ID D8TJC1_VOLCA Unreviewed; 1728 AA.
AC D8TJC1;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=alpha-mannosidase {ECO:0000256|ARBA:ARBA00012752};
DE EC=3.2.1.24 {ECO:0000256|ARBA:ARBA00012752};
DE Flags: Fragment;
GN ORFNames=VOLCADRAFT_115992 {ECO:0000313|EMBL:EFJ52516.1};
OS Volvox carteri f. nagariensis.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Volvocaceae; Volvox.
OX NCBI_TaxID=3068 {ECO:0000313|Proteomes:UP000001058};
RN [1] {ECO:0000313|EMBL:EFJ52516.1, ECO:0000313|Proteomes:UP000001058}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=f. Nagariensis / Eve {ECO:0000313|Proteomes:UP000001058};
RX PubMed=20616280; DOI=10.1126/science.1188800;
RA Prochnik S.E., Umen J., Nedelcu A.M., Hallmann A., Miller S.M., Nishii I.,
RA Ferris P., Kuo A., Mitros T., Fritz-Laylin L.K., Hellsten U., Chapman J.,
RA Simakov O., Rensing S.A., Terry A., Pangilinan J., Kapitonov V., Jurka J.,
RA Salamov A., Shapiro H., Schmutz J., Grimwood J., Lindquist E., Lucas S.,
RA Grigoriev I.V., Schmitt R., Kirk D., Rokhsar D.S.;
RT "Genomic analysis of organismal complexity in the multicellular green alga
RT Volvox carteri.";
RL Science 329:223-226(2010).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 38 family.
CC {ECO:0000256|ARBA:ARBA00009792}.
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DR EMBL; GL378324; EFJ52516.1; -; Genomic_DNA.
DR RefSeq; XP_002946589.1; XM_002946543.1.
DR STRING; 3068.D8TJC1; -.
DR GeneID; 9617735; -.
DR KEGG; vcn:VOLCADRAFT_115992; -.
DR eggNOG; KOG4342; Eukaryota.
DR InParanoid; D8TJC1; -.
DR OrthoDB; 2786490at2759; -.
DR Proteomes; UP000001058; Unassembled WGS sequence.
DR GO; GO:0004559; F:alpha-mannosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006013; P:mannose metabolic process; IEA:InterPro.
DR Gene3D; 3.20.110.10; Glycoside hydrolase 38, N terminal domain; 1.
DR Gene3D; 1.20.1270.50; Glycoside hydrolase family 38, central domain; 1.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR041147; GH38_C.
DR InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR InterPro; IPR011682; Glyco_hydro_38_C.
DR InterPro; IPR015341; Glyco_hydro_38_cen.
DR InterPro; IPR037094; Glyco_hydro_38_cen_sf.
DR InterPro; IPR000602; Glyco_hydro_38_N.
DR InterPro; IPR027291; Glyco_hydro_38_N_sf.
DR InterPro; IPR028995; Glyco_hydro_57/38_cen_sf.
DR InterPro; IPR009291; Vps62.
DR PANTHER; PTHR46017; ALPHA-MANNOSIDASE 2C1; 1.
DR PANTHER; PTHR46017:SF1; ALPHA-MANNOSIDASE 2C1; 1.
DR Pfam; PF09261; Alpha-mann_mid; 1.
DR Pfam; PF17677; Glyco_hydro38C2; 1.
DR Pfam; PF07748; Glyco_hydro_38C; 2.
DR Pfam; PF01074; Glyco_hydro_38N; 1.
DR Pfam; PF06101; Vps62; 1.
DR SMART; SM00872; Alpha-mann_mid; 1.
DR SUPFAM; SSF88688; Families 57/38 glycoside transferase middle domain; 1.
DR SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00023295};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000001058}.
FT DOMAIN 510..591
FT /note="Glycoside hydrolase family 38 central"
FT /evidence="ECO:0000259|SMART:SM00872"
FT REGION 721..753
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EFJ52516.1"
SQ SEQUENCE 1728 AA; 188474 MW; C0922001D3FA994F CRC64;
SSSSRVWVPQ HHRDITLGRL DGYLAADGQF SDRTIRADMW SRKCAECVSL EVYSHPRGIP
YPTYDEAIRM PYCPAKVGDS FGPSWTTHWF RVRARVPPDW DGLGPLMFRW DSGSEAMLYT
EGPTPRQGIT DQRNEYQLGE WAVGGQELLF YVEMAANGMF GNGPSTNNIQ PPDENRYFTL
KTAELAIPNL PVVALFHDLR ALTGLAKELP AGNATGEIAL YTANKIVNTY FQGAPPECVS
VCRSLAAEVL AVRDPGERLQ VYAVGHCHID TAWLWPFSET HRKTARSWSS QLRLAERYPW
HVFTASSAQQ YEWLLQDYPG LFSEIQEAAA RGTFVPVGGT WVEMDTNLPS GESLIRQFLY
GQRFFEAHFG SRCDVFWLPD TFGYSGQLPQ IARGAGIRYF LTQKLSWNNI NTFPHSTFQW
AGLDGSSLLT HFPPANTYNA QADAHDILLT ATNSKDKDRA PAGYMLYGNG DGGGGPTVDM
CESLSRLAGC RGLESLTVAS PSERGELYFE LHRGTYTSHA ANKSHNRSCE LLLREAEAAG
ALAAAVLPAD VYCYPRSEID AIWKDVLLFQ FHDVLPGSSI GQVYDYTAER YPILEFNIRK
IRDAALEALL AAAGGATATA AVGATVPCGS SSCNDSNYYC VGGGGGGGGV GTLHSAEVVG
ARPLNPHVCH SAPSPYNNPL SVAQDCYVVP RAGGQVSAIA RALARIVSCG HCWRRCGSQR
CTAGSGRPPP PPPPAQHQSH YRQGAEGETE GGRGALPRVV TAAAAAAAAA AAPVTGSGGF
SPGTVVGAAA RVRTTVGWVY NSMAFHRREV VSVPVEMLPP GVSVRQLSAD RTAALVVVDV
PPLSLTPLLQ QDLAAGYGSA APALAPAPSA PACGGRDDAP WVGGGATILR ETTRKDGVVY
VMQNSLIRAM FDSCGRLISL YDMIWQRELV PEGEAGNVFR LYEDIPLYWD AWDIEIYHLE
KGYPAGQGLP PPKVEWSENR TALKVEFPWL LDAPNASYEV QFGAVQRPTH TNTSWDWARF
EVCAHKWADL SEPGYGIALL NDCKYGHATH GNIMRLTLLR RREWWRSGWA FNGPLRVVGP
PQPPSPRKPH PAAARAVLAA AGGYDPSQPM FCATPRHLYT MSPSPSPSPS PAHSYSPLCT
PATTNTTNTI TCSLTSPVAS SVARGARAPA DEPPGALVVR LYEPHGGRGV ARVRWPAWLR
VSHVALCNLL EEDQGGVEGE GEGAEGGDGS GGKAGLLVVR WDGAGGSVDI EYGPFKVITL
KLYLEQELVV DDSGQPEAYE INYITFYAFN GHYHIPANVP LFRTGHHVGD WEHLTVRLDA
TSLELQVEPG AGPCTQGVWY NAHRNIEGEW VPGVAVPRTP CGRILGFVAI NGHGIYPKCG
TIHRLFFIVN DRTSRRGPVW APTRLVRLCG LEFLKVVEVL VLVLCYKVQS LFLPTIGGKL
DDRRFMRMKL IDESLKAWKL GLEGMPSSQR ITMLELAFPN MGVQIITEQH LRVIPGVAPG
QDGGYYFCSS HKHQIVRLLF NSDGMLWESW SGLEFSTTLT QLDAGWSSRS GFMKESRMYA
ALLTSSLLPM VSRNRLCTSS HNTRPPSHEE LLDGIAQHAG VGAEEGPHQH ILCSLQRTLP
HGNMFLPCPS QQHTQQVPQH GRSAFLQMQH NTTQRYRGRW GSVVSPTLQG WFLNAEPPVS
RGCLRRLFLP LARGVERLEP ACCVTSDFSF LGGQVDPDID PPGGVHDG
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