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Database: UniProt
Entry: U1HSZ5_ENDPU
LinkDB: U1HSZ5_ENDPU
Original site: U1HSZ5_ENDPU 
ID   U1HSZ5_ENDPU            Unreviewed;       941 AA.
AC   U1HSZ5;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   RecName: Full=Small COPII coat GTPase sar1 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=EPUS_00918 {ECO:0000313|EMBL:ERF73665.1};
OS   Endocarpon pusillum (strain Z07020 / HMAS-L-300199) (Lichen-forming
OS   fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Verrucariales; Verrucariaceae; Endocarpon.
OX   NCBI_TaxID=1263415 {ECO:0000313|EMBL:ERF73665.1, ECO:0000313|Proteomes:UP000019373};
RN   [1] {ECO:0000313|Proteomes:UP000019373}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Z07020 / HMAS-L-300199 {ECO:0000313|Proteomes:UP000019373};
RX   PubMed=24438332; DOI=10.1186/1471-2164-15-34;
RA   Wang Y.-Y., Liu B., Zhang X.-Y., Zhou Q.-M., Zhang T., Li H., Yu Y.-F.,
RA   Zhang X.-L., Hao X.-Y., Wang M., Wang L., Wei J.-C.;
RT   "Genome characteristics reveal the impact of lichenization on lichen-
RT   forming fungus Endocarpon pusillum Hedwig (Verrucariales, Ascomycota).";
RL   BMC Genomics 15:34-34(2014).
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. SAR1 family.
CC       {ECO:0000256|ARBA:ARBA00007507}.
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DR   EMBL; KE720941; ERF73665.1; -; Genomic_DNA.
DR   RefSeq; XP_007800668.1; XM_007802477.1.
DR   AlphaFoldDB; U1HSZ5; -.
DR   GeneID; 19235978; -.
DR   eggNOG; KOG0077; Eukaryota.
DR   HOGENOM; CLU_014084_0_0_1; -.
DR   OMA; ITLNDCM; -.
DR   OrthoDB; 2731604at2759; -.
DR   Proteomes; UP000019373; Unassembled WGS sequence.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   CDD; cd00879; Sar1; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR018853; DUF2457.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR006689; Small_GTPase_ARF/SAR.
DR   InterPro; IPR006687; Small_GTPase_SAR1.
DR   PANTHER; PTHR45684; RE74312P; 1.
DR   PANTHER; PTHR45684:SF2; RE74312P; 1.
DR   Pfam; PF00025; Arf; 2.
DR   Pfam; PF10446; DUF2457; 1.
DR   PRINTS; PR00328; SAR1GTPBP.
DR   SMART; SM00177; ARF; 1.
DR   SMART; SM00178; SAR; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51417; ARF; 1.
DR   PROSITE; PS51422; SAR1; 1.
PE   3: Inferred from homology;
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019373}.
FT   REGION          1..124
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          210..303
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          331..475
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          492..628
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        33..51
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        65..116
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        271..295
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        337..368
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        391..408
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        419..447
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        511..527
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        528..551
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        552..571
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   941 AA;  104852 MW;  14E07C102451C493 CRC64;
     MFHLSNTSNP LSSEEEITGD VDEPPDEPLS PLQMNPTMVQ QPQQPSTYTR SALPAMDRKE
     SLLTRALMTG SNGDISSSPT SPISGAASRA STFSNASVPS TAELTSDADD TSPTRSATPS
     PPLPVALYHE IHATNKTPLP PTRISFATGK QQEKLVADAS AESQIEAKMG RKRCITFACA
     SKPAVKEPHA AKEERMEIAQ PPKRKCLLTF ACPARPAQKQ DPGPEAAEAR RDSGSSSAND
     ITAPSNEPHG GERQEHAQPC KVPLITVDTR KNALKSPTSP KQSDVKSSDA SPFHEFATSN
     DHDDAWVREP IDTQRKLTLL DCMKKENAIR KIGEEAEEEA EQEEKEEDEF DDDNEDGINE
     DDFAPSDDGN ESDNEKGFAE SDDDSDGESE DQFWIPSNNT TAATSVDHSS PHRPFGRRRQ
     RGSSMDSLSD HGSRQEKRSE SVDIKHPKHR RTSKGHQMRP GTPELPDSTD FVCGTLDEDR
     PLEAAYISCR EQRKREKHIL IPQDIDPSFP TTDPEDMDED DDEDLDTPED HLWLKNQLEG
     SEDDSTRGHA SKHHKMCSKL RSPRRAHSPP PKHGVHCSPP PPRQTVRRSS PAPNSRLFGH
     SPQRLHSPPP AMKWRSPPGT RRSSPTGMAL MPHQTEGLVI SRLGQRPHMT RTASLPRTPN
     PFFHNYHART HQNDRVVYGG MTPGREMHVR GPVDIVIGLE KKRQKRKEKF WRQHCRKAAK
     EQAERKTLRG RGAERMLYDV LASLGLLNKH AKLLFLGLDN AGKTTLLHML KNDRVAILQP
     TLHPTSEELA IGNNRFTTFD LGGHQQGQCT PFFNITYVYQ QGFGGIAGAR RLWRDYFPEV
     SGIVFLVDAK DHERLPESKL ELDALLAMED LAKVPFLILG NKIDHPDAVS EDELRHQLGL
     YQTTGKGKVP LEGIRPIEVF MCSVVMRQGY GEGIRWMSQY V
//
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