ID Q0UBS8_PHANO Unreviewed; 1673 AA.
AC Q0UBS8;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 2.
DT 27-MAR-2024, entry version 110.
DE RecName: Full=RING-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=SNOG_10786 {ECO:0000313|EMBL:EAT82180.2};
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614 {ECO:0000313|EMBL:EAT82180.2, ECO:0000313|Proteomes:UP000001055};
RN [1] {ECO:0000313|Proteomes:UP000001055}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173
RC {ECO:0000313|Proteomes:UP000001055};
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G., Solomon P.S., Tan K.C., Schoch C.L., Spatafora J.W.,
RA Crous P.W., Kodira C., Birren B.W., Galagan J.E., Torriani S.F.,
RA McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(2007).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189;
CC Evidence={ECO:0000256|ARBA:ARBA00001270};
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000256|ARBA:ARBA00004374}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004374}.
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DR EMBL; CH445341; EAT82180.2; -; Genomic_DNA.
DR RefSeq; XP_001801045.1; XM_001800993.1.
DR STRING; 321614.Q0UBS8; -.
DR EnsemblFungi; SNOT_10786; SNOT_10786; SNOG_10786.
DR GeneID; 5977952; -.
DR KEGG; pno:SNOG_10786; -.
DR VEuPathDB; FungiDB:JI435_107860; -.
DR VEuPathDB; FungiDB:JI435_307240; -.
DR eggNOG; KOG0448; Eukaryota.
DR eggNOG; KOG0828; Eukaryota.
DR HOGENOM; CLU_002868_0_0_1; -.
DR InParanoid; Q0UBS8; -.
DR OrthoDB; 1381184at2759; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0008053; P:mitochondrial fusion; IBA:GO_Central.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR045063; Dynamin_N.
DR InterPro; IPR030381; G_DYNAMIN_dom.
DR InterPro; IPR027094; Mitofusin_fam.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR10465; TRANSMEMBRANE GTPASE FZO1; 1.
DR PANTHER; PTHR10465:SF0; TRANSMEMBRANE GTPASE MARF-RELATED; 1.
DR Pfam; PF00350; Dynamin_N; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51718; G_DYNAMIN_2; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Reference proteome {ECO:0000313|Proteomes:UP000001055};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT TRANSMEM 1252..1271
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1291..1312
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1318..1338
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1431..1452
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1458..1477
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1489..1509
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 271..565
FT /note="Dynamin-type G"
FT /evidence="ECO:0000259|PROSITE:PS51718"
FT DOMAIN 1606..1667
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 164..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 487..522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1385..1423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..522
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1409..1423
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1673 AA; 186549 MW; 995269531D98130F CRC64;
MHPDKRGKGK GKSSSSAGEP SSSRHNGQPS SGDATPGHRG MAPGYMTVGS GSTPEAAARL
VSMLDEDSGY GGSMMEGDSA SSWRANIGED RPSQPPSTIL NGEASSSEHD KQRSHVLQLR
YNQNKNALGR AIHGTIDTLK SFQEMNLKWP AHYPSVQVTE VQKHTQSAIG DFDPNMRSPE
RPRGPRRAGT TIGDDPVPGP STEPEPEKEA PRLVTPQLAQ DFSVLKLELR MGGRTQTDLV
HSLEKSSIAS LLDGQIQQSV RHLYALKERI EDTSSKVLVT GDLNAGKSTF CNALLRRKVL
PEDQQPCTSI FCEVLDFREN GGVEEVHAIP HGSTYNRHDE STYVVFDLKD LEKIVIDNDR
FSQCKIYIQD IRGVDESILN NGVVDIALID APGLNADSVM TTAVFARQEE IDVVVFVVSA
ANHFTESAKN FIFNAAREKA YIFMVVNGFD VIRDQERCQE MILKQVHGLS PATFKESSEL
VHFVSSNAIP MGGSGSGSSP PDDDGDDDPN DKGKGKEAEK RRDFGELETS LRRFVLEKRA
RSKLAPAKTY LLNVLGDMNN LATVNRDVSQ SELDRVKKEI EALEPEFEES KKSRVEAGEA
VERMVEDTTS DVYGYTRDTL NSCIQKVGEQ DLGIEYPGLF SAYQYAEDIR DSMLHEVSET
VRLCEEHART QTVQGYNAIK NIGVLHLGNN LYADVMFRPE RMFKKSVHAL ARQVDIDIEL
WDFFDVASLW ERQEKVAGTS MAVTVAGMVG GRLMGGAGWL DGALGAAKIM GTNNMKRLLV
PGLIAGLPKS LPHRLSAKLS QQLAAIDYTH QNALRISSEI RRALKGPAND VRIGLQRNVE
KLQNKKEQTT KFKAEAEVAR KYFGNLVRSS NDLRQTVHDT TALMEARRDP RSFLFFIILL
LLINSPEPQQ PTFNARARYE ELVQREYDHL GVLNSTQYGD FDPRNEKWLN VTGLRKEDGF
AWDMLEPVRQ RAKAMGERVL GDNAYDGHDV PVYKNLSGYV QGEWVRSPLS QVRHPIDMGN
SSMNPDSPFA QLMEYDRNLT GHAGSIRVHF TELEGMMRTD KNKTTSEISA KVVIGDDDSF
GGNWWEFIAH GVHFLKSGTA VLTTTSDRYA GIFGLPHLMF DQRLFDASQS FLNRTILETI
ERQQNRAFPL WNPWTSSADG GNEGLFQGHH CEVVVYLQEA PVANGIDTAW LEHEMRYPTG
APMPKQLSKQ MSMVAFSPDC GFVIESKGPP DFPPSEAYHL VGSKTEQFND RARHGIIAFA
MSLAFQLYFL IQQMKETATP SMRSRVSFYT IATMALGDGF TFLILVFMYL FLGTSQLALY
SIAFLALFSV LTHLRFLMDI WGVQAAERER QNRQQAAAAA LSTPQPPVAP TPPVAPVLNS
LPLPATAPRP RPPTPIIIAP DQDDDLDEPT PTPGNNTTTT TTNPRAELGA LYSRFCLLLI
VLFFITIQFG TARTTYRSIY FSMLSFLYLS FWVPQIYRNT MRNCRRAFRW DYVIGTSIVR
IIPVSYFYLK EDNVLFARTD STSMAILAGW VWCQVLMLAT QEILGPRWCV KNDWVPPAYD
YHPILREDEE GATMPLNITT ADGIDASAKA PGESKDRAKN KKVFDCSICA QDVEVPVIPA
GGAEEGMGGT GMILQRRMYM VTPCRHIFHT GCLEGWMRYR LMCPNCREVL PPL
//
