#=GF ID   Secapin
#=GF AC   PF17521.6
#=GF DE   Honey bee peptides
#=GF AU   El-Gebali S;0000-0003-1378-5495
#=GF SE   PRODOM:PD058010
#=GF GA   25.90 25.90;
#=GF TC   26.90 25.90;
#=GF NC   25.80 25.50;
#=GF BM   hmmbuild HMM.ann SEED.ann
#=GF SM   hmmsearch -Z 75585367 --cpu 4 -E 1000 HMM pfamseq
#=GF TP   Family
#=GF RN   [1]
#=GF RM   27208884
#=GF RT   Secapin, a bee venom peptide, exhibits anti-fibrinolytic,
#=GF RT   anti-elastolytic, and anti-microbial activities.
#=GF RA   Lee KS, Kim BY, Yoon HJ, Choi YS, Jin BR;
#=GF RL   Dev Comp Immunol. 2016;63:27-35.
#=GF RN   [2]
#=GF RM   25189650
#=GF RT   Production of antibacterial peptide from bee venom via a new
#=GF RT   strategy for heterologous expression.
#=GF RA   Hou C, Guo L, Lin J, You L, Wu W;
#=GF RL   Mol Biol Rep. 2014;41:8081-8091.
#=GF RN   [3]
#=GF RM   7213796
#=GF RT   A comparative structural study of apamin and related bee venom
#=GF RT   peptides.
#=GF RA   Hider RC, Ragnarsson U;
#=GF RL   Biochim Biophys Acta. 1981;667:197-208.
#=GF DR   INTERPRO; IPR020128;
#=GF DR   SO; 0100021; polypeptide_conserved_region;
#=GF CC   Family members are bee venom peptides such as Secapin. Mature
#=GF CC   secapin is composed of 25 amino acid residues that contain a
#=GF CC   disulfide link [1]. Secapin has been demonstrated to act as a
#=GF CC   potent neurotoxin. In Apis mellifera secapin exhibits
#=GF CC   anti-bacterial activity and induces inflammation and pain with
#=GF CC   anti-fibrinolytic, anti-elastolytic, and anti-microbial
#=GF CC   activities [2]. Secapin shares a common folding pattern with
#=GF CC   apamin, mast cell degranulating peptide and tertiapin; it is
#=GF CC   centred on a beta-turn covalently linked to an alpha-helical
#=GF CC   segment by one disulphide link (two disulphide links in the
#=GF CC   other peptides) [3].
#=GF SQ   10
#=GS A0A4S2KK16_9HYME/94-121  AC A0A4S2KK16.1
#=GS SECP_APIME/33-77         AC P02852.2
#=GS SECP2_APIME/33-77        AC I1VC85.1
#=GS A0A6I9VY29_9HYME/82-112  AC A0A6I9VY29.1
#=GS A0A195E0S3_9HYME/90-118  AC A0A195E0S3.1
#=GS A0A2A3EMG1_APICC/33-76   AC A0A2A3EMG1.1
#=GS A0A8B8IGR6_VANTA/20-48   AC A0A8B8IGR6.1
#=GS A0A8R2GBE8_BOMMO/39-85   AC A0A8R2GBE8.1
#=GS SECP1_APIME/1-25         AC C0HLU0.1
#=GS A0A6J2KMS0_BOMMA/39-85   AC A0A6J2KMS0.1
A0A4S2KK16_9HYME/94-121             ..........gtd------------------SRQIITVPIRCPPDHVVVKNRCRI---e..
SECP_APIME/33-77                    .............VSNDMQPLEARSADLVPEPRYIIDVPPRCPPGSKFIKNRCRVIVP...
SECP2_APIME/33-77                   .............VSNDMQPLEARTADLVQQPRYIIDVPPRCPPGSKFVHKRCRVIVP...
A0A6I9VY29_9HYME/82-112             ..........net-----------------ESRQIITAPIRCPPNHELVKNRCRLKV-r..
A0A195E0S3_9HYME/90-118             .........esdy-------------------REIIDAPIRCPPNQVLVKNRCRI---ea.
A0A2A3EMG1_APICC/33-76              .............VSNDMQPLEARTADLVQQPRYIIDVPPRCPPGSKFVHKRCR----kme
A0A8B8IGR6_VANTA/20-48              ..........gii------------------PQNVITVPPNCPPGQEFINGQCRDI--w..
A0A8R2GBE8_BOMMO/39-85              dndfqidrrqsnd----------RIDPLVIESRNIITVPPNCPKGQEWVQGQCR----evw
SECP1_APIME/1-25                    .............--------------------YIINVPPRCPPGSKFVKNKCRVIVP...
A0A6J2KMS0_BOMMA/39-85              dndfqidrrqsnd----------RIDPLVIESRNIITVPPNCPKGQEWVQGQCR----evw
#=GC seq_cons                       ..........s...................psRpIIsVPPRCPPGpcaV+sRCRl...c..
//