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Database: UniProt
Entry: A0A016W2J3_9BILA
LinkDB: A0A016W2J3_9BILA
Original site: A0A016W2J3_9BILA 
ID   A0A016W2J3_9BILA        Unreviewed;      1163 AA.
AC   A0A016W2J3;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=RhoGEF domain protein {ECO:0008006|Google:ProtNLM};
GN   Name=Acey_s0001.g11 {ECO:0000313|EMBL:EYC33821.1};
GN   Synonyms=Acey-tag-218 {ECO:0000313|EMBL:EYC33821.1};
GN   ORFNames=Y032_0001g11 {ECO:0000313|EMBL:EYC33821.1};
OS   Ancylostoma ceylanicum.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC   Ancylostomatinae; Ancylostoma.
OX   NCBI_TaxID=53326 {ECO:0000313|EMBL:EYC33821.1, ECO:0000313|Proteomes:UP000024635};
RN   [1] {ECO:0000313|Proteomes:UP000024635}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=HY135 {ECO:0000313|Proteomes:UP000024635};
RX   PubMed=25730766; DOI=10.1038/ng.3237;
RA   Schwarz E.M., Hu Y., Antoshechkin I., Miller M.M., Sternberg P.W.,
RA   Aroian R.V.;
RT   "The genome and transcriptome of the zoonotic hookworm Ancylostoma
RT   ceylanicum identify infection-specific gene families.";
RL   Nat. Genet. 47:416-422(2015).
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EYC33821.1}.
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DR   EMBL; JARK01001337; EYC33821.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A016W2J3; -.
DR   STRING; 53326.A0A016W2J3; -.
DR   Proteomes; UP000024635; Unassembled WGS sequence.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR   CDD; cd01221; PH_ephexin; 1.
DR   CDD; cd00160; RhoGEF; 1.
DR   CDD; cd11793; SH3_ephexin1_like; 1.
DR   Gene3D; 1.20.900.10; Dbl homology (DH) domain; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   InterPro; IPR035899; DBL_dom_sf.
DR   InterPro; IPR000219; DH-domain.
DR   InterPro; IPR047271; Ephexin-like.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR047270; PH_ephexin.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   PANTHER; PTHR12845:SF5; EPHEXIN, ISOFORM D; 1.
DR   PANTHER; PTHR12845; GUANINE NUCLEOTIDE EXCHANGE FACTOR; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00621; RhoGEF; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00325; RhoGEF; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF50044; SH3-domain; 1.
DR   PROSITE; PS50010; DH_2; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000024635};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}.
FT   DOMAIN          686..876
FT                   /note="DH"
FT                   /evidence="ECO:0000259|PROSITE:PS50010"
FT   DOMAIN          911..1034
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          1045..1106
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   REGION          24..53
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          70..309
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          334..407
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        94..109
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        156..208
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        209..224
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        238..261
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        357..385
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1163 AA;  130716 MW;  2FAE3FDE6C14B508 CRC64;
     MSMVQEPGLS GAADVRGGSR VRALAHRFET GDTSGAAAAP RAKSDDEVVK ERGSEQEMLL
     VVHVDVAGAA AAAAARKTTD QPARARLSRS RASQKKRPQS SSDPLQTSHR QPYAMRKCGS
     AHSNLCTVQP VEIKPRVRRE KPPPPQKPVD LAQRAMTWSK CSQPGPSSKR SPLPERESST
     PREQTNGNAT EVAEVPTVSS TPSTSRNSRP RLAPPPPPPP KKPARLISRD QTSENKPRLY
     REISSSSLNV ETISDSIYQQ LPSPEEALPR SPRLPSSAVP DERPRPSVPT IPLPLPPQSH
     EDPDDDDYEC YEQIDYSSDT LTIDGSVVDC SAESSVTYKA SGSEPTTARD RRSETFAESQ
     SWNTSSYPRH SLSLPGNSSM CPILDRPQTA ATVRKKPPSP RSAGASELEK LFRLKSSLQQ
     NISKKVDQLR QKVGERRIRT SQSVESRDID YSTRGDVTAV SESGSNYKNT DDDIYVYGDE
     WSSEDDDDQN VYEDRRSSMY KELEQQLNRA FPVAKMESEY EYDSADFVAS DEGQPRPEAL
     PFAALSVTTG SSTDEPSPEE EDYARQYTSR LPTDQPLYQI YMLAEHDKLF DSVLLRSSDS
     ACGQEEHAME STGTVDLFRR ESCASSDSGR GADCSTSASA LTSNTSMRRE RLIATSHFGS
     QRSLWCELEE VRAAGLLNTL DDETKMRQEA YFEVITSEAS YLRSLNILIT HFMASQELMG
     SKSSFSVISN SDRKQLFSNI FAVRDCSERL LSDLETRLEH SLVLDDLCGI LLHHFETNFD
     VYIKYCSNQV YQERTLRRLK AENPAFLTAI SRMEADKQCQ GLDMRSFLML PMQRVTRYPL
     LVYAILDRLK RGCDEYEVAT KALHAANRVV GECNEGARRM ERTEQLLEVD SRLVYKDPDL
     KKIALVSNCR YLVKRGSLVQ LMERKNRNIL QGKQKTRNVY IFLFSDIILV TKKKLNGTYE
     CKDYAARRYI DVQPLEVDPN RTTNGAISSL TTRPHLFLCV FMRNARGRQT ELLLNAESET
     DRERWLSALR PPISANPEEK IYAEWDCPQA VAVHTYNKNQ DDELSLEVGD MVNILRKMPD
     GWFFGEKTSD GQSGWFPSSY VQQILNDHVR ANNYRKRLRL IQAAGSVSTR ESPPRSSATP
     LMDRLRRMSN PRFLFQADPT SAL
//
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