ID A0A1Q7ZA32_9CYAN Unreviewed; 631 AA.
AC A0A1Q7ZA32;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=Cohesin domain-containing protein {ECO:0000259|Pfam:PF00963};
GN ORFNames=AUI36_09230 {ECO:0000313|EMBL:OLE64381.1};
OS Cyanobacteria bacterium 13_1_40CM_2_61_4.
OC Bacteria; Cyanobacteriota.
OX NCBI_TaxID=1805101 {ECO:0000313|EMBL:OLE64381.1, ECO:0000313|Proteomes:UP000186010};
RN [1] {ECO:0000313|EMBL:OLE64381.1, ECO:0000313|Proteomes:UP000186010}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27843720;
RA Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., Singh A.,
RA Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., Northen T., Pan C.,
RA Banfield J.F.;
RT "Proteogenomic analyses indicate bacterial methylotrophy and archaeal
RT heterotrophy are prevalent below the grass root zone.";
RL PeerJ 4:E2687-E2687(2016).
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:OLE64381.1}.
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DR EMBL; MNHI01001208; OLE64381.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q7ZA32; -.
DR Proteomes; UP000186010; Unassembled WGS sequence.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:InterPro.
DR CDD; cd14256; Dockerin_I; 1.
DR CDD; cd08547; Type_II_cohesin; 1.
DR Gene3D; 2.60.40.680; -; 1.
DR Gene3D; 2.60.40.1120; Carboxypeptidase-like, regulatory domain; 1.
DR Gene3D; 1.10.1330.10; Dockerin domain; 1.
DR InterPro; IPR013784; Carb-bd-like_fold.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR002102; Cohesin_dom.
DR InterPro; IPR002105; Dockerin_1_rpt.
DR InterPro; IPR036439; Dockerin_dom_sf.
DR Pfam; PF13620; CarboxypepD_reg; 1.
DR Pfam; PF00963; Cohesin; 1.
DR Pfam; PF00404; Dockerin_1; 1.
DR SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR SUPFAM; SSF49452; Starch-binding domain-like; 1.
DR SUPFAM; SSF63446; Type I dockerin domain; 1.
PE 4: Predicted;
FT DOMAIN 138..247
FT /note="Cohesin"
FT /evidence="ECO:0000259|Pfam:PF00963"
FT REGION 113..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 631 AA; 66709 MW; E972A76AA2BDBDA5 CRC64;
MFSGLGNGPY TVTPSKSPEV DGITSFDAAL VAQYVVGLIT LTPNQQIAAD VSNNGAITSF
DAALIAQASV GLPNASIAGT WKFVPSSRTY PNTAADQPNQ NYEAILVGDV SGNWTSGGQS
PSSQTAPESA VTSIPVALPN QASPPGATSM IPITVGDLTG QNVISYDFDI TFDPKVLQPR
VAATNSNGTL SGAMTITANT AAAGHFRVAA FGTTPLSGSG TLLILNFTVI GTPGASTPLT
WQSAALNEGN PQAGATNGQF SVSSPTAAPA TISGQVTTPD GAPLAGVVIR LSGTQSSKTI
TDGNGSYHFD NADTGGLYSV TPSRADFLFS PANRSFSLVA NKTDAIFTAV PDAIPTANPL
DTPEFFVRQQ YLDFLGREPD RGGFEYWSER ISACHSDTGC IRVRRIAVSN AFFYEQEYQQ
TGSYVFRLYR AAFGNNQAFP NPDDSNLTEA KKLPSYAAFA GDRGRVVGGS TLAQSQLDLA
NAFVQRPEFT NGYPVILDGP GFVDALLTTI KNDSGADLTL QRQALIDLFN AGGRGNVLYR
LADDNAQTNS VNNRAFIDAE YNRAFVFTQY AGYLRRDADI SGFLFWLGQV SSAPLREVSK
QHAMVCSFVT SAEYQKRFSS VVTHSNAECP Q
//
