ID A0A168PBG6_ABSGL Unreviewed; 1916 AA.
AC A0A168PBG6;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 28-JAN-2026, entry version 39.
DE RecName: Full=SH3 domain-containing protein {ECO:0008006|Google:ProtNLM};
GN Name=ABSGL_07855.1 scaffold 9181 {ECO:0000313|EMBL:SAM02092.1};
OS Absidia glauca (Pin mould).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Cunninghamellaceae; Absidia.
OX NCBI_TaxID=4829 {ECO:0000313|EMBL:SAM02092.1};
RN [1] {ECO:0000313|EMBL:SAM02092.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101.48 {ECO:0000313|EMBL:SAM02092.1};
RA Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA Babar A., Rosenke K.;
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LT553674; SAM02092.1; -; Genomic_DNA.
DR STRING; 4829.A0A168PBG6; -.
DR InParanoid; A0A168PBG6; -.
DR OrthoDB; 338531at2759; -.
DR Proteomes; UP000078561; Unassembled WGS sequence.
DR GO; GO:0051286; C:cell tip; IEA:TreeGrafter.
DR GO; GO:0015630; C:microtubule cytoskeleton; IEA:TreeGrafter.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0030950; P:establishment or maintenance of actin cytoskeleton polarity; IEA:TreeGrafter.
DR GO; GO:0008104; P:intracellular protein localization; IEA:TreeGrafter.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd17043; RA; 1.
DR Gene3D; 1.10.150.60; ARID DNA-binding domain; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR Gene3D; 3.10.20.90; Phosphatidylinositol 3-kinase Catalytic Subunit, Chain A, domain 1; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR001606; ARID_dom.
DR InterPro; IPR036431; ARID_dom_sf.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR053039; Polarity_Bud-Selection_Reg.
DR InterPro; IPR000159; RA_dom.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR048420; Zap1-like_Znf1.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR47775; BUD SITE SELECTION PROTEIN 14; 1.
DR PANTHER; PTHR47775:SF1; BUD SITE SELECTION PROTEIN 14; 1.
DR Pfam; PF01388; ARID; 1.
DR Pfam; PF00788; RA; 2.
DR Pfam; PF00018; SH3_1; 1.
DR Pfam; PF21816; Zap1_zf1; 1.
DR SMART; SM01014; ARID; 1.
DR SMART; SM00501; BRIGHT; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF46774; ARID-like; 1.
DR SUPFAM; SSF48371; ARM repeat; 2.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS51011; ARID; 1.
DR PROSITE; PS50002; SH3; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 4: Predicted;
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW Reference proteome {ECO:0000313|Proteomes:UP000078561};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 12..97
FT /note="ARID"
FT /evidence="ECO:0000259|PROSITE:PS51011"
FT DOMAIN 989..1050
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 123..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 638..657
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 751..785
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 798..845
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 904..985
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1136..1324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1375..1398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1453..1472
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1509..1605
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1672..1737
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..132
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..155
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..168
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 758..769
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 801..837
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 923..936
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 937..975
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 976..985
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1137..1147
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1148..1161
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1162..1182
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1192..1204
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1220..1239
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1240..1250
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1279..1311
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1312..1324
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1387..1398
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1458..1468
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1509..1522
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1527..1552
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1559..1570
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1579..1605
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1672..1684
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1691..1705
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1916 AA; 212636 MW; ED1EA5925FD54B38 CRC64;
MSKLTIDDIE RTPSYTQFVN DLKQFHISKG TTLQVEPVLG GKKVDLYKLF QSVINSGGFD
QASEREAFAF PPTCTNSAYI LKGLYIRNLI GWEEEKIWCK EWFPPAELLG PDAHKSSTLA
GKSFKKTVRQ RQHQQPQQQQ YPTVNHHHHH HHVHYHPSQQ PQQQQQRLIQ PQPSNMVMYP
SPHQHHCTSV HDQPFTPDIF VEFASQFVPP SDRDIIDQPH QCSISELHHR NQPSYHAHSK
EDSPGKEGQV SSSVVLLLIQ RFCLYIVHTS FDSNTKDQIL TALQFGTHTQ VEWALQIMVT
ISFECPEELR LDRNPLLLEL LLKIAEVSLQ QSDEAECMME HTLQILHILR NFSFIQENAK
LLAASTQLKQ MMIKNLVLSS SHYTHCIDVL ENVAAYIDIG PSDNYILCLA SLVYANERHV
LLGSMRVLTL LSLNKNNQTA LIPGSAQTAD RILQLLVVND EEVIGAALEY LYQYTRISNA
FRLQLLTTHS GADIGILVSL LMAKSKFFKP QLVQEEELTL VEQQQQQQQH TIHSSDSSSS
DLSRLSSAAA TSSSSSCSPL AGHGDIPCVP NLTSYQELDE PYRCLGWLKD KFELADSSCV
LSLDDMYLLY EIRFGHERAL KIKDFYTVLK IAFPRTSSAS STSSSTFGAH GQQESQQLTG
PVLEGTCVRG IQIKISILQD GSDVLCQWTN CSQTFQDEIL LQRHVLHDHI ESSDDVCMWT
DCEKLEPFND KVDIATHLRT HFGDEGLLNQ QQEYHPHPPQ HQHQPHYHHS SSSPSSEMVP
TLASLSLSTT PKSSAVQSYI SSSSSSPSSL SPSPSSPLTR SGSSSISTSP TTTTTTTAAT
NLRKPSIDLS PVRGVSLVAA HLLRQLSKDP KSHVYFMPYE RELTFIAQQR PKLTPYIQSM
FANFKDDDDD DDDNVALGRL GKHNSTADTT NNQSGGDDQD PDDEDDEDDD DDNEDDDDIE
DDEALGNEDE DEDDSSTFTS SPSIPDENID FDLVYTLHTF EATVEGQASV VKGDSLTLLD
DSNSYWWLVK VLKSNEVGYI PAENIETPFE RLARLNKHRN VEVTAIQQAS HYTNPDGESA
KAIINKKQRK QVTMSKDIYY QSHIILLGDD DEELEETYEE WEDDMVDEDS QSTMLASEDD
GLDTSDTEMD HHHGEGDHDH SNNTNTNGYQ SVDRNNPTTA ATTADEEVQG LRITTPSAAT
TSVGATEPTG DDESNDKSTK QLPSKPTPLT TTAPKASPLV SPTSNGTISS PKDDKESKKH
GGSFLRLFSR GKRQDGKKQQ SGVGQSYPMD NTSSDQGSTN SSTISDELQQ HPSTVPASSS
TSSMAALDPS ATVLRVYAGN INVNATYNSV LVYDHTNAEA LLRQAMDRFH ISQIEGKARG
KRSSVTSSPS QYPHQQHSSG VEYYISVKPN DGDELTLLPQ DKPLIIYQSL TAHLTTPMPS
LSNLKQQITN VEFGRIGSPS NNNSTNKRTG TKFGEDSIRF YLHKRIKRVN EQDGKLYVKV
SLYHDDAAKR DRKNSDSKDG KQRRAASNNS VGVSSSSLNN SNNGKHNNGT ENGNKHSLHS
GSYTSLSAGS FSMRRKKSTS SPSNSTLKIA TTSKATSTPG KPTQSQIDKL IAVSSMATVA
DLIDIALEKF HLLQQPGQEP PPRYRMLIVV NSQGPEKHLN PSSKLVEVLH DDTNAKNNTT
EKRFVLRKVA TSSSSSRSGN SNTRLSQHHR GTTPEPSQQK QRGEELDTLR SNATTSPLLT
PIPVMQLDTD TEMILRRLER ALVTFHDRKK ALSIGSVPPR LQLDPQQPKL AVMRNVNQGV
DVYLPHGILR SKPLPPQQTQ YVLMANDKNK DSSWELVTQR VLTNASASVN GAELVADADL
KALIKFATLF LEAAEAKGLD ASALPNEETL QPSSSLSSLD ELERELQRIM ASHTIS
//
