ID A0A177WBL5_BATDL Unreviewed; 1152 AA.
AC A0A177WBL5;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Scaffold protein Tuba {ECO:0008006|Google:ProtNLM};
GN ORFNames=BDEG_21512 {ECO:0000313|EMBL:OAJ37497.1};
OS Batrachochytrium dendrobatidis (strain JEL423).
OC Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC Chytridiomycota incertae sedis; Chytridiomycetes; Rhizophydiales;
OC Rhizophydiales incertae sedis; Batrachochytrium.
OX NCBI_TaxID=403673 {ECO:0000313|EMBL:OAJ37497.1, ECO:0000313|Proteomes:UP000077115};
RN [1] {ECO:0000313|EMBL:OAJ37497.1, ECO:0000313|Proteomes:UP000077115}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEL423 {ECO:0000313|EMBL:OAJ37497.1,
RC ECO:0000313|Proteomes:UP000077115};
RG The Broad Institute Genome Sequencing Platform;
RA Birren B., Lander E., Galagan J., Cuomo C., Devon K., Jaffe D., Butler J.,
RA Alvarez P., Gnerre S., Grabherr M., Kleber M., Mauceli E., Brockman W.,
RA Young S., LaButti K., Sykes S., DeCaprio D., Crawford M., Koehrsen M.,
RA Engels R., Montgomery P., Pearson M., Howarth C., Larson L., White J.,
RA O'Leary S., Kodira C., Zeng Q., Yandava C., Alvarado L., Longcore J.,
RA James T.;
RT "The Genome Sequence of Batrachochytrium dendrobatidis JEL423.";
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:OAJ37497.1, ECO:0000313|Proteomes:UP000077115}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEL423 {ECO:0000313|EMBL:OAJ37497.1,
RC ECO:0000313|Proteomes:UP000077115};
RA Cuomo C.A., Farrer R.A., James T., Longcore J., Birren B.;
RT "Lineage-specific infection strategies underlie the spectrum of fungal
RT disease in amphibians.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; DS022300; OAJ37497.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A177WBL5; -.
DR STRING; 403673.A0A177WBL5; -.
DR VEuPathDB; FungiDB:BDEG_21512; -.
DR eggNOG; KOG3519; Eukaryota.
DR Proteomes; UP000077115; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR CDD; cd00160; RhoGEF; 1.
DR CDD; cd00174; SH3; 1.
DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR Gene3D; 1.20.900.10; Dbl homology (DH) domain; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR004148; BAR_dom.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR22834; NUCLEAR FUSION PROTEIN FUS2; 1.
DR PANTHER; PTHR22834:SF20; NUCLEAR FUSION PROTEIN FUS2; 1.
DR Pfam; PF03114; BAR; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR SMART; SM00721; BAR; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS51021; BAR; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50002; SH3; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000077115};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 495..681
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 716..941
FT /note="BAR"
FT /evidence="ECO:0000259|PROSITE:PS51021"
FT DOMAIN 1085..1152
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 100..187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 204..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 327..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 368..421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..145
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..173
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..252
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..267
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..315
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 368..399
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1152 AA; 127468 MW; 12850E1F464B8280 CRC64;
MADLNRPTES SLSSLNHMDE NGQQQTLRHS VAALSRRFEQ INLVKTEDHP STVASLFAGH
SESVTITHPS GLLSSRPFHN SSSANAFNSI ELENTQTNCH LASSQPSSLS QTPSSLETSS
ATAFPSQLSA PYPTNTHSRS VSTPRLRTAG AVRVGSTQPI FPSNQASNSP RTRHPSHNET
DSVQKKRLSV SRISRMFEQQ ANINDGISIR SPKSVGANST ARRNLTAPST RNGSFVMPPF
STSISQSDLR PSRSLKPPPP KPPKPCALAA PAVASFNSSP QSTILPASPG QNPFSDSSGR
LSDSTPPKPY IHNNSVSDLQ TFIPSQQSQA NVPTNFEPNY DDESSDRPIS MASLDIQNRL
AVLSSMGASF TSPSHHRPTH GFVSQHSASH SQLPTDAKLS FHHSNPVRPV TPLRPKSLQQ
RESVATRLYY DDAGEDSNVA IQEESVAGNG MCYLDPNVGK LLEINRDASY HSFTTQSSSG
EDNQLLETEA KRAYKWTKIV EEIVETERTY LSDMHVLHSV YVLPSLQSGV LPATDHKLLF
GHLENVIATS TVFLKELEAA ANAHPQTMGE AFMRMIHSIE VTYCNYCKHN EAAVLKLSDY
ASPTCPESIK LFLETCRGQL QGKTGAWDLA SLIVKPVQRV LKYPLLIKSL IKEMEPNHPD
GENLLKSFDS MSLVAEKINE VKKRKDIVEK YVDGKGKINV MHGITKMIGR GTQQLKKKTG
LTDETTSDAV YDALVEKFTK QHEAIVQLRI EISAWLKSMK EYVEYEEGMA VCLDDLYYID
SIPANSIAGP DEIDYLGLIK RYRSTCGRLI TGPYRDAESQ IKLVMIPAVE QLLNHFKAPL
LVMRKRDAKL LDYDRANSMR AKGDVVDKLL AESAGTYSSI NAQLTEELPL FMNFVTDYIH
EILIQVIIVQ RDMYQNIRQI VVPLADALQI SVHETTEDIL KKFREHMRVG GPIEVATKNI
LLLHQWRSQI WGYDDNAHEA AMRLFDSPER KTGSLSNFSG SSGLARDDAT SFNNMPLVDL
TGSAPAPRQL RMDVDTDAIL RHNMLVTHST LAPTIAPIST HPTNSIQGER DINCNSESAQ
DPYATDPFEA VAIYPFASEF DDEVSLVPGM VVSVYRTGGR DETGDDWWYG EVVSNKHSGN
TFGWFPRSFV EY
//
