ID A0A150G5M5_GONPE Unreviewed; 1313 AA.
AC A0A150G5M5;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KXZ45131.1};
GN ORFNames=GPECTOR_58g580 {ECO:0000313|EMBL:KXZ45131.1};
OS Gonium pectorale (Green alga).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Volvocaceae; Gonium.
OX NCBI_TaxID=33097 {ECO:0000313|EMBL:KXZ45131.1, ECO:0000313|Proteomes:UP000075714};
RN [1] {ECO:0000313|Proteomes:UP000075714}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2863 {ECO:0000313|Proteomes:UP000075714};
RX PubMed=27102219; DOI=10.1038/ncomms11370;
RA Hanschen E.R., Marriage T.N., Ferris P.J., Hamaji T., Toyoda A.,
RA Fujiyama A., Neme R., Noguchi H., Minakuchi Y., Suzuki M.,
RA Kawai-Toyooka H., Smith D.R., Sparks H., Anderson J., Bakaric R., Luria V.,
RA Karger A., Kirschner M.W., Durand P.M., Michod R.E., Nozaki H., Olson B.J.;
RT "The Gonium pectorale genome demonstrates co-option of cell cycle
RT regulation during the evolution of multicellularity.";
RL Nat. Commun. 7:11370-11370(2016).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the peptidase M1 family.
CC {ECO:0000256|ARBA:ARBA00010136}.
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:KXZ45131.1}.
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DR EMBL; LSYV01000059; KXZ45131.1; -; Genomic_DNA.
DR STRING; 33097.A0A150G5M5; -.
DR OrthoDB; 318693at2759; -.
DR Proteomes; UP000075714; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR Gene3D; 2.60.40.1730; tricorn interacting facor f3 domain; 1.
DR InterPro; IPR045357; Aminopeptidase_N-like_N.
DR InterPro; IPR042097; Aminopeptidase_N-like_N_sf.
DR InterPro; IPR001930; Peptidase_M1.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR PANTHER; PTHR11533:SF174; PUROMYCIN-SENSITIVE AMINOPEPTIDASE-RELATED; 1.
DR Pfam; PF01433; Peptidase_M1; 1.
DR Pfam; PF17900; Peptidase_M1_N; 1.
DR PRINTS; PR00756; ALADIPTASE.
DR SUPFAM; SSF63737; Leukotriene A4 hydrolase N-terminal domain; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000075714};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT TRANSMEM 114..135
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 271..405
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 423..525
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT REGION 23..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 688..751
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 692..721
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 736..751
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1313 AA; 132233 MW; 71B18DEC5432F8B5 CRC64;
MIRQNWRPPG EGEVELADIQ LTDGSRQAGE ASTTGGAGAS WGPGGSPDPY RGGERPDNGL
MYGGAHGDTY DATPNENADG LRLLGADFSQ TYKAPSGGGP LERLSNRIAA RWKIVILAWL
AMAFVGIIIA VPVSLTLTTL PSDPRARPLA YELRLSLPAG AFVAPNISAN GVVQPPPAST
ASSAPLGSFD ASASLLLNMT TDTSCLVLQA AALNISRVNV SVVSNPDPGS GSGATSGGSG
GLGRRRLAQS ASASASWCLC GCDAVLSCAS SVLQASSESI VLDLGSRVLA AGSQVRLSLS
YSGPIRSTAE GYGLFVSDPW VGDTPANGSA LPADVLLTTQ LEGRGARHLL PSLDEPSYKA
TFKVSVELPA GLTALSNTPG TAAPAATDGR TVYSFLATPP MSSYLLAVAA GKMSSIGMVV
QTNYYLSYTQ VALPLAKLDM LVVPGKTYGM ENWGLIMYDV GRFMCPAAGA GTSAWDVFQA
VDVICHEMAH QWFGNLVTCK DFDNIALNEG VASYVEYDCI SAVLPYVLAG GAAAAAPLPS
YPPPLPLAPL LRRFVLPPIG QPHGSHEGPI SLSRWIDEDP SIGAVLGATA SRAAAVSNVV
AYAKAATALA AAAGLVGEAG VRAALRNLLT PSYVYGTATL ADLVGLVADQ AAGPLNASSP
ADAAALGGRD AVFAGMMGWL TTPGVPLLTA SDATPAPPPP PSPLPPAPPS PPAPPVPGFN
DTANPPTLLC PGALATPANA STSADPTANA TGATDASAWW LPVAVSAAGR TSSGGGDALF
VLNSPAGQQT QVSLSVPQPA DTWVLRRRGF TQMYLSAYDG PVASGASGTP HIASLLSAVK
AGFGLPPPAA AAPPAPEASD PALADRLAAV ADAQSVLQDE MMRLLSPFTP PADTLLPAGA
VPGAAAPGNA APVPAVLALM DTALTSPLAF TGAGLHSLLP LLMGLEYLQG ILATAAADAA
TASCNADLGN WVLRRLKPLA AAAMASATGA ANASAIAAGE CPHCASATDR FALRLATWAI
VTEAALWGDA DARAFACRQA ANLTAADPDL LPAALAVPLA APGGCGADGP DPDTAFNATL
AAFAAAADPD TLSTRLFALA YGRGLAGPRT RLLGLLRSGV LASQGNYSFD SAAQYYVRPV
PSNVATVVLS RMVASAQREL FFAVRDAAAA SNGTGAGPLV GTAPNLPPGN DVLSVVMLNA
KNFPFATLIS GQGSRALSML ENAVGRALTT RDQLATVAAL LNDEAFTGPA SAHSPGALDS
ARSRILGRAQ SRLSWLAANK GPICAFLKAE SDALVAAAAA AAATGGGSGS SGR
//