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Database: UniProt
Entry: Q1DES0_MYXXD
LinkDB: Q1DES0_MYXXD
Original site: Q1DES0_MYXXD 
ID   Q1DES0_MYXXD            Unreviewed;      1572 AA.
AC   Q1DES0;
DT   11-JUL-2006, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2006, sequence version 1.
DT   27-MAR-2024, entry version 97.
DE   RecName: Full=Alpha-2-macroglobulin {ECO:0008006|Google:ProtNLM};
GN   OrderedLocusNames=MXAN_0585 {ECO:0000313|EMBL:ABF86815.1};
OS   Myxococcus xanthus (strain DK1622).
OC   Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC   Myxococcaceae; Myxococcus.
OX   NCBI_TaxID=246197 {ECO:0000313|EMBL:ABF86815.1, ECO:0000313|Proteomes:UP000002402};
RN   [1] {ECO:0000313|EMBL:ABF86815.1, ECO:0000313|Proteomes:UP000002402}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DK1622 {ECO:0000313|Proteomes:UP000002402};
RX   PubMed=17015832; DOI=10.1073/pnas.0607335103;
RA   Goldman B.S., Nierman W.C., Kaiser D., Slater S.C., Durkin A.S.,
RA   Eisen J.A., Ronning C.M., Barbazuk W.B., Blanchard M., Field C.,
RA   Halling C., Hinkle G., Iartchuk O., Kim H.S., Mackenzie C., Madupu R.,
RA   Miller N., Shvartsbeyn A., Sullivan S.A., Vaudin M., Wiegand R.,
RA   Kaplan H.B.;
RT   "Evolution of sensory complexity recorded in a myxobacterial genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15200-15205(2006).
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; CP000113; ABF86815.1; -; Genomic_DNA.
DR   RefSeq; WP_011550716.1; NC_008095.1.
DR   STRING; 246197.MXAN_0585; -.
DR   EnsemblBacteria; ABF86815; ABF86815; MXAN_0585.
DR   GeneID; 41358064; -.
DR   KEGG; mxa:MXAN_0585; -.
DR   eggNOG; COG2373; Bacteria.
DR   HOGENOM; CLU_002018_1_0_7; -.
DR   OrthoDB; 9767116at2; -.
DR   Proteomes; UP000002402; Chromosome.
DR   GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR   GO; GO:0004866; F:endopeptidase inhibitor activity; IEA:InterPro.
DR   Gene3D; 1.50.10.20; -; 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; 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; 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; SSF48239; Terpenoid cyclases/Protein prenyltransferases; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000002402};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..1572
FT                   /note="Alpha-2-macroglobulin"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004188223"
FT   DOMAIN          668..815
FT                   /note="Alpha-2-macroglobulin bait region"
FT                   /evidence="ECO:0000259|SMART:SM01359"
FT   DOMAIN          881..973
FT                   /note="Alpha-2-macroglobulin"
FT                   /evidence="ECO:0000259|SMART:SM01360"
SQ   SEQUENCE   1572 AA;  168606 MW;  B743FCE461089992 CRC64;
     MKCLIRLAAL SALMLSGVAL AKPLYITVPR SYGTQEPVAV DVAFEDKGPV ELRVLKPENL
     DAFIRAQGDL RRAYQTPPTL KNPGRALSRG FNAVRTPGMF LLDTLSPAFR DEVGEVLPRA
     PQASGSGEPL AKVAEGPERL VGVPPGFTVT RSQWLNLDLG GAERDFNVPG FNASGSSGFQ
     ERRVTLAPLP AGTYVLQLVQ GRVEGQVVLV VSDLTVQLKQ TDGQVLLRVA GRDQKPREGA
     EVQVYLPKGK GPAGKTNAKG EVTLEVSEPR VIATATAGGD TAIVDTDFYS ALAVAPDVFI
     YSDRPIYKPG HEVKFRGVVR QPDTFLARLF TPKKRQVQVK LVSQEGRALT TRAAVDEFGA
     FHGTLKVPDD LGTGVLRVEA EVDGHPHQGE ARVQDYVKPT FYLEMEPASE TVVPGQTLRA
     KVRARRYAGG TPDATKYEVF LYRSLLDAPA WVDDAGKGGQ GSDVTYGSAS TTEGKLSVPE
     RLYSSVEARG AYEDPWSSAS AFDANGEAEI EVAVPALAAG EERLPYRYSL TVRARDDQET
     FANATSAFFL SKVEVLGLAR YSDAVVAKSG DATLAIRATT LSGKPYGVTQ GEVEFVLRKA
     DGSEKSLGKR SFSTAADGTH REKVPTSDVG SVLARVVVKD KNGETWQGEE SLLVIGGADE
     PVARVPNLTL ASLSGTLAPG DTAKLVALMP DSWGSGGRDA GPVWVTLSGA SLYDTQVVEL
     TGRTLVHSFN VEKRFGSAVY ASVAYPTATG RWEERTVAFR VIPRERTLTV ELQPRRAEAT
     PLTEQSIDVR VVDHEGRGVV AQLSVGVVDK AVYAIQSEFR PRVLDFFYPP ARNNVSNFFS
     SEFQGYGYGE ALARKMAGLP DHAFASIKPP SRQTKDLERD TAHWDPAVVT DRDGRATVRF
     TLPSNQTLWV VTAVAADTSG RFGEGTSEFA TRGGLNLYAA LPQFLREGDE AVASVRLSAG
     EKSPASQLLD VKLASLGALK ADQFEHKVEL AKGGEQVVPL TLKASSTGAA QLTVNVAGGK
     DSLRDLKRFD VGPAAVEDVV KVSAWGGGAL EVPAPQEATL ARVELVLQPS IVDAALSNVR
     ELLTYPYGCL EQLVSTTVPN VAVYQVLQKA GALAKLDTDT QALLAEARSR SVQGTARILD
     MSVKGGGFTW FGGYETPSLP QTLIALDGLA YAAEAGLVDR ADPRLVESAR WLEAQEGLPP
     EYEATRAYVL ARLEGSKQAA RVRALVQGAE GGDLYPLALA VLAAEKAGVI KEPALQTQIN
     ALVARSAQGY ATLAALGPGQ SLEQSEAFFR FPLRRVGMTA IAAHAASFGT LDITRARRRI
     LELLSEPDLS TFDRSTTLLH SLWLLERDAK AMQGMKAPEV KGVKTPVKFA PRGLGLVAVL
     APGTRTVDVG GFDGVATLRA TTRTPLSAVQ PKAEGMSIQR AYYVLRESGK VRLGAGDTVS
     QGEEVYVELT LDARGDNRVR SAYYVVEDAV PAGFVPLQED KAFRGPPHSL PLVPEALKRR
     VLNPERATFF FEEPAWWSDS PRTVGYVLRA QFAGTFSAPP AHIEDMYAAS IHGRTAADSL
     KVVPSKKHLG DL
//
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