ID G9FNK8_HETFR Unreviewed; 831 AA.
AC G9FNK8;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 13-SEP-2023, entry version 36.
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=RAG-1 {ECO:0000313|EMBL:AEL30898.1};
OS Heterodontus francisci (Horn shark) (Cestracion francisci).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Elasmobranchii; Galeomorphii; Heterodontoidea; Heterodontiformes;
OC Heterodontidae; Heterodontus.
OX NCBI_TaxID=7792 {ECO:0000313|EMBL:AEL30898.1};
RN [1] {ECO:0000313|EMBL:AEL30898.1}
RP NUCLEOTIDE SEQUENCE.
RA Aschliman N.C.;
RT "The Batoid tree of life: recovering the patterns and timing of the
RT evolution of skates, rays and allies (Chondrichthyes: Batoidea).";
RL Thesis (2011), The Florida State University, Tallahassee, FL, USA.
RN [2] {ECO:0000313|EMBL:AEL30898.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=22209858; DOI=10.1016/j.ympev.2011.12.012;
RA Aschliman N.C., Nishida M., Miya M., Inoue J.G., Rosana K.M., Naylor G.J.;
RT "Body plan convergence in the evolution of skates and rays (Chondrichthyes:
RT Batoidea).";
RL Mol. Phylogenet. Evol. 63:28-42(2012).
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|RuleBase:RU366024}.
CC -!- SIMILARITY: Belongs to the RAG1 family.
CC {ECO:0000256|RuleBase:RU366024}.
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DR EMBL; JN184089; AEL30898.1; -; Genomic_DNA.
DR AlphaFoldDB; G9FNK8; -.
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,
KW ECO:0000256|RuleBase:RU366024};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU366024};
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|RuleBase:RU366024};
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:PRU00175}.
FT DOMAIN 158..197
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 219..248
FT /note="RAG1-type"
FT /evidence="ECO:0000259|PROSITE:PS51765"
FT DOMAIN 259..326
FT /note="NBD"
FT /evidence="ECO:0000259|PROSITE:PS51487"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AEL30898.1"
FT NON_TER 831
FT /evidence="ECO:0000313|EMBL:AEL30898.1"
SQ SEQUENCE 831 AA; 95016 MW; 549F8D4EB04B72D2 CRC64;
DVTQEVLRKM GYGDCFWPEL IRNTFTLDVK TDTEARYPTH FCYNCWRIII QTINNTTNED
AFFPISTIVE WKPHSNLCSI CNFSSGTRKR KGLKRSPPVT KKPKVTVDAP IRPRVIKRKD
QQNSILLAKK IVNCKKIHLN SKLLVLDYPN NFIQSVSCQV CEHLLADPVQ SPCKHLFCRT
CILKCTAVLG KYCPVCRFPC GPAEFISPVK SFINVLNSLV LKCPVTDCEK EVKLSEFSNH
AQNHKETRMK YAYSPVNKGG RPRQHLLSLT RRAQKHRLRD LKLQVKAFAD KEEGGDVKSV
CLTLFLLALR AENEHRQADE LEAVMQGRGS ELKPAVCLAI RINTFLSCSQ YHKMYRTVKA
TTGKQIFQPL HALRNAEKTL LPGYCSFEWQ PPLANVSTNT EVGIIDGLSG WAQCIDDYPV
ETISRRFRYD VALASTVKEL EDDILEGLKC QKIDEFVSGP FTVVIKESCD GMGDVSEKHG
CGPAVPEKAV RYSFTIMSIS VMNENNEKVK VFEELKPNSE LCCRPLCLML ADESDHETLT
AILGPVIAER EAMKTSDLIL EIGNLHRSFQ FIFRGTGYDE KLVREVEGLE ASGSIYVCTL
CDATRSEASR NLVLHSITRS HGENLERYEI WRSNPYHETA EELRDRVKGV SAKPFIETQP
SIDALHCDIG NATEFYRLFQ DEIGEMHKNP HSSKEERKRW QAMLDNHLRK KMNLKPVMRL
NGNFARKLMT KETVEAVCEL IPSEERREIL RELMHLYLLM KPVWRTTFPV RECPDLLCQY
SFNSQRFAEL LHTKFKHRYE GKITNYLHKT LAHVPEIIER DGSIGAWASE G
//
