# STOCKHOLM 1.0
#=GF ID   RAG2_PHD
#=GF AC   PF13341.1
#=GF DE   RAG2 PHD domain
#=GF AU   Bateman A
#=GF SE   Bateman A
#=GF GA   27.00 27.00;
#=GF TC   27.10 27.20;
#=GF NC   26.90 26.90;
#=GF BM   hmmbuild HMM.ann SEED.ann
#=GF SM   hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
#=GF TP   Domain
#=GF RN   [1]
#=GF RM   18033247
#=GF RT   RAG2 PHD finger couples histone H3 lysine 4 trimethylation with
#=GF RT   V(D)J recombination.
#=GF RA   Matthews AG, Kuo AJ, Ramon-Maiques S, Han S, Champagne KS,
#=GF RA   Ivanov D, Gallardo M, Carney D, Cheung P, Ciccone DN, Walter KL,
#=GF RA   Utz PJ, Shi Y, Kutateladze TG, Yang W, Gozani O, Oettinger MA;
#=GF RL   Nature. 2007;450:1106-1110.
#=GF DR   INTERPRO; IPR025162;
#=GF CC   This domain is found at the C-terminus of the RAG2 protein. The
#=GF CC   structure of this domain has been shown bound to histone H3
#=GF CC   trimethylated at lysine 4 (H3K4me3) [1].
#=GF SQ   6
#=GS RAG2_ONCMY/417-495    AC Q91193.1
#=GS Q9W6A0_TAKRU/417-495  AC Q9W6A0.1
#=GS RAG2_DANRE/414-492    AC O13034.1
#=GS RAG2_XENLA/407-484    AC Q91830.1
#=GS RAG2_RABIT/414-491    AC P34089.1
#=GS RAG2_CHICK/415-492    AC P25022.1
RAG2_ONCMY/417-495               GYWVKCCLGCQVDPNTWEPYYSTELLRPAMIYCSKGEGGHWVHAQCMELTEGLLVRLSQGNGKYFCLDHGGLPRQEMTP
Q9W6A0_TAKRU/417-495             GYWIKCCLGCQVDPNTWEPYYSTELHRPAMIFCSRGEEGHWVHAQCMELSETLLLRLSQGNKKYFCLDHGGLPYQEMTP
RAG2_DANRE/414-492               GYWIKCCLSCQVDPNIWEPYYSTELTRPAMIFCSRGEGGHWVHAQCMELPESLLLQLSQDNSKYFCLDHGGLPKQEMTP
RAG2_XENLA/407-484               GYWIKCCPDCDMDRNTWEPFYSTELNKPSMIFCSKD.GGHWVHSQCMDLSETMLKYLSQNNIKYFCNEHVEVARGVQTP
RAG2_RABIT/414-491               GYWITCCPTCDVDINTWVPFYSTELNKPAMIYCSHG.DGHWVHAKCMDLAERTLIHLSEGSNKYYCNEHVEIARALQTP
RAG2_CHICK/415-492               GYWIICCASCNIDINTWVPFYSTELNKPAMILCSSG.SGHWVHAQCMDLSESMLLQLSEANVKYFCNEHVHLNKGLQTP
#=GC seq_cons                    GYWIKCChuCpVD.NTWEPaYSTELs+PAMIaCS+G.uGHWVHAQCM-LoEohLlpLSQuNsKYFC.-HstLs+t..TP
//