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Database: UniProt
Entry: Q1QLM2_NITHX
LinkDB: Q1QLM2_NITHX
Original site: Q1QLM2_NITHX 
ID   Q1QLM2_NITHX            Unreviewed;      1738 AA.
AC   Q1QLM2;
DT   16-MAY-2006, integrated into UniProtKB/TrEMBL.
DT   16-MAY-2006, sequence version 1.
DT   27-MAR-2024, entry version 90.
DE   SubName: Full=Alpha-2-macroglobulin-like protein {ECO:0000313|EMBL:ABE62875.1};
GN   OrderedLocusNames=Nham_2078 {ECO:0000313|EMBL:ABE62875.1};
OS   Nitrobacter hamburgensis (strain DSM 10229 / NCIMB 13809 / X14).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Nitrobacter.
OX   NCBI_TaxID=323097 {ECO:0000313|EMBL:ABE62875.1, ECO:0000313|Proteomes:UP000001953};
RN   [1] {ECO:0000313|EMBL:ABE62875.1, ECO:0000313|Proteomes:UP000001953}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10229 / NCIMB 13809 / X14
RC   {ECO:0000313|Proteomes:UP000001953};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Ivanova N., Ward B., Arp D., Klotz M., Stein L.,
RA   O'Mullan G., Starkenburg S., Sayavedra L., Poret-Peterson A.T.,
RA   Gentry M.E., Bruce D., Richardson P.;
RT   "Complete sequence of chromosome of Nitrobacter hamburgensis X14.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000319; ABE62875.1; -; Genomic_DNA.
DR   RefSeq; WP_011510554.1; NC_007964.1.
DR   STRING; 323097.Nham_2078; -.
DR   KEGG; nha:Nham_2078; -.
DR   eggNOG; COG2373; Bacteria.
DR   HOGENOM; CLU_000965_1_0_5; -.
DR   OrthoDB; 9767116at2; -.
DR   Proteomes; UP000001953; Chromosome.
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; 2.60.40.1930; -; 1.
DR   InterPro; IPR026284; A2-macglob_dom_prot_bac.
DR   InterPro; IPR049120; A2M_bMG2.
DR   InterPro; IPR011625; A2M_N_BRD.
DR   InterPro; IPR047565; Alpha-macroglob_thiol-ester_cl.
DR   InterPro; IPR021868; Alpha_2_Macroglob_MG3.
DR   InterPro; IPR041203; Bact_A2M_MG5.
DR   InterPro; IPR041462; Bact_A2M_MG6.
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; PF21142; A2M_bMG2; 1.
DR   Pfam; PF07703; A2M_BRD; 1.
DR   Pfam; PF17973; bMG10; 1.
DR   Pfam; PF11974; bMG3; 1.
DR   Pfam; PF17972; bMG5; 1.
DR   Pfam; PF17962; bMG6; 1.
DR   Pfam; PF01835; MG2; 1.
DR   PIRSF; PIRSF038980; A2M_bac; 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:UP000001953};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..1738
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004196197"
FT   DOMAIN          871..1015
FT                   /note="Alpha-2-macroglobulin bait region"
FT                   /evidence="ECO:0000259|SMART:SM01359"
FT   DOMAIN          1076..1165
FT                   /note="Alpha-2-macroglobulin"
FT                   /evidence="ECO:0000259|SMART:SM01360"
SQ   SEQUENCE   1738 AA;  185724 MW;  0E84BE0F1C4C2A49 CRC64;
     MTGMVRTVVL CVALAIGFVS AQAADKVFKR DDLADAAIKL EAQIKSEAGT IAKSAPTLRT
     DADAAFKRSD FRSGLHILGQ IATVAPDDSG NWLRLARTIF QIKPTTSQEQ TFLRERASTA
     AYIAYQRARD PGAEADALAM LGRAFSERKL WRPALDTLGL SLDLREVADV REQYEKMRDD
     HGFRLLDYTV DSDSASPRVC FQFSEDLAKR TDFSPFVALA GADRPALSSE DKQLCVDGLK
     HGERYNINLR AGLPSTVKES LPKSAEFNVY VRDRKPFVRF TGRAYVLPRT GQRGIPLVSV
     NTQAVSAQVF RIGDRNLINT VIDSDFQKTL SGYQLSDIGN ERGVKVWSGE VTTASTLNAD
     VTTALPVDEA LGNLQPGVYV MTAAPKGPGS ANDEESGSLA TQWFIVSDLG LTAYSGNDGI
     HVFVNSLATT DAVGKAEVRL IARNNEILAT RKTDESGHAL FEPGLAGGEG GLSPALLTVS
     TDKADYAFLS LKSSAFDLTD RGVSGRAVPA GADAFVYAER GVYRSGETVY LTALLRDGQG
     NAVTGGPLTL VVERPDGVEF RRAVLADQGA GGRSLTLPLN SAVPAGTWRV RAFTDPKGPS
     VGETTFMVED YVPDRIEFDL MTMAKQIDAQ APVELKVDGH FLYGAPASGL QLEGDMLVAP
     AASRPGYAGY QFGVADDETT SNERTPIENL PEADANGVAT FPVSLATPPS SSRPQEAQIF
     VRMAEAGGRA VERKLVLPVA PAAAMIGVKP LFADKNVAEG DKAGFDVAFV APDGTSLARE
     GLRYELLKLE SRYQWYRQNS YWEYEPVKST KRVADGDLTI AANKPARIEL SPQPGRYRLD
     VKSSDPNGPL TSVQFDVGWY SDGSADTPDL LETSIDKQDY LSGDTMIVSV NARAAGKLTI
     NVLGDRLLTT QTTEVKEGTS QVKIQVGKDW GTGAYVVATL RRPLDVAAQR MPGRAIGIKW
     FGIDKTARTL SVNLSPPTLV RPSTTLKLPV KIGGLSPGED AKIVVAAVDV GILNLTNYKP
     PAPDDYYLGQ RRMTSEIRDL YGQLIDGMQG TRGQLRTGGD SAGAELQGSP PTQKPLALYS
     GIVTVAADGT AEISFDIPEF AGTARVMAVA WSATKLGRAT VDVTVRDPVV LTATLPRFLL
     TGDQGTMSFD LDNVEGAPGD YTVNVKASGP VTVAGNPATT ITLAAKQRSS MALTLNAGGA
     AGAAQFDVDI KGPNGLTLAR HYDLDVKPAT QILARRSVRT LAKGESLTLT SDMFSDLVAG
     TGGVSMSVGL SSALDAATVL KALDRYPFGC SEQITSRAMP LLYVNDLAAG AHLAMDTGID
     ERIKSSIDRL LARQGSNGSF GMWSSGGDDA WLDTYVTDFL TRAREKGFAV PETLFKSALD
     RIRNSVVNAS EPEKDGGREL AYGLYVLARN GAAPIGDLRY LADTKLNNLA TPIAKAQLAA
     ALALVGDRAR AERVYAAAAE SLAPKPVVEF GRTDYGSALR DAAALVSLAS EGNAPRATVT
     QAVQRVEAAR GLTPFTSTQE NAWLVLAARA LAKESMSLDV DGTPVKTALY RSYKAAEMAD
     KPIKIANTGD APVQAVISVA GAPMTPEPAV SNGFEIERNY FTLDGTPADP TQARQNDRLA
     VVLRITEAKP EYGHIMVADY LPAGFEIDNP HLVSSGDAGT LDWIEEGQQP VNTEFRDDRF
     TAAFDRAGND KAVFTVAYVV RAVSPGKYVL PQAYVEDMYN PSRYGRTGTG RVEVRPAK
//
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