#=GF ID RC-P840_PscD
#=GF AC PF10657.13
#=GF DE Photosystem P840 reaction centre protein PscD
#=GF AU FIGfams;
#=GF AU Mistry J;0000-0003-2479-5322
#=GF AU Coggill P;0000-0001-5731-1588
#=GF SE FIG031038 (Release 2.0)
#=GF GA 23.50 23.50;
#=GF TC 23.70 104.90;
#=GF NC 22.90 21.90;
#=GF BM hmmbuild HMM.ann SEED.ann
#=GF SM hmmsearch -E 1000 --cpu 4 -Z 75585367 HMM pfamseq
#=GF TP Family
#=GF RN [1]
#=GF RM 11687219
#=GF RT The reaction center of green sulfur bacteria(1).
#=GF RA Hauska G, Schoedl T, Remigy H, Tsiotis G;
#=GF RL Biochim Biophys Acta. 2001;1507:260-277.
#=GF DR INTERPRO; IPR019608;
#=GF DR SO; 0100021; polypeptide_conserved_region;
#=GF CC The photosynthetic reaction centres (RCs) of aerotolerant
#=GF CC organisms contain a heterodimeric core, built up of two strongly
#=GF CC homologous polypeptides each of which contributes five
#=GF CC transmembrane peptide helices to hold a pseudo-symmetric double
#=GF CC set of redox components. Two molecules of PscD are housed within
#=GF CC a subunit. PscD may be involved in stabilising the PscB
#=GF CC component since it is found to co-precipitate with FMO
#=GF CC (Fenna-Mathews-Olson BChl a-protein) and PscB. It may also be
#=GF CC involved in the interaction with ferredoxin [1].
#=GF SQ 11
#=GS B4S6P6_PROA2/1-127 AC B4S6P6.1
#=GS Q0YPZ4_9CHLB/20-163 AC Q0YPZ4.1
#=GS PSCD_CHLTE/1-143 AC Q8KEP5.1
#=GS Q3B578_CHLL3/1-144 AC Q3B578.1
#=GS B4SDA1_PELPB/1-144 AC B4SDA1.1
#=GS B3QZ39_CHLT3/2-126 AC B3QZ39.1
#=GS B3EHQ9_CHLL2/1-144 AC B3EHQ9.1
#=GS A0A533TW14_CHLSQ/1-144 AC A0A533TW14.1
#=GS A1BET7_CHLPD/1-144 AC A1BET7.1
#=GS A0A1B1Q3F7_9CHLB/1-127 AC A0A1B1Q3F7.1
#=GS A0A317T430_9CHLB/1-127 AC A0A317T430.1
B4S6P6_PROA2/1-127 ..mq-------------------SAVWSGNALHKVTKYYITSAKRDRNGKLDITVSPASGRTNLKPTEKFIDQLKNGEIQLLVLTNQPDIALDMDKKVLDNENRYVIDFDKRGVKWTMRDLPVYFNTMKNTLCVEVDGVSYSLDSFFK
Q0YPZ4_9CHLB/20-163 ....MRSQLSRPNTATNQVRVSTAGPWSGNAAHKTKKYYITTAKRDNYGKLQIQICPASGRRKLSPTPEIISKIISGEIELFVLTTQPDIGIDLKQKVLDNENRYVIDFDKRGIKWTMRDIPVFYDSLHQQLAVEIDRQVYTLDKFFK
PSCD_CHLTE/1-143 ....MQPQLSRPQTASNQVRKAVSGPWSGNAVHKAEKYFITSAKRDRDGKLQIELVPASGRRKLSPTPEMIRRLIDGEIEIYILTTQPDIAIDMNKEIIDMENRYVIDFDKRGVKWTMREIPVFYHEGKG-LCVELHNKIYTLDQFFK
Q3B578_CHLL3/1-144 ....MQSQLSRPFTAQNQVRASTSGPWSGNAVHKAEKYFITSAKRDRSNALQLTISPASGRRKLLATREMINKVIAGEIELTVMSTLPDIGINLSQKILDNENRYVIDFDKRGVKWTMRDIPVFYNSIKRQLSVEIDRQNYTLDEFFK
B4SDA1_PELPB/1-144 ....MQPQLSRPNTGDNQVRVSTAGPWSGNAAHKAEKYFITSAKRDNRGNLQVQISPSSGRRKLSPTKVMIDKIISGEIELFVLTTQPDIGIDIKKKIIDNENRYVIDFDNRGIKWTMRDIPVFYSSLLRELCIEIDRRTYTLDEFFK
B3QZ39_CHLT3/2-126 siwr-----------------------TGNPVHKIDKYFITKAERDDYGRLNLTFASTGGYGQLTNIPEIKKLLKNHDIQVAVLSSNEDIAINLQEFVKSSEERYVTDFDGRGVRSTMREVQVFVNPNTDEMVVDINGRLYSLNEFFK
B3EHQ9_CHLL2/1-144 ....MQPQLSRPFTKDNQVRKSTSGPWSGNAVHKAEKYFITSAKRDRDDRLQLEIYPASGRRKLSPTREMIDKIISGEIELYVLTTQPDIAINLEQKVLDNENRYVIDFDKRGVKWTMRDIPVFYNSLDRQLSVEIDRRTYTLNEFFK
A0A533TW14_CHLSQ/1-144 ....MRPQLSRPDTAMNQVRVSTSGPWSGNAVHKAQKYFITSAKRDRSGKLQLEISPASGRRTLLPTKGMIDKVISGEIELYVLTTQPDIGINLQQKVLDNENRYVIDFDKRGVKWTMRDIPIFYDTLHRQLSVEIDRKTYTLDEFFK
A1BET7_CHLPD/1-144 ....MQPQLSRPFTKDNQVRTSKSGPWSGNAAHKAEKYFITAAKRGKNDNLQLEISPASGRRKLSPTTEMINKIISGEIELFVLTTQPDIAINLAQKVLDNENRYVIDFDKRGVKWTMRDIPVFYDSLHRELCVEIDRRTYTLNEFFK
A0A1B1Q3F7_9CHLB/1-127 ..mh-------------------SAVWSGNALHKVTKYYITSAKRDNNGRLDITISPASGRTKLKPTEQFIRQLENKEVQLLVLTTQPDIALDLNKMVIDNENRYVIDFDKRGVKWTMRDLPVYYNTMKRELCVEVDGVCYTLDKFFK
A0A317T430_9CHLB/1-127 ..mq-------------------SAVWSGNALHKVAKYFITSAKRDPNGKLELVISPASGRRKLFPTKEIIEQLKEGKIQLLVLTTQPDIAINLPQKVLDNENRYVIDFDKRGIKWTMRDIPVFYDNLRDQLCVEIDKETYTLDQFFK
#=GC seq_cons ....MpsQLSRP.Tt.NQVRhuhSGPWSGNAlHKscKYFITSAKRDcsG+LQlpISPASGRRKLpPTcEhIc+lIsGEIELhVLTTQPDIAIsLppKVLDNENRYVIDFDKRGVKWTMRDIPVFYsol+cpLsVEID+csYTLDcFFK
//