SMBP2_RAT
ID SMBP2_RAT Reviewed; 988 AA.
AC Q9EQN5;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=DNA-binding protein SMUBP-2;
DE EC=3.6.4.12 {ECO:0000250|UniProtKB:P38935};
DE EC=3.6.4.13 {ECO:0000250|UniProtKB:P38935};
DE AltName: Full=ATP-dependent helicase IGHMBP2;
DE AltName: Full=Antifreeze enhancer-binding protein ortholog;
DE Short=AEP;
GN Name=Ighmbp2; Synonyms=Smbp2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DNA-BINDING, AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley;
RX PubMed=11106437; DOI=10.1046/j.1432-1327.2000.01836.x;
RA Miao M., Chan S.-L., Fletcher G.L., Hew C.L.;
RT "The rat ortholog of the presumptive flounder antifreeze enhancer-binding
RT protein is a helicase domain-containing protein.";
RL Eur. J. Biochem. 267:7237-7246(2000).
CC -!- FUNCTION: 5' to 3' helicase that unwinds RNA and DNA duplexes in an
CC ATP-dependent reaction (By similarity). Specific to 5'-phosphorylated
CC single-stranded guanine-rich sequences (By similarity). May play a role
CC in RNA metabolism, ribosome biogenesis or initiation of translation (By
CC similarity). May play a role in regulation of transcription
CC (PubMed:11106437). Interacts with tRNA-Tyr (By similarity).
CC {ECO:0000250|UniProtKB:P38935, ECO:0000269|PubMed:11106437}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC Evidence={ECO:0000250|UniProtKB:P38935};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC Evidence={ECO:0000250|UniProtKB:P38935};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC Evidence={ECO:0000250|UniProtKB:P38935};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC Evidence={ECO:0000250|UniProtKB:P38935};
CC -!- SUBUNIT: Homooligomer (By similarity). Interacts with RUVBL1 (By
CC similarity). Interacts with RUVBL2 (By similarity). Interacts with
CC GTF3C1 (By similarity). Interacts with ABT1 (By similarity). Interacts
CC with ribosomes (By similarity). {ECO:0000250|UniProtKB:P38935}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P38935}. Cytoplasm
CC {ECO:0000250|UniProtKB:P38935}. Cell projection, axon
CC {ECO:0000250|UniProtKB:P40694}.
CC -!- TISSUE SPECIFICITY: Expressed in liver, skin, muscle, heart, brain,
CC spleen and kidney. {ECO:0000269|PubMed:11106437}.
CC -!- DOMAIN: The R3H domain recognizes phosphorylated 5'-ends of single-
CC stranded nucleic acids which promotes binding of nucleic acids and
CC stimulates ATPase activity. {ECO:0000250|UniProtKB:P38935}.
CC -!- SIMILARITY: Belongs to the DNA2/NAM7 helicase family. {ECO:0000305}.
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DR EMBL; AF199411; AAG28561.1; -; mRNA.
DR RefSeq; NP_113774.1; NM_031586.1.
DR AlphaFoldDB; Q9EQN5; -.
DR SMR; Q9EQN5; -.
DR STRING; 10116.ENSRNOP00000018487; -.
DR PaxDb; Q9EQN5; -.
DR PRIDE; Q9EQN5; -.
DR GeneID; 29532; -.
DR KEGG; rno:29532; -.
DR UCSC; RGD:68325; rat.
DR CTD; 3508; -.
DR RGD; 68325; Ighmbp2.
DR eggNOG; KOG1803; Eukaryota.
DR InParanoid; Q9EQN5; -.
DR OrthoDB; 633768at2759; -.
DR PhylomeDB; Q9EQN5; -.
DR PRO; PR:Q9EQN5; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0030424; C:axon; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0030426; C:growth cone; ISO:RGD.
DR GO; GO:0043025; C:neuronal cell body; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISO:RGD.
DR GO; GO:0043139; F:5'-3' DNA helicase activity; ISS:UniProtKB.
DR GO; GO:0032574; F:5'-3' RNA helicase activity; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISS:UniProtKB.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; ISS:UniProtKB.
DR GO; GO:0008186; F:ATP-dependent activity, acting on RNA; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:RGD.
DR GO; GO:0036121; F:double-stranded DNA helicase activity; ISS:UniProtKB.
DR GO; GO:1990955; F:G-rich single-stranded DNA binding; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0043621; F:protein self-association; ISS:UniProtKB.
DR GO; GO:0043022; F:ribosome binding; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR GO; GO:0003697; F:single-stranded DNA binding; ISS:UniProtKB.
DR GO; GO:0003727; F:single-stranded RNA binding; ISS:UniProtKB.
DR GO; GO:0000049; F:tRNA binding; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0032508; P:DNA duplex unwinding; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:RGD.
DR GO; GO:0050905; P:neuromuscular process; ISO:RGD.
DR GO; GO:0010501; P:RNA secondary structure unwinding; ISO:RGD.
DR GO; GO:0021522; P:spinal cord motor neuron differentiation; ISO:RGD.
DR CDD; cd02641; R3H_Smubp-2_like; 1.
DR CDD; cd18808; SF1_C_Upf1; 1.
DR Gene3D; 3.30.1370.50; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR Gene3D; 4.10.1110.10; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR035896; AN1-like_Znf.
DR InterPro; IPR041679; DNA2/NAM7-like_C.
DR InterPro; IPR041677; DNA2/NAM7_AAA_11.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001374; R3H_dom.
DR InterPro; IPR036867; R3H_dom_sf.
DR InterPro; IPR034072; R3H_Smubp-2.
DR InterPro; IPR004483; SMUBP-2/Hcs1-like.
DR InterPro; IPR000058; Znf_AN1.
DR Pfam; PF13086; AAA_11; 1.
DR Pfam; PF13087; AAA_12; 1.
DR Pfam; PF01424; R3H; 1.
DR Pfam; PF01428; zf-AN1; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00393; R3H; 1.
DR SMART; SM00154; ZnF_AN1; 1.
DR SUPFAM; SSF118310; SSF118310; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF82708; SSF82708; 1.
DR TIGRFAMs; TIGR00376; TIGR00376; 1.
DR PROSITE; PS51061; R3H; 1.
DR PROSITE; PS51039; ZF_AN1; 1.
PE 1: Evidence at protein level;
KW Acetylation; Activator; ATP-binding; Cell projection; Coiled coil;
KW Cytoplasm; DNA-binding; Helicase; Hydrolase; Metal-binding;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Ribonucleoprotein; RNA-binding; Transcription; Transcription regulation;
KW tRNA-binding; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P38935"
FT CHAIN 2..988
FT /note="DNA-binding protein SMUBP-2"
FT /id="PRO_0000372431"
FT DOMAIN 721..784
FT /note="R3H"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00382"
FT ZN_FING 884..933
FT /note="AN1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT REGION 637..783
FT /note="SS DNA-binding"
FT /evidence="ECO:0000250"
FT REGION 651..722
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 765..820
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 835..872
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 943..988
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 957..986
FT /evidence="ECO:0000255"
FT MOTIF 857..861
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 698..717
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 765..779
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 791..806
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 835..850
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 952..988
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 213..220
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00499"
FT BINDING 402
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q92900"
FT BINDING 441
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q92900"
FT BINDING 570
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q92900"
FT BINDING 890
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 895
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 906
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 909
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 914
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 917
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 923
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 925
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P38935"
FT MOD_RES 797
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P40694"
FT MOD_RES 800
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P40694"
SQ SEQUENCE 988 AA; 108440 MW; 624ED6122F8C8D8A CRC64;
MASYTVESFV AQQLQLLELE RDAEVEERRS WQEHSSLKEL QSRGVCLLKL QVSGQRTGLY
GQRLVTFEPR KFGPAVVLPS NSFTSGDIVG LYDTNESSQL ATGVLTRITQ KSVIVAFDES
HDFQLNLDRE NTYRLLKLAN DVTYKRLKKA LLTLKKYHSG PASSLIDVLL GGSTPSPATE
IPPLTFYNTT LDPSQKEAVS FALAQKEVAI IHGPPGTGKT TTVVEIILQA VKQGLKVLCC
APSNIAVDNL VERLALCKKQ ILRLGHPARL LESVQQHSLD AVLARSDNAQ IVADIRRDID
QVFGKNKKTQ DKREKSNFRN EIKLLRKELK EREEAAIVQS LSAADVVLAT NTGASTDGPL
KLLPEDYFDV VVVDECAQAL EASCWIPLLK APKCILAGDH KQLPPTTVSH KAALAGLSRS
LMERLAEKHG AAVVRMLAVQ YRMHQAITRW ASEAMYHGQL TAHPSVAGHL LKDLPGVADT
EETSVPLLLI DTAGCGLLEL EEEDSQSKGN PGEVRLVTLH IQALVDAGVQ AGDIAVIAPY
NLQVDLLRQS LSNKHPELEI KSVDGFQGRE KEAVILTFVR SNRKGEVGFL AEDRRINVAV
TRARRHVAVI CDSHTVNNHA FLKTLVDYFT EHGEVRTAFE YLDDIVPENY THEGSRSHSC
APKPKCPTTS VRKPASAQES RQEARAATGH SRRKPSEKPL GSQVQPQHSS KANGSDRTGG
TDRTEHFRAM IEEFVASKEA QLEFPTSLSS HDRLRVHQLA EEFGLKHDST GEGKARHITV
SRRSPAGSGS ATPQPPSPPS PAQAEPEPQV EQPVGQPHGS TQLDLKALHL ERLQRQQGCQ
AQSQLGGGSR PQKAPQKKKK KEPKGPAMAL PSEEDFDALV SAVVKADNTC SFTKCSASTT
TLGQFCMHCS RRYCLSHHLP EIHGCGEKAR AHARQRISRE GVLYAGSGTK DRALDPAKRA
QLQRKLDKKL GELSSQRTSK KKEKERGT
