ID A0A0N0V3A4_9RHOB Unreviewed; 1813 AA.
AC A0A0N0V3A4;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Apple domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=shim_33900 {ECO:0000313|EMBL:KPA20401.1};
OS Shimia sp. SK013.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae.
OX NCBI_TaxID=1389006 {ECO:0000313|EMBL:KPA20401.1, ECO:0000313|Proteomes:UP000037951};
RN [1] {ECO:0000313|EMBL:KPA20401.1, ECO:0000313|Proteomes:UP000037951}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK013 {ECO:0000313|EMBL:KPA20401.1,
RC ECO:0000313|Proteomes:UP000037951};
RA Voget S., Kanukollu S., Daniel R., Engelen B.;
RT "Genome Sequence of Shimia sp. SK013.";
RL Submitted (MAR-2015) 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:KPA20401.1}.
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DR EMBL; LAJH01000021; KPA20401.1; -; Genomic_DNA.
DR STRING; 1389006.shim_33900; -.
DR PATRIC; fig|1389006.3.peg.3487; -.
DR OrthoDB; 9767116at2; -.
DR Proteomes; UP000037951; Unassembled WGS sequence.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0004866; F:endopeptidase inhibitor activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd02891; A2M_like; 1.
DR CDD; cd01100; APPLE_Factor_XI_like; 1.
DR Gene3D; 1.50.10.20; -; 1.
DR Gene3D; 2.60.40.1930; -; 1.
DR Gene3D; 3.50.4.10; Hepatocyte Growth Factor; 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; IPR011626; Alpha-macroglobulin_TED.
DR InterPro; IPR021868; Alpha_2_Macroglob_MG3.
DR InterPro; IPR000177; Apple.
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; IPR003609; Pan_app.
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 Pfam; PF14295; PAN_4; 1.
DR Pfam; PF07678; TED_complement; 1.
DR PIRSF; PIRSF038980; A2M_bac; 1.
DR SMART; SM01360; A2M; 1.
DR SMART; SM01359; A2M_N_2; 1.
DR SMART; SM00223; APPLE; 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:UP000037951};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..1813
FT /note="Apple domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005860667"
FT DOMAIN 35..98
FT /note="Apple"
FT /evidence="ECO:0000259|SMART:SM00223"
FT DOMAIN 952..1096
FT /note="Alpha-2-macroglobulin bait region"
FT /evidence="ECO:0000259|SMART:SM01359"
FT DOMAIN 1158..1247
FT /note="Alpha-2-macroglobulin"
FT /evidence="ECO:0000259|SMART:SM01360"
SQ SEQUENCE 1813 AA; 194961 MW; 70FA3BD59719A815 CRC64;
MQRLARFVFS FISVMLVAQT ASAQQSYVPE RRVVVSRDLD FYGSDLTNLF DTTYEACVSA
CLSDSNCAAF TFNSRSNSCF PKSAVSDKQP YEGALSAEVL TTAPGAQSLG QTRAAEIGFL
GVSDLRRARD VAQDIGRIHA AGPWEVADML SAAAERRTAN ELLSAMRWTG GALSKKDSSD
LWLEYARLNA VVEGKKSSET RRYRDRAFFA AINGYLRADR DGARVSALLV LADRLEQRNR
GRNMVQTLRL AETIAPRDDV VAALDKAIAK YGFRITEHSV ESDLADPRLC VEFNEPLVKT
GVDYATYVKL PDARLAVQTE GSKLCVEGLS HGQRITATFR AGLPAESGET LIKDIEITTY
VRDRSPSVGF TGRAYVLPRT ADAGLPIETV NLDLVDLTLQ RVSDRNLLRA IQDSYFGKPM
SYWQIEDFGR DVAETIWTGS GEVQNTLNQT MSTRLPIGDA LKDQPAGVYA LTADLPGADI
YDETSTTQWF ILSDIGMTSL SGVDGLHVFV RHLNDASAWS NAKVTLLSRS NRVLGTTQSS
AEGYATFAAG LTRGTGGAAP ALVMIEAGED FSFLSLTDPA FDLSDRGVEG RLPAPPIDLF
VTTDRGAYRA GETIHVTALA RGDVAEALPG MPVTAILTRP DGVEYARHVS TNDAAGGHVF
SLHLGTTVPR GAWRISFKTD LDAPALATQK VLVEDFLPER IDFDLALPDA PLDSANMPPL
KVAARYLFGA PGADLEIEGE LRLTPRPDVA GFAGYTFGRH DAPFYSNTEY FSGDVTDAQG
NADVFLPLPD QTAEGLPLQA DIKVRVLEGS GRPVERSLTH PVAAAGAMIG LKPGFDRVVA
EGTSASFQVV ALNADLAPTK MKVQWSVNRV RTTYQWYQLY GDWQWEPTTR RTRIAGGELD
LTGGPVTIEA PVEWGQYEVV VEQIGGDSVA TSTDFYAGWY APADATDTPD TLELSLDKEG
YRSGDTANLR IVPRYAGTAL ISVMSNRLIA MKAVEVREGE NLIPLEVTDE WGAGAYVTAS
VIRPADGPAN QNPARSMGLS YAKIDPGAKQ LAVSIDTVAK ANPRGPLDVA VRVDGVAAGE
TAYVTVAAVD VGILNLTRFA SPDPSEHYFG QRRLGMEIRD LYGRLIDGMS GNMGALRSGG
DANAGGGFES PPPTEELVAY FSGPVEVGAD GNAQISFDLP EFNGTVRLMA VAWTATSVGQ
ADHDVIVRDP VVVTASLPRF LAPGDQSRLL LEIVHAEGSA GRMLLNVDAD GVTIAGAVPS
DVVLVDKGTA KLSVPVTAQD VGDHEIRVSL TTPDGKQLVK SLTIPVRAND PEISDTQQIT
LAAGETLTLG ADIFAELREG TGSAVISSGA LAKFDAPGLL QALDRYPYGC TEQVTSQALP
LLYFESVSTA LGLTQRDNVQ ERVDQAVAKV LTRQASNGAF GLWRAESGDF WLDAYVSDFL
SRARSKGYAV PDHAFRQAMD NLRSRVNYAP DFDEGGEDIA YAILVLAREG AAAMGDLRYY
ADVKSEAFAT PLAAAQIGAA LAYYGDQTRA DVMFRQAARL IEGQSAAEDA QLWRADYGTH
LRDAAGVLTL AMEAGSNAID ADAFAHRIAA SGQNLSTQES VWSLMAAHAL LEDDSASGLS
VDGTPLTGPL LRRFAGDIAT TPMAIRNDGD VPQSVTVTAI GVPDYPVTAG GYGYAIDREY
FAMDGTPLDP GNVRTGNRFV AVLTVEPFED GGARLMVNDP LPAGFEIDNP NLLESGDVRE
LDWLETVYSE SSEFRSDRFL AAVDWRSDMM FRLAYIVRAV SPGTYHHPAA SVEDMYRPQY
RANTDAQQLV VLE
//
