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Conserved domains on  [gi|143811366|sp|P11274|]
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RecName: Full=Breakpoint cluster region protein; AltName: Full=Renal carcinoma antigen NY-REN-26

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RhoGAP_Bcr cd04387
RhoGAP_Bcr: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of Bcr ...
1052-1252 2.46e-126

RhoGAP_Bcr: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of Bcr (breakpoint cluster region protein)-like proteins. Bcr is a multidomain protein with a variety of enzymatic functions. It contains a RhoGAP and a Rho GEF domain, a Ser/Thr kinase domain, an N-terminal oligomerization domain, and a C-terminal PDZ binding domain, in addition to PH and C2 domains. Bcr is a negative regulator of: i) RacGTPase, via the Rho GAP domain, ii) the Ras-Raf-MEK-ERK pathway, via phosphorylation of the Ras binding protein AF-6, and iii) the Wnt signaling pathway through binding beta-catenin. Bcr can form a complex with beta-catenin and Tcf1. The Wnt signaling pathway is involved in cell proliferation, differentiation, and cell renewal. Bcr was discovered as a fusion partner of Abl. The Bcr-Abl fusion is characteristic for a large majority of chronic myelogenous leukemias (CML). Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


:

Pssm-ID: 239852 [Multi-domain]  Cd Length: 196  Bit Score: 386.98  E-value: 2.46e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366 1052 FGVKIAVVTKRERSKVPYIVRQCVEEIERRGMEEVGIYRVSGVATDIQALKAAFDVNNKDVSVMMSEMDVNAIAGTLKLY 1131
Cdd:cd04387     1 FGVKISTVTKRERSKVPYIVRQCVEEVERRGMEEVGIYRISGVATDIQALKAAFDTNNKDVSVMLSEMDVNAIAGTLKLY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366 1132 FRELPEPLFTDEFYPNFAEGIALSDPVAKESCMLNLLLSLPEANLLTFLFLLDHLKRVAEKEAVNKMSLHNLATVFGPTL 1211
Cdd:cd04387    81 FRELPEPLFTDELYPNFAEGIALSDPVAKESCMLNLLLSLPDPNLVTFLFLLHHLKRVAEREEVNKMSLHNLATVFGPTL 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 143811366 1212 LRPSEKESKLPANpsqpiTMTDSWSLEVMSQVQVLLYFLQL 1252
Cdd:cd04387   161 LRPSEKESKIPTN-----TMTDSWSLEVMSQVQVLLYFLQL 196
PH_BCR_vertebrate cd13367
Breakpoint Cluster Region-related pleckstrin homology (PH) domain; The BCR gene is one of the ...
684-877 6.08e-125

Breakpoint Cluster Region-related pleckstrin homology (PH) domain; The BCR gene is one of the two genes in the BCR-ABL complex, which is associated with the Philadelphia chromosome, a product of a reciprocal translocation between chromosomes 22 and 9. BCR is a GTPase-activating protein (GAP) for RAC1 (primarily) and CDC42. The Dbl region of BCR has the most RhoGEF activity for Cdc42, and less activity towards Rac and Rho. Since BCR possesses both GAP and GEF activities, it may function to temporally regulate the activity of these GTPases. It also displays serine/threonine kinase activity. The BCR protein contains multiple domains including an N-terminal kinase domain, a RhoGEF domain, a PH domain, a C1 domain, a C2 domain, and a C-terminal RhoGAP domain. This hierarchy is composed of vertebrate BCRs. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


:

Pssm-ID: 270173  Cd Length: 194  Bit Score: 383.20  E-value: 6.08e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366  684 FLSSINEEITPRRQSMTVKKGEHRQLLKDSFMVELVEGARKLRHVFLFTDLLLCTKLKKQSGGKTQQYDCKWYIPLTDLS 763
Cdd:cd13367     1 FLSSINEEITPRRQSMTVKKGEHRQLLKDSFMVELVEGARKLRHVFLFTDLLLCAKLKKQIGGKSQQYDCKWYIPLADLS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366  764 FQMVDELEAVPNIPLVPDEELDALKIKISQIKNDIQREKRANKGSKATERLKKKLSEQESLLLLMSPSMAFRVHSRNGKS 843
Cdd:cd13367    81 FQTVDESEAVPNIPLIPDEEIDALKVKISQIKSDIQREKRANKGGKVLERLRKKLSEQESLLLLMSPSMAFRVHNRNGKS 160
                         170       180       190
                  ....*....|....*....|....*....|....
gi 143811366  844 YTFLISSDYERAEWRENIREQQKKCFRSFSLTSV 877
Cdd:cd13367   161 YTFLISSDYERAEWRENIREQQKKCFKSFSLTSL 194
C2_ABR cd08686
C2 domain in the Active BCR (Breakpoint cluster region) Related protein; The ABR protein is ...
913-1033 3.13e-70

C2 domain in the Active BCR (Breakpoint cluster region) Related protein; The ABR protein is similar to the breakpoint cluster region protein. It has homology to guanine nucleotide exchange proteins and GTPase-activating proteins (GAPs). ABR is expressed primarily in the brain, but also includes non-neuronal tissues such as the heart. It has been associated with human diseases such as Miller-Dieker syndrome in which mental retardation and malformations of the heart are present. ABR contains a RhoGEF domain and a PH-like domain upstream of its C2 domain and a RhoGAP domain downstream of this domain. A few members also contain a Bcr-Abl oncoprotein oligomerization domain at the very N-terminal end. Splice variants of ABR have been identified. ABR is found in a wide variety of organisms including chimpanzee, dog, mouse, rat, fruit fly, and mosquito. The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


:

Pssm-ID: 176068  Cd Length: 118  Bit Score: 230.09  E-value: 3.13e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366  913 LNVIVHSATGFKQSSNLYCTLEVDSFGYFVNKAKTRVYRDTAEPNWNEEFEIELEGSQTLRILCYEKCYNKTKIpkeDGE 992
Cdd:cd08686     1 LNVIVHSAQGFKQSANLYCTLEVDSFGYFVKKAKTRVCRDTTEPNWNEEFEIELEGSQTLRILCYEKCYSKVKL---DGE 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 143811366  993 STDRLMGKGQVQLDPQALQDRDWQRTVIAMNGIEVKLSVKF 1033
Cdd:cd08686    78 GTDAIMGKGQIQLDPQSLQTKKWQEKVISMNGITVNLSIKF 118
RhoGEF cd00160
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous ...
499-689 1.88e-40

Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous (DH) domain. It appears that PH domains invariably occur C-terminal to RhoGEF/DH domains.


:

Pssm-ID: 238091 [Multi-domain]  Cd Length: 181  Bit Score: 147.44  E-value: 1.88e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366  499 RKWVLSGILASEETYLSHLEALLLP-MKPLKAaattSQPVLTSQQIETIFFKVPELYEIHKEFYDGLFPRVQQW-SHQQR 576
Cdd:cd00160     1 RQEVIKELLQTERNYVRDLKLLVEVfLKPLDK----ELLPLSPEEVELLFGNIEEIYEFHRIFLKSLEERVEEWdKSGPR 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366  577 VGDLFQKLASQLGVYRAFVDNYGVAMEMAEKCCQANAQFAEISENLRARSNKdakdpttkNSLETLLYKPVDRVTRSTLV 656
Cdd:cd00160    77 IGDVFLKLAPFFKIYSEYCSNHPDALELLKKLKKFNKFFQEFLEKAESECGR--------LKLESLLLKPVQRLTKYPLL 148
                         170       180       190
                  ....*....|....*....|....*....|...
gi 143811366  657 LHDLLKHTPASHPDHPLLQDALRISQNFLSSIN 689
Cdd:cd00160   149 LKELLKHTPDGHEDREDLKKALEAIKEVASQVN 181
Bcr-Abl_Oligo pfam09036
Bcr-Abl oncoprotein oligomerization domain; The Bcr-Abl oncoprotein oligomerization domain ...
3-75 2.39e-40

Bcr-Abl oncoprotein oligomerization domain; The Bcr-Abl oncoprotein oligomerization domain consists of a short N-terminal helix (alpha-1), a flexible loop and a long C-terminal helix (alpha-2). Together these form an N-shaped structure, with the loop allowing the two helices to assume a parallel orientation. The monomeric domains associate into a dimer through the formation of an antiparallel coiled coil between the alpha-2 helices and domain swapping of two alpha-1 helices, where one alpha-1 helix swings back and packs against the alpha-2 helix from the second monomer. Two dimers then associate into a tetramer. The oligomerization domain is essential for the oncogenicity of the Bcr-Abl protein.


:

Pssm-ID: 430380  Cd Length: 73  Bit Score: 143.08  E-value: 2.39e-40
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 143811366     3 DPVGFAEAWKAQFPDSEPPRMELRSVGDIEQELERCKASIRRLEQEVNQERFRMIYLQTLLAKEKKSYDRQRW 75
Cdd:pfam09036    1 EPAGFERHWRAEFPEGQVPKMELGSVEDIEQELERCKASLRRLQQELNEEKFKVIYLQTLLARERKSYDRQRW 73
PHA03307 super family cl33723
transcriptional regulator ICP4; Provisional
80-387 2.40e-06

transcriptional regulator ICP4; Provisional


The actual alignment was detected with superfamily member PHA03307:

Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 52.10  E-value: 2.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366   80 AAQAPDGASEPRASAS-RPQPAPADGADPPPAEEPEARPDGEGSPGKARPGTARRPGAAASGERDDRGPPASVAAlrSNF 158
Cdd:PHA03307   98 ASPAREGSPTPPGPSSpDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQA--ALP 175
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366  159 ERIRKGHGQPGADAEKPFYVNVEFHHERGLVKVNDKEVSDRISSLGSQamqmerkksqhGAGSSVGDASRPPYRGRSSES 238
Cdd:PHA03307  176 LSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPA-----------PGRSAADDAGASSSDSSSSES 244
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366  239 S-CGVDGDyedaelnprflkdnliDANGGSRPPWPPLEYQPYQSIyvggMMEGEGKGPLLRSQSTSEQEkrltwpRRSYS 317
Cdd:PHA03307  245 SgCGWGPE----------------NECPLPRPAPITLPTRIWEAS----GWNGPSSRPGPASSSSSPRE------RSPSP 298
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 143811366  318 PRSFEDCGGGYTPDCSSNENLTSSEEDFSSGQSSRVSPSPTTYRMFRDKSRSPS-QNSQQSFDSSSPPTPQ 387
Cdd:PHA03307  299 SPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSpSRPPPPADPSSPRKRP 369
 
Name Accession Description Interval E-value
RhoGAP_Bcr cd04387
RhoGAP_Bcr: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of Bcr ...
1052-1252 2.46e-126

RhoGAP_Bcr: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of Bcr (breakpoint cluster region protein)-like proteins. Bcr is a multidomain protein with a variety of enzymatic functions. It contains a RhoGAP and a Rho GEF domain, a Ser/Thr kinase domain, an N-terminal oligomerization domain, and a C-terminal PDZ binding domain, in addition to PH and C2 domains. Bcr is a negative regulator of: i) RacGTPase, via the Rho GAP domain, ii) the Ras-Raf-MEK-ERK pathway, via phosphorylation of the Ras binding protein AF-6, and iii) the Wnt signaling pathway through binding beta-catenin. Bcr can form a complex with beta-catenin and Tcf1. The Wnt signaling pathway is involved in cell proliferation, differentiation, and cell renewal. Bcr was discovered as a fusion partner of Abl. The Bcr-Abl fusion is characteristic for a large majority of chronic myelogenous leukemias (CML). Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239852 [Multi-domain]  Cd Length: 196  Bit Score: 386.98  E-value: 2.46e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366 1052 FGVKIAVVTKRERSKVPYIVRQCVEEIERRGMEEVGIYRVSGVATDIQALKAAFDVNNKDVSVMMSEMDVNAIAGTLKLY 1131
Cdd:cd04387     1 FGVKISTVTKRERSKVPYIVRQCVEEVERRGMEEVGIYRISGVATDIQALKAAFDTNNKDVSVMLSEMDVNAIAGTLKLY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366 1132 FRELPEPLFTDEFYPNFAEGIALSDPVAKESCMLNLLLSLPEANLLTFLFLLDHLKRVAEKEAVNKMSLHNLATVFGPTL 1211
Cdd:cd04387    81 FRELPEPLFTDELYPNFAEGIALSDPVAKESCMLNLLLSLPDPNLVTFLFLLHHLKRVAEREEVNKMSLHNLATVFGPTL 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 143811366 1212 LRPSEKESKLPANpsqpiTMTDSWSLEVMSQVQVLLYFLQL 1252
Cdd:cd04387   161 LRPSEKESKIPTN-----TMTDSWSLEVMSQVQVLLYFLQL 196
PH_BCR_vertebrate cd13367
Breakpoint Cluster Region-related pleckstrin homology (PH) domain; The BCR gene is one of the ...
684-877 6.08e-125

Breakpoint Cluster Region-related pleckstrin homology (PH) domain; The BCR gene is one of the two genes in the BCR-ABL complex, which is associated with the Philadelphia chromosome, a product of a reciprocal translocation between chromosomes 22 and 9. BCR is a GTPase-activating protein (GAP) for RAC1 (primarily) and CDC42. The Dbl region of BCR has the most RhoGEF activity for Cdc42, and less activity towards Rac and Rho. Since BCR possesses both GAP and GEF activities, it may function to temporally regulate the activity of these GTPases. It also displays serine/threonine kinase activity. The BCR protein contains multiple domains including an N-terminal kinase domain, a RhoGEF domain, a PH domain, a C1 domain, a C2 domain, and a C-terminal RhoGAP domain. This hierarchy is composed of vertebrate BCRs. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270173  Cd Length: 194  Bit Score: 383.20  E-value: 6.08e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366  684 FLSSINEEITPRRQSMTVKKGEHRQLLKDSFMVELVEGARKLRHVFLFTDLLLCTKLKKQSGGKTQQYDCKWYIPLTDLS 763
Cdd:cd13367     1 FLSSINEEITPRRQSMTVKKGEHRQLLKDSFMVELVEGARKLRHVFLFTDLLLCAKLKKQIGGKSQQYDCKWYIPLADLS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366  764 FQMVDELEAVPNIPLVPDEELDALKIKISQIKNDIQREKRANKGSKATERLKKKLSEQESLLLLMSPSMAFRVHSRNGKS 843
Cdd:cd13367    81 FQTVDESEAVPNIPLIPDEEIDALKVKISQIKSDIQREKRANKGGKVLERLRKKLSEQESLLLLMSPSMAFRVHNRNGKS 160
                         170       180       190
                  ....*....|....*....|....*....|....
gi 143811366  844 YTFLISSDYERAEWRENIREQQKKCFRSFSLTSV 877
Cdd:cd13367   161 YTFLISSDYERAEWRENIREQQKKCFKSFSLTSL 194
C2_ABR cd08686
C2 domain in the Active BCR (Breakpoint cluster region) Related protein; The ABR protein is ...
913-1033 3.13e-70

C2 domain in the Active BCR (Breakpoint cluster region) Related protein; The ABR protein is similar to the breakpoint cluster region protein. It has homology to guanine nucleotide exchange proteins and GTPase-activating proteins (GAPs). ABR is expressed primarily in the brain, but also includes non-neuronal tissues such as the heart. It has been associated with human diseases such as Miller-Dieker syndrome in which mental retardation and malformations of the heart are present. ABR contains a RhoGEF domain and a PH-like domain upstream of its C2 domain and a RhoGAP domain downstream of this domain. A few members also contain a Bcr-Abl oncoprotein oligomerization domain at the very N-terminal end. Splice variants of ABR have been identified. ABR is found in a wide variety of organisms including chimpanzee, dog, mouse, rat, fruit fly, and mosquito. The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


Pssm-ID: 176068  Cd Length: 118  Bit Score: 230.09  E-value: 3.13e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366  913 LNVIVHSATGFKQSSNLYCTLEVDSFGYFVNKAKTRVYRDTAEPNWNEEFEIELEGSQTLRILCYEKCYNKTKIpkeDGE 992
Cdd:cd08686     1 LNVIVHSAQGFKQSANLYCTLEVDSFGYFVKKAKTRVCRDTTEPNWNEEFEIELEGSQTLRILCYEKCYSKVKL---DGE 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 143811366  993 STDRLMGKGQVQLDPQALQDRDWQRTVIAMNGIEVKLSVKF 1033
Cdd:cd08686    78 GTDAIMGKGQIQLDPQSLQTKKWQEKVISMNGITVNLSIKF 118
RhoGAP smart00324
GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac ...
1067-1230 5.84e-62

GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases. etter domain limits and outliers.


Pssm-ID: 214618  Cd Length: 174  Bit Score: 209.04  E-value: 5.84e-62
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366   1067 VPYIVRQCVEEIERRGMEEVGIYRVSGVATDIQALKAAFDvNNKDVSVMMSEMDVNAIAGTLKLYFRELPEPLFTDEFYP 1146
Cdd:smart00324    3 IPIIVEKCIEYLEKRGLDTEGIYRVSGSKSRVKELRDAFD-SGPDPDLDLSEYDVHDVAGLLKLFLRELPEPLITYELYE 81
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366   1147 NFAEGIALSDPVAKESCMLNLLLSLPEANLLTFLFLLDHLKRVAEKEAVNKMSLHNLATVFGPTLLRPSEKESKLPANPS 1226
Cdd:smart00324   82 EFIEAAKLEDETERLRALRELLSLLPPANRATLRYLLAHLNRVAEHSEENKMTARNLAIVFGPTLLRPPDGEVASLKDIR 161

                    ....
gi 143811366   1227 QPIT 1230
Cdd:smart00324  162 HQNT 165
RhoGAP pfam00620
RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.
1068-1219 7.52e-60

RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.


Pssm-ID: 425782  Cd Length: 152  Bit Score: 202.03  E-value: 7.52e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366  1068 PYIVRQCVEEIERRGMEEVGIYRVSGVATDIQALKAAFDvNNKDVSVMMSEMDVNAIAGTLKLYFRELPEPLFTDEFYPN 1147
Cdd:pfam00620    1 PLIVRKCVEYLEKRGLDTEGIFRVSGSASRIKELREAFD-SGEDVDLDLEEEDVHDVASLLKLFLRELPEPLLTFELYEE 79
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 143811366  1148 FAEGIALSDPVAKESCMLNLLLSLPEANLLTFLFLLDHLKRVAEKEAVNKMSLHNLATVFGPTLLRPSEKES 1219
Cdd:pfam00620   80 FIEAAKSEDEEERIEALRELLEKLPPANRDTLRYLLAHLNRVAQNSDVNKMNAHNLAIVFGPTLLRPPDSES 151
RhoGEF cd00160
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous ...
499-689 1.88e-40

Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous (DH) domain. It appears that PH domains invariably occur C-terminal to RhoGEF/DH domains.


Pssm-ID: 238091 [Multi-domain]  Cd Length: 181  Bit Score: 147.44  E-value: 1.88e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366  499 RKWVLSGILASEETYLSHLEALLLP-MKPLKAaattSQPVLTSQQIETIFFKVPELYEIHKEFYDGLFPRVQQW-SHQQR 576
Cdd:cd00160     1 RQEVIKELLQTERNYVRDLKLLVEVfLKPLDK----ELLPLSPEEVELLFGNIEEIYEFHRIFLKSLEERVEEWdKSGPR 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366  577 VGDLFQKLASQLGVYRAFVDNYGVAMEMAEKCCQANAQFAEISENLRARSNKdakdpttkNSLETLLYKPVDRVTRSTLV 656
Cdd:cd00160    77 IGDVFLKLAPFFKIYSEYCSNHPDALELLKKLKKFNKFFQEFLEKAESECGR--------LKLESLLLKPVQRLTKYPLL 148
                         170       180       190
                  ....*....|....*....|....*....|...
gi 143811366  657 LHDLLKHTPASHPDHPLLQDALRISQNFLSSIN 689
Cdd:cd00160   149 LKELLKHTPDGHEDREDLKKALEAIKEVASQVN 181
Bcr-Abl_Oligo pfam09036
Bcr-Abl oncoprotein oligomerization domain; The Bcr-Abl oncoprotein oligomerization domain ...
3-75 2.39e-40

Bcr-Abl oncoprotein oligomerization domain; The Bcr-Abl oncoprotein oligomerization domain consists of a short N-terminal helix (alpha-1), a flexible loop and a long C-terminal helix (alpha-2). Together these form an N-shaped structure, with the loop allowing the two helices to assume a parallel orientation. The monomeric domains associate into a dimer through the formation of an antiparallel coiled coil between the alpha-2 helices and domain swapping of two alpha-1 helices, where one alpha-1 helix swings back and packs against the alpha-2 helix from the second monomer. Two dimers then associate into a tetramer. The oligomerization domain is essential for the oncogenicity of the Bcr-Abl protein.


Pssm-ID: 430380  Cd Length: 73  Bit Score: 143.08  E-value: 2.39e-40
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 143811366     3 DPVGFAEAWKAQFPDSEPPRMELRSVGDIEQELERCKASIRRLEQEVNQERFRMIYLQTLLAKEKKSYDRQRW 75
Cdd:pfam09036    1 EPAGFERHWRAEFPEGQVPKMELGSVEDIEQELERCKASLRRLQQELNEEKFKVIYLQTLLARERKSYDRQRW 73
RhoGEF pfam00621
RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called ...
502-689 4.42e-40

RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called Dbl-homologous (DH) domain. It appears that pfam00169 domains invariably occur C-terminal to RhoGEF/DH domains.


Pssm-ID: 425783 [Multi-domain]  Cd Length: 176  Bit Score: 146.29  E-value: 4.42e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366   502 VLSGILASEETYLSHLEALL-----LPMKPLKaaattsqpvLTSQQIETIFFKVPELYEIHKEFYdgLFPRVQQWSHQQR 576
Cdd:pfam00621    1 VIKELLQTERSYVRDLEILVevflpPNSKPLS---------ESEEEIKTIFSNIEEIYELHRQLL--LEELLKEWISIQR 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366   577 VGDLFQKLASQLGVYRAFVDNYGVAMEMAEKCCQANAQFAEISENLRARSNkdakdpTTKNSLETLLYKPVDRVTRSTLV 656
Cdd:pfam00621   70 IGDIFLKFAPGFKVYSTYCSNYPKALELLKKLLKKNPKFRAFLEELEANPE------CRGLDLNSFLIKPVQRIPRYPLL 143
                          170       180       190
                   ....*....|....*....|....*....|...
gi 143811366   657 LHDLLKHTPASHPDHPLLQDALRISQNFLSSIN 689
Cdd:pfam00621  144 LKELLKHTPPDHPDYEDLKKALEAIKEVAKQIN 176
RhoGEF smart00325
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange ...
502-690 4.05e-39

Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called Dbl-homologous (DH) domain. It appears that PH domains invariably occur C-terminal to RhoGEF/DH domains. Improved coverage.


Pssm-ID: 214619 [Multi-domain]  Cd Length: 180  Bit Score: 143.60  E-value: 4.05e-39
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366    502 VLSGILASEETYLSHLEALL-LPMKPLKAaattSQPVLTSQQIETIFFKVPELYEIHKEFYDGLFPRVQQWSH-QQRVGD 579
Cdd:smart00325    1 VLKELLQTERNYVRDLKLLVeVFLKPLKK----ELKLLSPNELETLFGNIEEIYEFHRDFLDELEERIEEWDDsVERIGD 76
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366    580 LFQKLASQLGVYRAFVDNYGVAMEMAEKCcQANAQFAEISENLRARSNKDAKDpttknsLETLLYKPVDRVTRSTLVLHD 659
Cdd:smart00325   77 VFLKLEEFFKIYSEYCSNHPDALELLKKL-KKNPRFQKFLKEIESSPQCRRLT------LESLLLKPVQRLTKYPLLLKE 149
                           170       180       190
                    ....*....|....*....|....*....|.
gi 143811366    660 LLKHTPASHPDHPLLQDALRISQNFLSSINE 690
Cdd:smart00325  150 LLKHTPEDHEDREDLKKALKAIKELANQVNE 180
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
912-1016 9.11e-12

Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, protein kinases C, and synaptotagmins (among others). Some do not appear to contain Ca2+-binding sites. Particular C2s appear to bind phospholipids, inositol polyphosphates, and intracellular proteins. Unusual occurrence in perforin. Synaptotagmin and PLC C2s are permuted in sequence with respect to N- and C-terminal beta strands. SMART detects C2 domains using one or both of two profiles.


Pssm-ID: 214577 [Multi-domain]  Cd Length: 101  Bit Score: 62.50  E-value: 9.11e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366    912 FLNVIVHSATGFK-----QSSNLYCTLEVDsfGYFVNKAKTRVYRDTAEPNWNEEFEIEL--EGSQTLRILCYEKcynkt 984
Cdd:smart00239    1 TLTVKIISARNLPpkdkgGKSDPYVKVSLD--GDPKEKKKTKVVKNTLNPVWNETFEFEVppPELAELEIEVYDK----- 73
                            90       100       110
                    ....*....|....*....|....*....|..
gi 143811366    985 kipkeDGESTDRLMGKGQVQLDPQALQDRDWQ 1016
Cdd:smart00239   74 -----DRFGRDDFIGQVTIPLSDLLLGGRHEK 100
C2 pfam00168
C2 domain;
911-1013 3.47e-08

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 52.71  E-value: 3.47e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366   911 GFLNVIVHSATG-----FKQSSNLYCTLEVDSFgyfVNKAKTRVYRDTAEPNWNEEFEIEL--EGSQTLRILCYEKcynk 983
Cdd:pfam00168    1 GRLTVTVIEAKNlppkdGNGTSDPYVKVYLLDG---KQKKKTKVVKNTLNPVWNETFTFSVpdPENAVLEIEVYDY---- 73
                           90       100       110
                   ....*....|....*....|....*....|
gi 143811366   984 tkipkeDGESTDRLMGKGQVQLDPQALQDR 1013
Cdd:pfam00168   74 ------DRFGRDDFIGEVRIPLSELDSGEG 97
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
80-387 2.40e-06

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 52.10  E-value: 2.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366   80 AAQAPDGASEPRASAS-RPQPAPADGADPPPAEEPEARPDGEGSPGKARPGTARRPGAAASGERDDRGPPASVAAlrSNF 158
Cdd:PHA03307   98 ASPAREGSPTPPGPSSpDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQA--ALP 175
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366  159 ERIRKGHGQPGADAEKPFYVNVEFHHERGLVKVNDKEVSDRISSLGSQamqmerkksqhGAGSSVGDASRPPYRGRSSES 238
Cdd:PHA03307  176 LSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPA-----------PGRSAADDAGASSSDSSSSES 244
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366  239 S-CGVDGDyedaelnprflkdnliDANGGSRPPWPPLEYQPYQSIyvggMMEGEGKGPLLRSQSTSEQEkrltwpRRSYS 317
Cdd:PHA03307  245 SgCGWGPE----------------NECPLPRPAPITLPTRIWEAS----GWNGPSSRPGPASSSSSPRE------RSPSP 298
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 143811366  318 PRSFEDCGGGYTPDCSSNENLTSSEEDFSSGQSSRVSPSPTTYRMFRDKSRSPS-QNSQQSFDSSSPPTPQ 387
Cdd:PHA03307  299 SPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSpSRPPPPADPSSPRKRP 369
PH_19 pfam19057
PH domain; This entry contains a PH domain found in RhoGEF proteins.
707-768 3.37e-05

PH domain; This entry contains a PH domain found in RhoGEF proteins.


Pssm-ID: 436928  Cd Length: 154  Bit Score: 45.17  E-value: 3.37e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 143811366   707 RQLLKDSFMVELVEGAR------KLRHVFLFTDLLLCTKLKKQSG---------GKTQQYDCKWYIPLTDLSFQMVD 768
Cdd:pfam19057   11 RYLIRQDDVVETVYNERgeviktKERRLFLLNDLLVCVTVNSKSGssfgssslvPTGEKYKLKWSVPLSDVEVVESG 87
KLF14_N cd21576
N-terminal domain of Kruppel-like factor 14; Kruppel-like factor 14 (KLF14; also known as ...
90-148 1.40e-04

N-terminal domain of Kruppel-like factor 14; Kruppel-like factor 14 (KLF14; also known as Krueppel-like factor 14 or basic transcription element-binding protein 5/BTEB5) is a protein that in humans is encoded by the KLF14 gene. KLF14 regulates the transcription of various genes, including TGFbetaRII (the type II receptor for TGFbeta). KLF14 is expressed in many tissues, lacks introns, and is subject to parent-specific expression. It also appears to be a master regulator of gene expression in adipose tissue. KLF14 is associated with coronary artery disease, hypercholesterolemia, and type 2 diabetes. KLF9, KLF10, KLF11, KLF13, KLF14, and KLF16 share a conserved alpha-helical motif AA/VXXL that mediates their binding to Sin3A and their activities as transcriptional repressors. KLF14 belongs to a family of proteins, called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specificity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the N-terminal domain of KLF14.


Pssm-ID: 409238 [Multi-domain]  Cd Length: 195  Bit Score: 44.43  E-value: 1.40e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 143811366   90 PRASASRPQPA----PADGADPPPAEEPEARPDGEGSPGK-ARPGTARRPGAAASGERDDRGPP 148
Cdd:cd21576   107 PRASSGSSDPArgssPTLGSEPAPASGEDAVSGPESSFGApAIPSAPAAPGAPAVSGEVPGGAP 170
 
Name Accession Description Interval E-value
RhoGAP_Bcr cd04387
RhoGAP_Bcr: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of Bcr ...
1052-1252 2.46e-126

RhoGAP_Bcr: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of Bcr (breakpoint cluster region protein)-like proteins. Bcr is a multidomain protein with a variety of enzymatic functions. It contains a RhoGAP and a Rho GEF domain, a Ser/Thr kinase domain, an N-terminal oligomerization domain, and a C-terminal PDZ binding domain, in addition to PH and C2 domains. Bcr is a negative regulator of: i) RacGTPase, via the Rho GAP domain, ii) the Ras-Raf-MEK-ERK pathway, via phosphorylation of the Ras binding protein AF-6, and iii) the Wnt signaling pathway through binding beta-catenin. Bcr can form a complex with beta-catenin and Tcf1. The Wnt signaling pathway is involved in cell proliferation, differentiation, and cell renewal. Bcr was discovered as a fusion partner of Abl. The Bcr-Abl fusion is characteristic for a large majority of chronic myelogenous leukemias (CML). Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239852 [Multi-domain]  Cd Length: 196  Bit Score: 386.98  E-value: 2.46e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366 1052 FGVKIAVVTKRERSKVPYIVRQCVEEIERRGMEEVGIYRVSGVATDIQALKAAFDVNNKDVSVMMSEMDVNAIAGTLKLY 1131
Cdd:cd04387     1 FGVKISTVTKRERSKVPYIVRQCVEEVERRGMEEVGIYRISGVATDIQALKAAFDTNNKDVSVMLSEMDVNAIAGTLKLY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366 1132 FRELPEPLFTDEFYPNFAEGIALSDPVAKESCMLNLLLSLPEANLLTFLFLLDHLKRVAEKEAVNKMSLHNLATVFGPTL 1211
Cdd:cd04387    81 FRELPEPLFTDELYPNFAEGIALSDPVAKESCMLNLLLSLPDPNLVTFLFLLHHLKRVAEREEVNKMSLHNLATVFGPTL 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 143811366 1212 LRPSEKESKLPANpsqpiTMTDSWSLEVMSQVQVLLYFLQL 1252
Cdd:cd04387   161 LRPSEKESKIPTN-----TMTDSWSLEVMSQVQVLLYFLQL 196
PH_BCR_vertebrate cd13367
Breakpoint Cluster Region-related pleckstrin homology (PH) domain; The BCR gene is one of the ...
684-877 6.08e-125

Breakpoint Cluster Region-related pleckstrin homology (PH) domain; The BCR gene is one of the two genes in the BCR-ABL complex, which is associated with the Philadelphia chromosome, a product of a reciprocal translocation between chromosomes 22 and 9. BCR is a GTPase-activating protein (GAP) for RAC1 (primarily) and CDC42. The Dbl region of BCR has the most RhoGEF activity for Cdc42, and less activity towards Rac and Rho. Since BCR possesses both GAP and GEF activities, it may function to temporally regulate the activity of these GTPases. It also displays serine/threonine kinase activity. The BCR protein contains multiple domains including an N-terminal kinase domain, a RhoGEF domain, a PH domain, a C1 domain, a C2 domain, and a C-terminal RhoGAP domain. This hierarchy is composed of vertebrate BCRs. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270173  Cd Length: 194  Bit Score: 383.20  E-value: 6.08e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366  684 FLSSINEEITPRRQSMTVKKGEHRQLLKDSFMVELVEGARKLRHVFLFTDLLLCTKLKKQSGGKTQQYDCKWYIPLTDLS 763
Cdd:cd13367     1 FLSSINEEITPRRQSMTVKKGEHRQLLKDSFMVELVEGARKLRHVFLFTDLLLCAKLKKQIGGKSQQYDCKWYIPLADLS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366  764 FQMVDELEAVPNIPLVPDEELDALKIKISQIKNDIQREKRANKGSKATERLKKKLSEQESLLLLMSPSMAFRVHSRNGKS 843
Cdd:cd13367    81 FQTVDESEAVPNIPLIPDEEIDALKVKISQIKSDIQREKRANKGGKVLERLRKKLSEQESLLLLMSPSMAFRVHNRNGKS 160
                         170       180       190
                  ....*....|....*....|....*....|....
gi 143811366  844 YTFLISSDYERAEWRENIREQQKKCFRSFSLTSV 877
Cdd:cd13367   161 YTFLISSDYERAEWRENIREQQKKCFKSFSLTSL 194
PH_ABR cd13366
Active breakpoint cluster region-related protein pleckstrin homology (PH) domain; The ABR ...
684-867 1.19e-82

Active breakpoint cluster region-related protein pleckstrin homology (PH) domain; The ABR protein contains multiple domains including a RhoGEF domain, a PH domain, a C1 domain, a C2 domain, and a C-terminal RhoGAP domain. It is related to a slightly larger protein, BCR, which is structurally similar, but has an additional N-terminal kinase domain. ABR has GAP activity for both Rac and Cdc42. It promotes the exchange of RAC or CDC42-bound GDP by GTP, thereby activating them. It is highly enriched in the brain and found to a lesser extent in heart, lung and muscle. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270172  Cd Length: 185  Bit Score: 268.03  E-value: 1.19e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366  684 FLSSINEEITPRRQSMTVKKGEHRQLLKDSFMVELVEGARKLRHVFLFTDLLLCTKLKKQSGGKTQQYDCKWYIPLTDLS 763
Cdd:cd13366     1 FLSSINEDIDPRRTAVTTPKGETRQLVKDGFLVEVSEGSRKLRHVFLFTDLLLCAKLKKTAVGKHQQYDCKWYIPLADLV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366  764 FQMVDELEAVPNIPLVPDEELDALKIKISQIKNDIQREKRANKG-SKATERLKKKLSEQESLLLLMSPSMAFRVHSRNGK 842
Cdd:cd13366    81 FPSPEESESLPQVHTLPDHEIEEMKMKISAIKSEIQKEKKNKKGqSRAIERLKKKMFENESWLLLNSPTIPFRIHNKNGK 160
                         170       180
                  ....*....|....*....|....*
gi 143811366  843 SYTFLISSDYERAEWRENIREQQKK 867
Cdd:cd13366   161 SYLFLLSSDYERSEWREAIQKLQKK 185
PH_BCR-related cd01228
Breakpoint Cluster Region-related pleckstrin homology (PH) domain; The BCR gene is one of the ...
707-867 5.28e-74

Breakpoint Cluster Region-related pleckstrin homology (PH) domain; The BCR gene is one of the two genes in the BCR-ABL complex, which is associated with the Philadelphia chromosome, a product of a reciprocal translocation between chromosomes 22 and 9. BCR is a GTPase-activating protein (GAP) for RAC1 (primarily) and CDC42. The Dbl region of BCR has the most RhoGEF activity for Cdc42, and less activity towards Rac and Rho. Since BCR possesses both GAP and GEF activities, it may function to temporally regulate the activity of these GTPases. It also displays serine/threonine kinase activity. The BCR protein contains multiple domains including an N-terminal kinase domain, a RhoGEF domain, a PH domain, a C1 domain, a C2 domain, and a C-terminal RhoGAP domain. ABR, a related smaller protein, is structurally similar to BCR, but lacks the N-terminal kinase domain and has GAP activity for both Rac and Cdc42. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 269935  Cd Length: 166  Bit Score: 242.64  E-value: 5.28e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366  707 RQLLKDSFMVELVEGARKLRHVFLFTDLLLCTKLKKQSGGKTQQYDCKWYIPLTDLSFQMVDELEAVPNIPLVPDEELDA 786
Cdd:cd01228     1 RQLVKDGFLVELSEGSRKLRHLFLFTDVLLCAKLKSAGRGFQGQYECKWYIPLRDLSLHPKDESEASPIVPVTSDKELEV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366  787 LKIKISQIK-----NDIQREKRANKGSKATERLKKKLSEQESLLLLMSPSMAFRVHSRNGKSYTFLISSDYERAEWRENI 861
Cdd:cd01228    81 LKSKIAELKkqirdDDAQRKKASSSGSKAIEKLRKKLAEQEAALLLASPSLPLRLYHRNGKTYTFLLSSDYERSEWKEAI 160

                  ....*.
gi 143811366  862 REQQKK 867
Cdd:cd01228   161 LKLQKK 166
C2_ABR cd08686
C2 domain in the Active BCR (Breakpoint cluster region) Related protein; The ABR protein is ...
913-1033 3.13e-70

C2 domain in the Active BCR (Breakpoint cluster region) Related protein; The ABR protein is similar to the breakpoint cluster region protein. It has homology to guanine nucleotide exchange proteins and GTPase-activating proteins (GAPs). ABR is expressed primarily in the brain, but also includes non-neuronal tissues such as the heart. It has been associated with human diseases such as Miller-Dieker syndrome in which mental retardation and malformations of the heart are present. ABR contains a RhoGEF domain and a PH-like domain upstream of its C2 domain and a RhoGAP domain downstream of this domain. A few members also contain a Bcr-Abl oncoprotein oligomerization domain at the very N-terminal end. Splice variants of ABR have been identified. ABR is found in a wide variety of organisms including chimpanzee, dog, mouse, rat, fruit fly, and mosquito. The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


Pssm-ID: 176068  Cd Length: 118  Bit Score: 230.09  E-value: 3.13e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366  913 LNVIVHSATGFKQSSNLYCTLEVDSFGYFVNKAKTRVYRDTAEPNWNEEFEIELEGSQTLRILCYEKCYNKTKIpkeDGE 992
Cdd:cd08686     1 LNVIVHSAQGFKQSANLYCTLEVDSFGYFVKKAKTRVCRDTTEPNWNEEFEIELEGSQTLRILCYEKCYSKVKL---DGE 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 143811366  993 STDRLMGKGQVQLDPQALQDRDWQRTVIAMNGIEVKLSVKF 1033
Cdd:cd08686    78 GTDAIMGKGQIQLDPQSLQTKKWQEKVISMNGITVNLSIKF 118
RhoGAP smart00324
GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac ...
1067-1230 5.84e-62

GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases. etter domain limits and outliers.


Pssm-ID: 214618  Cd Length: 174  Bit Score: 209.04  E-value: 5.84e-62
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366   1067 VPYIVRQCVEEIERRGMEEVGIYRVSGVATDIQALKAAFDvNNKDVSVMMSEMDVNAIAGTLKLYFRELPEPLFTDEFYP 1146
Cdd:smart00324    3 IPIIVEKCIEYLEKRGLDTEGIYRVSGSKSRVKELRDAFD-SGPDPDLDLSEYDVHDVAGLLKLFLRELPEPLITYELYE 81
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366   1147 NFAEGIALSDPVAKESCMLNLLLSLPEANLLTFLFLLDHLKRVAEKEAVNKMSLHNLATVFGPTLLRPSEKESKLPANPS 1226
Cdd:smart00324   82 EFIEAAKLEDETERLRALRELLSLLPPANRATLRYLLAHLNRVAEHSEENKMTARNLAIVFGPTLLRPPDGEVASLKDIR 161

                    ....
gi 143811366   1227 QPIT 1230
Cdd:smart00324  162 HQNT 165
RhoGAP pfam00620
RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.
1068-1219 7.52e-60

RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.


Pssm-ID: 425782  Cd Length: 152  Bit Score: 202.03  E-value: 7.52e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366  1068 PYIVRQCVEEIERRGMEEVGIYRVSGVATDIQALKAAFDvNNKDVSVMMSEMDVNAIAGTLKLYFRELPEPLFTDEFYPN 1147
Cdd:pfam00620    1 PLIVRKCVEYLEKRGLDTEGIFRVSGSASRIKELREAFD-SGEDVDLDLEEEDVHDVASLLKLFLRELPEPLLTFELYEE 79
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 143811366  1148 FAEGIALSDPVAKESCMLNLLLSLPEANLLTFLFLLDHLKRVAEKEAVNKMSLHNLATVFGPTLLRPSEKES 1219
Cdd:pfam00620   80 FIEAAKSEDEEERIEALRELLEKLPPANRDTLRYLLAHLNRVAQNSDVNKMNAHNLAIVFGPTLLRPPDSES 151
RhoGAP cd00159
RhoGAP: GTPase-activator protein (GAP) for Rho-like GTPases; GAPs towards Rho/Rac/Cdc42-like ...
1068-1221 3.25e-52

RhoGAP: GTPase-activator protein (GAP) for Rho-like GTPases; GAPs towards Rho/Rac/Cdc42-like small GTPases. Small GTPases (G proteins) cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when bound to GDP. The Rho family of small G proteins, which includes Cdc42Hs, activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. G proteins generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude. The RhoGAPs are one of the major classes of regulators of Rho G proteins.


Pssm-ID: 238090  Cd Length: 169  Bit Score: 180.96  E-value: 3.25e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366 1068 PYIVRQCVEEIERRGMEEVGIYRVSGVATDIQALKAAFDVNNKDVsvMMSEMDVNAIAGTLKLYFRELPEPLFTDEFYPN 1147
Cdd:cd00159     1 PLIIEKCIEYLEKNGLNTEGIFRVSGSASKIEELKKKFDRGEDID--DLEDYDVHDVASLLKLYLRELPEPLIPFELYDE 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 143811366 1148 FAEGIALSDPVAKESCMLNLLLSLPEANLLTFLFLLDHLKRVAEKEAVNKMSLHNLATVFGPTLLRPSEKESKL 1221
Cdd:cd00159    79 FIELAKIEDEEERIEALKELLKSLPPENRDLLKYLLKLLHKISQNSEVNKMTASNLAIVFAPTLLRPPDSDDEL 152
RhoGAP_ARHGAP27_15_12_9 cd04403
RhoGAP_ARHGAP27_15_12_9: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
1052-1224 3.42e-50

RhoGAP_ARHGAP27_15_12_9: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ARHGAP27 (also called CAMGAP1), ARHGAP15, 12 and 9-like proteins; This subgroup of ARHGAPs are multidomain proteins that contain RhoGAP, PH, SH3 and WW domains. Most members that are studied show GAP activity towards Rac1, some additionally show activity towards Cdc42. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239868 [Multi-domain]  Cd Length: 187  Bit Score: 175.66  E-value: 3.42e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366 1052 FGVKIAVVTKRERSKVPYIVRQCVEEIERRGMEEVGIYRVSGVATDIQALKAAFDVNNKDVSVMMSEMDVNAIAGTLKLY 1131
Cdd:cd04403     1 FGCHLEALCQRENSTVPKFVRLCIEAVEKRGLDVDGIYRVSGNLAVIQKLRFAVDHDEKLDLDDSKWEDIHVITGALKLF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366 1132 FRELPEPLFTDEFYPNFAEGIALSDPVAKESCMLNLLLSLPEANLLTFLFLLDHLKRVAEKEAVNKMSLHNLATVFGPTL 1211
Cdd:cd04403    81 FRELPEPLFPYSLFNDFVAAIKLSDYEQRVSAVKDLIKSLPKPNHDTLKMLFRHLCRVIEHGEKNRMTTQNLAIVFGPTL 160
                         170
                  ....*....|...
gi 143811366 1212 LRPSEKESKLPAN 1224
Cdd:cd04403   161 LRPEQETGNIAVH 173
RhoGAP_fRGD1 cd04398
RhoGAP_fRGD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
1052-1212 7.79e-49

RhoGAP_fRGD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of fungal RGD1-like proteins. Yeast Rgd1 is a GAP protein for Rho3 and Rho4 and plays a role in low-pH response. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239863  Cd Length: 192  Bit Score: 172.20  E-value: 7.79e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366 1052 FGVKIAVVTKRERSKVPYIVRQCVEEIERRGMEEVGIYRVSGVATDIQALKAAFDVNNKDVSVMMS---EMDVNAIAGTL 1128
Cdd:cd04398     1 FGVPLEDLILREGDNVPNIVYQCIQAIENFGLNLEGIYRLSGNVSRVNKLKELFDKDPLNVLLISPedyESDIHSVASLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366 1129 KLYFRELPEPLFTDEFYPNFAEGIALSDPVAKESCMLNLLLSLPEANLLTFLFLLDHLKRVAEKEAVNKMSLHNLATVFG 1208
Cdd:cd04398    81 KLFFRELPEPLLTKALSREFIEAAKIEDESRRRDALHGLINDLPDANYATLRALMFHLARIKEHESVNRMSVNNLAIIWG 160

                  ....
gi 143811366 1209 PTLL 1212
Cdd:cd04398   161 PTLM 164
RhoGAP_chimaerin cd04372
RhoGAP_chimaerin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
1052-1216 1.11e-48

RhoGAP_chimaerin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of chimaerins. Chimaerins are a family of phorbolester- and diacylglycerol-responsive GAPs specific for the Rho-like GTPase Rac. Chimaerins exist in two alternative splice forms that each contain a C-terminal GAP domain, and a central C1 domain which binds phorbol esters, inducing a conformational change that activates the protein; one splice form is lacking the N-terminal Src homology-2 (SH2) domain. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239837  Cd Length: 194  Bit Score: 171.55  E-value: 1.11e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366 1052 FGVKIAVVTKRERSKVPYIVRQCVEEIERRGMEEVGIYRVSGVATDIQALKAAFDVNNK--DVSVMMSEmDVNAIAGTLK 1129
Cdd:cd04372     1 YGCDLTTLVKAHNTQRPMVVDMCIREIEARGLQSEGLYRVSGFAEEIEDVKMAFDRDGEkaDISATVYP-DINVITGALK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366 1130 LYFRELPEPLFTDEFYPNFAEGIALSDPVAKESCMLNLLLSLPEANLLTFLFLLDHLKRVAEKEAVNKMSLHNLATVFGP 1209
Cdd:cd04372    80 LYFRDLPIPVITYDTYPKFIDAAKISNPDERLEAVHEALMLLPPAHYETLRYLMEHLKRVTLHEKDNKMNAENLGIVFGP 159

                  ....*..
gi 143811366 1210 TLLRPSE 1216
Cdd:cd04372   160 TLMRPPE 166
RhoGAP_ARHGAP21 cd04395
RhoGAP_ARHGAP21: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
1051-1216 2.20e-41

RhoGAP_ARHGAP21: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ArhGAP21-like proteins. ArhGAP21 is a multi-domain protein, containing RhoGAP, PH and PDZ domains, and is believed to play a role in the organization of the cell-cell junction complex. It has been shown to function as a GAP of Cdc42 and RhoA, and to interact with alpha-catenin and Arf6. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239860  Cd Length: 196  Bit Score: 150.63  E-value: 2.20e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366 1051 VFGVKIA-VVTKRERSKVPYIVRQCVEEIERRGMEEVGIYRVSGVATDIQALKAafDVNNKDVSVMMSE---MDVNAIAG 1126
Cdd:cd04395     1 TFGVPLDdCPPSSENPYVPLIVEVCCNIVEARGLETVGIYRVPGNNAAISALQE--ELNRGGFDIDLQDprwRDVNVVSS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366 1127 TLKLYFRELPEPLFTDEFYPNFAEGIALSDPVAKESCMLNLLLSLPEANLLTFLFLLDHLKRVAEKEAVNKMSLHNLATV 1206
Cdd:cd04395    79 LLKSFFRKLPEPLFTNELYPDFIEANRIEDPVERLKELRRLIHSLPDHHYETLKHLIRHLKTVADNSEVNKMEPRNLAIV 158
                         170
                  ....*....|
gi 143811366 1207 FGPTLLRPSE 1216
Cdd:cd04395   159 FGPTLVRTSD 168
RhoGEF cd00160
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous ...
499-689 1.88e-40

Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous (DH) domain. It appears that PH domains invariably occur C-terminal to RhoGEF/DH domains.


Pssm-ID: 238091 [Multi-domain]  Cd Length: 181  Bit Score: 147.44  E-value: 1.88e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366  499 RKWVLSGILASEETYLSHLEALLLP-MKPLKAaattSQPVLTSQQIETIFFKVPELYEIHKEFYDGLFPRVQQW-SHQQR 576
Cdd:cd00160     1 RQEVIKELLQTERNYVRDLKLLVEVfLKPLDK----ELLPLSPEEVELLFGNIEEIYEFHRIFLKSLEERVEEWdKSGPR 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366  577 VGDLFQKLASQLGVYRAFVDNYGVAMEMAEKCCQANAQFAEISENLRARSNKdakdpttkNSLETLLYKPVDRVTRSTLV 656
Cdd:cd00160    77 IGDVFLKLAPFFKIYSEYCSNHPDALELLKKLKKFNKFFQEFLEKAESECGR--------LKLESLLLKPVQRLTKYPLL 148
                         170       180       190
                  ....*....|....*....|....*....|...
gi 143811366  657 LHDLLKHTPASHPDHPLLQDALRISQNFLSSIN 689
Cdd:cd00160   149 LKELLKHTPDGHEDREDLKKALEAIKEVASQVN 181
Bcr-Abl_Oligo pfam09036
Bcr-Abl oncoprotein oligomerization domain; The Bcr-Abl oncoprotein oligomerization domain ...
3-75 2.39e-40

Bcr-Abl oncoprotein oligomerization domain; The Bcr-Abl oncoprotein oligomerization domain consists of a short N-terminal helix (alpha-1), a flexible loop and a long C-terminal helix (alpha-2). Together these form an N-shaped structure, with the loop allowing the two helices to assume a parallel orientation. The monomeric domains associate into a dimer through the formation of an antiparallel coiled coil between the alpha-2 helices and domain swapping of two alpha-1 helices, where one alpha-1 helix swings back and packs against the alpha-2 helix from the second monomer. Two dimers then associate into a tetramer. The oligomerization domain is essential for the oncogenicity of the Bcr-Abl protein.


Pssm-ID: 430380  Cd Length: 73  Bit Score: 143.08  E-value: 2.39e-40
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 143811366     3 DPVGFAEAWKAQFPDSEPPRMELRSVGDIEQELERCKASIRRLEQEVNQERFRMIYLQTLLAKEKKSYDRQRW 75
Cdd:pfam09036    1 EPAGFERHWRAEFPEGQVPKMELGSVEDIEQELERCKASLRRLQQELNEEKFKVIYLQTLLARERKSYDRQRW 73
RhoGEF pfam00621
RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called ...
502-689 4.42e-40

RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called Dbl-homologous (DH) domain. It appears that pfam00169 domains invariably occur C-terminal to RhoGEF/DH domains.


Pssm-ID: 425783 [Multi-domain]  Cd Length: 176  Bit Score: 146.29  E-value: 4.42e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366   502 VLSGILASEETYLSHLEALL-----LPMKPLKaaattsqpvLTSQQIETIFFKVPELYEIHKEFYdgLFPRVQQWSHQQR 576
Cdd:pfam00621    1 VIKELLQTERSYVRDLEILVevflpPNSKPLS---------ESEEEIKTIFSNIEEIYELHRQLL--LEELLKEWISIQR 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366   577 VGDLFQKLASQLGVYRAFVDNYGVAMEMAEKCCQANAQFAEISENLRARSNkdakdpTTKNSLETLLYKPVDRVTRSTLV 656
Cdd:pfam00621   70 IGDIFLKFAPGFKVYSTYCSNYPKALELLKKLLKKNPKFRAFLEELEANPE------CRGLDLNSFLIKPVQRIPRYPLL 143
                          170       180       190
                   ....*....|....*....|....*....|...
gi 143811366   657 LHDLLKHTPASHPDHPLLQDALRISQNFLSSIN 689
Cdd:pfam00621  144 LKELLKHTPPDHPDYEDLKKALEAIKEVAKQIN 176
RhoGEF smart00325
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange ...
502-690 4.05e-39

Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called Dbl-homologous (DH) domain. It appears that PH domains invariably occur C-terminal to RhoGEF/DH domains. Improved coverage.


Pssm-ID: 214619 [Multi-domain]  Cd Length: 180  Bit Score: 143.60  E-value: 4.05e-39
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366    502 VLSGILASEETYLSHLEALL-LPMKPLKAaattSQPVLTSQQIETIFFKVPELYEIHKEFYDGLFPRVQQWSH-QQRVGD 579
Cdd:smart00325    1 VLKELLQTERNYVRDLKLLVeVFLKPLKK----ELKLLSPNELETLFGNIEEIYEFHRDFLDELEERIEEWDDsVERIGD 76
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366    580 LFQKLASQLGVYRAFVDNYGVAMEMAEKCcQANAQFAEISENLRARSNKDAKDpttknsLETLLYKPVDRVTRSTLVLHD 659
Cdd:smart00325   77 VFLKLEEFFKIYSEYCSNHPDALELLKKL-KKNPRFQKFLKEIESSPQCRRLT------LESLLLKPVQRLTKYPLLLKE 149
                           170       180       190
                    ....*....|....*....|....*....|.
gi 143811366    660 LLKHTPASHPDHPLLQDALRISQNFLSSINE 690
Cdd:smart00325  150 LLKHTPEDHEDREDLKKALKAIKELANQVNE 180
RhoGAP_SYD1 cd04379
RhoGAP_SYD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
1052-1252 2.64e-37

RhoGAP_SYD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in SYD-1_like proteins. Syd-1, first identified and best studied in C.elegans, has been shown to play an important role in neuronal development by specifying axonal properties. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239844  Cd Length: 207  Bit Score: 139.52  E-value: 2.64e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366 1052 FGVKIAVVTKRERSK--VPYIVRQCVEEIERRGMEEVGIYRVSGVATDIQALKAAFDVNNKDVSVMMSEM-DVNAIAGTL 1128
Cdd:cd04379     1 FGVPLSRLVEREGESrdVPIVLQKCVQEIERRGLDVIGLYRLCGSAAKKKELRDAFERNSAAVELSEELYpDINVITGVL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366 1129 KLYFRELPEPLFTDEFYPNFAEGIAL---SDPVAKESCMLNLLLSLPEANLLTFLFLLDHLKRVAEKEAVNKMSLHNLAT 1205
Cdd:cd04379    81 KDYLRELPEPLITPQLYEMVLEALAValpNDVQTNTHLTLSIIDCLPLSAKATLLLLLDHLSLVLSNSERNKMTPQNLAV 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 143811366 1206 VFGPTLLRPSEKESKLPANPSQpiTMTDSWSLEVMSQVQVLLYFLQL 1252
Cdd:cd04379   161 CFGPVLMFCSQEFSRYGISPTS--KMAAVSTVDFKQHIEVLHYLLQI 205
RhoGAP_GMIP_PARG1 cd04378
RhoGAP_GMIP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
1052-1224 3.59e-37

RhoGAP_GMIP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of GMIP (Gem interacting protein) and PARG1 (PTPL1-associated RhoGAP1). GMIP plays important roles in neurite growth and axonal guidance, and interacts with Gem, a member of the RGK subfamily of the Ras small GTPase superfamily, through the N-terminal half of the protein. GMIP contains a C-terminal RhoGAP domain. GMIP inhibits RhoA function, but is inactive towards Rac1 and Cdc41. PARG1 interacts with Rap2, also a member of the Ras small GTPase superfamily whose exact function is unknown, and shows strong preference for Rho. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239843  Cd Length: 203  Bit Score: 139.09  E-value: 3.59e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366 1052 FGVKIAVVTKRERSKVPYIVRQCVEEIERRGMEEVGIYRVSGVATDIQALKAAFDvNNKDVsVMMSEMDVNAIAGTLKLY 1131
Cdd:cd04378     1 FGVDFSQVPRDFPDEVPFIIKKCTSEIENRALGVQGIYRVSGSKARVEKLCQAFE-NGKDL-VELSELSPHDISSVLKLF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366 1132 FRELPEPLFTDEFYPNFaegIALS--------DPVAKESC---------MLNLLLSLPEANLLTFLFLLDHLKRVAEKEA 1194
Cdd:cd04378    79 LRQLPEPLILFRLYNDF---IALAkeiqrdteEDKAPNTPievnriirkLKDLLRQLPASNYNTLQHLIAHLYRVAEQFE 155
                         170       180       190
                  ....*....|....*....|....*....|
gi 143811366 1195 VNKMSLHNLATVFGPTLLRPSEKESKLPAN 1224
Cdd:cd04378   156 ENKMSPNNLGIVFGPTLIRPRPGDADVSLS 185
RhoGAP_MgcRacGAP cd04382
RhoGAP_MgcRacGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
1067-1246 4.25e-36

RhoGAP_MgcRacGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in MgcRacGAP proteins. MgcRacGAP plays an important dual role in cytokinesis: i) it is part of centralspindlin-complex, together with the mitotic kinesin MKLP1, which is critical for the structure of the central spindle by promoting microtuble bundling. ii) after phosphorylation by aurora B MgcRacGAP becomes an effective regulator of RhoA and plays an important role in the assembly of the contractile ring and the initiation of cytokinesis. MgcRacGAP-like proteins contain a N-terminal C1-like domain, and a C-terminal RhoGAP domain. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239847  Cd Length: 193  Bit Score: 135.50  E-value: 4.25e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366 1067 VPYIVRQCVEEIERRGMEEVGIYRVSGVATDIQALKAAFdVNNKDVSvMMSEMDVNAIAGTLKLYFRELPEPLFTDEFYP 1146
Cdd:cd04382    17 IPALIVHCVNEIEARGLTEEGLYRVSGSEREVKALKEKF-LRGKTVP-NLSKVDIHVICGCLKDFLRSLKEPLITFALWK 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366 1147 NFAEGIALSDPVAKESCMLNLLLSLPEANLLTFLFLLDHLKRVAEKEAvNKMSLHNLATVFGPTLLrpsekeSKLPANPS 1226
Cdd:cd04382    95 EFMEAAEILDEDNSRAALYQAISELPQPNRDTLAFLILHLQRVAQSPE-CKMDINNLARVFGPTIV------GYSVPNPD 167
                         170       180
                  ....*....|....*....|
gi 143811366 1227 QPITMTDswsleVMSQVQVL 1246
Cdd:cd04382   168 PMTILQD-----TVRQPRVV 182
RhoGAP_nadrin cd04386
RhoGAP_nadrin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
1051-1219 3.61e-34

RhoGAP_nadrin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of Nadrin-like proteins. Nadrin, also named Rich-1, has been shown to be involved in the regulation of Ca2+-dependent exocytosis in neurons and recently has been implicated in tight junction maintenance in mammalian epithelium. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239851  Cd Length: 203  Bit Score: 130.27  E-value: 3.61e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366 1051 VFGVKIAVVTKRERSKVPYIVRQCVEEIERRGMEEVGIYRVSGVATDIQALKAAFDVNNKDVSVMMSEMDVNAIAGTLKL 1130
Cdd:cd04386     4 VFGTPLEEHLKRTGREIALPIEACVMCLLETGMNEEGLFRVGGGASKLKRLKAALDAGTFSLPLDEFYSDPHAVASALKS 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366 1131 YFRELPEPLFTDEFYPNFAEGIALSDPVAKESCMLNLLLSLPEANLLTFLFLLDHLKRVAEKEAVNKMSLHNLATVFGPT 1210
Cdd:cd04386    84 YLRELPDPLLTYNLYEDWVQAANKPDEDERLQAIWRILNKLPRENRDNLRYLIKFLSKLAQKSDENKMSPSNIAIVLAPN 163

                  ....*....
gi 143811366 1211 LLRPSEKES 1219
Cdd:cd04386   164 LLWAKNEGS 172
RhoGAP_CdGAP cd04384
RhoGAP_CdGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
1051-1219 1.52e-33

RhoGAP_CdGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of CdGAP-like proteins; CdGAP contains an N-terminal RhoGAP domain and a C-terminal proline-rich region, and it is active on both Cdc42 and Rac1 but not RhoA. CdGAP is recruited to focal adhesions via the interaction with the scaffold protein actopaxin (alpha-parvin). Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239849 [Multi-domain]  Cd Length: 195  Bit Score: 128.39  E-value: 1.52e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366 1051 VFGVKIAVVTKRERSKVPYIVRQCVEEIERRGMEEvGIYRVSGVATDIQALKAAFDVNN-KDVSVMMSEMDVNAIAGTLK 1129
Cdd:cd04384     2 VFGCDLTEHLLNSGQDVPQVLKSCTEFIEKHGIVD-GIYRLSGIASNIQRLRHEFDSEQiPDLTKDVYIQDIHSVSSLCK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366 1130 LYFRELPEPLFTDEFYPNFAEGIALSDPVAKESCMLNLLLSLPEANLLTFLFLLDHLKRVAEKEAVNKMSLHNLATVFGP 1209
Cdd:cd04384    81 LYFRELPNPLLTYQLYEKFSEAVSAASDEERLEKIHDVIQQLPPPHYRTLEFLMRHLSRLAKYCSITNMHAKNLAIVWAP 160
                         170
                  ....*....|
gi 143811366 1210 TLLRPSEKES 1219
Cdd:cd04384   161 NLLRSKQIES 170
RhoGAP_myosin_IX cd04377
RhoGAP_myosin_IX: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
1052-1213 6.88e-33

RhoGAP_myosin_IX: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in class IX myosins. Class IX myosins contain a characteristic head domain, a neck domain, a tail domain which contains a C6H2-zinc binding motif and a RhoGAP domain. Class IX myosins are single-headed, processive myosins that are partly cytoplasmic, and partly associated with membranes and the actin cytoskeleton. Class IX myosins are implicated in the regulation of neuronal morphogenesis and function of sensory systems, like the inner ear. There are two major isoforms, myosin IXA and IXB with several splice variants, which are both expressed in developing neurons. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239842  Cd Length: 186  Bit Score: 126.01  E-value: 6.88e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366 1052 FGVKIAVVTKrERSKVPYIVRQCVEEIERRGMEEVGIYRVSGVATDIQALKAAFDVNNKdvSVMMSEMDVNAIAGTLKLY 1131
Cdd:cd04377     1 FGVSLSSLTS-EDRSVPLVLEKLLEHIEMHGLYTEGIYRKSGSANKIKELRQGLDTDPD--SVNLEDYPIHVITSVLKQW 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366 1132 FRELPEPLFTDEFYPNFAEGIALSDPVAKESCMLNLLLSLPEANLLTFLFLLDHLKRVAEKEAVNKMSLHNLATVFGPTL 1211
Cdd:cd04377    78 LRELPEPLMTFELYENFLRAMELEEKQERVRALYSVLEQLPRANLNTLERLIFHLVRVALQEEVNRMSANALAIVFAPCI 157

                  ..
gi 143811366 1212 LR 1213
Cdd:cd04377   158 LR 159
PH_BCR_arthropod cd13368
Breakpoint Cluster Region-related pleckstrin homology (PH) domain; The BCR gene is one of the ...
707-868 7.77e-33

Breakpoint Cluster Region-related pleckstrin homology (PH) domain; The BCR gene is one of the two genes in the BCR-ABL complex, which is associated with the Philadelphia chromosome, a product of a reciprocal translocation between chromosomes 22 and 9. BCR is a GTPase-activating protein (GAP) for RAC1 (primarily) and CDC42. The Dbl region of BCR has the most RhoGEF activity for Cdc42, and less activity towards Rac and Rho. Since BCR possesses both GAP and GEF activities, it may function to temporally regulate the activity of these GTPases. It also displays serine/threonine kinase activity. The BCR protein contains multiple domains including an N-terminal kinase domain, a RhoGEF domain, a PH domain, a C1 domain, a C2 domain, and a C-terminal RhoGAP domain. This hierarchy is composed of arthropod BCRs. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270174  Cd Length: 180  Bit Score: 125.72  E-value: 7.77e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366  707 RQLLKDSFMVELVEGARKLRHVFLFTDLLLCTKLKKqSGGKTQQYDCKWYIPLTDLSfqMVDELEAVPNIPLVPDEEldA 786
Cdd:cd13368    22 RRLVKNSFIVELADGHRKLRHLFLFNDVIACAKYKS-SGRTRITFELKWFIPLNDVT--ILEEEAPAPKESSPPNIE--Q 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366  787 LKIKISQIKNDIQREKRANkgSKATERLKKKLSEQESLLLLMSPSMAFRVHSRNGKSYTFLISSDYERAEWRENIREQQK 866
Cdd:cd13368    97 LKSNACQVRDQLADRSRAS--TSGSDKIRKKLADLEAQLVLASPNLVFRIGNKNNKTYTFFLSSEFERTQWIEAILTLQQ 174

                  ..
gi 143811366  867 KC 868
Cdd:cd13368   175 TC 176
RhoGAP_Graf cd04374
RhoGAP_Graf: GTPase-activator protein (GAP) domain for Rho-like GTPases found in GRAF (GTPase ...
1070-1216 1.30e-32

RhoGAP_Graf: GTPase-activator protein (GAP) domain for Rho-like GTPases found in GRAF (GTPase regulator associated with focal adhesion kinase); Graf is a multi-domain protein, containing SH3 and PH domains, that binds focal adhesion kinase and influences cytoskeletal changes mediated by Rho proteins. Graf exhibits GAP activity toward RhoA and Cdc42, but only weakly activates Rac1. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239839  Cd Length: 203  Bit Score: 125.97  E-value: 1.30e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366 1070 IVRQCVEEIERRGMEEVGIYRVSGVATDIQALKAA-FDVNNK---DVSVMMSEMDVNAIAGTLKLYFRELPEPLFTDEFY 1145
Cdd:cd04374    31 FVRKCIEAVETRGINEQGLYRVVGVNSKVQKLLSLgLDPKTStpgDVDLDNSEWEIKTITSALKTYLRNLPEPLMTYELH 110
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 143811366 1146 PNFAEGIALSDPVAKESCMLNLLLSLPEANLLTFLFLLDHLKRVAEKEAVNKMSLHNLATVFGPTLLRPSE 1216
Cdd:cd04374   111 NDFINAAKSENLESRVNAIHSLVHKLPEKNREMLELLIKHLTNVSDHSKKNLMTVSNLGVVFGPTLLRPQE 181
RhoGap_RalBP1 cd04381
RhoGap_RalBP1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
1052-1211 1.95e-31

RhoGap_RalBP1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in RalBP1 proteins, also known as RLIP, RLIP76 or cytocentrin. RalBP1 plays an important role in endocytosis during interphase. During mitosis, RalBP1 transiently associates with the centromere and has been shown to play an essential role in the proper assembly of the mitotic apparatus. RalBP1 is an effector of the Ral GTPase which itself is an effector of Ras. RalBP1 contains a RhoGAP domain, which shows weak activity towards Rac1 and Cdc42, but not towards Ral, and a Ral effector domain binding motif. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239846 [Multi-domain]  Cd Length: 182  Bit Score: 121.77  E-value: 1.95e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366 1052 FGVKIAVVTKRERS----KVPYIVRQCVEEIERRGMEEVGIYRVSGVATDIQALKAAFdvnNKDVSVMMSEMDVNAIAGT 1127
Cdd:cd04381     1 FGASLSLAVERSRChdgiDLPLVFRECIDYVEKHGMKCEGIYKVSGIKSKVDELKAAY---NRRESPNLEEYEPPTVASL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366 1128 LKLYFRELPEPLFTDEFYPNFAEGIALSDPVAKESCMLNLLLSLPEANLLTFLFLLDHLKRVAEKEAVNKMSLHNLATVF 1207
Cdd:cd04381    78 LKQYLRELPEPLLTKELMPRFEEACGRPTEAEREQELQRLLKELPECNRLLLAWLIVHMDHVIAQELETKMNIQNISIVL 157

                  ....
gi 143811366 1208 GPTL 1211
Cdd:cd04381   158 SPTV 161
RhoGAP_PARG1 cd04409
RhoGAP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
1052-1219 2.98e-30

RhoGAP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of PARG1 (PTPL1-associated RhoGAP1). PARG1 was originally cloned as an interaction partner of PTPL1, an intracellular protein-tyrosine phosphatase. PARG1 interacts with Rap2, also a member of the Ras small GTPase superfamily whose exact function is unknown, and shows strong preference for Rho. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239874  Cd Length: 211  Bit Score: 119.53  E-value: 2.98e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366 1052 FGVKIAVVTKRERSKVPYIVRQCVEEIERRGMEEVGIYRVSGVATDIQALKAAFDvNNKDVsVMMSEMDVNAIAGTLKLY 1131
Cdd:cd04409     1 FGADFAQVAKKSPDGIPFIIKKCTSEIESRALCLKGIYRVNGAKSRVEKLCQAFE-NGKDL-VELSELSPHDISNVLKLY 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366 1132 FRELPEPLFTDEFYPNF-------------AEGIALSDPVAKESC---------MLNLLLSLPEANLLTFLFLLDHLKRV 1189
Cdd:cd04409    79 LRQLPEPLILFRLYNEFiglakesqhvnetQEAKKNSDKKWPNMCtelnrillkSKDLLRQLPAPNYNTLQFLIVHLHRV 158
                         170       180       190
                  ....*....|....*....|....*....|
gi 143811366 1190 AEKEAVNKMSLHNLATVFGPTLLRPSEKES 1219
Cdd:cd04409   159 SEQAEENKMSASNLGIIFGPTLIRPRPTDA 188
RhoGAP_p190 cd04373
RhoGAP_p190: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
1052-1214 1.24e-29

RhoGAP_p190: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of p190-like proteins. p190, also named RhoGAP5, plays a role in neuritogenesis and axon branch stability. p190 shows a preference for Rho, over Rac and Cdc42, and consists of an N-terminal GTPase domain and a C-terminal GAP domain. The central portion of p190 contains important regulatory phosphorylation sites. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239838  Cd Length: 185  Bit Score: 116.79  E-value: 1.24e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366 1052 FGVKIAVVTKRERsKVPYIVRQCVEEIERRGMEEVGIYRVSGVATDIQALKAAFDvnnKDVSVMMSEMD--VNAIAGTLK 1129
Cdd:cd04373     1 FGVPLANVVTSEK-PIPIFLEKCVEFIEATGLETEGIYRVSGNKTHLDSLQKQFD---QDHNLDLVSKDftVNAVAGALK 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366 1130 LYFRELPEPLFTDEFYPNFAEGIALSDPVAKESCMLNLLLSLPEANLLTFLFLLDHLKRVAEKEAVNKMSLHNLATVFGP 1209
Cdd:cd04373    77 SFFSELPDPLIPYSMHLELVEAAKINDREQRLHALKELLKKFPPENFDVFKYVITHLNKVSQNSKVNLMTSENLSICFWP 156

                  ....*
gi 143811366 1210 TLLRP 1214
Cdd:cd04373   157 TLMRP 161
RhoGAP_ARAP cd04385
RhoGAP_ARAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
1064-1219 1.25e-29

RhoGAP_ARAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in ARAPs. ARAPs (also known as centaurin deltas) contain, besides the RhoGAP domain, an Arf GAP, ankyrin repeat ras-associating, and PH domains. Since their ArfGAP activity is PIP3-dependent, ARAPs are considered integration points for phosphoinositide, Arf and Rho signaling. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239850  Cd Length: 184  Bit Score: 116.64  E-value: 1.25e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366 1064 RSKVPYIVRQCVEEIERRGMEEVGIYRVSGVATDIQALKAAFDVNNKDVSVMMSEMDVNAIAGTLKLYFRELPEPLFTDE 1143
Cdd:cd04385    12 DNDIPVIVDKCIDFITQHGLMSEGIYRKNGKNSSVKKLLEAFRKDARSVQLREGEYTVHDVADVLKRFLRDLPDPLLTSE 91
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 143811366 1144 FYPNFAEgiALSDPVAKESCML--NLLLSLPEANLLTFLFLLDHLKRVAEKEAVNKMSLHNLATVFGPTLLRPSEKES 1219
Cdd:cd04385    92 LHAEWIE--AAELENKDERIARykELIRRLPPINRATLKVLIGHLYRVQKHSDENQMSVHNLALVFGPTLFQTDEHSV 167
RhoGAP_GMIP cd04408
RhoGAP_GMIP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of GMIP ...
1052-1214 3.19e-29

RhoGAP_GMIP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of GMIP (Gem interacting protein). GMIP plays important roles in neurite growth and axonal guidance, and interacts with Gem, a member of the RGK subfamily of the Ras small GTPase superfamily, through the N-terminal half of the protein. GMIP contains a C-terminal RhoGAP domain. GMIP inhibits RhoA function, but is inactive towards Rac1 and Cdc41. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239873  Cd Length: 200  Bit Score: 116.07  E-value: 3.19e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366 1052 FGVKIAVVTKRERSKVPYIVRQCVEEIERRGMEEVGIYRVSGVATDIQALKAAFDvNNKDVsVMMSEMDVNAIAGTLKLY 1131
Cdd:cd04408     1 FGVDFSQLPRDFPEEVPFVVVRCTAEIENRALGVQGIYRISGSKARVEKLCQAFE-NGRDL-VDLSGHSPHDITSVLKHF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366 1132 FRELPEPLFTDEFYPNFaegIALS-----DPVAKESC----------MLNLLLSLPEANLLTFLFLLDHLKRVAEKEAVN 1196
Cdd:cd04408    79 LKELPEPVLPFQLYDDF---IALAkelqrDSEKAAESpsiveniirsLKELLGRLPVSNYNTLRHLMAHLYRVAERFEDN 155
                         170
                  ....*....|....*...
gi 143811366 1197 KMSLHNLATVFGPTLLRP 1214
Cdd:cd04408   156 KMSPNNLGIVFGPTLLRP 173
RhoGAP_ARHGAP18 cd04391
RhoGAP_ARHGAP18: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
1051-1231 4.58e-29

RhoGAP_ARHGAP18: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ArhGAP18-like proteins. The function of ArhGAP18 is unknown. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239856  Cd Length: 216  Bit Score: 116.29  E-value: 4.58e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366 1051 VFGVKIAVVTKRER-----SKVPYIVRQCVEEIERRGMEEVGIYRVSGVATDIQALKAAFDVNNKDVSVMMSEMDVNAIA 1125
Cdd:cd04391     1 LFGVPLSTLLERDQkkvpgSKVPLIFQKLINKLEERGLETEGILRIPGSAQRVKFLCQELEAKFYEGTFLWDQVKQHDAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366 1126 GTLKLYFRELPEPLFTDEFYPNFAEGIALSDPVAKeSCMLNLL-LSLPEANLLTFLFLLDHLKRVAEKEAVNKMSLHNLA 1204
Cdd:cd04391    81 SLLKLFIRELPQPLLTVEYLPAFYSVQGLPSKKDQ-LQALNLLvLLLPEANRDTLKALLEFLQKVVDHEEKNKMNLWNVA 159
                         170       180
                  ....*....|....*....|....*..
gi 143811366 1205 TVFGPTLLRPSEKESKLPANPSQPITM 1231
Cdd:cd04391   160 MIMAPNLFPPRGKHSKDNESLQEEVNM 186
RhoGAP_fBEM3 cd04400
RhoGAP_fBEM3: RhoGAP (GTPase-activator [GAP] protein for Rho-like small GTPases) domain of ...
1051-1216 8.36e-29

RhoGAP_fBEM3: RhoGAP (GTPase-activator [GAP] protein for Rho-like small GTPases) domain of fungal BEM3-like proteins. Bem3 is a GAP protein of Cdc42, and is specifically involved in the control of the initial assembly of the septin ring in yeast bud formation. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239865 [Multi-domain]  Cd Length: 190  Bit Score: 114.38  E-value: 8.36e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366 1051 VFGVKIAVVT-----KRERSKVPYIVRQCVEEIERRG--MEEvGIYRVSGVATDIQALKAAFDvNNKDVSVMMS--EMDV 1121
Cdd:cd04400     1 IFGSPLEEAVelsshKYNGRDLPSVVYRCIEYLDKNRaiYEE-GIFRLSGSASVIKQLKERFN-TEYDVDLFSSslYPDV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366 1122 NAIAGTLKLYFRELPEPLFTDEFYPNFaEGIA--LSDPVAKESCMLNLLLSLPEANLLTFLFLLDHLKRVAEKEAVNKMS 1199
Cdd:cd04400    79 HTVAGLLKLYLRELPTLILGGELHNDF-KRLVeeNHDRSQRALELKDLVSQLPQANYDLLYVLFSFLRKIIEHSDVNKMN 157
                         170
                  ....*....|....*..
gi 143811366 1200 LHNLATVFGPTLLRPSE 1216
Cdd:cd04400   158 LRNVCIVFSPTLNIPAG 174
RhoGAP_ARHGAP22_24_25 cd04390
RhoGAP_ARHGAP22_24_25: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
1050-1214 2.83e-28

RhoGAP_ARHGAP22_24_25: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ARHGAP22, 24 and 25-like proteins; longer isoforms of these proteins contain an additional N-terminal pleckstrin homology (PH) domain. ARHGAP25 (KIA0053) has been identified as a GAP for Rac1 and Cdc42. Short isoforms (without the PH domain) of ARHGAP24, called RC-GAP72 and p73RhoGAP, and of ARHGAP22, called p68RacGAP, has been shown to be involved in angiogenesis and endothelial cell capillary formation. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239855 [Multi-domain]  Cd Length: 199  Bit Score: 113.31  E-value: 2.83e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366 1050 GVFGVKIAVVTKRERS----KVPYIVRQCVEEIERRGMEEVGIYRVSGVATDIQALKAAFDVNNKdvSVMMSEMDVNAIA 1125
Cdd:cd04390     1 GVFGQRLEDTVAYERKfgprLVPILVEQCVDFIREHGLKEEGLFRLPGQANLVKQLQDAFDAGER--PSFDSDTDVHTVA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366 1126 GTLKLYFRELPEPLFTDEFYPNF--AEGIALSDPVAKESCMLNLLLSLPEANLLTFLFLLDHLKRVAEKEAVNKMSLHNL 1203
Cdd:cd04390    79 SLLKLYLRELPEPVIPWAQYEDFlsCAQLLSKDEEKGLGELMKQVSILPKVNYNLLSYICRFLDEVQSNSSVNKMSVQNL 158
                         170
                  ....*....|.
gi 143811366 1204 ATVFGPTLLRP 1214
Cdd:cd04390   159 ATVFGPNILRP 169
RhoGAP-p50rhoGAP cd04404
RhoGAP-p50rhoGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
1052-1225 1.12e-27

RhoGAP-p50rhoGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of p50RhoGAP-like proteins; p50RhoGAP, also known as RhoGAP-1, contains a C-terminal RhoGAP domain and an N-terminal Sec14 domain which binds phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3). It is ubiquitously expressed and preferentially active on Cdc42. This subgroup also contains closely related ARHGAP8. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239869  Cd Length: 195  Bit Score: 111.28  E-value: 1.12e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366 1052 FGVKIAVVTKR--ERSKVPYIVRQCVEEIERRGMEEVGIYRVSGVATDIQALKAAF----DVNNKDVSvmmsemDVNAIA 1125
Cdd:cd04404     6 FGVSLQFLKEKnpEQEPIPPVVRETVEYLQAHALTTEGIFRRSANTQVVKEVQQKYnmgePVDFDQYE------DVHLPA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366 1126 GTLKLYFRELPEPLFTDEFYPNFAEGIALSDPVAKESCmLNLLLSLPEANLLTFLFLLDHLKRVAEKEAVNKMSLHNLAT 1205
Cdd:cd04404    80 VILKTFLRELPEPLLTFDLYDDIVGFLNVDKEERVERV-KQLLQTLPEENYQVLKYLIKFLVQVSAHSDQNKMTNSNLAV 158
                         170       180
                  ....*....|....*....|.
gi 143811366 1206 VFGPTLLRPSEKESKLPA-NP 1225
Cdd:cd04404   159 VFGPNLLWAKDASMSLSAiNP 179
RhoGAP_myosin_IXB cd04407
RhoGAP_myosin_IXB: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
1052-1213 3.43e-27

RhoGAP_myosin_IXB: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in myosins IXB. Class IX myosins contain a characteristic head domain, a neck domain and a tail domain which contains a C6H2-zinc binding motif and a Rho-GAP domain. Class IX myosins are single-headed, processive myosins that are partly cytoplasmic, and partly associated with membranes and the actin cytoskeleton. Class IX myosins are implicated in the regulation of neuronal morphogenesis and function of sensory systems, like the inner ear. There are two major isoforms, myosin IXA and IXB with several splice variants, which are both expressed in developing neurons Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239872 [Multi-domain]  Cd Length: 186  Bit Score: 109.70  E-value: 3.43e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366 1052 FGVKIAVVTKrERSKVPYIVRQCVEEIERRGMEEVGIYRVSGVATDIQALKAAFDVNNKdvSVMMSEMDVNAIAGTLKLY 1131
Cdd:cd04407     1 FGVRVGSLTS-NKTSVPIVLEKLLEHVEMHGLYTEGIYRKSGSANRMKELHQLLQADPE--NVKLENYPIHAITGLLKQW 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366 1132 FRELPEPLFTDEFYPNFAEGIALSDPVAKESCMLNLLLSLPEANLLTFLFLLDHLKRVAEKEAVNKMSLHNLATVFGPTL 1211
Cdd:cd04407    78 LRELPEPLMTFAQYNDFLRAVELPEKQEQLQAIYRVLEQLPTANHNTLERLIFHLVKVALEEDVNRMSPNALAIVFAPCL 157

                  ..
gi 143811366 1212 LR 1213
Cdd:cd04407   158 LR 159
RhoGAP_srGAP cd04383
RhoGAP_srGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
1067-1213 1.96e-25

RhoGAP_srGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in srGAPs. srGAPs are components of the intracellular part of Slit-Robo signalling pathway that is important for axon guidance and cell migration. srGAPs contain an N-terminal FCH domain, a central RhoGAP domain and a C-terminal SH3 domain; this SH3 domain interacts with the intracellular proline-rich-tail of the Roundabout receptor (Robo). This interaction with Robo then activates the rhoGAP domain which in turn inhibits Cdc42 activity. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239848  Cd Length: 188  Bit Score: 104.81  E-value: 1.96e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366 1067 VPYIVRQCVEEIERRGMEEVGIYRVSGVATDIQALKAAFDVNNKDVSVMMSEMDVNAIAGTLKLYFRELPEPLFTDEFYP 1146
Cdd:cd04383    18 IPLVVESCIRFINLYGLQHQGIFRVSGSQVEVNDIKNAFERGEDPLADDQNDHDINSVAGVLKLYFRGLENPLFPKERFE 97
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 143811366 1147 NFAEGIALSDPVAKESCMLNLLLSLPEANLLTFLFLLDHLKRVAEKEAVNKMSLHNLATVFGPTLLR 1213
Cdd:cd04383    98 DLMSCVKLENPTERVHQIREILSTLPRSVIIVMRYLFAFLNHLSQFSDENMMDPYNLAICFGPTLMP 164
RhoGAP_ARHGAP6 cd04376
RhoGAP_ARHGAP6: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
1066-1219 6.48e-24

RhoGAP_ARHGAP6: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ArhGAP6-like proteins. ArhGAP6 shows GAP activity towards RhoA, but not towards Cdc42 and Rac1. ArhGAP6 is often deleted in microphthalmia with linear skin defects syndrome (MLS); MLS is a severe X-linked developmental disorder. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239841  Cd Length: 206  Bit Score: 100.98  E-value: 6.48e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366 1066 KVPYIVRQCVEEIERRGMEEVGIYRVSGVATDIQALKAAFDvNNKDVsVMMSEMDVNAIAGTLKLYFRELPEPLFTDEFY 1145
Cdd:cd04376     8 QVPRLVESCCQHLEKHGLQTVGIFRVGSSKKRVRQLREEFD-RGIDV-VLDENHSVHDVAALLKEFFRDMPDPLLPRELY 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366 1146 PNFAeGIALSDPVAKESCMLNLLLSLPEANLLTFLFLLDHLKRVAE---------KEAV--NKMSLHNLATVFGPTLLR- 1213
Cdd:cd04376    86 TAFI-GTALLEPDEQLEALQLLIYLLPPCNCDTLHRLLKFLHTVAEhaadsidedGQEVsgNKMTSLNLATIFGPNLLHk 164

                  ....*...
gi 143811366 1214 --PSEKES 1219
Cdd:cd04376   165 qkSGEREF 172
RhoGAP_FAM13A1a cd04393
RhoGAP_FAM13A1a: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
1051-1209 6.63e-23

RhoGAP_FAM13A1a: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of FAM13A1, isoform a-like proteins. The function of FAM13A1a is unknown. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by up several orders of magnitude.


Pssm-ID: 239858 [Multi-domain]  Cd Length: 189  Bit Score: 97.53  E-value: 6.63e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366 1051 VFGVKIAVVTKR--ERSKVPYIVRQCVEEIERRGMEEVGIYRVSGVATDIQALKAAFDvNNKDVSvMMSEMDVNAIAGTL 1128
Cdd:cd04393     2 VFGVPLQELQQAgqPENGVPAVVRHIVEYLEQHGLEQEGLFRVNGNAETVEWLRQRLD-SGEEVD-LSKEADVCSAASLL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366 1129 KLYFRELPEPLFTDEFYPNF--------AEGIALSDpvakescMLNLLLSLPEANLLTFLFLLDHLKRVAEKEAVNKMSL 1200
Cdd:cd04393    80 RLFLQELPEGLIPASLQIRLmqlyqdynGEDEFGRK-------LRDLLQQLPPVNYSLLKFLCHFLSNVASQHHENRMTA 152

                  ....*....
gi 143811366 1201 HNLATVFGP 1209
Cdd:cd04393   153 ENLAAVFGP 161
RhoGAP_myosin_IXA cd04406
RhoGAP_myosin_IXA: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
1052-1213 2.08e-21

RhoGAP_myosin_IXA: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in myosins IXA. Class IX myosins contain a characteristic head domain, a neck domain and a tail domain which contains a C6H2-zinc binding motif and a Rho-GAP domain. Class IX myosins are single-headed, processive myosins that are partly cytoplasmic, and partly associated with membranes and the actin cytoskeleton. Class IX myosins are implicated in the regulation of neuronal morphogenesis and function of sensory systems, like the inner ear. There are two major isoforms, myosin IXA and IXB with several splice variants, which are both expressed in developing neurons. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239871  Cd Length: 186  Bit Score: 93.14  E-value: 2.08e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366 1052 FGVKIAVVTKRERSkVPYIVRQCVEEIERRGMEEVGIYRVSGVATDIQALKAAFDVNNKDVSvmMSEMDVNAIAGTLKLY 1131
Cdd:cd04406     1 FGVELSRLTSEDRS-VPLVVEKLINYIEMHGLYTEGIYRKSGSTNKIKELRQGLDTDANSVN--LDDYNIHVIASVFKQW 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366 1132 FRELPEPLFTDEFYPNFAEGIALSDPVAKESCMLNLLLSLPEANLLTFLFLLDHLKRVAEKEAVNKMSLHNLATVFGPTL 1211
Cdd:cd04406    78 LRDLPNPLMTFELYEEFLRAMGLQERRETVRGVYSVIDQLSRTHLNTLERLIFHLVRIALQEETNRMSANALAIVFAPCI 157

                  ..
gi 143811366 1212 LR 1213
Cdd:cd04406   158 LR 159
RhoGAP_DLC1 cd04375
RhoGAP_DLC1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
1051-1227 1.31e-20

RhoGAP_DLC1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of DLC1-like proteins. DLC1 shows in vitro GAP activity towards RhoA and CDC42. Beside its C-terminal GAP domain, DLC1 also contains a SAM (sterile alpha motif) and a START (StAR-related lipid transfer action) domain. DLC1 has tumor suppressor activity in cell culture. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239840  Cd Length: 220  Bit Score: 91.71  E-value: 1.31e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366 1051 VFGVKIAVVTKRERSKVPYIVRQCVEEIERRGMEEVGIYRVSGVATDIQALKAAFDVNNKDvsVMMSEMDVNAIAGTLKL 1130
Cdd:cd04375     4 VFGVPLLVNLQRTGQPLPRSIQQAMRWLRNNALDQVGLFRKSGVKSRIQKLRSMIESSTDN--VNYDGQQAYDVADMLKQ 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366 1131 YFRELPEPLFTDEFYPNFAEGIALSDPVAKESCMLNLLLSLPEANLLTFLFLLDHLKRVAEKEAVNKMSLHNLATVFGPT 1210
Cdd:cd04375    82 YFRDLPEPLLTNKLSETFIAIFQYVPKEQRLEAVQCAILLLPDENREVLQTLLYFLSDVAANSQENQMTATNLAVCLAPS 161
                         170
                  ....*....|....*....
gi 143811366 1211 L--LRPSEKESKLPANPSQ 1227
Cdd:cd04375   162 LfhLNTSRRENSSPARRMQ 180
RhoGAP_KIAA1688 cd04389
RhoGAP_KIAA1688: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
1052-1213 1.02e-18

RhoGAP_KIAA1688: GTPase-activator protein (GAP) domain for Rho-like GTPases found in KIAA1688-like proteins; KIAA1688 is a protein of unknown function that contains a RhoGAP domain and a myosin tail homology 4 (MyTH4) domain. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239854  Cd Length: 187  Bit Score: 85.52  E-value: 1.02e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366 1052 FGVKIAVVTKRERS-----KVPYIVRQCVEEIERRGMEEV-GIYRVSGVATDIQALKAAFDVNNKDVSVMMsemDVNAIA 1125
Cdd:cd04389     1 FGSSLEEIMDRQKEkypelKLPWILTFLSEKVLALGGFQTeGIFRVPGDIDEVNELKLRVDQWDYPLSGLE---DPHVPA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366 1126 GTLKLYFRELPEPLFTDEFYpnfAEGIALSDPVAKescMLNLLLSLPEANLLTFLFLLDHLKRVAEKEAV--NKMSLHNL 1203
Cdd:cd04389    78 SLLKLWLRELEEPLIPDALY---QQCISASEDPDK---AVEIVQKLPIINRLVLCYLINFLQVFAQPENVahTKMDVSNL 151
                         170
                  ....*....|
gi 143811366 1204 ATVFGPTLLR 1213
Cdd:cd04389   152 AMVFAPNILR 161
RhoGAP-ARHGAP11A cd04394
RhoGAP-ARHGAP11A: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
1087-1224 5.50e-18

RhoGAP-ARHGAP11A: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ArhGAP11A-like proteins. The mouse homolog of human ArhGAP11A has been detected as a gene exclusively expressed in immature ganglion cells, potentially playing a role in retinal development. The exact function of ArhGAP11A is unknown. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239859 [Multi-domain]  Cd Length: 202  Bit Score: 83.68  E-value: 5.50e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366 1087 GIYRVSGVATDIQALKAAfdVNNKDVSvmMSEMDVNAIAGTLKLYFRELPEPLFTDEFYPNFAEGIALSDPVAKESCMLN 1166
Cdd:cd04394    39 GLFRKSGSVVRQKELKAK--LEGGEAC--LSSALPCDVAGLLKQFFRELPEPLLPYDLHEALLKAQELPTDEERKSATLL 114
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 143811366 1167 LLLSLPEANLLTFLFLLDHLKRVAEKEAVNKMSLHNLATVFGPTLLRPSEKESKLPAN 1224
Cdd:cd04394   115 LTCLLPDEHVNTLRYFFSFLYDVAQRCSENKMDSSNLAVIFAPNLFQSEEGGEKMSSS 172
RhoGAP_ARHGAP19 cd04392
RhoGAP_ARHGAP19: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
1087-1224 4.86e-17

RhoGAP_ARHGAP19: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ArhGAP19-like proteins. The function of ArhGAP19 is unknown. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239857  Cd Length: 208  Bit Score: 80.97  E-value: 4.86e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366 1087 GIYRVSGVATDIQALKAAFDvNNKDVSVMMSEMDVNAIAGTLKLYFRELPEPLFTDEFYP---------NFAEGiALSDP 1157
Cdd:cd04392    28 GLFRKPGNSARQQELRDLLN-SGTDLDLESGGFHAHDCATVLKGFLGELPEPLLTHAHYPahlqiadlcQFDEK-GNKTS 105
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 143811366 1158 VAKESCMLN----LLLSLPEANLLTFLFLLDHLKRVAEKEAVNKMSLHNLATVFGPTLLRPsekeSKLPAN 1224
Cdd:cd04392   106 APDKERLLEalqlLLLLLPEENRNLLKLILDLLYQTAKHEDKNKMSADNLALLFTPHLICP----RNLTPE 172
RhoGAP_fLRG1 cd04397
RhoGAP_fLRG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
1052-1219 2.77e-15

RhoGAP_fLRG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of fungal LRG1-like proteins. Yeast Lrg1p is required for efficient cell fusion, and mother-daughter cell separation, possibly through acting as a RhoGAP specifically regulating 1,3-beta-glucan synthesis. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239862  Cd Length: 213  Bit Score: 76.25  E-value: 2.77e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366 1052 FGVKIAVVTKRE-----------RSKVPYIVRQCVEEIERRGMEEVGIYRVSGVATDIQALKAAFDvNNKDVSVMMSEMD 1120
Cdd:cd04397     1 FGVPLEILVEKFgadstlgvgpgKLRIPALIDDIISAMRQMDMSVEGVFRKNGNIRRLKELTEEID-KNPTEVPDLSKEN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366 1121 VNAIAGTLKLYFRELPEPLFTDEFYPNFAEGIALSDPVAKESCMLNLLLSLPEANLLTFLFLLDHLKRVA-----EKEAV 1195
Cdd:cd04397    80 PVQLAALLKKFLRELPDPLLTFKLYRLWISSQKIEDEEERKRVLHLVYCLLPKYHRDTMEVLFSFLKWVSsfshiDEETG 159
                         170       180
                  ....*....|....*....|....
gi 143811366 1196 NKMSLHNLATVFGPTLLRPSEKES 1219
Cdd:cd04397   160 SKMDIHNLATVITPNILYSKTDNP 183
RhoGAP_ARHGAP20 cd04402
RhoGAP_ARHGAP20: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
1067-1215 2.37e-14

RhoGAP_ARHGAP20: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ArhGAP20-like proteins. ArhGAP20, also known as KIAA1391 and RA-RhoGAP, contains a RhoGAP, a RA, and a PH domain, and ANXL repeats. ArhGAP20 is activated by Rap1 and induces inactivation of Rho, which in turn leads to neurite outgrowth. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239867  Cd Length: 192  Bit Score: 72.72  E-value: 2.37e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366 1067 VPYIVRQCVEEIERRGMEEVGIYRVSGVATDIQALKAAFdvnNKDVSVMMSEMDVNAIAGTLKLYFRELPEPLFTDEFYP 1146
Cdd:cd04402    15 LPKPILDMLSLLYQKGPSTEGIFRRSANAKACKELKEKL---NSGVEVDLKAEPVLLLASVLKDFLRNIPGSLLSSDLYE 91
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 143811366 1147 NFAEGIALSDPVAKESCMLNLLLSLPEANLLtflfLLDHLKRV----AEKEAVNKMSLHNLATVFGPTLLRPS 1215
Cdd:cd04402    92 EWMSALDQENEEEKIAELQRLLDKLPRPNVL----LLKHLICVlhniSQNSETNKMDAFNLAVCIAPSLLWPP 160
RhoGAP_p85 cd04388
RhoGAP_p85: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
1068-1239 3.77e-12

RhoGAP_p85: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in the p85 isoforms of the regulatory subunit of the class IA PI3K (phosphatidylinositol 3'-kinase). This domain is also called Bcr (breakpoint cluster region protein) homology (BH) domain. Class IA PI3Ks are heterodimers, containing a regulatory subunit (p85) and a catalytic subunit (p110) and are activated by growth factor receptor tyrosine kinases (RTKs); this activation is mediated by the p85 subunit. p85 isoforms, alpha and beta, contain a C-terminal p110-binding domain flanked by two SH2 domains, an N-terminal SH3 domain, and a RhoGAP domain flanked by two proline-rich regions. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239853  Cd Length: 200  Bit Score: 66.82  E-value: 3.77e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366 1068 PYIVRQCVEEIERRGMEEVGIYR--VSGVATDiqaLKAAFDVNNKdvSVMMSEMDVNAIAGTLKLYFRELPEPLFTDEFY 1145
Cdd:cd04388    16 PPLLIKLVEAIEKKGLESSTLYRtqSSSSLTE---LRQILDCDAA--SVDLEQFDVAALADALKRYLLDLPNPVIPAPVY 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366 1146 PNFAEGIALSDPVAKESCMLNLLL---SLPEANLLTFLFLLDHLKRVAEKEAVNKMSLHNLATVFGPTLLRPSEKESKLP 1222
Cdd:cd04388    91 SEMISRAQEVQSSDEYAQLLRKLIrspNLPHQYWLTLQYLLKHFFRLCQSSSKNLLSARALAEIFSPLLFRFQPASSDSP 170
                         170
                  ....*....|....*....
gi 143811366 1223 ANPSQ--PITMTDSWSLEV 1239
Cdd:cd04388   171 EFHIRiiEVLITSEWNERQ 189
RhoGAP_fSAC7_BAG7 cd04396
RhoGAP_fSAC7_BAG7: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
1066-1212 3.95e-12

RhoGAP_fSAC7_BAG7: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of fungal SAC7 and BAG7-like proteins. Both proteins are GTPase activating proteins of Rho1, but differ functionally in vivo: SAC7, but not BAG7, is involved in the control of Rho1-mediated activation of the PKC-MPK1 pathway. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239861  Cd Length: 225  Bit Score: 67.05  E-value: 3.95e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366 1066 KVPYIVRQCVEEIERRGMEEVGIYRVSGVATDIQALKAAFDVNNK-DVSVMMSEMDVNAIAGTLKLYFRELPEPLFTDEF 1144
Cdd:cd04396    31 YIPVVVAKCGVYLKENATEVEGIFRVAGSSKRIRELQLIFSTPPDyGKSFDWDGYTVHDAASVLRRYLNNLPEPLVPLDL 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366 1145 YPNFAEGIALSDPVAKESCMLN-----------------LLLSLPEANLLTFLFLLDHLKRVAEKEAVNKMSLHNLATVF 1207
Cdd:cd04396   111 YEEFRNPLRKRPRILQYMKGRIneplntdidqaikeyrdLITRLPNLNRQLLLYLLDLLAVFARNSDKNLMTASNLAAIF 190

                  ....*
gi 143811366 1208 GPTLL 1212
Cdd:cd04396   191 QPGIL 195
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
912-1016 9.11e-12

Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, protein kinases C, and synaptotagmins (among others). Some do not appear to contain Ca2+-binding sites. Particular C2s appear to bind phospholipids, inositol polyphosphates, and intracellular proteins. Unusual occurrence in perforin. Synaptotagmin and PLC C2s are permuted in sequence with respect to N- and C-terminal beta strands. SMART detects C2 domains using one or both of two profiles.


Pssm-ID: 214577 [Multi-domain]  Cd Length: 101  Bit Score: 62.50  E-value: 9.11e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366    912 FLNVIVHSATGFK-----QSSNLYCTLEVDsfGYFVNKAKTRVYRDTAEPNWNEEFEIEL--EGSQTLRILCYEKcynkt 984
Cdd:smart00239    1 TLTVKIISARNLPpkdkgGKSDPYVKVSLD--GDPKEKKKTKVVKNTLNPVWNETFEFEVppPELAELEIEVYDK----- 73
                            90       100       110
                    ....*....|....*....|....*....|..
gi 143811366    985 kipkeDGESTDRLMGKGQVQLDPQALQDRDWQ 1016
Cdd:smart00239   74 -----DRFGRDDFIGQVTIPLSDLLLGGRHEK 100
RhoGAP_OCRL1 cd04380
RhoGAP_OCRL1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
1014-1218 2.77e-11

RhoGAP_OCRL1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in OCRL1-like proteins. OCRL1 (oculocerebrorenal syndrome of Lowe 1)-like proteins contain two conserved domains: a central inositol polyphosphate 5-phosphatase domain and a C-terminal Rho GAP domain, this GAP domain lacks the catalytic residue and therefore maybe inactive. OCRL-like proteins are type II inositol polyphosphate 5-phosphatases that can hydrolyze lipid PI(4,5)P2 and PI(3,4,5)P3 and soluble Ins(1,4,5)P3 and Ins(1,3,4,5)P4, but their individual specificities vary. The functionality of the RhoGAP domain is still unclear. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239845  Cd Length: 220  Bit Score: 64.67  E-value: 2.77e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366 1014 DWQRTVIAMNgIEvklsvkfnsrefSLKRMPsRKQTGVFGVKIAVVTKRERSKVPYIVRQ----CVEEIERRGMEEVGIY 1089
Cdd:cd04380     7 VYLPSCFGSS-LE------------TLIRLP-DPGIRNLIDQLELGDNPDYSEVPLSIPKeiwrLVDYLYTRGLAQEGLF 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366 1090 RVSGVATD----IQALKAAFDVNNKDVSVMMSEMdvnaIAGTLKLYFRELPEPLFTDEFYPNFAEGIALSDpvakESCML 1165
Cdd:cd04380    73 EEPGLPSEpgelLAEIRDALDTGSPFNSPGSAES----VAEALLLFLESLPDPIIPYSLYERLLEAVANNE----EDKRQ 144
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 143811366 1166 NLLLSLPEANLLTFLFLLDHLKRVAEKEAVNKMSLHNLATVFGPTLLRPSEKE 1218
Cdd:cd04380   145 VIRISLPPVHRNVFVYLCSFLRELLSESADRGLDENTLATIFGRVLLRDPPRA 197
C2 cd00030
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
913-1007 1.30e-10

C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


Pssm-ID: 175973 [Multi-domain]  Cd Length: 102  Bit Score: 59.39  E-value: 1.30e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366  913 LNVIVHSATGFKQ-----SSNLYCTLEVDSFgyfvNKAKTRVYRDTAEPNWNEEFEIELE--GSQTLRILCYEKcynktk 985
Cdd:cd00030     1 LRVTVIEARNLPAkdlngKSDPYVKVSLGGK----QKFKTKVVKNTLNPVWNETFEFPVLdpESDTLTVEVWDK------ 70
                          90       100
                  ....*....|....*....|..
gi 143811366  986 ipkeDGESTDRLMGKGQVQLDP 1007
Cdd:cd00030    71 ----DRFSKDDFLGEVEIPLSE 88
C2 pfam00168
C2 domain;
911-1013 3.47e-08

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 52.71  E-value: 3.47e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366   911 GFLNVIVHSATG-----FKQSSNLYCTLEVDSFgyfVNKAKTRVYRDTAEPNWNEEFEIEL--EGSQTLRILCYEKcynk 983
Cdd:pfam00168    1 GRLTVTVIEAKNlppkdGNGTSDPYVKVYLLDG---KQKKKTKVVKNTLNPVWNETFTFSVpdPENAVLEIEVYDY---- 73
                           90       100       110
                   ....*....|....*....|....*....|
gi 143811366   984 tkipkeDGESTDRLMGKGQVQLDPQALQDR 1013
Cdd:pfam00168   74 ------DRFGRDDFIGEVRIPLSELDSGEG 97
RhoGAP_fRGD2 cd04399
RhoGAP_fRGD2: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
1052-1214 9.40e-07

RhoGAP_fRGD2: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of fungal RGD2-like proteins. Yeast Rgd2 is a GAP protein for Cdc42 and Rho5. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239864  Cd Length: 212  Bit Score: 51.18  E-value: 9.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366 1052 FGVKIAVVTKRERSKVPYIVrQCV------------EEIERRGmeeVGIYRVSgvATDIQALKAAFDVNNKDVSVMMSEM 1119
Cdd:cd04399     1 FGVDLETRCRLDKKVVPLIV-SAIlsyldqlypdliNDEVRRN---VWTDPVS--LKETHQLRNLLNKPKKPDKEVIILK 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366 1120 DVNA--IAGTLKLYFRELPEPLFTDEF-------YPNFAEGIALSDPvAKESCMLNLLLSLPEANLLTFLFLLDHLKRVA 1190
Cdd:cd04399    75 KFEPstVASVLKLYLLELPDSLIPHDIydlirslYSAYPPSQEDSDT-ARIQGLQSTLSQLPKSHIATLDAIITHFYRLI 153
                         170       180
                  ....*....|....*....|....*...
gi 143811366 1191 E----KEAVNKMSLHnLATVFGPTLLRP 1214
Cdd:cd04399   154 EitkmGESEEEYADK-LATSLSREILRP 180
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
80-387 2.40e-06

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 52.10  E-value: 2.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366   80 AAQAPDGASEPRASAS-RPQPAPADGADPPPAEEPEARPDGEGSPGKARPGTARRPGAAASGERDDRGPPASVAAlrSNF 158
Cdd:PHA03307   98 ASPAREGSPTPPGPSSpDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQA--ALP 175
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366  159 ERIRKGHGQPGADAEKPFYVNVEFHHERGLVKVNDKEVSDRISSLGSQamqmerkksqhGAGSSVGDASRPPYRGRSSES 238
Cdd:PHA03307  176 LSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPA-----------PGRSAADDAGASSSDSSSSES 244
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366  239 S-CGVDGDyedaelnprflkdnliDANGGSRPPWPPLEYQPYQSIyvggMMEGEGKGPLLRSQSTSEQEkrltwpRRSYS 317
Cdd:PHA03307  245 SgCGWGPE----------------NECPLPRPAPITLPTRIWEAS----GWNGPSSRPGPASSSSSPRE------RSPSP 298
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 143811366  318 PRSFEDCGGGYTPDCSSNENLTSSEEDFSSGQSSRVSPSPTTYRMFRDKSRSPS-QNSQQSFDSSSPPTPQ 387
Cdd:PHA03307  299 SPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSpSRPPPPADPSSPRKRP 369
C2A_Tricalbin-like cd04044
C2 domain first repeat present in Tricalbin-like proteins; 5 to 6 copies of the C2 domain are ...
911-1044 5.43e-06

C2 domain first repeat present in Tricalbin-like proteins; 5 to 6 copies of the C2 domain are present in Tricalbin, a yeast homolog of Synaptotagmin, which is involved in membrane trafficking and sorting. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-II topology.


Pssm-ID: 176009 [Multi-domain]  Cd Length: 124  Bit Score: 46.78  E-value: 5.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366  911 GFLNVIVHSATGFKQSS------NLYCTLEVDSFGyfvNKAKTRVYRDTAEPNWNEEFEIELEG-SQTLRILCYEkcYNK 983
Cdd:cd04044     2 GVLAVTIKSARGLKGSDiiggtvDPYVTFSISNRR---ELARTKVKKDTSNPVWNETKYILVNSlTEPLNLTVYD--FND 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 143811366  984 TKipkedgesTDRLMgkGQVQLDPQALQDRDWQrtviamNGIEVKLSVKFNSR---EFSLKRMP 1044
Cdd:cd04044    77 KR--------KDKLI--GTAEFDLSSLLQNPEQ------ENLTKNLLRNGKPVgelNYDLRFFP 124
PH_puratrophin-1 cd13242
Puratrophin-1 pleckstrin homology (PH) domain; Puratrophin-1 (also called Purkinje cell ...
705-748 6.25e-06

Puratrophin-1 pleckstrin homology (PH) domain; Puratrophin-1 (also called Purkinje cell atrophy-associated protein 1 or PLEKHG4/Pleckstrin homology domain-containing family G member 4) contains a spectrin repeat, a RhoGEF (DH) domain, and a PH domain. It is thought to function in intracellular signaling and cytoskeleton dynamics at the Golgi. Puratrophin-1 is expressed in kidney, Leydig cells in the testis, epithelial cells in the prostate gland and Langerhans islet in the pancreas. A single nucleotide substitution in the puratrophin-1 gene were once thought to result in autosomal dominant cerebellar ataxia (ADCA), but now it has been demonstrated that this ataxia is a result of defects in the BEAN gene. Puratrophin contains a domain architecture similar to that of Dbl family members Dbs and Trio. Dbs is a guanine nucleotide exchange factor (GEF), which contains spectrin repeats, a RhoGEF (DH) domain and a PH domain. The Dbs PH domain participates in binding to both the Cdc42 and RhoA GTPases. Trio plays an essential role in regulating the actin cytoskeleton during axonal guidance and branching. Trio is a multidomain signaling protein that contains two RhoGEF(DH)-PH domains in tandem. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270062  Cd Length: 136  Bit Score: 46.90  E-value: 6.25e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 143811366  705 EHRQLLK-DSFMVelVEGARK-LRHVFLFTDLLLCTKLKKQSGGKT 748
Cdd:cd13242    25 EQGQLLRqDEFLV--WQGRKKcLRHVFLFEDLILFSKPKKTPGGKD 68
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
80-156 1.20e-05

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 49.85  E-value: 1.20e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 143811366   80 AAQAPDGASEPrASASRPQPAPADGADPPPAEEPEARPDGEGSPGKARPGTARRPGAAasgERDDRGPPASVAALRS 156
Cdd:PRK07003  460 DSRCDERDAQP-PADSGSASAPASDAPPDAAFEPAPRAAAPSAATPAAVPDARAPAAA---SREDAPAAAAPPAPEA 532
PH_19 pfam19057
PH domain; This entry contains a PH domain found in RhoGEF proteins.
707-768 3.37e-05

PH domain; This entry contains a PH domain found in RhoGEF proteins.


Pssm-ID: 436928  Cd Length: 154  Bit Score: 45.17  E-value: 3.37e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 143811366   707 RQLLKDSFMVELVEGAR------KLRHVFLFTDLLLCTKLKKQSG---------GKTQQYDCKWYIPLTDLSFQMVD 768
Cdd:pfam19057   11 RYLIRQDDVVETVYNERgeviktKERRLFLLNDLLVCVTVNSKSGssfgssslvPTGEKYKLKWSVPLSDVEVVESG 87
PHA03378 PHA03378
EBNA-3B; Provisional
79-175 4.89e-05

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 47.75  E-value: 4.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366   79 RAAQAPDGASEPRASASRPQPAPAdgADPPPAEEPEARPdGEGSPGKARPGTARRPGAAASGERDDRGPPASVAALRSNF 158
Cdd:PHA03378  685 LPIQWAPGTMQPPPRAPTPMRPPA--APPGRAQRPAAAT-GRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAP 761
                          90
                  ....*....|....*..
gi 143811366  159 ERIRKGHGQPGADAEKP 175
Cdd:PHA03378  762 GRARPPAAAPGAPTPQP 778
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
72-148 6.50e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 47.29  E-value: 6.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366   72 RQRWGfRRAAQAPDGASEPR---ASASRPQPAPADGADPPPAEEPEARPDGEGSPGKARPGTARRPGAAASGERDDRGPP 148
Cdd:PRK07764  704 APAAT-PPAGQADDPAAQPPqaaQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEE 782
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
79-153 7.64e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 46.90  E-value: 7.64e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 143811366   79 RAAQAPDGASEPRASAS-RPQPAPADGADPPPAEEPEARPDGEGSPGKARPGTARRPGAAASGERDDRGPPASVAA 153
Cdd:PRK07764  412 PAAAAPAAAAAPAPAAApQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAPAPAPPAA 487
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
75-148 8.18e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 46.90  E-value: 8.18e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 143811366   75 WGFRRAAQAPDGASEPRASASRPQPAPADGADPPPAEEPEARPDGEGSPGKARPGTARRPGAAASGERDDRGPP 148
Cdd:PRK07764  667 DGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVP 740
KLF14_N cd21576
N-terminal domain of Kruppel-like factor 14; Kruppel-like factor 14 (KLF14; also known as ...
90-148 1.40e-04

N-terminal domain of Kruppel-like factor 14; Kruppel-like factor 14 (KLF14; also known as Krueppel-like factor 14 or basic transcription element-binding protein 5/BTEB5) is a protein that in humans is encoded by the KLF14 gene. KLF14 regulates the transcription of various genes, including TGFbetaRII (the type II receptor for TGFbeta). KLF14 is expressed in many tissues, lacks introns, and is subject to parent-specific expression. It also appears to be a master regulator of gene expression in adipose tissue. KLF14 is associated with coronary artery disease, hypercholesterolemia, and type 2 diabetes. KLF9, KLF10, KLF11, KLF13, KLF14, and KLF16 share a conserved alpha-helical motif AA/VXXL that mediates their binding to Sin3A and their activities as transcriptional repressors. KLF14 belongs to a family of proteins, called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specificity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the N-terminal domain of KLF14.


Pssm-ID: 409238 [Multi-domain]  Cd Length: 195  Bit Score: 44.43  E-value: 1.40e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 143811366   90 PRASASRPQPA----PADGADPPPAEEPEARPDGEGSPGK-ARPGTARRPGAAASGERDDRGPP 148
Cdd:cd21576   107 PRASSGSSDPArgssPTLGSEPAPASGEDAVSGPESSFGApAIPSAPAAPGAPAVSGEVPGGAP 170
C2_Munc13_fungal cd04043
C2 domain in Munc13 (mammalian uncoordinated) proteins; fungal group; C2-like domains are ...
917-1012 1.48e-04

C2 domain in Munc13 (mammalian uncoordinated) proteins; fungal group; C2-like domains are thought to be involved in phospholipid binding in a Ca2+ independent manner in both Unc13 and Munc13. Caenorabditis elegans Unc13 has a central domain with sequence similarity to PKC, which includes C1 and C2-related domains. Unc13 binds phorbol esters and DAG with high affinity in a phospholipid manner. Mutations in Unc13 results in abnormal neuronal connections and impairment in cholinergic neurotransmission in the nematode. Munc13 is the mammalian homolog which are expressed in the brain. There are 3 isoforms (Munc13-1, -2, -3) and are thought to play a role in neurotransmitter release and are hypothesized to be high-affinity receptors for phorbol esters. Unc13 and Munc13 contain both C1 and C2 domains. There are two C2 related domains present, one central and one at the carboxyl end. Munc13-1 contains a third C2-like domain. Munc13 interacts with syntaxin, synaptobrevin, and synaptotagmin suggesting a role for these as scaffolding proteins. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the second C2 repeat, C2B, and has a type-II topology.


Pssm-ID: 176008 [Multi-domain]  Cd Length: 126  Bit Score: 42.64  E-value: 1.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366  917 VHSATGFKqSSNLYCTLeVDSFGYfVNKAKTRVYRDTAEPNWNEEFEIELEGSQTLRILcyekcynkTKIPKEDGESTDR 996
Cdd:cd04043    13 LKADSSNG-LSDPYVTL-VDTNGK-RRIAKTRTIYDTLNPRWDEEFELEVPAGEPLWIS--------ATVWDRSFVGKHD 81
                          90
                  ....*....|....*.
gi 143811366  997 LMGKGQVQLDPQALQD 1012
Cdd:cd04043    82 LCGRASLKLDPKRFGD 97
PHA03378 PHA03378
EBNA-3B; Provisional
78-152 2.35e-04

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 45.44  E-value: 2.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366   78 RRAAQAPDGASEPRASASRPQ-PAPADGADPPPAEEPEARPDGEGSPGKAR-----PGTARRPGAAASGERDDRGPPASV 151
Cdd:PHA03378  695 QPPPRAPTPMRPPAAPPGRAQrPAAATGRARPPAAAPGRARPPAAAPGRARppaaaPGRARPPAAAPGRARPPAAAPGAP 774

                  .
gi 143811366  152 A 152
Cdd:PHA03378  775 T 775
Coatomer_E pfam04733
Coatomer epsilon subunit; This family represents the epsilon subunit of the coatomer complex, ...
540-684 2.54e-04

Coatomer epsilon subunit; This family represents the epsilon subunit of the coatomer complex, which is involved in the regulation of intracellular protein trafficking between the endoplasmic reticulum and the Golgi complex.


Pssm-ID: 398419 [Multi-domain]  Cd Length: 288  Bit Score: 44.39  E-value: 2.54e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366   540 SQQIETIFFKVPELYEIHK-EFYDGLFPRVQQWSHQQRVGDLFQ---KLASQLGVYRafvDNYGVAMEMAEK-------- 607
Cdd:pfam04733  126 GENLEAMALNVQILLKMHRiDLAEQQLKKMQQIDEDATLTQLANawvKLAVGGEKIQ---DAYYIFQEFSEKydstplll 202
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366   608 -----CCQANAQFAEISENLRARSNKDAKDPTTKNSL---ETLLYKPVDRVTRSTLVLHDllkhtpaSHPDHPLLQDALR 679
Cdd:pfam04733  203 ngqavCCMCLGRYEEAESLLKEALDKDAKDPETLINLvvcALHLGKPAEVSNRNLSQLKL-------SHPTHPLVKDLNE 275

                   ....*
gi 143811366   680 ISQNF 684
Cdd:pfam04733  276 KEAEF 280
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
78-163 2.59e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 45.36  E-value: 2.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366   78 RRAAQAPDGASEPRASASRPQPAPADGADPPPAEEPEARPDGEGSPGkARPGTARRPGAAASGeRDDRGP----PASVAA 153
Cdd:PRK07764  445 AGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAPAPAPPAAPAPA-AAPAAPAAPAAPAGA-DDAATLrerwPEILAA 522
                          90
                  ....*....|
gi 143811366  154 LRsnfERIRK 163
Cdd:PRK07764  523 VP---KRSRK 529
C2_C21orf25-like cd08678
C2 domain found in the Human chromosome 21 open reading frame 25 (C21orf25) protein; The ...
925-1006 3.28e-04

C2 domain found in the Human chromosome 21 open reading frame 25 (C21orf25) protein; The members in this cd are named after the Human C21orf25 which contains a single C2 domain. Several other members contain a C1 domain downstream of the C2 domain. No other information on this protein is currently known. The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


Pssm-ID: 176060 [Multi-domain]  Cd Length: 126  Bit Score: 41.97  E-value: 3.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366  925 QSSNLYCTLEVDsfgYFVNKAKTRVYRDTAEPNWNEEFEIELEG-SQTLRILCYEKcynktkipkeDGESTDRLMGKGQV 1003
Cdd:cd08678    16 GSSNPYCVLEMD---EPPQKYQSSTQKNTSNPFWDEHFLFELSPnSKELLFEVYDN----------GKKSDSKFLGLAIV 82

                  ...
gi 143811366 1004 QLD 1006
Cdd:cd08678    83 PFD 85
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
78-175 5.96e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 44.21  E-value: 5.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366   78 RRAAQAPDGASEPRASASRPQPAPADGADPPPAEEPEARPDGEGSPGKARPGTARRPGAAASGERDDRGPPASVAALRSN 157
Cdd:PRK07764  400 SAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAA 479
                          90
                  ....*....|....*...
gi 143811366  158 FERIRKGHGQPGADAEKP 175
Cdd:PRK07764  480 PAPAPPAAPAPAAAPAAP 497
PHA03378 PHA03378
EBNA-3B; Provisional
78-149 7.11e-04

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 43.90  E-value: 7.11e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 143811366   78 RRAAQAPDGASEPRASASRPQ-PAPADGADPPPAEEPEARPDGEGSPGKARPGTARrPGAAASgERDDRGPPA 149
Cdd:PHA03378  715 QRPAAATGRARPPAAAPGRARpPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAA-PGAPTP-QPPPQAPPA 785
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
78-153 7.96e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 43.71  E-value: 7.96e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 143811366   78 RRAAQAPDGASEPRASASRP-QPAPADGADPPPAEEPEARPDGEGSPGKARPGTARRPGAAASGERDDRGPPASVAA 153
Cdd:PRK12323  375 ATAAAAPVAQPAPAAAAPAAaAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPA 451
PHA03247 PHA03247
large tegument protein UL36; Provisional
79-153 9.08e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.77  E-value: 9.08e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 143811366   79 RAAQAPDGASEPRASASRPQPAP-ADGADPPPAE-EPEARPDGEGSPGKARPGTARRPGAAASGERDDRGPPASVAA 153
Cdd:PHA03247 2672 RAAQASSPPQRPRRRAARPTVGSlTSLADPPPPPpTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGP 2748
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
80-153 9.11e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 43.44  E-value: 9.11e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 143811366   80 AAQAPDGASEPRASASRPQPAPAdgADPPPAEEPEARPDGEGSPGKARPGTARRPGAAASGERDDRGPPASVAA 153
Cdd:PRK07764  396 AAAPSAAAAAPAAAPAPAAAAPA--AAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPA 467
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
79-148 9.20e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 43.33  E-value: 9.20e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366   79 RAAQAPDGASEPRASASRPQPAPADGADPPPAEEPEARPdGEGSPGKARPGTARRPGAAASGERDDRGPP 148
Cdd:PRK12323  430 PEALAAARQASARGPGGAPAPAPAPAAAPAAAARPAAAG-PRPVAAAAAAAPARAAPAAAPAPADDDPPP 498
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
79-175 9.66e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 43.68  E-value: 9.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366   79 RAAQAPDGASEPRASASRPQPAPADGADPPPAE-EPEARPdgeGSPGKARPgtARRPGAAAsgerddrgppASVAALRSN 157
Cdd:PRK07003  495 RAAAPSAATPAAVPDARAPAAASREDAPAAAAPpAPEARP---PTPAAAAP--AARAGGAA----------AALDVLRNA 559
                          90
                  ....*....|....*...
gi 143811366  158 FERIRKGHGQPGADAEKP 175
Cdd:PRK07003  560 GMRVSSDRGARAAAAAKP 577
C2A_C2C_Synaptotagmin_like cd08391
C2 domain first and third repeat in Synaptotagmin-like proteins; Synaptotagmin is a ...
923-979 1.44e-03

C2 domain first and third repeat in Synaptotagmin-like proteins; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. Previously all synaptotagmins were thought to be calcium sensors in the regulation of neurotransmitter release and hormone secretion, but it has been shown that not all of them bind calcium. Of the 17 identified synaptotagmins only 8 bind calcium (1-3, 5-7, 9, 10). The function of the two C2 domains that bind calcium are: regulating the fusion step of synaptic vesicle exocytosis (C2A) and binding to phosphatidyl-inositol-3,4,5-triphosphate (PIP3) in the absence of calcium ions and to phosphatidylinositol bisphosphate (PIP2) in their presence (C2B). C2B also regulates also the recycling step of synaptic vesicles. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains either the first or third repeat in Synaptotagmin-like proteins with a type-I topology.


Pssm-ID: 176037 [Multi-domain]  Cd Length: 121  Bit Score: 39.97  E-value: 1.44e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366  923 FKQSSNLYCTLEVDSFGYfvnkaKTRVYRDTAEPNWNEEFEI---ELEGsQTLRILCYEK 979
Cdd:cd08391    24 VKGKSDPYVIVRVGAQTF-----KSKVIKENLNPKWNEVYEAvvdEVPG-QELEIELFDE 77
kgd PRK12270
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ...
80-152 1.61e-03

multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;


Pssm-ID: 237030 [Multi-domain]  Cd Length: 1228  Bit Score: 42.96  E-value: 1.61e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 143811366   80 AAQAPDGASEPRASASRPQPAPADGADPPPAEEPEARPDGEGSPGKARPGTARRPGAAASGERDDRGPPASVA 152
Cdd:PRK12270   56 SAPAAAPAAKAPAAPAPAPPAAAAPAAPPKPAAAAAAAAAPAAPPAAAAAAAPAAAAVEDEVTPLRGAAAAVA 128
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
69-148 1.81e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 42.67  E-value: 1.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366   69 SYDRQRWGFRRAAQAPDGASEPRASASRPQPAPADGADPPPAEEPEARPDGEGSPGKARPGTARRPGAAASGERDDRGPP 148
Cdd:PRK07764  663 SDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLP 742
PH_PLEKHG1_G2_G3 cd13243
Pleckstrin homology domain-containing family G members 1, 2, and 3 pleckstrin homology (PH) ...
709-778 1.82e-03

Pleckstrin homology domain-containing family G members 1, 2, and 3 pleckstrin homology (PH) domain; PLEKHG1 (also called ARHGEF41), PLEKHG2 (also called ARHGEF42 or CLG/common-site lymphoma/leukemia guanine nucleotide exchange factor2), and PLEKHG3 (also called ARHGEF43) have RhoGEF DH/double-homology domains in tandem with a PH domain which is involved in phospholipid binding. They function as a guanine nucleotide exchange factor (GEF) and are involved in the regulation of Rho protein signal transduction. Mutations in PLEKHG1 have been associated panic disorder (PD), an anxiety disorder characterized by panic attacks and anticipatory anxiety. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270063 [Multi-domain]  Cd Length: 147  Bit Score: 40.03  E-value: 1.82e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366  709 LLKDSFmveLVEGARKLRHVFLFTDLLLCTKlKKQSGGktqqYDCKWYIPLTDLsfqMVdeLEAVPNIPL 778
Cdd:cd13243    53 VLEGTF---RMAGAKNERLLFLFDKMLLITK-KREDGI----LQYKTHIMCSNL---ML--SESIPKEPL 109
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
80-153 2.19e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 42.17  E-value: 2.19e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 143811366   80 AAQAPDGASEPRAsasRPQPAPADGADPPPAEEPEARPDGEGSPGKARPGTARRPGAAASGERddRGPPASVAA 153
Cdd:PRK12323  388 AAAAPAAAAPAPA---APPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGA--PAPAPAPAA 456
PHA03247 PHA03247
large tegument protein UL36; Provisional
78-171 2.27e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.62  E-value: 2.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366   78 RRAAQAPDGASEPRASASrPQPAPADGADPPPAEEPeARPDGEGSPGKARPGTARRPGAAASgerDDRGPPASVAALRSn 157
Cdd:PHA03247  406 RPAAPVPASVPTPAPTPV-PASAPPPPATPLPSAEP-GSDDGPAPPPERQPPAPATEPAPDD---PDDATRKALDALRE- 479
                          90
                  ....*....|....
gi 143811366  158 feriRKGHGQPGAD 171
Cdd:PHA03247  480 ----RRPPEPPGAD 489
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
78-163 2.33e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 42.01  E-value: 2.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366   78 RRAAQAPDGASEPRASASR-PQPAPAdGADPPPAEEPEARPdgegSPGKARPGTARRPGAAASGERDDRGPPASVAALRS 156
Cdd:PRK14951  383 RPEAAAPAAAPVAQAAAAPaPAAAPA-AAASAPAAPPAAAP----PAPVAAPAAAAPAAAPAAAPAAVALAPAPPAQAAP 457

                  ....*..
gi 143811366  157 NFERIRK 163
Cdd:PRK14951  458 ETVAIPV 464
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
79-153 2.82e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 41.90  E-value: 2.82e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 143811366   79 RAAQAPDGASEPRASASRPQPAPADGADPPPAEEPEARPDGEGSPGkARPGTARRPGAAASGERDDRGPPASVAA 153
Cdd:PRK07764  428 APQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAA-PEPTAAPAPAPPAAPAPAAAPAAPAAPA 501
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
78-173 3.05e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 42.08  E-value: 3.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366   78 RRAAQAPDGASEPRASASRPQPAPADGADPPPAEEPEARPdgEGSPGKARPGTARRPGAAASGERddRGPPASVAALRSN 157
Cdd:PHA03307  146 PPPAASPPAAGASPAAVASDAASSRQAALPLSSPEETARA--PSSPPAEPPPSTPPAAASPRPPR--RSSPISASASSPA 221
                          90
                  ....*....|....*.
gi 143811366  158 FERIRKGHGQPGADAE 173
Cdd:PHA03307  222 PAPGRSAADDAGASSS 237
PHA03169 PHA03169
hypothetical protein; Provisional
82-146 3.14e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 41.49  E-value: 3.14e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 143811366   82 QAPDGASEPRASASRPQPAPADGADPPPAEEPEARPDGEGSPGKARPGTARRPGAAASGERDDRG 146
Cdd:PHA03169  161 QQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDEPGEPQSPTPQQAPSP 225
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
80-153 3.82e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 41.51  E-value: 3.82e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 143811366   80 AAQAPDGASEPRASASRPQPAPADGADPPPAEEPEARPdgegspgkARPGTARRPGAAASGERDDRGPPASVAA 153
Cdd:PRK07764  389 GGAGAPAAAAPSAAAAAPAAAPAPAAAAPAAAAAPAPA--------AAPQPAPAPAPAPAPPSPAGNAPAGGAP 454
motB PRK05996
MotB family protein;
78-153 3.89e-03

MotB family protein;


Pssm-ID: 235665 [Multi-domain]  Cd Length: 423  Bit Score: 41.22  E-value: 3.89e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 143811366   78 RRAAQAPDGASEPrASASRPQPAPADGADPPPAEEPEARPDGEGSPGKArpgtarrPGAAASGERDDRGPPASVAA 153
Cdd:PRK05996  206 EQAQGAKSATAAP-ATVPQAAPLPQAQPKKAATEEELIADAKKAATGEP-------AANAAKAAKPEPMPDDQQKE 273
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
80-151 4.57e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 41.12  E-value: 4.57e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 143811366   80 AAQAPDGASEPRASASRPQPAPADGADPPPAEEPEARPDGEGSPGKARPGTARRPGAAASGERDDRGPPASV 151
Cdd:PRK07764  668 GWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPV 739
kgd PRK12270
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ...
65-153 5.34e-03

multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;


Pssm-ID: 237030 [Multi-domain]  Cd Length: 1228  Bit Score: 41.03  E-value: 5.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366   65 KEKKSYDRQRWGF---RRAAQAPDGASEPRASASRPQPAPADGADPPPAEEPEARPDGEGSPGKARPGTARRPGAAASGE 141
Cdd:PRK12270   20 ADPNSVDPSWREFfadYGPGSTAAPTAAAAAAAAAASAPAAAPAAKAPAAPAPAPPAAAAPAAPPKPAAAAAAAAAPAAP 99
                          90
                  ....*....|..
gi 143811366  142 RDDRGPPASVAA 153
Cdd:PRK12270  100 PAAAAAAAPAAA 111
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
64-172 6.52e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 40.92  E-value: 6.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366   64 AKEKKSYDRQRWGFRRA---AQAPDGASEPRASASRPQPAPADGADPPPAEEPEARPDGEGSPGKARPGTARRPGAAASG 140
Cdd:PHA03307  816 ASKRKSRSHTPDGGSESsgpARPPGAAARPPPARSSESSKSKPAAAGGRARGKNGRRRPRPPEPRARPGAAAPPKAAAAA 895
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 143811366  141 ERD----DRGPPASVAAL----------RSNFERIRKG--HGQPGADA 172
Cdd:PHA03307  896 PPAgapaPRPRPAPRVKLgpmppggpdpRGGFRRVPPGdlHTPAPSAA 943
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
74-175 7.28e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 40.74  E-value: 7.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366   74 RWGFRrAAQAPDGAS----EPRASASRPQPAPADGADPPPAEEPEARPDGEGSPGKARPGTARRPGAAASGERDDRGPPA 149
Cdd:PRK07764  581 DWQVE-AVVGPAPGAaggeGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAV 659
                          90       100
                  ....*....|....*....|....*.
gi 143811366  150 SVAALRSNFERIRKGHGQPGADAEKP 175
Cdd:PRK07764  660 PDASDGGDGWPAKAGGAAPAAPPPAP 685
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
75-153 7.47e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 40.74  E-value: 7.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366   75 WGFRRAAQAPDGASEPRASASRPQPAPADGADPPPAEEPEARPDGE-GSPGKARPGTARRPGAAASGERDDRGPPASVAA 153
Cdd:PRK07764  657 VAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPApAPAATPPAGQADDPAAQPPQAAQGASAPSPAAD 736
C2A_fungal cd04041
C2 domain first repeat; fungal group; C2 domains were first identified in Protein Kinase C ...
911-1016 8.96e-03

C2 domain first repeat; fungal group; C2 domains were first identified in Protein Kinase C (PKC). C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


Pssm-ID: 176006 [Multi-domain]  Cd Length: 111  Bit Score: 37.24  E-value: 8.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 143811366  911 GFLNVIVHSATGFKQ------SSNLYCTLEVDSFGYFVnkAKTRVYRDTAEPNWNEEFEI-----ELEGSQTLRILCYEk 979
Cdd:cd04041     1 GVLVVTIHRATDLPKadfgtgSSDPYVTASFAKFGKPL--YSTRIIRKDLNPVWEETWFVlvtpdEVKAGERLSCRLWD- 77
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 143811366  980 cynktkipkEDGESTDRLMGKGQVQLDPqALQDRDWQ 1016
Cdd:cd04041    78 ---------SDRFTADDRLGRVEIDLKE-LIEDRNWM 104
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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