ID A0A1X7RN70_ZYMTR Unreviewed; 659 AA.
AC A0A1X7RN70;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=t-SNARE coiled-coil homology domain-containing protein {ECO:0000259|PROSITE:PS50192};
GN ORFNames=ZT3D7_G4032 {ECO:0000313|EMBL:SMQ48882.1};
OS Zymoseptoria tritici ST99CH_3D7.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX NCBI_TaxID=1276538 {ECO:0000313|EMBL:SMQ48882.1, ECO:0000313|Proteomes:UP000215127};
RN [1] {ECO:0000313|EMBL:SMQ48882.1, ECO:0000313|Proteomes:UP000215127}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the syntaxin family.
CC {ECO:0000256|ARBA:ARBA00009063}.
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DR EMBL; LT853694; SMQ48882.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X7RN70; -.
DR STRING; 1276538.A0A1X7RN70; -.
DR Proteomes; UP000215127; Chromosome 3.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:InterPro.
DR GO; GO:0016774; F:phosphotransferase activity, carboxyl group as acceptor; IEA:InterPro.
DR GO; GO:0005484; F:SNAP receptor activity; IEA:InterPro.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:InterPro.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
DR CDD; cd15845; SNARE_syntaxin16; 1.
DR Gene3D; 1.20.58.70; -; 1.
DR Gene3D; 3.30.420.40; -; 1.
DR InterPro; IPR000890; Aliphatic_acid_kin_short-chain.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR010989; SNARE.
DR InterPro; IPR006012; Syntaxin/epimorphin_CS.
DR InterPro; IPR000727; T_SNARE_dom.
DR PANTHER; PTHR21060; ACETATE KINASE; 1.
DR PANTHER; PTHR21060:SF19; ACETATE KINASE; 1.
DR Pfam; PF00871; Acetate_kinase; 1.
DR Pfam; PF05739; SNARE; 1.
DR SMART; SM00397; t_SNARE; 1.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 1.
DR SUPFAM; SSF47661; t-snare proteins; 1.
DR PROSITE; PS00914; SYNTAXIN; 1.
DR PROSITE; PS50192; T_SNARE; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000215127};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 325..342
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 251..313
FT /note="T-SNARE coiled-coil homology"
FT /evidence="ECO:0000259|PROSITE:PS50192"
FT REGION 200..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 349..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..226
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..367
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 659 AA; 73772 MW; 9DC4B9781DC97C5E CRC64;
MSISAGGAFR DRTNLFISYR HSYAHDTAKR TRFTGPSSGR FNDDVGDSER EGLMSNLGGD
GDAVIEMDVL PPRWLDLQDE VTQHLANVRS KMKRLDQMHA KHVLPGFDDE SVKAKEEREI
EALTRDITKD FTSCQKAIKG IDRMVQEQQQ HSSSAVSNSE LTMAKNLKMS LASQVGDVST
LFRKKQSAYL KKLRSLGGMG GTSSPFDRSN TPMAQNPYTD PAMMESETDR SSAQSTLLQT
AQVRRRTGVL DSAIEQRERE IERIAQGVID LSNLFQDLQT MVIDQGTVLD RIDYNVERTA
EHVKEADKEL KVATGYQRRS VKRKAILLLI LIVVGMFILL LIKPKRGSQP PPAPSPIEDP
TPNDPGAGLP PKVRDTRDVV GTAPFDGLNS RHAEWKKRRR RYPVHLFAVA KVLTRAKCNP
ACVYHLMVPL LGITGWLTTS LGELQRPSIF NNEQQQRKPE FSVYSYEDHS HEPKQLADIQ
VAGLTAPPVK LTYSRGDEHI KNKELKDISS QESAYEYILK HLTSDSGLPQ LSHPDDIEFA
CHRVVHGGDY DKPTRIDRET YHHLEELSDL APLHNAGALT IVEAVHKACP KTTNIAFFDS
AFHSTIPLPA RTYAIDPKVA AHNKLRKYGF HGLSYAFITR AVAAHLAKPE SKFDIPLYP
//
