ID A0A0V1NNY9_9BILA Unreviewed; 1628 AA.
AC A0A0V1NNY9;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Rho guanine nucleotide exchange factor 12 {ECO:0000313|EMBL:KRZ85691.1};
GN Name=Arhgef12 {ECO:0000313|EMBL:KRZ85691.1};
GN ORFNames=T08_3365 {ECO:0000313|EMBL:KRZ85691.1};
OS Trichinella sp. T8.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92180 {ECO:0000313|EMBL:KRZ85691.1, ECO:0000313|Proteomes:UP000054924};
RN [1] {ECO:0000313|EMBL:KRZ85691.1, ECO:0000313|Proteomes:UP000054924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS272 {ECO:0000313|EMBL:KRZ85691.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Membrane {ECO:0000256|ARBA:ARBA00004370}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the eukaryotic
CC ribosomal protein eS31 family. {ECO:0000256|ARBA:ARBA00009891}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the ubiquitin family.
CC {ECO:0000256|ARBA:ARBA00008373}.
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:KRZ85691.1}.
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DR EMBL; JYDM01000135; KRZ85691.1; -; Genomic_DNA.
DR Proteomes; UP000054924; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005840; C:ribosome; IEA:InterPro.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:InterPro.
DR CDD; cd00029; C1; 1.
DR CDD; cd00992; PDZ_signaling; 1.
DR CDD; cd00160; RhoGEF; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 3.30.60.20; -; 1.
DR Gene3D; 6.20.50.150; -; 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; 1.10.167.10; Regulator of G-protein Signalling 4, domain 2; 1.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR001331; GDS_CDC24_CS.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR041020; PH_16.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR015212; RGS-like_dom.
DR InterPro; IPR036305; RGS_sf.
DR InterPro; IPR044926; RGS_subdomain_2.
DR InterPro; IPR002906; Ribosomal_eS31.
DR InterPro; IPR038582; Ribosomal_eS31_euk-type_sf.
DR InterPro; IPR011332; Ribosomal_zn-bd.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR45872; RHO GUANINE NUCLEOTIDE EXCHANGE FACTOR 2, ISOFORM D; 1.
DR PANTHER; PTHR45872:SF2; RHO GUANINE NUCLEOTIDE EXCHANGE FACTOR 2, ISOFORM D; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF00595; PDZ; 1.
DR Pfam; PF17838; PH_16; 1.
DR Pfam; PF09128; RGS-like; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR Pfam; PF01599; Ribosomal_S27; 1.
DR Pfam; PF00240; ubiquitin; 1.
DR SMART; SM00109; C1; 1.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SMART; SM01402; Ribosomal_S27; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF48097; Regulator of G-protein signaling, RGS; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR SUPFAM; SSF57829; Zn-binding ribosomal proteins; 1.
DR PROSITE; PS00741; DH_1; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Guanine-nucleotide releasing factor {ECO:0000256|ARBA:ARBA00022658};
KW Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000054924};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274};
KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 13..75
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 531..581
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 785..971
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 1013..1128
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1478..1538
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000259|PROSITE:PS50053"
FT REGION 85..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 216..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 656..725
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1133..1156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 160..187
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 85..99
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..126
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 656..678
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 679..705
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 706..725
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1141..1155
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1628 AA; 184340 MW; 418F732FBDBF20EC CRC64;
MHFHGEHFAE ERNVLIKRDE NGYGLTVCGN NPVFVQSVRE GSAAAKAGVH VGECIIKVNG
VTVTSLDHLE VVKLISVAPY TTLTLSGGPS SSSAASSMGN DHYEKRDRCL ERRSTENAIR
PNSKKKQSEW HLKRKKIIQQ ILTEEKRQLQ VMLKGSDAHA DADQRIIEKM TRRIHNLEDQ
LNEVEKLDFE QVELFYKNLI YQENISLSNS GFRSHSDDLS SSLTMKSSKS HSDDVVASSS
TDDERLLTKS GNIDEIRDHQ IPVPVSEVPP ESPLLVHTLS MSNECDSAAV ELNSSSFDEP
FSKLPMLKTH LGHLAVFLHY LLSNSDPSYL LFYLLTDIFA LYIGKESKKW AYEIHSSFLL
PYSPCRVSFT DSSSWETVDA VLNDPNKHAD SAQWRRLFST ARGLAVQAIN EQLADFRSKR
ILGLGNVFGE SMLQRLQAGD SAHERKIFDA LIAPHLIAFF EEAADFDQLP KRIQVIVAAL
ATLYKHNNVK CRNAAMEKLL ERCPTYIAKE KQRFARPLLP KASRRALQIK AHCFNIAPVL
QTTFCYQCQK LIWGIGAMSL FCGKCGVVLH KSCVENLAES CFGSMNLRRP LILKKIVGRK
NVESSMDNIE QSIEEGKVST AKTDASMLLK ENSGEGDGSS EKNLTRNFDK SGVTNAAVSK
QSAHIHNLSR SQSMNIEEES YRGARRRSSD TSRRSHSDAD KTESLTRIST TESSTTVSVQ
DVSRERSPMI SELDSPLTSS VSFSNTLHDI HIELDSDFKV ENEIPLLEDL LDLESFQYLD
KREKNRLEVI YELFHTEQTH VRNLKILYRL FYKQLLNFNV ISFEFASLLF SNLEDVLNLH
VEMNEAMKNM MQNNKLIGDI SIMMLQFDGK ERMRNIDSLH CQKLQSAIEA LKHRVVKDQK
LREFLQVVES LPVCRKLQLK DMLPMEMQRL TKYPLLLENV LKYTEDPSEE ADRLRTCIEC
SRSILESVNS AKRNAENVLR LQRLQQMLDT TQFDKVNHPI VSEFCPLDVR RFSLIHEGPL
IWRLNKSKIV DLHVVLLDEI LLLLSPTSDG HLALRFHNIN ISCGKDEVKW THCPLLKLNS
LIAKDVATDK KAFFLVSTSP SGPQIYELAT QSKAEKQNWF KFIVEQIEAS KEHEQKTSVR
HGQAGQESKS GDSFYEIPNS ARKKSLTVRS QRTMKNPNFD ERVRVTCQPR LISPSEINIC
QPTVFQHSKP ILNPLEKLKQ EDKLVIRLLN EKLQIISSFF GQKNDLPPSS AVDSRTSREA
REFVISAIKQ TNRLLEAINE QTRLIEMENF ENGSVKYQVP EVECPSVPCY QLTQIAAGLM
TCLTNLLHSL QIMGDDLKRV QRELHQYKLS PERLLPFPEK ICQAVGTDIP TDVTHEAACR
KSLTDAAVQT EPASFLQTNN CDAVKKNAGK STENFHTDDQ PTELSGRSII KDALPTGSCN
TAASEKPILR NGKMGTDGLC LFDTDIAKLE EQPCSEIITI ESNCTIGEIK KQIQEEEESL
CSSYLVLGGR PLEDDWTLAQ CNIQEFSTLD LSYRLLGGAK KRKKKMYTTP KKIKHKKKKV
KLAVLKYYKI DENGKVSRLR KECTSESCGA GVFMANHYNR QYCGKCYCTM VVQDPVQREQ
KPGKGKGH
//
