ID A0A1G1CP50_9BACT Unreviewed; 1725 AA.
AC A0A1G1CP50;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 13-SEP-2023, entry version 21.
DE RecName: Full=Intein C-terminal splicing domain-containing protein {ECO:0000259|PROSITE:PS50818};
GN ORFNames=A2W24_01835 {ECO:0000313|EMBL:OGV96781.1};
OS Microgenomates group bacterium RBG_16_45_19.
OC Bacteria.
OX NCBI_TaxID=1817747 {ECO:0000313|EMBL:OGV96781.1, ECO:0000313|Proteomes:UP000178440};
RN [1] {ECO:0000313|EMBL:OGV96781.1, ECO:0000313|Proteomes:UP000178440}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGV96781.1}.
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DR EMBL; MHDC01000018; OGV96781.1; -; Genomic_DNA.
DR STRING; 1817747.A2W24_01835; -.
DR Proteomes; UP000178440; Unassembled WGS sequence.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004866; F:endopeptidase inhibitor activity; IEA:InterPro.
DR CDD; cd02891; A2M_like; 1.
DR CDD; cd00081; Hint; 1.
DR Gene3D; 1.50.10.20; -; 1.
DR Gene3D; 2.20.130.20; -; 1.
DR Gene3D; 2.60.40.1930; -; 1.
DR Gene3D; 2.170.16.10; Hedgehog/Intein (Hint) domain; 1.
DR InterPro; IPR011625; A2M_N_BRD.
DR InterPro; IPR047565; Alpha-macroglob_thiol-ester_cl.
DR InterPro; IPR011626; Alpha-macroglobulin_TED.
DR InterPro; IPR041246; Bact_MG10.
DR InterPro; IPR036844; Hint_dom_sf.
DR InterPro; IPR030934; Intein_C.
DR InterPro; IPR001599; Macroglobln_a2.
DR InterPro; IPR002890; MG2.
DR InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR NCBIfam; TIGR01443; intein_Cterm; 1.
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; PF01835; MG2; 1.
DR Pfam; PF07591; PT-HINT; 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; SSF51294; Hedgehog/intein (Hint) domain; 1.
DR SUPFAM; SSF48239; Terpenoid cyclases/Protein prenyltransferases; 1.
DR PROSITE; PS50818; INTEIN_C_TER; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..36
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1674..1696
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 945..967
FT /note="Intein C-terminal splicing"
FT /evidence="ECO:0000259|PROSITE:PS50818"
FT REGION 1703..1725
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1706..1725
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1725 AA; 190496 MW; EA3EB2563C89F38B CRC64;
MKRLLRRLGC LNPTLPVFLG LTVMILSLGL TNVMLWGTRF NFSSNSPPSP ALPTPPEVLG
SWYQKEPAIM ISGGEGWSAN GGVIALASTD EPSVTIESYR VTGDVTVKLY PATEAQLFAY
LTYNDDYQQI NPAVTPSTNP ITEFTYTLPG ENNQGSPLVL PLEPSGLYHL NISNGSAHAD
AFVIRSQTGV LVKEGDNQFV FWGQDYQTKR SLNQGTIRIL SAKNQATDLT TAVFNDSGIA
TAPISYQADF AWVSRDADRA LVPLNLKYLN SRYQSSTYVE KYRHVKHFVF TDRPLYQPGD
PVYFKAVIRD DDDARYTLPT SPVTIRVSNG YGNDQEVIYE NTYSVNSFGS IDGQFKLPQD
VKTTYYTITL DPGPTGKPDN YYDYDSWSDS HTSFQVEFYR KPDYFLTVTS DKNEYIAGDS
ITYTLQGQYF SGQPLTYKSV DYELRTSSWG DYDYHVDATF DKDNYRYGRF GSDKLESNRV
RLDDKGQAKV TLPAKNHEGK SQLYTLTTKL VDETGTADEA FKNVLVYSGE FGLYRTDYAY
GFTIGEPIAV PLKAVSRLNQ SVANLTLNVK SLRSWYEKQP LQTGEKYHRY LRQTEDLPNQ
TLKTDTDGQA TLNLTPQKGG NYEFTVTGQD NRGNQVVKST SVWVNDTTNP VYFEEYRQGL
DLSVDTKLAQ PDGSVKLTLI SDIPDRDIFL GFERDRLNRF QIIRLTGTST TETIPLTLTD
MPNIFLTASS FSTDWLDTDS LNLPIDTAQK HLVVHLTPNE AQYGPGDTVN LNLVATDKLG
RPVSAELAVW AVDKAIFELV DPSNLNIFNA FWRERYDTTP EDHSLEGITV LTAEGGGCFV
GDTPILMADG TQQPISQVRS GDHLLTRISQ TDPTLVPALV TSTHHASDTG YLTINGVLKV
TVNHKLWVNQ VFTEAGTIMV GDVLVDSGNR PVVVETIEYT RLKVPVYNLE VANYHTFFAG
GVWVHNQKGE ARSIFKDTAY WNPRVVTDNN GRAQLSFKLP DNLTTWTIAA VGTSLDTIAG
DAKQDIVVSK DIIVRPVLPN LLRLGDQATV RALLHNFSDK KYTFNLDLAF DSGDIDTATR
SGLVLEPNDF AQVEFKVKPI KVTDAAKFRF RGLSVDDPKV NDIITVTIPI RPFGFYDSRG
SASAQGNHTF NLVLPVQIDP DLSTITLNLA PTLLGTLPQA MQFLLDYPYG CVEQTTSRFV
PLVIAKTNPD LFSQALLDQD TDAMVKKGIE RLTTLQNPDG GWGWWSEGNS DPFITAYVIE
YLVTAQKYGL AIPQELIDRA ADYYDQATYL TESQGNRQLF AGSAQVAKAY ALTFLSETRD
RSLLNQFDHY PPDLLSWAVI TNVKNSHTDS NQNGAHTLLA KAIVQGDGLS WSAGEDSHFG
SVDATTAMAV RALTAAGLKN DAYKGVLYLT RSRTKPYWSN TFATAQVAQA LVDYGRSGTE
LTPNYTYTVT LDGQTLKTGQ VTSKTQVIPP LTVPVASLKS SNPTVAVAFD GEGQLYSTLS
QKILITDPQS SPVTDGIAVT REYVNDKDPT FSLGVGDTVS VRLTVNNPGN FGAYAVIDDE
LPAGLVPINP AFNNESSGRF DRYGQGVWGQ EITENGMILS LAGLDPGNSV FTYKARVVTE
GSYLTPPARV HLMYAPEVYA RTGSETVTID REAVFDPARA VRNVISPPAK RPPWLIIGVG
VSIVIILISL FVSIWYRRRH RSKVQPPLSP PSPSSLPPTP VPPAA
//
