HARB1_XENLA
ID HARB1_XENLA Reviewed; 347 AA.
AC Q5U538;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 50.
DE RecName: Full=Putative nuclease HARBI1;
DE EC=3.1.-.-;
DE AltName: Full=Harbinger transposase-derived nuclease;
GN Name=harbi1;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP TISSUE SPECIFICITY.
RX PubMed=15169610; DOI=10.1089/104454904323090949;
RA Kapitonov V.V., Jurka J.;
RT "Harbinger transposons and an ancient HARBI1 gene derived from a
RT transposase.";
RL DNA Cell Biol. 23:311-324(2004).
CC -!- FUNCTION: Transposase-derived protein that may have nuclease activity
CC (Potential). Does not have transposase activity (By similarity).
CC {ECO:0000250, ECO:0000305}.
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000305};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Detected in adult eye and in embryo.
CC {ECO:0000269|PubMed:15169610}.
CC -!- SIMILARITY: Belongs to the HARBI1 family. {ECO:0000305}.
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DR EMBL; BC084846; AAH84846.1; -; mRNA.
DR RefSeq; NP_001088509.1; NM_001095040.1.
DR RefSeq; XP_018112355.1; XM_018256866.1.
DR RefSeq; XP_018112356.1; XM_018256867.1.
DR RefSeq; XP_018112357.1; XM_018256868.1.
DR RefSeq; XP_018112358.1; XM_018256869.1.
DR RefSeq; XP_018112359.1; XM_018256870.1.
DR AlphaFoldDB; Q5U538; -.
DR DNASU; 495378; -.
DR GeneID; 495378; -.
DR KEGG; xla:495378; -.
DR CTD; 495378; -.
DR Xenbase; XB-GENE-6077434; harbi1.L.
DR OrthoDB; 698280at2759; -.
DR Proteomes; UP000186698; Chromosome 4L.
DR Bgee; 495378; Expressed in egg cell and 19 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004518; F:nuclease activity; IEA:UniProtKB-KW.
DR InterPro; IPR045249; HARBI1-like.
DR InterPro; IPR026103; HARBI1_animal.
DR InterPro; IPR027806; HARBI1_dom.
DR PANTHER; PTHR22930; PTHR22930; 1.
DR Pfam; PF13359; DDE_Tnp_4; 1.
DR PRINTS; PR02086; PUTNUCHARBI1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Hydrolase; Metal-binding; Nuclease; Nucleus; Reference proteome.
FT CHAIN 1..347
FT /note="Putative nuclease HARBI1"
FT /id="PRO_0000263617"
FT DOMAIN 148..300
FT /note="DDE Tnp4"
FT /evidence="ECO:0000255"
FT BINDING 149
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT BINDING 199
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT BINDING 225
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT BINDING 261
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
SQ SEQUENCE 347 AA; 38928 MW; 8BD4E5DB2FF33D0E CRC64;
MAVPITVLDC DLLLYGRGHR TLDRFRLDDV TDDYLVTTYG FPRPFIDYLV DLLGASLSRP
THRSRAISPE TQIMAALGFY TSGSFQTRMG DTIGISQASM SRCVTNVTEA LVERASQFIS
FPRDERSVQG LKDEFYNLAG VPGVLGVVDC TQVNIKAPNS EDLSYVNSRG LHSLNCLLVC
DARGSLLWAE TSRLGSMQDN AVLHQSELSG LFETKMHKQG WLLADNAFIL RPWLMTPVQI
PESPSDYRYN MAHTATHSVM ERTQRSLRLR FRCLDGSRAT LQYSPEKSAQ IVLACCILHN
IALQHDLDIV SESGATSLEP EEECVHMEPL ESEAYRMRQE LILTHFS