ID M5G3N3_DACPD Unreviewed; 2241 AA.
AC M5G3N3;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Peptide hydrolase {ECO:0008006|Google:ProtNLM};
GN ORFNames=DACRYDRAFT_16916 {ECO:0000313|EMBL:EJU00467.1};
OS Dacryopinax primogenitus (strain DJM 731) (Brown rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC Dacrymycetales; Dacrymycetaceae; Dacryopinax.
OX NCBI_TaxID=1858805 {ECO:0000313|EMBL:EJU00467.1, ECO:0000313|Proteomes:UP000030653};
RN [1] {ECO:0000313|EMBL:EJU00467.1, ECO:0000313|Proteomes:UP000030653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DJM-731 SS1 {ECO:0000313|EMBL:EJU00467.1,
RC ECO:0000313|Proteomes:UP000030653};
RX PubMed=22745431; DOI=10.1126/science.1221748;
RA Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA Hibbett D.S.;
RT "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT 31 fungal genomes.";
RL Science 336:1715-1719(2012).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; JH795867; EJU00467.1; -; Genomic_DNA.
DR STRING; 1858805.M5G3N3; -.
DR HOGENOM; CLU_230761_0_0_1; -.
DR OrthoDB; 277019at2759; -.
DR Proteomes; UP000030653; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:0008235; F:metalloexopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR CDD; cd03875; M28_Fxna_like; 1.
DR Gene3D; 1.10.840.10; Ras guanine-nucleotide exchange factors catalytic domain; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR048024; Fxna-like_M28_dom.
DR InterPro; IPR045175; M28_fam.
DR InterPro; IPR007484; Peptidase_M28.
DR InterPro; IPR023578; Ras_GEF_dom_sf.
DR InterPro; IPR001895; RASGEF_cat_dom.
DR InterPro; IPR036964; RASGEF_cat_dom_sf.
DR PANTHER; PTHR12147:SF54; ENDOPLASMIC RETICULUM METALLOPEPTIDASE 1-RELATED; 1.
DR PANTHER; PTHR12147; METALLOPEPTIDASE M28 FAMILY MEMBER; 1.
DR Pfam; PF04389; Peptidase_M28; 1.
DR Pfam; PF00617; RasGEF; 1.
DR SUPFAM; SSF48366; Ras GEF; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 4: Predicted;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00023049};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000030653};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 375..397
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 409..431
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 443..466
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 478..497
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 503..523
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 535..558
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 570..590
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 602..622
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 157..340
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
FT DOMAIN 1997..2091
FT /note="Ras-GEF"
FT /evidence="ECO:0000259|Pfam:PF00617"
FT REGION 979..1018
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1304..1340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1368..1390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1708..1783
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 983..1014
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1319..1333
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1712..1737
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1765..1783
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2241 AA; 249002 MW; 3BEAEFA731537C0C CRC64;
MAPAHPHPRP AKSLLELLLI MCPLVIGIPW LALHIHYTIS HPVICDSLPE PIIEQYHPLT
GTPQLSEHHI LNTARYLSES IGYRTVGTRE HALADVWMSE QLQEVQSLCE EEASRRRERG
EGGVECEIWR QEGSGKHRVY KSYHGLTNHI LRLSANTTQS KAHAVLVNSH LDSTLPSPGA
ADDAVCVGVM LELIRVLVHG GWSGEWSIIF LFNHAEESLQ DASHLFSTQH PLAPTVQAVI
NLEAAGTTGP ELLFQATSQE MIAAYSHVPR PHGSVLANDV FNSGIIISDT DFGQFVKYLN
VTGLDMAIVG NSYLYHTRKD LVENIQPGAA QHMAENVLAL LNYLTSARSP LPHLTEYTAP
ATVYYSLLSS IFFSYSYDLA LVMSVSLLFW ALALALVTTR DWTVVPRAWA GIVGGMAGAL
GAANLMAYFF ASILCKPLSW FAREWLCILL YAPPALLGAV FVQLLVHPPP ARPQIEHQSL
TSLMLFYSFV AFAGQMAGIG SSYLYFINAL SLWVATALNE LLVRVLKHEP GDVNHWTYAV
GSVIPLIAGS EALAPTLQTG RLGRDAPVEH IIASIVSFLT FYMAPFVLPF AHRFGRPALR
TITLVLLGVS VGISAVFAAP GWREFDRQHQ NRFFVVHIEN ITSHDYGLHV ATLNSASGFS
EIVNSLAGDF AEVKGVPRLT TELGDKLAWD VFHPVSDLVT SYAMDLSPPE EYVSHWRQEF
SVHALDIVLD PHTDTRTFTL HIDHPGLIWT VVSFQAEVLE WDLPDAPVEG HALHKIKEAS
FYMADQWSIR MTLNGTAPVL VNFVGIEERS MWPGKKARQG ENREEKPSMR MFERLETWLE
QKSDGGIDVN MFGCIAGAVE HGWERAAGAT KVTSSHTQRH APSKLLYFDG ARTLDTQDVL
LYGNVSTGTR WNPFGRIVEL CDWGKQFGID GFLRMEFDFE IMYCNFTNGM ELISSVNVVP
CTWERTPSSV ELIEHRLSVP TMGNPPLPEP TGPPRRGPGR PDRNPTPPEP PVGWQGSLRT
PSQVTFEALH AGYWHNFAPL TGIKLEYWGL TTFYDPKYGS LVPGRWGLDA AQYRLANISE
KDASAWKREL EGVLIRPETE GSGIDWGNIM RHIVERHADR LEFFRHLLRT ATRKDGGDRV
TPTQNLTKIV ENARLQVLTM LSPYLSRAAV PPGKSASNDR AWLEPTVSLC TGSFTQHMNV
SRFTPQEHVL KQATDTTARE ICRTLGLIWL SAFSAESVTL PSQQEQLLNS WLLEVERLMA
WLDWAVWLRC TPVCGDDEIC SPPQWPFDGV RTGDEGREPH CISRVDFQRG GRGPGGPDEP
ESPGGPGEPH PPRGPEYTRS SALLQGSSSN ISTQSSLAAS STCTCPDSFV PPSAPRPSPS
ISRTSDLTDP EATMNVLCDT SAVTATMSGS IEVSASRTLP ERRSSDERQS TGLLSSIHVA
FEVITIRTEL TIEYVPSLNC KYTPDLPNAA WKSLSAAGQS IDGRIPNSFC CMDASPSSAN
MDDTAQTQLA LLPSPIRTAV QNILNYLSRA AETAIGIPQN DEEIVHITER LDYIKQFLGL
YPAHLLQSRD NRTDTSNAIS PKSNIRPLEP EEQKDLLHHL TREFQRINDL MVKYRDKRST
ATRRMAFQPE AAVLVRKMKE ASERASTYLL VYKVVDADTT GDRFSRFENF ISFHYRDLVR
HGPHAMRSKP SLDTLSTWEP RHKIPRQISA PGVSSRAHQS YLPTTRPVST TPAGRSITPT
VKDDLHTRSF RGGRGRGRGR ARGKVVNSHN NSQATPTDVD TPNIAEQTGV DIRPAPVSHK
ESESEFGSPL PQITMSTTAP LVPFLENERF DDVHATRNLG ILDAHNDVPS DKDPVIHMVL
KHMLTPGGKS KDCSEECEAF AATYKACMTS EVMFSHFFDV SSTLLDRVGS SGLPSILNFV
VYWLYHVQVG VEARDLLLRI QSFVLGIQDF VSGEVTKSQT LAILQVLQEL PLKKPRVLKR
RIKPSTKELE DFEAIQLADQ LTILLSLGFR RIQVKHLIAW VSPEEKSETN PVNKFKEVCA
KVQSWVKAAL LGCSKGSSGR ERVKKKFLYI AQRCLESYNL AGTVSITSTL LQLQEAGEIK
LRFTREQEGH PINGLVAPSP GEELYWNALA SKPADTACVP WLDPHESGLQ EAGDDVRTAR
PISIANHRAL FMEAKKLIAY GAKQYEVPFS LQDMSYLEFH FKVSSQDLRD EVKKGELCTN
GLRLSWWKPD DRTRLPEAEA T
//
