ID A0A444EMA5_ENSVE Unreviewed; 439 AA.
AC A0A444EMA5;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Ribonuclease {ECO:0000256|RuleBase:RU003515};
DE EC=3.1.26.4 {ECO:0000256|RuleBase:RU003515};
GN ORFNames=GW17_00024885 {ECO:0000313|EMBL:RWW11509.1};
OS Ensete ventricosum (Abyssinian banana) (Musa ensete).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Zingiberales; Musaceae; Ensete.
OX NCBI_TaxID=4639 {ECO:0000313|EMBL:RWW11509.1, ECO:0000313|Proteomes:UP000288739};
RN [1] {ECO:0000313|EMBL:RWW11509.1, ECO:0000313|Proteomes:UP000288739}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Bedadit {ECO:0000313|Proteomes:UP000288739};
RC TISSUE=Leaf {ECO:0000313|EMBL:RWW11509.1};
RX PubMed=29896517; DOI=10.1016/j.dib.2018.03.026;
RA Yemataw Z., Muzemil S., Ambachew D., Tripathi L., Tesfaye K., Chala A.,
RA Farbos A., O'Neill P., Moore K., Grant M., Studholme D.J.;
RT "Genome sequence data from 17 accessions of Ensete ventricosum, a staple
RT food crop for millions in Ethiopia.";
RL Data Brief 18:285-293(2018).
CC -!- FUNCTION: Endonuclease that specifically degrades the RNA of RNA-DNA
CC hybrids. {ECO:0000256|RuleBase:RU003515}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4;
CC Evidence={ECO:0000256|ARBA:ARBA00000077, ECO:0000256|PROSITE-
CC ProRule:PRU01319, ECO:0000256|RuleBase:RU003515};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|PROSITE-ProRule:PRU01319};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PROSITE-ProRule:PRU01319};
CC Note=Manganese or magnesium. Binds 1 divalent metal ion per monomer in
CC the absence of substrate. May bind a second metal ion after substrate
CC binding. {ECO:0000256|PROSITE-ProRule:PRU01319};
CC -!- SIMILARITY: Belongs to the RNase HII family. Eukaryotic subfamily.
CC {ECO:0000256|ARBA:ARBA00007058}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. {ECO:0000256|PROSITE-ProRule:PRU00283}.
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:RWW11509.1}.
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DR EMBL; JTFG03002871; RWW11509.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A444EMA5; -.
DR Proteomes; UP000288739; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR GO; GO:0003777; F:microtubule motor activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR GO; GO:0006401; P:RNA catabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd07181; RNase_HII_eukaryota_like; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR Gene3D; 1.10.10.460; Ribonuclease hii. Domain 2; 1.
DR InterPro; IPR001752; Kinesin_motor_dom.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR004649; RNase_H2_suA.
DR InterPro; IPR001352; RNase_HII/HIII.
DR InterPro; IPR024567; RNase_HII/HIII_dom.
DR InterPro; IPR023160; RNase_HII_hlx-loop-hlx_cap_dom.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR NCBIfam; TIGR00729; ribonuclease HII; 1.
DR PANTHER; PTHR10954; RIBONUCLEASE H2 SUBUNIT A; 1.
DR PANTHER; PTHR10954:SF7; RIBONUCLEASE H2 SUBUNIT A; 1.
DR Pfam; PF00225; Kinesin; 1.
DR Pfam; PF01351; RNase_HII; 1.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
DR PROSITE; PS51975; RNASE_H_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00283};
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759, ECO:0000256|PROSITE-
KW ProRule:PRU01319};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01319};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU01319}; Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW Motor protein {ECO:0000256|ARBA:ARBA00023175, ECO:0000256|PROSITE-
KW ProRule:PRU00283};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|PROSITE-
KW ProRule:PRU01319};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00283};
KW Reference proteome {ECO:0000313|Proteomes:UP000288739}.
FT DOMAIN 25..249
FT /note="RNase H type-2"
FT /evidence="ECO:0000259|PROSITE:PS51975"
FT DOMAIN 267..439
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT BINDING 31
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01319"
FT BINDING 32
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01319"
FT BINDING 140
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01319"
FT BINDING 382..389
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 439 AA; 49421 MW; DA67712A5C366DD8 CRC64;
MLSNEDLLWD NLPRVVTRID YSREPCIMGI DEAGRGPVLG PMVYGCLYCA LSYQKILTTL
NFADSKTLKE EKREELFENL KADGSIGWEV DVIDPRELSA KMLKRSVTKI NLNEISHNSA
IGLVKRVLDM GVLLTEVYVD TVGDAEKYRV KLSERFPGVK FVVAKKADSL YPVVSGASIV
AKVTRDRALR NWVLDETAEN MQRNFGSGYP GDPETKAWLN HHKHMVFGFP TIVRFSWGTC
TPYFKDFVEV VCLPEMGSRH EKEKAVNVQV LLRCRYDNDT PPFFALRSAK CGLGPFNEDE
LRNNAPQVVT CNDYQREVSV TQTIAGKQFD RVFTFDKVRF IDHLFSQVFG PSAKQRDLYD
QAVVPIVNEV LEGFNCTIFA YGQTGTGKTY TMEGECRKAK SGPKGQLPAD AGVIPRAVKQ
IFDTLESQNA EYSVKKVKS
//
