ID A9V273_MONBE Unreviewed; 1620 AA.
AC A9V273;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 24-JAN-2024, entry version 67.
DE RecName: Full=Fibronectin type III-like domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=MONBRDRAFT_32870 {ECO:0000313|EMBL:EDQ88329.1};
OS Monosiga brevicollis (Choanoflagellate).
OC Eukaryota; Choanoflagellata; Craspedida; Salpingoecidae; Monosiga.
OX NCBI_TaxID=81824 {ECO:0000313|EMBL:EDQ88329.1, ECO:0000313|Proteomes:UP000001357};
RN [1] {ECO:0000313|EMBL:EDQ88329.1, ECO:0000313|Proteomes:UP000001357}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MX1 / ATCC 50154 {ECO:0000313|Proteomes:UP000001357};
RX PubMed=18273011; DOI=10.1038/nature06617;
RG JGI Sequencing;
RA King N., Westbrook M.J., Young S.L., Kuo A., Abedin M., Chapman J.,
RA Fairclough S., Hellsten U., Isogai Y., Letunic I., Marr M., Pincus D.,
RA Putnam N., Rokas A., Wright K.J., Zuzow R., Dirks W., Good M.,
RA Goodstein D., Lemons D., Li W., Lyons J.B., Morris A., Nichols S.,
RA Richter D.J., Salamov A., Bork P., Lim W.A., Manning G., Miller W.T.,
RA McGinnis W., Shapiro H., Tjian R., Grigoriev I.V., Rokhsar D.;
RT "The genome of the choanoflagellate Monosiga brevicollis and the origin of
RT metazoans.";
RL Nature 451:783-788(2008).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the SYF2 family.
CC {ECO:0000256|ARBA:ARBA00010028}.
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DR EMBL; CH991555; EDQ88329.1; -; Genomic_DNA.
DR RefSeq; XP_001746922.1; XM_001746870.1.
DR STRING; 81824.A9V273; -.
DR EnsemblProtists; EDQ88329; EDQ88329; MONBRDRAFT_32870.
DR GeneID; 5892241; -.
DR KEGG; mbr:MONBRDRAFT_32870; -.
DR eggNOG; KOG2609; Eukaryota.
DR InParanoid; A9V273; -.
DR Proteomes; UP000001357; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046556; F:alpha-L-arabinofuranosidase activity; IBA:GO_Central.
DR GO; GO:0009044; F:xylan 1,4-beta-xylosidase activity; IBA:GO_Central.
DR GO; GO:0031222; P:arabinan catabolic process; IBA:GO_Central.
DR GO; GO:0045493; P:xylan catabolic process; IBA:GO_Central.
DR CDD; cd00161; RICIN; 1.
DR Gene3D; 2.80.10.50; -; 1.
DR Gene3D; 3.40.50.1700; Glycoside hydrolase family 3 C-terminal domain; 1.
DR Gene3D; 3.20.20.300; Glycoside hydrolase, family 3, N-terminal domain; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR044993; BXL.
DR InterPro; IPR026891; Fn3-like.
DR InterPro; IPR002772; Glyco_hydro_3_C.
DR InterPro; IPR036881; Glyco_hydro_3_C_sf.
DR InterPro; IPR001764; Glyco_hydro_3_N.
DR InterPro; IPR036962; Glyco_hydro_3_N_sf.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013260; mRNA_splic_SYF2.
DR InterPro; IPR035992; Ricin_B-like_lectins.
DR InterPro; IPR000772; Ricin_B_lectin.
DR PANTHER; PTHR42721:SF3; BETA-D-XYLOSIDASE 5-RELATED; 1.
DR PANTHER; PTHR42721; SUGAR HYDROLASE-RELATED; 1.
DR Pfam; PF14310; Fn3-like; 1.
DR Pfam; PF00933; Glyco_hydro_3; 1.
DR Pfam; PF01915; Glyco_hydro_3_C; 1.
DR Pfam; PF08231; SYF2; 1.
DR SMART; SM01217; Fn3_like; 1.
DR SMART; SM00458; RICIN; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
DR SUPFAM; SSF50370; Ricin B-like lectins; 1.
DR PROSITE; PS50231; RICIN_B_LECTIN; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000001357};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 34..53
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 65..84
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 716..737
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 749..767
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 754..891
FT /note="Ricin B lectin"
FT /evidence="ECO:0000259|SMART:SM00458"
FT DOMAIN 1541..1611
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 1620 AA; 174373 MW; 46DB774A655F300E CRC64;
MLHNPTARVC VCVSLSFSLS LSLSLSLSLS LSLSLSLSLS LCLSLSLFIS LSVSHQFFAH
TVSMAVTHYC IAALVAVACL AASVQAQANL GLSMPLKAFN GALTTAAQTV ANDLNNVALP
TCCYDDVGAK HVHLDMQDMK ISGSTVTFSI VKSSSTTYAL NGAVSMTVSG SYRLCIHDDP
FGHGCSTIKG CKGDWQLQPD FSFSMPINME AATSGAPKIT PGTVTIPTYT LNNNFCSLFS
DAISKGLDGM KANLAQSLQS AAVNVAAKLQ AAIPQTVNAG KLGQMSLNYL VPASGGLTNL
DTAAVAGFAA AAPRAQAGTM PNIDDGYYHI TMGDSLLTSA FDTIVAEGLF NVTIKEDGLV
LGLTFVRSVP PQVNISSNEF TVMLGLHYDL SDNGTHSSGD IILQAGIDTK FSAGANQTIV
LQLALTNATN VGMGPNCQGA CEIVVQTIRK YQAPIINGIN NYLQDKPVVF PAPPSDMSSV
VEEDRVSKLP KGYEKRKANA EWELEDQAKR EAAEAEGKDY ARVKAMQMSV DQAERHVKKR
THKNVDETID RTAYSYTALK QYENMTKKIK PNMGQYSASM QGDQDHRPSA AAIDDMVEDL
EKAYVTASVA NDGLKIKRKE KLKDRRRRGD VVFEESDVNF INDKNMKYNR SLEKFYGSYS
REIKDNLERG TAFSVIVAFV CEETGLLRVV PNLKLVANLR QSKHPPRPKF QKGTRFVSVF
LFYFLSLSLS LSLSLSLSLS LSLRKRTSAM KLGGCTVWAV ALLALSVNGD AGPLLGLNKC
DASNPNQIFA RGTADEIILN STGACVDVPS YATAHTHLTA MSTGPFLALC WHDQFGFLHK
QNEAWLVNSN KTITERSTGL CIAPAFDAAS VGQTVMINTC TGSTAQKWIF TSEGLLQNGA
DTSLCIDAAP PRPRPCDELP AKNFPFCNAS LDLDTRIRDV ISRLSIQDKV ALTANTAGAA
ADAGLPAYQW WSEALHGVGF SPGVTFMGKV QAATSFPQVI HTSASFNKTL WHHIGMTIST
EARAMNNVNQ AGLTFWAPNI NIIRDPRWGR GQETPGEDPY ATGLYAANFV PGMQEGEDTR
YIKASSCCKH FFDYNLEDWH NVDRHHFNAI ATDQDIADTY LPAFESCVRF GRASSLMCSY
NAVNGVPSCA NADIMTTLAR EAWGFDGYIT SDCGAVEDVY SNHKYYNTTG ATVNGVLSAG
MDVDCGSFLS QHLADAIDSG DVTNATVDQA LYNLFRVQFR LGMFDPAEDQ PYLNLTTDAV
NTPEHQQLAL EAARQGMTLL ENRDSRLPLD ASSIKQLALI GPNANATGVM QGNYNGKAPF
LISPQQGVQQ YVSNVALELG AVTAAKAADT VVMVIGLDQT QESEGHDREI IALPGMQAEL
VAQVANASSS PIVVVVMTGG AVDLTPVKDL DNVGQAGGQA LAETLFGDNN PGGRLPYTLY
PADLVNQVSM FDDGMRPNAT SGNPGRTYRF YTGTPVYAYG TGLSYTSFSY ETSTPSLRVS
AERVRAWVAA RGQTSFIRDE VDAEDYITVT VQNNGTVAGA DVVQVFIKTT TPGADGNPIK
SLCGFERVFL KPGETTSIQF PVTPHDLSVV NSRGERVAVP GTWTVEVHHE ARLSIPISVE
//
