ID C4JML8_UNCRE Unreviewed; 1102 AA.
AC C4JML8;
DT 07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 07-JUL-2009, sequence version 1.
DT 24-JAN-2024, entry version 74.
DE SubName: Full=GTP-binding protein ypt1 {ECO:0000313|EMBL:EEP79230.1};
GN ORFNames=UREG_04076 {ECO:0000313|EMBL:EEP79230.1};
OS Uncinocarpus reesii (strain UAMH 1704).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Uncinocarpus.
OX NCBI_TaxID=336963 {ECO:0000313|EMBL:EEP79230.1, ECO:0000313|Proteomes:UP000002058};
RN [1] {ECO:0000313|Proteomes:UP000002058}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 1704 {ECO:0000313|Proteomes:UP000002058};
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(2009).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR634016-3};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR634016-3};
CC -!- SIMILARITY: Belongs to the peptidase M1 family.
CC {ECO:0000256|ARBA:ARBA00010136}.
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DR EMBL; CH476616; EEP79230.1; -; Genomic_DNA.
DR RefSeq; XP_002544559.1; XM_002544513.1.
DR AlphaFoldDB; C4JML8; -.
DR STRING; 336963.C4JML8; -.
DR MEROPS; M01.006; -.
DR GeneID; 8444779; -.
DR KEGG; ure:UREG_04076; -.
DR VEuPathDB; FungiDB:UREG_04076; -.
DR eggNOG; KOG0084; Eukaryota.
DR eggNOG; KOG1046; Eukaryota.
DR HOGENOM; CLU_003705_0_0_1; -.
DR InParanoid; C4JML8; -.
DR OMA; NVWSQFV; -.
DR OrthoDB; 3085317at2759; -.
DR Proteomes; UP000002058; Unassembled WGS sequence.
DR GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd09601; M1_APN-Q_like; 1.
DR CDD; cd01869; Rab1_Ypt1; 1.
DR Gene3D; 1.25.50.20; -; 1.
DR Gene3D; 2.60.40.1910; -; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; IPR024571; ERAP1-like_C_dom.
DR InterPro; IPR034016; M1_APN-typ.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR11533:SF171; AMINOPEPTIDASE; 1.
DR PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR Pfam; PF11838; ERAP1_C; 1.
DR Pfam; PF01433; Peptidase_M1; 1.
DR Pfam; PF17900; Peptidase_M1_N; 1.
DR Pfam; PF00071; Ras; 1.
DR PRINTS; PR00449; RASTRNSFRMNG.
DR SMART; SM00177; ARF; 1.
DR SMART; SM00175; RAB; 1.
DR SMART; SM00176; RAN; 1.
DR SMART; SM00173; RAS; 1.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF63737; Leukotriene A4 hydrolase N-terminal domain; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51419; RAB; 1.
DR PROSITE; PS51421; RAS; 1.
DR PROSITE; PS51420; RHO; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|PIRSR:PIRSR634016-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000002058};
KW Zinc {ECO:0000256|PIRSR:PIRSR634016-3}.
FT DOMAIN 30..195
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 308..413
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 487..802
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT REGION 1082..1102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1082..1096
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 308
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT BINDING 307
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT SITE 354
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ SEQUENCE 1102 AA; 123098 MW; AA8BCE212F7183BE CRC64;
MGKDDRETLP DVAKPSNYAI SLYNLQLGGS WGYNGNVKID IKVARPTSEL VLNVKAIDVQ
TAKAISKDER AIMKFSEEIK EGDYVLELEF TGTMNNHMAG FARAKYQSSE TPAPGTPKEG
DNYYMLSTQF EACDARQAFP CFDEPNLKAT FDFEIEVPKD LVAISNMPIK STREGSNANL
KFVSFDRTPI MSTYLLAWAV GDFEYVEAYT ERKYNGAPIP VRVYTTRGLK EQARFALDCA
HKTVDYFSEV FEIDYPLPKS DLLAVHEFAM GAMENWGLVT YRTTAVLFEE GKSDDRFKTR
VAYVVAHEWD VWSRFVAEGV QQAFQLDSLR ASHAIEVPVK NALEVDQIFD HISYMKGSSV
IRMLSSHLGQ ETFLRGVASY LKAHAYGNAT TNDLWSALSK ASGKDVTSFM DPWIRKIGFP
LVTVVEEPKQ ITVAQKRFLA SGDVKPEEDE TLWWIPLGLK SGQQATEADK RNLTTKSDVV
RDIDEDFYKL NKDQCGFYRT NYPPERLAKL GKSRDLLSTE DKIGLIGDAA ALAVSGEATT
AATLALVENF HDEQNYLVWM QLVVSLSHIR SVFAANEEIA TGLKNFVRKL VSPAVEKLGW
EFKPNEDYLT GQLRQLLIST AGNAGHEGTI AEAKRRFNAW ASGEDKNAIH PNLRSAIFTI
NVAEGGQKEY DTVKEEFSKT DSVDGKEICV GSLARTKNPD ILKEYFEFLF SGSVATQDIH
TGGAGLAANS KARDAFWIWL KANWARVEQR MGSNKVVYER FVRMSLTKFA DHSTEQDITK
FFENKDKAGI DRGLLVVADT IRTNANYKER DEKGVLEWLK AHQQPNVTCQ MGGRLQVQLV
PAGTGVSWQL IMLPPSESTT ATLSFSWIPS VFSLWLIYPA GKLMISWPSF LPTFASSITV
ANNFRYDYLF KLLLIGDSGV GKSCLLLRFA DDTYTESYIS TIGVDFKIRT IELDGKTVKL
QIWDTAGQER FRTITSSYYR GAHGICVVYD VTDMDSFNNV KQWLQEIDRY ATEGVNKLLV
GNKSDMEDKK AVEYTVAKEF ADSLGIPFLE TSAKNASNVE QAFLTMARQI KERMGTATVN
NKPTVQVGQG QGVQSGSAGG CC
//
