ID A0A9R1PHJ0_TRITD Unreviewed; 994 AA.
AC A0A9R1PHJ0;
DT 13-SEP-2023, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2023, sequence version 1.
DT 10-JUN-2026, entry version 14.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:VAH43450.1};
GN ORFNames=TRITD_2Bv1G059380 {ECO:0000313|EMBL:VAH43450.1};
OS Triticum turgidum subsp. durum (Durum wheat) (Triticum durum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4567 {ECO:0000313|EMBL:VAH43450.1, ECO:0000313|Proteomes:UP000324705};
RN [1] {ECO:0000313|Proteomes:UP000324705}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Svevo {ECO:0000313|Proteomes:UP000324705};
RX PubMed=34830231; DOI=10.3390/ijms222212349;
RA Muslu T., Akpinar B.A., Biyiklioglu-Kaya S., Yuce M., Budak H.;
RT "Comparative analysis of coding and non-coding features within insect
RT tolerance loci in wheat with their homologs in cereal genomes.";
RL Int. J. Mol. Sci. 22:12349-12349(2021).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the DExH box helicase family. SKI2 subfamily.
CC {ECO:0000256|ARBA:ARBA00061045}.
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DR EMBL; LT934114; VAH43450.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A9R1PHJ0; -.
DR Gramene; TRITD2Bv1G059380.12; TRITD2Bv1G059380.12; TRITD2Bv1G059380.
DR Proteomes; UP000324705; Chromosome 2B.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
DR GO; GO:0000460; P:maturation of 5.8S rRNA; IEA:TreeGrafter.
DR GO; GO:0006401; P:RNA catabolic process; IEA:InterPro.
DR CDD; cd18024; DEXHc_Mtr4-like; 1.
DR CDD; cd18795; SF2_C_Ski2; 1.
DR FunFam; 3.40.50.300:FF:000083; ATP-dependent RNA helicase DOB1; 1.
DR FunFam; 3.40.50.300:FF:000141; ATP-dependent RNA helicase DOB1; 1.
DR FunFam; 1.10.3380.30:FF:000006; DExH-box ATP-dependent RNA helicase DExH10; 1.
DR FunFam; 2.40.30.300:FF:000001; Mtr4 exosome RNA helicase; 1.
DR Gene3D; 1.10.3380.30; -; 1.
DR Gene3D; 2.40.30.300; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR025696; Beta-barrel_MTR4.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C-like.
DR InterPro; IPR048392; MTR4-like_stalk.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR050699; RNA-DNA_Helicase.
DR InterPro; IPR016438; SKI2-like.
DR InterPro; IPR012961; Ski2/MTR4_C.
DR PANTHER; PTHR12131; ATP-DEPENDENT RNA AND DNA HELICASE; 1.
DR PANTHER; PTHR12131:SF7; EXOSOME RNA HELICASE MTR4; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF08148; DSHCT; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF21408; MTR4-like_stalk; 1.
DR Pfam; PF13234; MTR4_beta-barrel; 1.
DR PIRSF; PIRSF005198; Antiviral_helicase_SKI2; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM01142; DSHCT; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000324705}.
FT DOMAIN 93..249
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 327..528
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 295..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 665..687
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..13
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 994 AA; 111732 MW; 818BF81D4D39EFE2 CRC64;
MEEVENSSKR KAPELSSEDN SSAAVLDEQQ SLPGSTAKRP NLARSCIHEV AVPNGYDLSK
DEAVHGTLSN PAFNGEMAKT YPFQLDPFQS ISIACLERNE SVLVSAHTSA GKTAIAEYAI
AMSFRDKQRV IYTSPLKALS NQKYRELSQE FSDVGLMTGD VTLQPNATCL VMTTEILRAM
LYRGSEVIKE VGWVIFDEIH YMKDRERGVV WEESIVFLPP AIKMVFLSAT MSNATEFAEW
ICNLHKQPCH VVYTDFRPTP LQHYVFPIGG SGLYLVVDEN GQFREDNFLK LQDTFAKQPS
QPDGRKGGGP KASGRIAKGG NASGTSDIYR IVKMIMDRKF QPVIIFSFSR RECEHHAMSM
SKLDFNTQEE KDNIEQVFRS AIFCLSEEDR GLPAIELMLP LLKRGIAVHH SGLLPLIKEL
VELLFQEGLV KALFATETFA MGLNMPAKTV VFTSVKKWDG DSNRYIASGE YIQMSGRAGR
RGMDARGICV IMIDEKMEMS VIKDMVLGKP APLISTFRLS YYTILNLLSR AEGQFTAEHV
IRNSFHQFQY EKALPEVIQK ITKLENEATL LDSSGENDLA EYHKLGLDIS ELEKKIMSEM
IRPERALLYL VPGRLVKVRD GSTDWGWGVV VNVVKKPPAS STLPPALSAP RNNYIVDTLL
HCSSSSSENG ANGPRSKPCP PRQGEKGEMH VVPVPLPLLS GLSSVRISIP TDLRPPEARQ
NILFAVQELG KRYPQGLPKL HPITDMGIEE PELVDLVHKL DGLEQKLCSH PLNKSDQSEQ
QLSWYQRKAE LNHEIQQLKS KMRDSQLQKF RDELKNRSRV LKMLGHIDTD GVLQLKGRAA
CLIDTGDELL ITELMFNGTF NELDHHQVAS VVSCFVPCEK SSEQIRLRNE LSKPMMQLSE
AARKIAEVQR ECKLDVNVEE YVESTCKPYL MDVIYCWSKG ATFGEVIEMT DIFEGSIIRL
VRRLDEFLNQ VRVAYATPYQ YLLSPFADTC HLGY
//
