ID C6HE80_AJECH Unreviewed; 2124 AA.
AC C6HE80;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE SubName: Full=SH3 and Ded_cyto domain-containing protein {ECO:0000313|EMBL:EER41864.1};
GN ORFNames=HCDG_04511 {ECO:0000313|EMBL:EER41864.1};
OS Ajellomyces capsulatus (strain H143) (Darling's disease fungus)
OS (Histoplasma capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX NCBI_TaxID=544712 {ECO:0000313|EMBL:EER41864.1, ECO:0000313|Proteomes:UP000002624};
RN [1] {ECO:0000313|Proteomes:UP000002624}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H143 {ECO:0000313|Proteomes:UP000002624};
RA Champion M., Cuomo C.A., Ma L.-J., Henn M.R., Sil A., Goldman B.,
RA Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A.M.,
RA Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA Griggs A., Gujja S., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S.,
RA Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J.,
RA Yandava C., Klein B., McEwen J.G., Puccia R., Goldman G.H., Felipe M.S.,
RA Nino-Vega G., San-Blas G., Taylor J.W., Mendoza L., Galagan J.E.,
RA Nusbaum C., Birren B.W.;
RT "The genome sequence of Ajellomyces capsulatus strain H143.";
RL Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the DOCK family. {ECO:0000256|PROSITE-
CC ProRule:PRU00983}.
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DR EMBL; GG692423; EER41864.1; -; Genomic_DNA.
DR STRING; 544712.C6HE80; -.
DR VEuPathDB; FungiDB:HCDG_04511; -.
DR eggNOG; KOG1998; Eukaryota.
DR HOGENOM; CLU_000595_0_1_1; -.
DR OMA; LWDNQAF; -.
DR Proteomes; UP000002624; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR CDD; cd08679; C2_DOCK180_related; 1.
DR CDD; cd11684; DHR2_DOCK; 1.
DR Gene3D; 1.25.40.410; -; 1.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR Gene3D; 1.20.1270.350; Dedicator of cytokinesis N-terminal subdomain; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR027007; C2_DOCK-type_domain.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR026791; DOCK.
DR InterPro; IPR043161; DOCK_C_lobe_A.
DR InterPro; IPR032376; DOCK_N.
DR InterPro; IPR042455; DOCK_N_sub1.
DR InterPro; IPR027357; DOCKER_dom.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR45653; DEDICATOR OF CYTOKINESIS; 1.
DR PANTHER; PTHR45653:SF10; MYOBLAST CITY, ISOFORM B; 1.
DR Pfam; PF14429; DOCK-C2; 1.
DR Pfam; PF16172; DOCK_N; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS51650; C2_DOCK; 1.
DR PROSITE; PS51651; DOCKER; 1.
DR PROSITE; PS50002; SH3; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000002624};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 7..88
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 611..792
FT /note="C2 DOCK-type"
FT /evidence="ECO:0000259|PROSITE:PS51650"
FT DOMAIN 1352..1774
FT /note="DOCKER"
FT /evidence="ECO:0000259|PROSITE:PS51651"
FT REGION 94..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 157..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 417..496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1773..1981
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1994..2031
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..124
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..444
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..491
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1784..1798
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1813..1897
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1928..1942
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1943..1957
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1958..1981
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2124 AA; 235225 MW; 077CE61B338EEF78 CRC64;
MPWRPLPRIA FAVAIYPFQP SSPADLPLEL GDELYIIEQG GANGSWYRGY LVAPPSLLAG
LTSVKGRTLE ARVFSGIFPK NCVEVREVLG DVDGSRDGRL STQLPPRKYA GSRTSTASPD
SFSLTDGRTL ATSVGDLKAS RKISQITIIK LEEKGGSRRS VSPSLPLTPI SLGPRDPSAV
KPPAPVPMLK IGDETPTSAA EPLVDEIASC LREWHSTNIH QLLLTRQYTT LENMSNIVLE
LDLARRQLLH NVLTAQERAA LREETVWNLV RGNKMLSGEV VVRDPKQRGR LLTGDDSAVE
LTKLQSEMSM LDRGLTPQLD NISLHHLLLE VNAVSGTDAG SITLAASLWL KQANGDIRQL
SETYSLDLPT TETFATLVNN TKLKTLFTDL SATDIGEGSN SDSKLYLVIK ALGSESPRIN
APPKSRSSSS RDGSLSNKVA SGINSAGKGS LKARRSMMWG AKSRGLGPEI GKEQPRHPPQ
SSDSVTTKPS ETDTPGKERT VIRVVGLGAL DISAIAKQGR EVEQVVNIWS PLRANDEEDD
YSDGFDEIVR SLLYSPTKQY VRSLRAARVH VQLHPFTSED AETLVRNNPT SLHNVTHTKR
IGFSGAPTKP RSDIYVTINR ATISQEALLS HPINCQVPVP QVTGLRNLQL TLEVRNTAGV
RIEHCIYPSS NGPGQTAWRT TVAERGVPWN QTIRLDIPPD QVPTAHLVMS IADAPELPFA
LSWMPLWDQQ AFIRDGPHSL LLHAYDKSTS NIENGRGAYL SLPWSALGKN ESTKDEAVTG
PLATLSLETD LCSTEYSQDH VILNLINWRE RSPTEVLELL KRIVFVPEIE IVKQLRDVFD
ALFGIIVENS GNEEYEDLVF NDLVTVLGIV HDRRFNLVPL VDHYAEKHFN FPFATPCLIR
SYCRLLQATP DSQQSRNLRA AFKVGRHILK FIINAREQQK AKEEGIGITK VQSTFNRDLH
FIFKSVEALM QNPAPILVGS KTLVVQHFHT WLPELSNALT KEEIINIAVS FMDSCEDVKS
MLILYKLVLI LNYIRLPLFE SPKDREALFS HCVDWLSPYW GQTDDATDQY RDQVRLCSSI
VAEQLKHPSA EMYAYMPKAV ASYCALVADG VEGTNWLSML FSKTFPFQLK QSNVTQKFEE
SLVELAAIIA SLATIPNPTP LSLKGDDLAL FLSQALETHK SILSCEAYPS TWLSLHIYHH
RSTMKNDADN FDMELWKLFL ETLLKLVSSD ALTLETFPEQ KRRAVWKIAG DVREHGADLL
RRAWEAIGWD TSSEEQERYL VKKLGGYQVQ YVPSLVCPII ELCLSVHEGL RHVAVMILQT
MIVSEWQLNE DLSFVEAEII SSLDLLFKTK NVSESGTQKL FINELLDVFE INSSNPDADL
LVALKELVAT VDELLDLLVA SQNGNITGSL NTLKLMEFMK DMEKEDIFIR YVHELALGQI
AARNYTEAGL ALQFHADLYD WDISKRTQAS MAKIYDAIVK DNSPSQRYFR VTFKGLGFPA
TLRDKQYIFE GSPTDRIATF TDRMQKQYPA AHIVSSDDID DLEGQFLRIS AVSVQKDMTH
PVYQRSKVPY SVREHLLSSV PSQFSITSKR HTSGNDVKEQ WVVKTVFTTA EPFPNILRRS
EIISAEEIAL TPLQTAIERT WRKTQELMIL ERQASSGEDF NLTGLTEVLS RLLDLESSPS
SCVALYRQFI VDESKAYMNS EDGGTEEQAP HPANPLNNAM AVALIDHTLA LKRCLALYNR
PAYQATQAEL SSRFQVVFAP EVASLTPVFS APESGEPLNL LSSRPEPPIA PRPQPLTQPR
STSPEQELIR STRRFETPSA TNKSHEKTIT THRISLNPFK RSNHSATNSN STITASTINE
ARRQSESKLN GTHTSRPSTA KTEATDPVSV GLSRSASRRS RNRNRDSGSK RRSWFGGGGG
IDVRKNSLSI SAPATSTEDI RTTQQRITER ARSSRSQDEK NGNIAPQPSN AENNDNVGVS
NSISNAATKV SQLTRAVSNA GRGTKSSSNN KNNSTIASAS SNNNGRPVTS ERLVTKVTMP
VPTTMTTTVQ NNNSKHTVYN SHGANVGATV TADVAAAASV ADSNGGGGVR DSMMKRLSML
KVGRKTSRYN VRDGVRAGEV LREE
//
