ID C6VTY2_DYAFD Unreviewed; 1819 AA.
AC C6VTY2;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE SubName: Full=Alpha-2-macroglobulin domain protein {ECO:0000313|EMBL:ACT94750.1};
GN OrderedLocusNames=Dfer_3542 {ECO:0000313|EMBL:ACT94750.1};
OS Dyadobacter fermentans (strain ATCC 700827 / DSM 18053 / CIP 107007 / KCTC
OS 52180 / NS114).
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC Dyadobacter.
OX NCBI_TaxID=471854 {ECO:0000313|EMBL:ACT94750.1, ECO:0000313|Proteomes:UP000002011};
RN [1] {ECO:0000313|EMBL:ACT94750.1, ECO:0000313|Proteomes:UP000002011}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700827 / DSM 18053 / CIP 107007 / KCTC 52180 / NS114
RC {ECO:0000313|Proteomes:UP000002011};
RX PubMed=21304649; DOI=10.4056/sigs.19262;
RA Lang E., Lapidus A., Chertkov O., Brettin T., Detter J.C., Han C.,
RA Copeland A., Glavina Del Rio T., Nolan M., Chen F., Lucas S., Tice H.,
RA Cheng J.F., Land M., Hauser L., Chang Y.J., Jeffries C.D., Kopitz M.,
RA Bruce D., Goodwin L., Pitluck S., Ovchinnikova G., Pati A., Ivanova N.,
RA Mavrommatis K., Chen A., Palaniappan K., Chain P., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Goker M., Rohde M., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Dyadobacter fermentans type strain (NS114).";
RL Stand. Genomic Sci. 1:133-140(2009).
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; CP001619; ACT94750.1; -; Genomic_DNA.
DR RefSeq; WP_015812994.1; NC_013037.1.
DR STRING; 471854.Dfer_3542; -.
DR KEGG; dfe:Dfer_3542; -.
DR eggNOG; COG2373; Bacteria.
DR HOGENOM; CLU_000965_1_0_10; -.
DR OrthoDB; 9767116at2; -.
DR Proteomes; UP000002011; Chromosome.
DR GO; GO:0005615; C:extracellular space; 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; 2.60.40.1930; -; 1.
DR Gene3D; 2.60.40.3710; -; 1.
DR InterPro; IPR011625; A2M_N_BRD.
DR InterPro; IPR047565; Alpha-macroglob_thiol-ester_cl.
DR InterPro; IPR011626; Alpha-macroglobulin_TED.
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; 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 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000002011};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..1819
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002972036"
FT DOMAIN 932..1070
FT /note="Alpha-2-macroglobulin bait region"
FT /evidence="ECO:0000259|SMART:SM01359"
FT DOMAIN 1134..1222
FT /note="Alpha-2-macroglobulin"
FT /evidence="ECO:0000259|SMART:SM01360"
SQ SEQUENCE 1819 AA; 200112 MW; 0805B6D46437AE8D CRC64;
MKKTAILCSF CVLFLVWVFT SCSSFNEIRV AGTNFTEEVG QSQNLVFTFN KDLVSTAELN
SWDSTQFVTF EPAVRGKFKW TAPNELVFSP VAGFGAATSY KAQLTDLITE KSYKDKKYKL
SQDPITFHTP YLQLAETESW WTLSSETGRQ EARIRLHFNY PVNAQHVAEK LKVLSGNQAL
EYRILPSQDE SAVTLAFAKV GAADNNETAV NITIDKGVKV QNTSYSSQEA LSKTVSIPSP
LHLEVVDIKT GFENNAGYAR VITTQELDKE SIAGSVAVNP EAAVETEPTE NGFIVRGAFN
ETETYVLQLK QSLKGVLGQT LEEEASRDLF FGKMPAAISF ANKKGLYLST KSSRNIGVNI
VNVPKVQVRI SKLYANNILH YIHNNRWNDY AYVGDDWQPT GNFNYSDDRE SQLSDVIVNK
IVETANLSKN KGISALNIAL PDDNKRQGVY LVAVNSEEEA YLGATKLVSI SDIGLIAKQG
KDELWIFANS IKTNEPIKDL ELTVVSSNNQ SVHTFKTDAD GIAHVDKLSE KAPGFKVAMI
TASTQDDFNF LLLEDSQVLT SRFDVEGLRD NASGYQVFIY GQRDIYRPGE TMHFNTVLRT
QDWKTAGKVP LKLRLLTPNG REFRTWRKTT NEQGAVESEI PLDAGVLTGT YVLEVYNANE
VLLGSQAVSV EEFMPDRIKV DLSRAAKDYM SGQKVSLTAT AINLFGPPAS NRNYQMDFQL
QRKGFTAKAF PEYSFNIPAQ TAFERDSRQG ITNEQGQASE QFALAAGLQD IGVLEGKIYV
TVFDENGRPV NRLQRFDVYT QPVFYGIRLP DSYVGTNAPV PVDIVGVGKS GALQNGATAS
IEVVRLEYQT VVEKKYERLQ YTSRKKEKLV YSNKLTLAGG KGTFRYVPTV SGEYEVRVKR
PGATHYTLAN FYAYGYGYTQ YSSFEVSNEG QVLMETDKDS YKMGESARVL FKTPFDGRLL
VTVERNNVLE QHILTTEKKA AELTFKIKEA HLPNVFVTAT LIRPLDASNM PLTVAHGFQP
IAVEDPDRRL PVSITAVEKS RSKMKQQIRI KTEPNAEVTL AIVDEGILQI KNSKTPDIHG
HFYQKRALEV TSYDLYAQLF PELSISGTSS SGGDGYDLER RINPLSNGRT ELVSFWSGQL
KANGSGDVTF DVNIPQFSGD LRIMAVAYKD NAFGSATKNM KVADPIVISA GLPRFLSPGD
ELVLPVNISN TEAKGTTATV SVQLAGPLAA GQAPVTQNIS IPAGKESRAV FSLKALTAIG
VGKVTVKVNA FKETFVNQTE ITVRPASPLL KTNVSGLIAA DKQGQIDLRS SFIPATASSQ
VVLSRSPLVQ GGGKALSTLL GYPYGCLEQT VSKAFPQIYF ADLTKAMATP VYTVKSGESD
FNPMTNVQQA IRKVESQQLF NGGVGMWPGA TREDWWATAY AVHFLEEARR AGFEVNAKTL
SRAVEYLTAQ SGTTANREVV VASTGNGLAY DAQPTGTQTR KTVARREAIY SLYVLALNGH
PNRASMNYYK QNPHLLTADS KYLLAGAFQL AGDARSFNAL LPRTYVAENA GRYTDDSYSS
PLRNMSLVLN TLIESDPSNA QIQVLGRQLS QAIQSASYLN TQEAAFAVLA LGKLARKTAN
STVTASVSAN GKPLGQFTGK ELKISKGIIN QKLQVKTQGK GDLYWFAQTA GMSATGNYVE
EDQGISIRRQ FLTRSGAPVQ SFRQNDLVVV KLTLASTNGL PVENIVVTDL LPSGFEIENP
RITEPRDMPW ITKASVPEYY DIRDDRIHFF TTADAQEKTF YYQVRVVSKG TFTVGPAAAD
AMYQGEYRSY SGGGKITVE
//
