ID A0A117LGI3_9CHLR Unreviewed; 1082 AA.
AC A0A117LGI3;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 13-SEP-2023, entry version 21.
DE RecName: Full=Alpha-2-macroglobulin domain-containing protein {ECO:0008006|Google:ProtNLM};
DE Flags: Fragment;
GN ORFNames=XD73_1246 {ECO:0000313|EMBL:KUK45880.1};
OS Anaerolinea thermophila.
OC Bacteria; Chloroflexota; Anaerolineae; Anaerolineales; Anaerolineaceae;
OC Anaerolinea.
OX NCBI_TaxID=167964 {ECO:0000313|EMBL:KUK45880.1, ECO:0000313|Proteomes:UP000064249};
RN [1] {ECO:0000313|EMBL:KUK45880.1, ECO:0000313|Proteomes:UP000064249}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=46_16 {ECO:0000313|EMBL:KUK45880.1};
RX PubMed=26787827; DOI=10.1128/mbio.01669-15;
RA Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M.,
RA Andersen G.L., Banfield J.F.;
RT "Genome-Resolved Metagenomic Analysis Reveals Roles for Candidate Phyla and
RT Other Microbial Community Members in Biogeochemical Transformations in Oil
RT Reservoirs.";
RL MBio 7:e01669-15(2015).
CC -!- SIMILARITY: Belongs to the protease inhibitor I39 (alpha-2-
CC macroglobulin) family. Bacterial alpha-2-macroglobulin subfamily.
CC {ECO:0000256|ARBA:ARBA00010556}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KUK45880.1}.
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DR EMBL; LGFU01000125; KUK45880.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A117LGI3; -.
DR PATRIC; fig|167964.4.peg.1373; -.
DR Proteomes; UP000064249; Unassembled WGS sequence.
DR GO; GO:0004866; F:endopeptidase inhibitor activity; IEA:InterPro.
DR Gene3D; 1.50.10.20; -; 1.
DR Gene3D; 2.20.130.20; -; 1.
DR Gene3D; 2.60.40.1930; -; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR011625; A2M_N_BRD.
DR InterPro; IPR013783; Ig-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; PF01835; MG2; 1.
DR SMART; SM01360; A2M; 1.
DR SMART; SM01359; A2M_N_2; 1.
DR SUPFAM; SSF48239; Terpenoid cyclases/Protein prenyltransferases; 1.
PE 3: Inferred from homology;
FT DOMAIN 566..711
FT /note="Alpha-2-macroglobulin bait region"
FT /evidence="ECO:0000259|SMART:SM01359"
FT DOMAIN 772..862
FT /note="Alpha-2-macroglobulin"
FT /evidence="ECO:0000259|SMART:SM01360"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KUK45880.1"
FT NON_TER 1082
FT /evidence="ECO:0000313|EMBL:KUK45880.1"
SQ SEQUENCE 1082 AA; 118313 MW; DA500B328226F042 CRC64;
FEIAPITVGD LLTLVHPDNY EYRQMFLPSD IERSTHNLEL TRNINQAVRL PLTYQGNPLS
PGMYFLGMTS ADLVENGEQV YQRYYLIVSD NHAVMKIAPK QAFIWGTTLS DHAPLAGAPV
TVYNTEGDIL ASGETDSDGF FIDGITRSEE PYANFLAVIG KPEQDDFAFS ISTWGQGYAL
HEQGIRQNTL PREIEAYIYT DRPIYRPGDT VHFKAVLFSR ENGLPVPSGM EQVDVAVYGD
PGMSGIPVNL YSNTLTLSQF GTLEGSVAIP PDASPGLFQI ALTQGEKAIE SLYFDVAAYR
KPEIEFSADL VPDEIVFGED LNAQLQAAYY FGLPVADQGY TWSLYRDDGR FNLPGYQVGP
MSSDWLMPRF PEYSVFGERV AYGEGFTDKQ GQSNLVFSEA DMALDEVQAG SIQELTLEVT
ISDQSGFPVS HRESAKIHPD TFYIGVKPET YFGNVNSSFS FTILTVDWEQ EPVGQLALEA
SFEAIEWEVE ETGRMEMPYQ YVERKTLIDT ANPITGDDGL SRLSFVPPEP GTYLLTVTSG
DAVTESLVWA AGEGTAVWPK QTQNLIELTP DAELYQPGQS ANIFFPNPFP GDAKALVTLE
RGQVMETQVV EVTGAGYSIE FPITSDSIPN VYISVMLFGR DEDGNPGFRQ GINNIKVSPE
SKNLNVELIL DPQVTTPGAP VSAQLLVTDQ QGNPVQGEFS VAVVDKALLA LVEPNSQPIL
EAFYSSQPLA VQTSFSLKTY ALQLALTSEL GIGGGGGDMA AEKSLRENFP DTALWEGRVV
TGSDGTAQLT IPLPDSLTTW VVDVRGLTED YLVGQAEGEI ITQKELMVRP VTPRFLVDGD
RVELAAIVHN NTTETMEVDV SLLGSGFTLE EGTDQSQKLV IDSGTNVRVN WWCLVQSQES
VELIFQAESD GYEDASKPVW GDLQVLRYAM PVTFSTAGQI EEEGQVLELV SLPISTDPSS
GSLSLELQPS LTASILDTSQ AFDSPSFSDT ISIVSRMLAN VNTYQALQDL GIETPQFESD
LSILVGESLQ ELLEIQKFDG GWSWWGGSGA GFLSSDAFIT AYVLHGLQLA SDAGFEVGEY
YL
//