ID C4JVI3_UNCRE Unreviewed; 2133 AA.
AC C4JVI3;
DT 07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 07-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EEP81710.1};
GN ORFNames=UREG_06575 {ECO:0000313|EMBL:EEP81710.1};
OS Uncinocarpus reesii (strain UAMH 1704).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Uncinocarpus.
OX NCBI_TaxID=336963 {ECO:0000313|EMBL:EEP81710.1, ECO:0000313|Proteomes:UP000002058};
RN [1] {ECO:0000313|Proteomes:UP000002058}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 1704 {ECO:0000313|Proteomes:UP000002058};
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(2009).
CC -!- SIMILARITY: Belongs to the DOCK family. {ECO:0000256|PROSITE-
CC ProRule:PRU00983}.
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DR EMBL; CH476618; EEP81710.1; -; Genomic_DNA.
DR RefSeq; XP_002583608.1; XM_002583562.1.
DR STRING; 336963.C4JVI3; -.
DR GeneID; 8438404; -.
DR KEGG; ure:UREG_06575; -.
DR VEuPathDB; FungiDB:UREG_06575; -.
DR eggNOG; KOG1998; Eukaryota.
DR HOGENOM; CLU_000595_0_1_1; -.
DR InParanoid; C4JVI3; -.
DR OMA; LWDNQAF; -.
DR OrthoDB; 8258at2759; -.
DR Proteomes; UP000002058; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
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; 1.20.58.740; -; 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; IPR043162; DOCK_C_lobe_C.
DR InterPro; IPR032376; DOCK_N.
DR InterPro; IPR042455; DOCK_N_sub1.
DR InterPro; IPR027357; DOCKER_dom.
DR InterPro; IPR046769; DOCKER_Lobe_A.
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; PF06920; DHR-2_Lobe_A; 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 Guanine-nucleotide releasing factor {ECO:0000256|ARBA:ARBA00022658};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000002058};
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 608..789
FT /note="C2 DOCK-type"
FT /evidence="ECO:0000259|PROSITE:PS51650"
FT DOMAIN 1433..1846
FT /note="DOCKER"
FT /evidence="ECO:0000259|PROSITE:PS51651"
FT REGION 151..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 418..449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 461..491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1860..1914
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1931..2100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..449
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 471..490
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1860..1878
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1931..1953
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1983..1997
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2029..2046
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2047..2070
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2083..2097
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2133 AA; 236850 MW; 10E10626FBBE558A CRC64;
MPWRPLPRIA FAVAVYPFQP SSPADLPLEL GDELYIIEQG GKDGAWYRGY LVAPPSLLAG
LTSVKGQALE ARVFSGIFPK NCVEVREVLG ETNRNKENGS AELALSNGNL KPIDGKAADG
SKTNSFIGLA DLKSSRKTSQ ITVIKLEDDV KKRRSGSPLQ SPSMALTPRS TGSRDPNAPK
PPAPVPMLKI GDETPTSLSE PLVDEIASCL REWHSTNIHE LLLTRQYTAL ENMSNIVLEL
DLARRQFLHN VLTAQERASL REATVWNLVR GNKTLSGDVI VRDPKQRGRL LTGDDSAIEM
AKLQSEMSML DGETKPHIDN VSLHHLLFEV NAVTGTKAGS APLSISLWLQ SAKGEIKQLT
ESYALDIPSA ETFVAMSQNG SLKTLFTDLN AADIGDSSAS DSKLYLVVRV LGPESARPSF
VAKSRTSSRD GPSGNKSTPA LNNVGKGSLK SRRSMIWGQK TRGLPHLDQN EISRLPQSSG
SSTSVSTHPE RPVKEISVLR TAGIGVLEIG SILKSDKDVD QVVSIWSPLG PTDEEDNYTE
GFDDIVRSLL PSPTGRYGRC YRASRLHAHL SPFASEDTET LIRNNPTLLH NVTQTRRIGF
PAAPTKPRSD IYVNLSKVNI SQDALLSHPI NGQVAVPQVT GLRNLQLTLE ARNASGARIE
HCIYPSSNAS GVTAWRTTVA ERGSAWNQII RLNIPSDEVQ GSHLIMSVAD APEFPFALSW
LPLWDQQAFI RDGRHSLLLH AYDKSTSSVE NGRGSYLSLP WSALGKNEST KDEALTGPLA
TLTLETELCS TQYSQDQALL GLVNWKEKPA TQLLELLRTI VFVPEIEIVK HLRDVFDALF
GIMVEQAGNE EFEDLIFRDL VTVLGIVHDR RFNLGPLVDR YAEQEFNFPF ATPCLIRSFL
RLLQATADSQ QARNLRAALK VGRHLLKFII NARGQQKAKE ECIGITNIQS TFNRDLHSIF
KSVEALMQNP APTLVGSKTL AVQHFHTWLP ELLNAVDKEE VVNIAFSFMD ACKDVKKMLV
LYKILLILNY TRLPLFGESA ERSRLISKSI EWLSPYWGET QDITDQYRDQ VRLCSSVVAE
QLKTPESGLF GYMPMAVASY CAIVADGVEE TEWLSLLFSK SFPFQLKQSK TKQRFDEALV
ELSAIIAAMS KLQMPKDLPL SHDELAIFLS HIFNAHKSVL DNEAYPATWL SLHIYHHQSI
MKSLEDLSSI LIQSFLPAPD EADTFDMELW KLFFVTLLKL VSSDALALET FPEQRRRAVW
KIAGDVREQG AELLQKTWRS IGWDTTVEER ARYGLVKLGG YQVQYVPGLV PPIIELCLSV
HEGPRRVAVE ILQTMIVSEW QLNEDLSVVE AEIISSLDEL FKTKNLTESI TQKLFINELL
ELFETSSTSP DAELLVTLKE LIATVDELLD LLVASHNGNI TESLNTIKLM EFMKDMERGD
IFIRYVHELA HGQAAARNYT EAGLALQFHA DLYEWDISKT VEALSNPTYP EQTAFERKET
LYFEIIQHFE DGKAWAHALS CYRELADHYE HTIIDFSKLS RTQASMARIY EAIVKEDILI
PRYFRVTFKG LGFPPTLRDK QYIFEGSQSD RMTTFTDRMQ KQYPTAQLVH YGEIEDLEGQ
FLQIAPVSVH KDVSHPVYQR PKVPQSVREH LLTAVASNFS ITSKKHLSSN QVKEQYITKS
VFTTAEPFPN VLRRSEIVAT EEVVLTPLQT AIERTSRKTQ ELLMLEKRIA SGDDTNLNSL
TDVLGQMLDV ESSVPTCVAQ YRAFLTGDEL NDHSALGEDL DIIPVDPLNN ALAVALVDHA
ISLKRCIALY SRPAYQATQA ELAQRLETVF APELATLAIS PSQHLPSEPS IQFGSRQEQF
TNGSMQGASS TSQPRLASLK SDPGRPSRDS IARPLMDKPP ASNRLSLNPF KRSNHVASGS
NATITAVNTA VSAQKDQSQQ SIVKPNGVPT DQVTRAPQPA GVKLEQDREP SDTVSRARSQ
SRGGKSDTSR KRRSFFGGSE KFAVGTSDPQ RGAHSVPPAS PPTEDMRTTQ QRIMERANKS
RAQQSHKEPR TPNSIPNSAG QRQTPPSNAI DHRLVASDKN PPRPKTGHSS VSDHTGSGVR
DSMMKRFSLL KVGRKGSKAN FHEKPLGGVL REE
//
