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Database: UniProt
Entry: Q5VCK9_9SAUR
LinkDB: Q5VCK9_9SAUR
Original site: Q5VCK9_9SAUR 
ID   Q5VCK9_9SAUR            Unreviewed;       906 AA.
AC   Q5VCK9;
DT   07-DEC-2004, integrated into UniProtKB/TrEMBL.
DT   07-DEC-2004, sequence version 1.
DT   13-SEP-2023, entry version 86.
DE   RecName: Full=V(D)J recombination-activating protein 1 {ECO:0000256|ARBA:ARBA00021277, ECO:0000256|RuleBase:RU366024};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483, ECO:0000256|RuleBase:RU366024};
DE            EC=3.1.-.- {ECO:0000256|RuleBase:RU366024};
DE   Flags: Fragment;
GN   Name=RAG1 {ECO:0000313|EMBL:AAT36607.1};
OS   Rieppeleon kerstenii.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Iguania; Acrodonta; Chamaeleonidae; Rieppeleon.
OX   NCBI_TaxID=338557 {ECO:0000313|EMBL:AAT36607.1};
RN   [1] {ECO:0000313|EMBL:AAT36607.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=23 {ECO:0000313|EMBL:AAT36607.1};
RX   PubMed=15347522; DOI=10.1098/rspb.2004.2806;
RA   Matthee C.A., Tilbury C.R., Townsend T.;
RT   "A phylogenetic review of the African leaf chameleons: genus Rhampholeon
RT   (Chamaeleonidae): the role of vicariance and climate change in
RT   speciation.";
RL   Proc. R. Soc. B 271:1967-1975(2004).
CC   -!- FUNCTION: Catalytic component of the RAG complex, a multiprotein
CC       complex that mediates the DNA cleavage phase during V(D)J
CC       recombination. V(D)J recombination assembles a diverse repertoire of
CC       immunoglobulin and T-cell receptor genes in developing B and T-
CC       lymphocytes through rearrangement of different V (variable), in some
CC       cases D (diversity), and J (joining) gene segments. In the RAG complex,
CC       RAG1 mediates the DNA-binding to the conserved recombination signal
CC       sequences (RSS) and catalyzes the DNA cleavage activities by
CC       introducing a double-strand break between the RSS and the adjacent
CC       coding segment. RAG2 is not a catalytic component but is required for
CC       all known catalytic activities. DNA cleavage occurs in 2 steps: a first
CC       nick is introduced in the top strand immediately upstream of the
CC       heptamer, generating a 3'-hydroxyl group that can attack the
CC       phosphodiester bond on the opposite strand in a direct
CC       transesterification reaction, thereby creating 4 DNA ends: 2 hairpin
CC       coding ends and 2 blunt, 5'-phosphorylated ends.
CC       {ECO:0000256|RuleBase:RU366024}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC         [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC         cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC         EC=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900,
CC         ECO:0000256|RuleBase:RU366024};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946,
CC         ECO:0000256|RuleBase:RU366024};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|RuleBase:RU366024};
CC       Note=Binds 1 divalent metal cation per subunit. Mg(2+) or Mn(2+).
CC       {ECO:0000256|RuleBase:RU366024};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|RuleBase:RU366024}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00820,
CC       ECO:0000256|RuleBase:RU366024}.
CC   -!- DOMAIN: The NBD (nonamer binding) DNA-binding domain mediates the
CC       specific binding to the nonamer RSS motif by forming a tightly
CC       interwoven homodimer that binds and synapses 2 nonamer elements, with
CC       each NBD making contact with both DNA molecules. Each RSS is composed
CC       of well-conserved heptamer (consensus 5'-CACAGTG-3') and nonamer
CC       (consensus 5'-ACAAAAACC-3') sequences separated by a spacer of either
CC       12 bp or 23 bp. {ECO:0000256|PROSITE-ProRule:PRU00820}.
CC   -!- SIMILARITY: Belongs to the RAG1 family. {ECO:0000256|PROSITE-
CC       ProRule:PRU00820, ECO:0000256|RuleBase:RU366024}.
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DR   EMBL; AY524965; AAT36607.1; -; Genomic_DNA.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0042393; F:histone binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0042803; F:protein homodimerization activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0030183; P:B cell differentiation; IEA:UniProtKB-UniRule.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   GO; GO:0033077; P:T cell differentiation in thymus; IEA:UniProtKB-UniRule.
DR   GO; GO:0033151; P:V(D)J recombination; IEA:UniProtKB-UniRule.
DR   CDD; cd16530; RING-HC_RAG1; 1.
DR   Gene3D; 6.10.140.510; -; 1.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR024627; RAG1.
DR   InterPro; IPR035714; RAG1_imp-bd.
DR   InterPro; IPR019485; RAG1_Znf.
DR   InterPro; IPR023336; RAG_nonamer-bd_dom.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR018957; Znf_C3HC4_RING-type.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR11539:SF0; V(D)J RECOMBINATION-ACTIVATING PROTEIN 1; 1.
DR   PANTHER; PTHR11539; VDJ RECOMBINATION ACTIVATING PROTEIN 1 RAG1; 1.
DR   Pfam; PF12940; RAG1; 1.
DR   Pfam; PF12560; RAG1_imp_bd; 1.
DR   Pfam; PF00097; zf-C3HC4; 1.
DR   Pfam; PF10426; zf-RAG1; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS51487; NBD; 1.
DR   PROSITE; PS51765; ZF_RAG1; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   3: Inferred from homology;
KW   Chromatin regulator {ECO:0000256|ARBA:ARBA00022853,
KW   ECO:0000256|RuleBase:RU366024};
KW   DNA recombination {ECO:0000256|ARBA:ARBA00023172, ECO:0000256|PROSITE-
KW   ProRule:PRU00820};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PROSITE-
KW   ProRule:PRU00820};
KW   Endonuclease {ECO:0000256|ARBA:ARBA00022759,
KW   ECO:0000256|RuleBase:RU366024};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU366024};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU366024};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268,
KW   ECO:0000256|RuleBase:RU366024};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|RuleBase:RU366024};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW   ProRule:PRU00820};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU366024};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|RuleBase:RU366024};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU366024};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU01101}.
FT   DOMAIN          236..274
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          297..326
FT                   /note="RAG1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51765"
FT   DOMAIN          337..404
FT                   /note="NBD"
FT                   /evidence="ECO:0000259|PROSITE:PS51487"
FT   DNA_BIND        337..404
FT                   /note="NBD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00820"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AAT36607.1"
FT   NON_TER         906
FT                   /evidence="ECO:0000313|EMBL:AAT36607.1"
SQ   SEQUENCE   906 AA;  103207 MW;  B127A32EC91E0044 CRC64;
     PEPAFSLDKV REKQVSHVHS EKDTELNKSV QTVNKDVFHL SQREIEKHQA NLHHLCRICG
     GPFKSNAHKR SYPVHGPVDD DTQALLRKKE KKATSWPDLL SKVFKVDVRG DVDTIYPTNF
     CHNCRNVIRR KFCRSPSEVC FPSKSTMDWL PHSSSCDICA TSFHGVKGQK QFLNPQLSKK
     PRIVTRCARK GKQVKNVKQV NKKSAMKKIA NCNKIHLSTK ILGVDYPEDF VKSISCXVCD
     HILADPVETT CKHLFCRVCI LKCIKVMGSF CPACYYPCFP TDLVSPVKSF LNILNSLILR
     CPIINCQEEV ILGKYTHHLS SHKDAKDKES YGYINKGGRP RQHLLSLTRR AQKHRLRELK
     FQVKTFAEKE EGGDVKSVCQ TLFLLALRAR NEHRQADELE AIIQGKGSGL PPAVCLAIRV
     NTFLSCSQYH KMYRTVKAIT GRQIFQPLHA LRTAEKSLLP GYHLFEWKPP LKNVSSNTDV
     GIIDGLSGIQ HLVDDYPVDT IAKRFRYDVA LVSTLMDIEE DILEGLKTQG LDDYLKGPFT
     VVIKESCDGM GDVSEKHGCG PAVPEKAVRF SFTLMSISVA QSKANVKIFE ETKPNSEFCC
     KPLCLMLADE SDHEMLTTIL SPFVAEREAM KNSLLILDIA GIPRMFKFIF RGTGYDEKLV
     REVEGLEASG STYICTLCDT TRQEASRNFI LHSITRSHAQ NLERYEIWRS NPYQETVDEL
     RDRVKGVSAK PFIETVPSID ALHCDIGNAA EFYKIFQFEI GEGYKNPMAS KEERKRWQST
     LDKHLRKKMN LKPVTRMNGN FARKLMSMET VEAVCELIKC EERHEALREL MDLYLKMKPV
     WRSSCPTKEC PELVCQYSFN SQCFAELLST KFHYRYEGKI TNYFHKTLAH VPEIIERDGS
     IGAWAS
//
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