ID   Q2JJS1_SYNJB            Unreviewed;      1595 AA.
AC   Q2JJS1;
DT   07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   07-MAR-2006, sequence version 1.
DT   27-MAR-2024, entry version 90.
DE   SubName: Full=Alpha-2-macroglobulin family protein {ECO:0000313|EMBL:ABD03086.1};
GN   OrderedLocusNames=CYB_2140 {ECO:0000313|EMBL:ABD03086.1};
OS   Synechococcus sp. (strain JA-2-3B'a(2-13)) (Cyanobacteria bacterium
OS   Yellowstone B-Prime).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=321332 {ECO:0000313|EMBL:ABD03086.1, ECO:0000313|Proteomes:UP000001938};
RN   [1] {ECO:0000313|EMBL:ABD03086.1, ECO:0000313|Proteomes:UP000001938}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JA-2-3B'a(2-13) {ECO:0000313|Proteomes:UP000001938};
RX   PubMed=18059494; DOI=10.1038/ismej.2007.46;
RA   Bhaya D., Grossman A.R., Steunou A.S., Khuri N., Cohan F.M., Hamamura N.,
RA   Melendrez M.C., Bateson M.M., Ward D.M., Heidelberg J.F.;
RT   "Population level functional diversity in a microbial community revealed by
RT   comparative genomic and metagenomic analyses.";
RL   ISME J. 1:703-713(2007).
CC   -!- SIMILARITY: Belongs to the protease inhibitor I39 (alpha-2-
CC       macroglobulin) family. Bacterial alpha-2-macroglobulin subfamily.
CC       {ECO:0000256|ARBA:ARBA00010556}.
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DR   EMBL; CP000240; ABD03086.1; -; Genomic_DNA.
DR   RefSeq; WP_011433721.1; NC_007776.1.
DR   STRING; 321332.CYB_2140; -.
DR   MEROPS; I39.008; -.
DR   KEGG; cyb:CYB_2140; -.
DR   eggNOG; COG2373; Bacteria.
DR   HOGENOM; CLU_002018_1_0_3; -.
DR   OrthoDB; 9767116at2; -.
DR   Proteomes; UP000001938; Chromosome.
DR   GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0004866; F:endopeptidase inhibitor activity; IEA:InterPro.
DR   CDD; cd02891; A2M_like; 1.
DR   Gene3D; 1.50.10.20; -; 1.
DR   Gene3D; 2.20.130.20; -; 1.
DR   Gene3D; 2.60.40.1930; -; 1.
DR   InterPro; IPR011625; A2M_N_BRD.
DR   InterPro; IPR047565; Alpha-macroglob_thiol-ester_cl.
DR   InterPro; IPR011626; Alpha-macroglobulin_TED.
DR   InterPro; IPR041246; Bact_MG10.
DR   InterPro; IPR013784; Carb-bd-like_fold.
DR   InterPro; IPR001599; Macroglobln_a2.
DR   InterPro; IPR002890; MG2.
DR   InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR   PANTHER; PTHR40094; ALPHA-2-MACROGLOBULIN HOMOLOG; 1.
DR   PANTHER; PTHR40094:SF1; UBIQUITIN DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00207; A2M; 1.
DR   Pfam; PF07703; A2M_BRD; 1.
DR   Pfam; PF17973; bMG10; 1.
DR   Pfam; PF13620; CarboxypepD_reg; 1.
DR   Pfam; PF01835; MG2; 1.
DR   Pfam; PF07678; TED_complement; 1.
DR   SMART; SM01360; A2M; 1.
DR   SMART; SM01359; A2M_N_2; 1.
DR   SMART; SM01419; Thiol-ester_cl; 1.
DR   SUPFAM; SSF49452; Starch-binding domain-like; 1.
DR   SUPFAM; SSF48239; Terpenoid cyclases/Protein prenyltransferases; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000001938}.
FT   DOMAIN          713..853
FT                   /note="Alpha-2-macroglobulin bait region"
FT                   /evidence="ECO:0000259|SMART:SM01359"
FT   DOMAIN          901..991
FT                   /note="Alpha-2-macroglobulin"
FT                   /evidence="ECO:0000259|SMART:SM01360"
SQ   SEQUENCE   1595 AA;  177072 MW;  AEDC2A304312EC11 CRC64;
     MLRRWLAALV LLLGVGLAVL LSEQPTGSLV GRVELPAGVA LESVRVIAAG PATRSSSLTA
     DGEYRLDRLP VGEYQVTVQG SGLETVGSQG SVLVREGATA RIPTLRPQLV PPGLYLYSTS
     QVFTTAEPAR LQWRATSLGS VQLSLYRFSL TELQGSPLLR DLADAGYGSL NPALYPTLRR
     ELVRSWQQPV PRRAGEGWTA QTLELGILPP GAYWVEAEGR EPLAQTAAPL PRFDHWFLVS
     DLGLIQKQDA SQLVVQAVHL RELRPLAGIQ IQVFGEWGDP LTATTDAEGL ARFGLPAREG
     SSLVVYGRSA DNTLQALSRS YAYGWNQPHR IYAYTDRPLY RPGQTVYFRA LVREQTRLTP
     PPPGQAVQLT LTAPNGDVLS EQTLATNAFG SVHGEFQLPE EASLGSYGLE WQVSGPQGSS
     REYTSFQVEA YRKPEFEVAV VPDRPWLVRG GSLKVQVEAE YLFGAPVAAA QLRYRVYSSP
     DWSLRYGLLP RSAEEDYFAD DLGEEQGYYG GYGQLVAEGE GVTDAQGRAV FHLPRLLADL
     DWEEDSYWGP QEVQQLRIEV EVTDISRRTV TGSARAWVTA GEFALFAEVN RHLPAPGDTL
     TYRLQARDYD GRPVSATGEL SLERWRWDPK SNTYQRQGTL LRQPFQIVNG EGSLDLHLPA
     DLEPGDYRVR LTAWDPRRQS APHRWRERVQ EVDYLWVVEP GSPLQSWGSL PSLEVVADRQ
     IYQVGEEAQI LIVSPLPDVA VLVGIEGSRL HQVQVLRLQG HTATLRLPIR GDYRPNLYVT
     ATAIGPERRL YRSEALLRVS PLDRFLQVEL QTDKPTYRPG ETAQIQIRTR DAQGQPVSAE
     VGLGIVDNAL YLLRPDFTPD IRRFFYGRQY NQVTTTTSFP QQYPGGADKL AGQVREDFRD
     TAAWFPDLVT NADGLAQVQV RWPDNLTTWR LTARAATADT QVGSALATVS VSKDLLVRLA
     APRFFRVGDQ LTLAAIVQNR TGQAQAVEVR LEVPVPAGGI LKLQGPERQR LTVPAQGAGR
     VEWPLQVLGA GDTSLRVWAE GNGLKDALQL RIPSQPFGAV QRFSQVGRVQ EGSLDLSLDW
     PATWVPGSRQ LHLELAASPA ATLLEPLDYL VEFPYGCTEQ TLSRFLPALA VAQVSKQLGL
     NLRSQTLERL PQVLRSGLQR LEGSQNYDGG WGWWAHDRSN PYLTGYILQG YHLAQAAGYA
     LKDWQVRQAL DYLAAQLAQP QALSPDLQAF VAYSLALWDP ALVTADLPPP ERLSTFGLAY
     RGLAALQLGQ RDLAQAALDE VLERRQQDPQ GRWFIPAASS LATHERSTYD DMEVAGPLLQ
     LAVRLQDDRA AQIAEALLQQ RQNNRWRTTK ATADALLGLS AYYQAQQQQL PGPGEVRVLD
     GTTGSLLDRW QAGAGDPRYG LDWADAEVGN LSSLRLEKSG PGPLYYSLRG EAFVPNPLPS
     QAQGFAVSRS YFRLQPQPQP NGEIRYREQP LRPGDTVRAG EILLARLTVE AERDSHYVVV
     EDPLPSGAEI TSQDPREFTG LAPDYWWDWF WTRQENRDDR VAFFSTELKQ GRHEFVYLFR
     PEIPGQFQVA PALAEEMYDP SRHGRSAAYS LEVLP
//