ID A0A1B9Y335_9FLAO Unreviewed; 2140 AA.
AC A0A1B9Y335;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Alpha-2-macroglobulin {ECO:0000313|EMBL:OCK44224.1};
GN ORFNames=BA195_05950 {ECO:0000313|EMBL:OCK44224.1};
OS Tenacibaculum soleae.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Tenacibaculum.
OX NCBI_TaxID=447689 {ECO:0000313|EMBL:OCK44224.1, ECO:0000313|Proteomes:UP000093186};
RN [1] {ECO:0000313|EMBL:OCK44224.1, ECO:0000313|Proteomes:UP000093186}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCD-KL19 {ECO:0000313|EMBL:OCK44224.1,
RC ECO:0000313|Proteomes:UP000093186};
RA Eisen J.A., Coil D.A., Lujan K.M.;
RT "Draft Genome Sequence of Tenacibaculum soleae UCD-KL19.";
RL Submitted (JUN-2016) 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}.
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:OCK44224.1}.
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DR EMBL; MAKX01000001; OCK44224.1; -; Genomic_DNA.
DR RefSeq; WP_068703392.1; NZ_MAKX01000001.1.
DR STRING; 447689.BA195_05950; -.
DR OrthoDB; 9767116at2; -.
DR Proteomes; UP000093186; Unassembled WGS sequence.
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; IPR041246; Bact_MG10.
DR InterPro; IPR008969; CarboxyPept-like_regulatory.
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; PF13715; CarbopepD_reg_2; 1.
DR Pfam; PF01835; MG2; 1.
DR SMART; SM01360; A2M; 1.
DR SMART; SM01359; A2M_N_2; 1.
DR SUPFAM; SSF49464; Carboxypeptidase regulatory domain-like; 1.
DR SUPFAM; SSF48239; Terpenoid cyclases/Protein prenyltransferases; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000093186};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..2140
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008640128"
FT DOMAIN 986..1127
FT /note="Alpha-2-macroglobulin bait region"
FT /evidence="ECO:0000259|SMART:SM01359"
FT DOMAIN 1361..1451
FT /note="Alpha-2-macroglobulin"
FT /evidence="ECO:0000259|SMART:SM01360"
FT REGION 1322..1347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1328..1347
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2140 AA; 245699 MW; C9D2A7C7455E5341 CRC64;
MKKITPFLLL ILFSSLVNAQ ENYKNLWNEV QEFEKDNLPK SALKVVNNIY AKAEATKNSP
QIIKALFYKS KFSLALEEGA QLKIINQFKE QIDKSSFPTK NLLENVLANL YWQYFNQNRW
KFYQRTKTSE KIDENDFRTW DLDTLFAEIH SYYQKSLANG LLLQQADIYE FSDILHTAKN
SKEYRPTLFD FLAHNALKFY KTSETNITKP AYQFKIDNPK LISDAGSFST INLTSKDAIS
LQLNALKIYQ ELLSFHLKDN NLKALATVDL ERLNFVNQHT TLNDKEQLLL QTLKSAENNY
KKQEIAGLYS YKIAEIYKQQ ASSYNSNKNE TFRFKNKEVL TICNRVITQF PKSIGAKKCE
ALKQQITTKK LTVLTEKFSP INTASRLLLT YNNIDTLYFT TYKISRDQVE ELNTIYKEEE
RVNFIKKLTI ATSWNTKLRN ELDYLSHTTE VIVPKLAQGN YLIIAHENET LNTTDLLATA
NIQVSNLVLI ESTDNNIKTY QVVDRNTGKP IKNAQLLLKN KEYRNRKSIN QKLITDKNGF
ATYKSNQTFY NVFITVTTKN DKAIFGDYYL YKYQKPTIDT QNESIKIKPF IFTDRSIYRP
GQTVYFKTIF IQKKDDKSTP FTNKYVEITL NDVNGQEVKK LDLKLNEFGS ASGEIVLPNN
GLTGEYSFNI DESNKEESTF YNTVDFDFER DDYITTISVE EYKRPKFETD FKPVTETFKL
NDSITVNGFA KAFSGANITD AKVVYRVHRK VQYPNWWYWR RPNSSSEAQE ITHGESITDA
AGNFAIKFKA LPDESVSKEG LPIFNYEITA DVTDINGETR SATTIVKVGY HALTASLQIN
SIIDKDEKQH KIKINTENLN NEFVAASGTV KIYKLKAPKN PLRKRPWNTP DYQDIPEDEF
RKLFPHDAYT KEEQGEAFWK KGKLVFEKEF DTKKSKEHVF KTTKSWSSGK YIAVLTTRDK
FKQQVTDKAN FTVTSAREKK IADSKLLFIT KNKTNYSIGD MVSLELASAS KDITVVVQIE
KNHKIVNTQL VHLNNNKKSI EIPVTKEDIG SFSVKYYFVN YNSFSSGALN ISVPKKDELI
TIETTTFRDK IQPGVQEKWS FTIKNDKRNK VTAEVLASMY DASLDEFKPH NWQFNPITTS
NYYSYGNTAN AHQSFGNNSF RVYNRSYSNN RYQPQQYDQF NWFGFSLNNH SWTNERYLKK
LKLRDKIKTS GKYSGTIKGI VSDESGPLPG VTITIKGNTE GTETDFDGDF TIKAKKGDIL
VLSFVGMQTI EKVIGDFSNL NILMINNSNT LDEVVVMGYG TSPKKAFTGT ARKAISGKVS
GLNIENNEAD ESEEKSPKNV QEKQEKTSLK GIQIRKNLQE TAFFFPHLTT DKKGNITFSF
TTPEALTKWK LQLLAHTKKA QSVVKTLTTV TQKELMITPN APRFLREGDK ITLSAKISNL
SDKNLRGISQ LILTDAITGK EIHLLENTTK NQSFKVDTNG NTNVSWNLTI PETVQAVQYK
IIAKAGDFSD GEQNVLPVLS NRMLVTETLP MWVRSNQTKT FTLDKLKNNT STSLKHHKLT
LEVTSNPAWY AVQALPYLME YPYECSEQTF TRYYANTLAS HIANSNPRIQ EVFKQWKSSD
ALVSNLEKNQ ELKSLIIQET PWLRDAQSET EQKKRIALLF DLNKMKNEQQ KSVHKLRNMQ
LNTGGFPWFK GSDYANTYIT QHIVSGFGHL KKLGIKNFDA STNEMLQKAI RFLDQEIVVQ
YSDLLKQAAK IKATKGVVKY EEYLKKNHLN YFTIQYLYMR SFHPEITFSN ATKSAIKYYK
NQTAIYWNAY NLYAKGQIAL IQFRADNQSI STKIIKSLKE NSITSDELGM YWKANVAGYY
NYEAPIETQA LLIEAFSEIE NNTKTIDNLK IWLLKNKQTN RWQTTKATTE AVYALLLQGN
DWLSITDMVD LKIGNQKIAP TKLKNVKVEA GTGYFKTSWN KEEIKSDMAE VTISKKGKGI
AWGGLYWQYF EDLDKITTAE TPLKIKKKLF KKVNSDTGKE LVEVTTKTNL KVGDLITVRI
ELRSDRDMEF IHMKDMRASG VEPINVLSQY KWQDGLGYYQ ATKDAATNFF FDRLPKGVYV
FEYDVRANNK GNFSNGITTI QNMYAPEFNS HSNGKSLIIK
//
