ID A0A2U9BPE6_SCOMX Unreviewed; 1283 AA.
AC A0A2U9BPE6;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Putative DENN domain-containing protein 1C-like {ECO:0000313|EMBL:AWP06028.1};
GN ORFNames=SMAX5B_007341 {ECO:0000313|EMBL:AWP06028.1};
OS Scophthalmus maximus (Turbot) (Psetta maxima).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Scophthalmidae;
OC Scophthalmus.
OX NCBI_TaxID=52904 {ECO:0000313|EMBL:AWP06028.1, ECO:0000313|Proteomes:UP000246464};
RN [1] {ECO:0000313|EMBL:AWP06028.1, ECO:0000313|Proteomes:UP000246464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Martinez P.;
RT "Integrating genomic resources of turbot (Scophthalmus maximus) in depth
RT evaluation of genetic and physical mapping variation across individuals.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}.
CC -!- SIMILARITY: Belongs to the tubulin family.
CC {ECO:0000256|ARBA:ARBA00009636}.
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DR EMBL; CP026250; AWP06028.1; -; Genomic_DNA.
DR STRING; 52904.ENSSMAP00000004997; -.
DR Proteomes; UP000246464; Chromosome 8.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IEA:InterPro.
DR GO; GO:0007017; P:microtubule-based process; IEA:InterPro.
DR CDD; cd02187; beta_tubulin; 1.
DR Gene3D; 3.30.450.200; -; 1.
DR Gene3D; 3.40.50.11500; -; 1.
DR Gene3D; 6.10.140.1000; -; 1.
DR Gene3D; 1.10.287.600; Helix hairpin bin; 1.
DR Gene3D; 3.30.1330.20; Tubulin/FtsZ, C-terminal domain; 1.
DR Gene3D; 3.40.50.1440; Tubulin/FtsZ, GTPase domain; 1.
DR InterPro; IPR013838; Beta-tubulin_BS.
DR InterPro; IPR002453; Beta_tubulin.
DR InterPro; IPR001194; cDENN_dom.
DR InterPro; IPR005112; dDENN_dom.
DR InterPro; IPR043153; DENN_C.
DR InterPro; IPR040032; DENND1A/B/C.
DR InterPro; IPR037516; Tripartite_DENN.
DR InterPro; IPR008280; Tub_FtsZ_C.
DR InterPro; IPR000217; Tubulin.
DR InterPro; IPR037103; Tubulin/FtsZ-like_C.
DR InterPro; IPR018316; Tubulin/FtsZ_2-layer-sand-dom.
DR InterPro; IPR036525; Tubulin/FtsZ_GTPase_sf.
DR InterPro; IPR023123; Tubulin_C.
DR InterPro; IPR017975; Tubulin_CS.
DR InterPro; IPR003008; Tubulin_FtsZ_GTPase.
DR InterPro; IPR005113; uDENN_dom.
DR PANTHER; PTHR13196; DENN DOMAIN-CONTAINING; 1.
DR PANTHER; PTHR13196:SF25; DENN DOMAIN-CONTAINING PROTEIN 1C; 1.
DR Pfam; PF03455; dDENN; 1.
DR Pfam; PF02141; DENN; 1.
DR Pfam; PF00091; Tubulin; 1.
DR Pfam; PF03953; Tubulin_C; 1.
DR Pfam; PF03456; uDENN; 1.
DR PRINTS; PR01163; BETATUBULIN.
DR PRINTS; PR01161; TUBULIN.
DR SMART; SM00801; dDENN; 1.
DR SMART; SM00799; DENN; 1.
DR SMART; SM00864; Tubulin; 1.
DR SMART; SM00865; Tubulin_C; 1.
DR SMART; SM00800; uDENN; 1.
DR SUPFAM; SSF55307; Tubulin C-terminal domain-like; 1.
DR SUPFAM; SSF52490; Tubulin nucleotide-binding domain-like; 1.
DR PROSITE; PS50211; DENN; 1.
DR PROSITE; PS00227; TUBULIN; 1.
DR PROSITE; PS00228; TUBULIN_B_AUTOREG; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Guanine-nucleotide releasing factor {ECO:0000256|ARBA:ARBA00022658};
KW Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000246464}.
FT DOMAIN 404..766
FT /note="UDENN"
FT /evidence="ECO:0000259|PROSITE:PS50211"
FT REGION 860..921
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1019..1271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 877..891
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 905..921
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1019..1036
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1047..1134
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1145..1167
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1178..1192
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1198..1223
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1238..1260
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1283 AA; 144195 MW; B9AE49C5CFDF100C CRC64;
MREIVHLQAG QCGNQIGAKF WEVISDEHGI DPTGTYHGDS DLQLDRINVY YNEASGGKYV
PRAILVDLEP GTMDSVRSGP FGQIFRPDNF VFGQSGAGNN WAKGHYTEGA ELVDSVLDVV
RKEAESCDCL QGFQLTHSLG GGTGSGMGTL LISKIREEYP DRIMNTFSVV PSPKVSDTVV
EPYNATLSVH QLVENTDETY CIDNEALYDI CFRTLKLTTP TYGDLNHLVS ATMSGVTTCL
RFPGQLNADL RKLAVNMVPF PRLHFFMPGF APLTSRGSQQ YRALSVPELT QQMFDAKNMM
AACDPRHGRY LTVAAVFRGR MSMKEVDEQM LNVQNKNSSY FVEWIPNNVK TAVCDIPPRG
LKMAATFIGN STAIQELFKR ISEQFTAMFR RKAFLHWQNP ERTFHWFFEA NCPVARDKDP
GVLFQFPEDF SDEESCQTLP KFCFPYDIQR VRGGVAVQHF TFVLTDLEGC QRFGFCRLTN
STQTCLCILS YLPWFEVFYK LLNNLADYLT KGQTSEMKAL LASLYKQPIP LAAGSITLQM
VPYFIAPDPR SLPSIPENRN LTELIVAVDV GNLLQIYASM LFERRILIFA SKLSTLTSCV
HALSAVLYPM YWQHIFIPVL PPHLLDYCCA PMPFLIGVHS SLSEWVRSRG LEEVVILNVD
TNTLETPFDD LKRIPSDVMS GLKLCLKRQA VSPGSGVSRA FLRAQALLFG GYRDALQGHE
EGEIFFSERL FLDHKSHSMG QFLQSAVHLQ FFKQFIDGRL DILNTGEEPD DLFEDEILKC
ETTAGRSKSY QQLVGNLKKG GGALILNMKS KANMRAKGLA KSGWKNLLMH KANNEAHSLQ
RGGSVSHRRA QSDCLQNRLP ITPHFGMSRP RRPVHKHRPP RDQDNMKDTE DTWDGAVSGP
AVEPDAELQE DEEDGEGTLL SDPEEMDLLG EIFDTLSSRS SHERGLLYGT RSLDLFGPDS
HDYITKFGPV NPSQESLCLS ISGSGSLHSW NPDSDWPYLD PSVPEEEGSE CLLATCEMEE
KDRGQREDEE KQEEVKVAIN GNQGQEKENR HTFEEVRFEE MRVSLGAEPE EETSEKREDE
GLKAKREDER NQSDELAEGQ ETQIETKEMQ KVVASEEEGN ENQEEKEVTR SFNELRKLNN
HYPNMVEERQ GQQETDIPDS TVCPGPQSPT ADPKPPAVQE QRSEEAVKKE EWESGQMPSP
PKVQSTVARF QSQASSQSFQ VKSRIKGLAE PGRPCNALWS TEKTQTHRPC DSNISEENNC
SGAHEGKDPT PIKVSELKKR FEA
//
