEAT 1304..1331
FT /note="LRR 1"
FT REPEAT 1477..1501
FT /note="LRR 2"
FT REPEAT 1730..1753
FT /note="LRR 3"
FT REPEAT 1826..1853
FT /note="LRR 4"
FT REPEAT 1855..1873
FT /note="LRR 5"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 160..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 467..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 666..687
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1323..1345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 639..642
FT /note="DEAH box"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 666..684
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1325..1339
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 538..545
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 2154 AA; 238523 MW; A31A536E731EFF9C CRC64;
MDSDSSKSRI DQFYVSKKRK HQSPNLKSGR NEKNVKVTGE RSPGDKGTLD SYLKASLDDK
STTNSGLQAR QEAFTRKLDL EVSASSVGQN IHPCLPKPVS FATFKECLGQ NGSQDLHKEG
VAAETHATDG LLCANQKDNS ELRDFATSFL SLYCSGVQSV VGSPPHQKEN ELKRRSSSSS
LAQDIQISHK RRCESENIPS LDDLTNPLGS KPESLARNGN NRDKPVSDPT KKMPSNESVE
IPMGLRKCSK APESSAHLTE FHTPGSAIKS CPVGTPKSGC GSSMFSPGEA FWNEAIQVAD
GLTIPIENFG SVEAKVRDQH VTILSCSKKT DKCTEKLERS LDLDEIRVKD KDAIGFSKVV
EKHGRDFNKE VYQLPVKNLE LLFQDKNING GIQERCASFD QNNITLGSSR ISESAFVGNK
GCENLDIANN AQADKGLIGK MYPEPEGKKV LLCEENRGVR SVSMISNMRK PVGSSESEES
HTPSSSHRNY DGLSLSTWLP SEVCSVYNKK GISKLYPWQV ECLQVDGVLQ KRNLVYCAST
SAGKSFVAEV LMLRRVIRTG KMALLVLPYV SICAEKAEHL EVLLEPLGKH VRSYYGNQGG
GTLPKDTSVA VCTIEKANSL INRLLEEGRL SELGIIVIDE LHMVGDQHRG YLLELMLTKL
RYAAGEGSSE SSSGESSGTS SGKADPAHGL QIVGMSATMP NVGAVADWLQ AALYQTEFRP
VPLEEYIKVG STIYNKKMEV VRTIPKAADM GGKDPDHIVE LCNEVVQEGN SVLIFCSSRK
GCESTARHIS KLIKNVPVNV DGENSEFMDI RSAIDALRRS PSGVDPVLEE TLPSGVAYHH
AGLTVEEREI VETCYRKGLV RVLTATSTLA AGVNLPARRV IFRQPMIGRD FIDGTRYKQM
SGRAGRTGID TKGDSVLICK PGELKRIMAL LNETCPPLQS CLSEDKNGMT HAILEVVAGG
IVQTAKDIHR YVRCTLLNST KPFQDVVKSA QDSLRWLCHR KFLEWNEETK LYTTTPLGRG
SFGSSLCPEE SLIVLDDLLR AREGLVMASD LHLVYLVTPI NVGVEPNWEL YYERFMELSP
LEQSVGNRVG VVEPFLMRMA HGATVRTLNR PQDVKKNLRG EYDSRHGSTS MKMLSDEQML
RVCKRFFVAL ILSKLVQEAS VTEVCEAFKV ARGMVQALQE NAGRFSSMVS VFCERLGWHD
LEGLVAKFQN RVSFGVRAEI VELTSIPYIK GSRARALYKA GLRTSQAIAE ASIPEIVKAL
FESSAWAAEG TGQRRIHLGL AKKIKNGARK IVLEKAEEAR AAAFSAFKSL GLDVNELSKP
LPLAPASSLN GQETTERDIS RGSVGPDGLQ QSIEGHMECE NFDMDNHREK PSEVLGDATL
GVSSEINLTS RLPNFRPIGT AVGTNGPSAV SILSSDTFPI PVYDNREIKP KDNVEQHLTR
NDHIPLSSNK DGTGEKGPVT AGNISGGFDS FLELWGSAGE FFFDLHYNKL QDLNSRISYE
IHGIAICWNC SPVYYVNLNK DLPNLECVEK QKLIEDAVIG KSEVLASHNM LDVIKSRWNK
ISKIMGNVNT RKFTWNLKVQ IQVLKSPAIS IQRCTRLNLP EGIRDELVDG SWLMMPPLHT
SHTIDMSIVI WILWPDEERH SNPNIDKEVK KRLSPEAAEA ANRSGRWRNQ IRRVAHNGCC
RRVAQTRALC SALWKILVSE ELLQALTTIE MPLVNVLADM ELWGIGIDIE GCLRARNILR
DKLRSLEKKA FELAGMTFSL HNPADIANVL FGQLKLPIPE NQSKGKLHPS TDKHCLDLLR
NEHPVVPIIK EHRTLAKLLN CTLGSICSLA KLRLSTQRYT LHGRWLQTST ATGRLSIEEP
NLQSVEHEVE FKLDKNGRDV SSDADRYKIN ARDFFVPTQE NWLLLTADYS QIELRLMAHF
SRDSSLISKL SQPEGDVFTM IAAKWTGKAE DSVSPHDRDQ TKRLIYGILY GMGANRLAEQ
LECTSDEAKE KIRSFKSSFP AVTSWLNETI SFCQEKGYIQ TLKGRRRFLS KIKFGNAKEK
SKAQRQAVNS MCQGSAADII KIAMINIYSA IAEDVDTAAS SSSSETRFHM LKGRCRILLQ
VHDELVLEVD PSYVKLAAML LQTSMENAVS LLVPLHVKLK VGKTWGSLEP FQTD
