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Conserved domains on  [gi|1953103015|ref|XP_038443536|]
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stAR-related lipid transfer protein 8 isoform X4 [Canis lupus familiaris]

Protein Classification

SRPBCC family protein; START domain-containing protein( domain architecture ID 10175859)

SRPBCC (START/RHOalphaC/PITP/Bet v1/CoxG/CalC) family protein may have a deep hydrophobic ligand-binding pocket; START (steroidogenic acute regulatory protein (StAR)-related lipid transfer) domain-containing protein may bind lipids

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SRPBCC super family cl14643
START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC (SRPBCC) ligand-binding domain superfamily; SRPBCC ...
 881-1085 2.72e-142

START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC (SRPBCC) ligand-binding domain superfamily; SRPBCC domains have a deep hydrophobic ligand-binding pocket; they bind diverse ligands. Included in this superfamily are the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD1-STARD15, and the C-terminal catalytic domains of the alpha oxygenase subunit of Rieske-type non-heme iron aromatic ring-hydroxylating oxygenases (RHOs_alpha_C), as well as the SRPBCC domains of phosphatidylinositol transfer proteins (PITPs), Bet v 1 (the major pollen allergen of white birch, Betula verrucosa), CoxG, CalC, and related proteins. Other members of this superfamily include PYR/PYL/RCAR plant proteins, the aromatase/cyclase (ARO/CYC) domains of proteins such as Streptomyces glaucescens tetracenomycin, and the SRPBCC domains of Streptococcus mutans Smu.440 and related proteins.


The actual alignment was detected with superfamily member cd08907:

Pssm-ID: 472699  Cd Length: 205  Bit Score: 425.49  E-value: 2.72e-142
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953103015  881 QAAGISLSLYMEESVQELLRDAAERFKGWMSMPGPQHTELACRKAPDGHPLRVWKVSTEVAAPPPVVLHRVLRERALWDE 960
Cdd:cd08907      1 QGEGVDLRAYLEDNVQCLLREASERFKGWHSAPGPDNTELACKKVGDGHPLRLWKVSTEVEAPPSVVLQRVLRERHLWDE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953103015  961 DLLRAQVLEALMPGVELYHYVTDSMAPHPCRDFVVLRMWRSDLPRGGCLLVSQSLDPEQPVPESGVRAMMLTSQYLMEPC 1040
Cdd:cd08907     81 DLLHSQVIEALENNTEVYHYVTDSMAPHPRRDFVVLRMWRSDLPRGGCLLVSQSVDHDNPQLEAGVRAVLLTSQYLIEPC 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1953103015 1041 GLGRSRLTHICRADLRGRSPDWYNKVFGHLCAMEVAKIRDSFPTL 1085
Cdd:cd08907    161 GMGRSRLTHICRADLRGRSPDWYNKVFGHLCAMEVARIRDSFPTL 205
RhoGAP super family cl02570
RhoGAP: GTPase-activator protein (GAP) for Rho-like GTPases; GAPs towards Rho/Rac/Cdc42-like ...
 640-854 2.39e-110

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.


The actual alignment was detected with superfamily member cd04375:

Pssm-ID: 470621  Cd Length: 220  Bit Score: 342.09  E-value: 2.39e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953103015  640 VFGVPPLIHVQRTGQPLPQSIQQAMRYLRSQCLDQVGIFRKSGVKSRIQNLRQMNEANPDHVCYEGQSAYDVADLLKQYF 719
Cdd:cd04375      4 VFGVPLLVNLQRTGQPLPRSIQQAMRWLRNNALDQVGLFRKSGVKSRIQKLRSMIESSTDNVNYDGQQAYDVADMLKQYF 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953103015  720 RDLPEPIFTSKLTTTFLQIYQLLPKDQWLAAAQAATLLLPDENREVLQTLLYFLSDIAS-AEENQMTAGNLAVCLAPSIF 798
Cdd:cd04375     84 RDLPEPLLTNKLSETFIAIFQYVPKEQRLEAVQCAILLLPDENREVLQTLLYFLSDVAAnSQENQMTATNLAVCLAPSLF 163

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1953103015  799 HLNVSKKD-SPSPRIRSKRSLVGRPGPRDLSENMAATQGLSHMISDCKKLFQVPQDM 854
Cdd:cd04375    164 HLNTSRREnSSPARRMQRKKSLGKPDQKELSENKAAHQCLAYMIEECNTLFMVPKEM 220
SAM_DLC1,2-like cd09538
SAM domain of DLC1,2-like subfamily; SAM (sterile alpha motif) domain of DLC-1,2-like (Deleted ...
 18-77 1.15e-32

SAM domain of DLC1,2-like subfamily; SAM (sterile alpha motif) domain of DLC-1,2-like (Deleted in liver cancer) subfamily is a protein-protein interaction domain located at the N-terminus of the protein. Members of this subfamily do not form dimers/oligomers through their SAM domains. They participate in regulation of cell migration and lipid transfer. SAM domain of human DLC1 protein contains the EF1A1 (eukaryotic elongation factor) binding motif, thus SAM facilitates recruitment of EF1A1 to the membrane periphery and suppresses cell migration. Human Dlc2 gene is known as a tumor suppressor gene. It was found underexpressed in hepatocellular carcinoma.


:

Pssm-ID: 188937  Cd Length: 60  Bit Score: 120.60  E-value: 1.15e-32
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953103015   18 KRACKWLRATGFPQYAQLFEEGLFPLDIGSVKKDHSFLDKDSLGALCRRLMTLNNCASMK 77
Cdd:cd09538      1 KEACKWLRAAGFPQYAQLYEDSQFPIDISAVKRDHDFLDRDSLQALIRRLNTLNKCASMK 60
 
Name Accession Description Interval E-value
START_STARD8-like cd08907
C-terminal lipid-binding START domain of mammalian STARD8 and related proteins, which also ...
 881-1085 2.72e-142

C-terminal lipid-binding START domain of mammalian STARD8 and related proteins, which also have an N-terminal Rho GTPase-activating protein (RhoGAP) domain; This subgroup includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of STARD8 (also known as deleted in liver cancer 3/DLC3, and Arhgap38) and related proteins. It belongs to the START domain family, and in turn to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. Proteins belonging to this subfamily also have a RhoGAP domain. The precise function of the START domain in this subgroup is unclear.


Pssm-ID: 176916  Cd Length: 205  Bit Score: 425.49  E-value: 2.72e-142
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953103015  881 QAAGISLSLYMEESVQELLRDAAERFKGWMSMPGPQHTELACRKAPDGHPLRVWKVSTEVAAPPPVVLHRVLRERALWDE 960
Cdd:cd08907      1 QGEGVDLRAYLEDNVQCLLREASERFKGWHSAPGPDNTELACKKVGDGHPLRLWKVSTEVEAPPSVVLQRVLRERHLWDE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953103015  961 DLLRAQVLEALMPGVELYHYVTDSMAPHPCRDFVVLRMWRSDLPRGGCLLVSQSLDPEQPVPESGVRAMMLTSQYLMEPC 1040
Cdd:cd08907     81 DLLHSQVIEALENNTEVYHYVTDSMAPHPRRDFVVLRMWRSDLPRGGCLLVSQSVDHDNPQLEAGVRAVLLTSQYLIEPC 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1953103015 1041 GLGRSRLTHICRADLRGRSPDWYNKVFGHLCAMEVAKIRDSFPTL 1085
Cdd:cd08907    161 GMGRSRLTHICRADLRGRSPDWYNKVFGHLCAMEVARIRDSFPTL 205
RhoGAP_DLC1 cd04375
RhoGAP_DLC1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 640-854 2.39e-110

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: 342.09  E-value: 2.39e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953103015  640 VFGVPPLIHVQRTGQPLPQSIQQAMRYLRSQCLDQVGIFRKSGVKSRIQNLRQMNEANPDHVCYEGQSAYDVADLLKQYF 719
Cdd:cd04375      4 VFGVPLLVNLQRTGQPLPRSIQQAMRWLRNNALDQVGLFRKSGVKSRIQKLRSMIESSTDNVNYDGQQAYDVADMLKQYF 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953103015  720 RDLPEPIFTSKLTTTFLQIYQLLPKDQWLAAAQAATLLLPDENREVLQTLLYFLSDIAS-AEENQMTAGNLAVCLAPSIF 798
Cdd:cd04375     84 RDLPEPLLTNKLSETFIAIFQYVPKEQRLEAVQCAILLLPDENREVLQTLLYFLSDVAAnSQENQMTATNLAVCLAPSLF 163

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1953103015  799 HLNVSKKD-SPSPRIRSKRSLVGRPGPRDLSENMAATQGLSHMISDCKKLFQVPQDM 854
Cdd:cd04375    164 HLNTSRREnSSPARRMQRKKSLGKPDQKELSENKAAHQCLAYMIEECNTLFMVPKEM 220
START smart00234
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ...
 890-1087 9.14e-57

in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and phosphatidylcholine transfer protein


Pssm-ID: 214575  Cd Length: 205  Bit Score: 194.96  E-value: 9.14e-57
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953103015   890 YMEESVQELLRDAAERFKGWMSMPgPQHTELACRKAP-----DGHPLRVWKVSTEVAAPPPVVLHRVLRERALWDEDLLR 964
Cdd:smart00234    1 VAEEAAAELLKMAAASEEGWVLSS-ENENGDEVRSIFspgrkPGEAFRLVGVVPMVCADLVEELMDDLEYRPEWDKNVAK 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953103015   965 AQVLEALMPGVELYHYVTDSMA-PHPCRDFVVLRMWRSDlPRGGCLLVSQSLDPEQPVPESG-VRAMMLTSQYLMEPCGL 1042
Cdd:smart00234   80 AETLEVIDNGTVIYHYVSKFAAgPVSPRDFVFVRYWRED-EDGSYAVVDVSVTHPTSPPESGyVRAENLPSGLLIEPLGN 158

                           170       180       190       200
                    ....*....|....*....|....*....|....*....|....*
gi 1953103015  1043 GRSRLTHICRADLRGRSPDWYNKVFGHLCAMEVAKirDSFPTLQA 1087
Cdd:smart00234  159 GPSKVTWVSHADLKGWLPHWLVRSLIKSGLAEFAK--TLVATLQK 201
START pfam01852
START domain;
889-1082 1.16e-56

START domain;


Pssm-ID: 426476  Cd Length: 205  Bit Score: 194.54  E-value: 1.16e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953103015  889 LYMEESVQELLRDAAERFKGWMSMPGpQHTELACRKAPD---GHPLRVWKVSTEVAAPPP-VVLHRVLReRALWDEDLLR 964
Cdd:pfam01852    1 ELAEEAAQELLKLALSDEPGWVLLSS-NENGDVVLQIVEpdhGEASRASGVVPMVAALLVaELLKDMEY-RAQWDKDVRS 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953103015  965 AQVLEALMPGVELYHYVTDSMA--PHPCRDFVVLRMWRSDlPRGGCLLVSQSLDPEQPVPESG-VRAMMLTSQYLMEPCG 1041
Cdd:pfam01852   79 AETLEVISSGGDLQYYVAALVApsPLSPRDFVFLRYWRRL-GGGVYVIVDRSVTHPQFPPSSGyVRAERLPSGYLIQPCG 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1953103015 1042 LGRSRLTHICRADLRGRSPDWYNKVFGHLCAMEVAKIRDSF 1082
Cdd:pfam01852  158 NGPSKVTWVSHADLKGWLPSWLLRSLYKSGMPEGAKTWVAT 198
RhoGAP smart00324
GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac ...
 654-809 1.49e-43

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: 155.89  E-value: 1.49e-43
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953103015   654 QPLPQSIQQAMRYLRSQCLDQVGIFRKSGVKSRIQNLRQMNEANPD-HVCYEGQSAYDVADLLKQYFRDLPEPIFTSKLT 732
Cdd:smart00324    1 KPIPIIVEKCIEYLEKRGLDTEGIYRVSGSKSRVKELRDAFDSGPDpDLDLSEYDVHDVAGLLKLFLRELPEPLITYELY 80

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1953103015   733 TTFLQIYQLLPKDQWLAAAQAATLLLPDENREVLQTLLYFLSDIAS-AEENQMTAGNLAVCLAPSIFHLNVSKKDSPS 809
Cdd:smart00324   81 EEFIEAAKLEDETERLRALRELLSLLPPANRATLRYLLAHLNRVAEhSEENKMTARNLAIVFGPTLLRPPDGEVASLK 158
RhoGAP pfam00620
RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.
 657-799 1.37e-38

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


Pssm-ID: 459875  Cd Length: 148  Bit Score: 140.76  E-value: 1.37e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953103015  657 PQSIQQAMRYLRSQCLDQVGIFRKSGVKSRIQNLRQMNEANPD-HVCYEGQSAYDVADLLKQYFRDLPEPIFTSKLTTTF 735
Cdd:pfam00620    1 PLIVRKCVEYLEKRGLDTEGIFRVSGSASRIKELREAFDRGPDvDLDLEEEDVHVVASLLKLFLRELPEPLLTFELYEEF 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953103015  736 LQIYQLLPKDQWLAAAQAATLLLPDENREVLQTLLYFLSDIAS-AEENQMTAGNLAVCLAPSIFH 799
Cdd:pfam00620   81 IEAAKLPDEEERLEALRELLRKLPPANRDTLRYLLAHLNRVAQnSDVNKMNAHNLAIVFGPTLLR 145
SAM_DLC1,2-like cd09538
SAM domain of DLC1,2-like subfamily; SAM (sterile alpha motif) domain of DLC-1,2-like (Deleted ...
 18-77 1.15e-32

SAM domain of DLC1,2-like subfamily; SAM (sterile alpha motif) domain of DLC-1,2-like (Deleted in liver cancer) subfamily is a protein-protein interaction domain located at the N-terminus of the protein. Members of this subfamily do not form dimers/oligomers through their SAM domains. They participate in regulation of cell migration and lipid transfer. SAM domain of human DLC1 protein contains the EF1A1 (eukaryotic elongation factor) binding motif, thus SAM facilitates recruitment of EF1A1 to the membrane periphery and suppresses cell migration. Human Dlc2 gene is known as a tumor suppressor gene. It was found underexpressed in hepatocellular carcinoma.


Pssm-ID: 188937  Cd Length: 60  Bit Score: 120.60  E-value: 1.15e-32
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953103015   18 KRACKWLRATGFPQYAQLFEEGLFPLDIGSVKKDHSFLDKDSLGALCRRLMTLNNCASMK 77
Cdd:cd09538      1 KEACKWLRAAGFPQYAQLYEDSQFPIDISAVKRDHDFLDRDSLQALIRRLNTLNKCASMK 60
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
16-77 9.15e-03

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 35.71  E-value: 9.15e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1953103015   16 EAKRACKWLRATGFPQYAQLFEEGLFPLDIGSVKKDHSFLDKDSLGALCRRLMTLNNCASMK 77
Cdd:pfam07647    5 SLESVADWLRSIGLEQYTDNFRDQGITGAELLLRLTLEDLKRLGITSVGHRRKILKKIQELK 66
 
Name Accession Description Interval E-value
START_STARD8-like cd08907
C-terminal lipid-binding START domain of mammalian STARD8 and related proteins, which also ...
 881-1085 2.72e-142

C-terminal lipid-binding START domain of mammalian STARD8 and related proteins, which also have an N-terminal Rho GTPase-activating protein (RhoGAP) domain; This subgroup includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of STARD8 (also known as deleted in liver cancer 3/DLC3, and Arhgap38) and related proteins. It belongs to the START domain family, and in turn to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. Proteins belonging to this subfamily also have a RhoGAP domain. The precise function of the START domain in this subgroup is unclear.


Pssm-ID: 176916  Cd Length: 205  Bit Score: 425.49  E-value: 2.72e-142
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953103015  881 QAAGISLSLYMEESVQELLRDAAERFKGWMSMPGPQHTELACRKAPDGHPLRVWKVSTEVAAPPPVVLHRVLRERALWDE 960
Cdd:cd08907      1 QGEGVDLRAYLEDNVQCLLREASERFKGWHSAPGPDNTELACKKVGDGHPLRLWKVSTEVEAPPSVVLQRVLRERHLWDE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953103015  961 DLLRAQVLEALMPGVELYHYVTDSMAPHPCRDFVVLRMWRSDLPRGGCLLVSQSLDPEQPVPESGVRAMMLTSQYLMEPC 1040
Cdd:cd08907     81 DLLHSQVIEALENNTEVYHYVTDSMAPHPRRDFVVLRMWRSDLPRGGCLLVSQSVDHDNPQLEAGVRAVLLTSQYLIEPC 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1953103015 1041 GLGRSRLTHICRADLRGRSPDWYNKVFGHLCAMEVAKIRDSFPTL 1085
Cdd:cd08907    161 GMGRSRLTHICRADLRGRSPDWYNKVFGHLCAMEVARIRDSFPTL 205
START_RhoGAP cd08869
C-terminal lipid-binding START domain of mammalian STARD8, -12, -13 and related proteins, ...
 890-1085 2.17e-114

C-terminal lipid-binding START domain of mammalian STARD8, -12, -13 and related proteins, which also have an N-terminal Rho GTPase-activating protein (RhoGAP) domain; This subfamily includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of STARD8 (also known as deleted in liver cancer 3/DLC3, and Arhgap38), STARD12 (also known as DLC-1, Arhgap7, and p122-RhoGAP), and STARD13 (also known as DLC-2, Arhgap37, and SDCCAG13). The START domain family belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. Proteins belonging to this subfamily also have a RhoGAP domain. Some, including STARD12, -and -13, also have an N-terminal SAM (sterile alpha motif) domain; these have a SAM-RhoGAP-START domain organization. This subfamily is involved in cancer development. A large spectrum of cancers have dysregulated genes encoding these proteins. The precise function of the START domain in this subfamily is unclear.


Pssm-ID: 176878  Cd Length: 197  Bit Score: 352.00  E-value: 2.17e-114
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953103015  890 YMEESVQELLRDAAERFKGWMSMPGPQHTELACRKAPDGHPLRVWKVSTEVAAPPPVVLHRVLRERALWDEDLLRAQVLE 969
Cdd:cd08869      2 YLERCVQDLLREARDKSKGWVSVSSSDHVELAFKKVDDGHPLRLWRASTEVEAPPEEVLQRILRERHLWDDDLLQWKVVE 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953103015  970 ALMPGVELYHYVTDSMAPHPCRDFVVLRMWRSDLPRGGCLLVSQSLDPEQPVPESGVRAMMLTSQYLMEPCGLGRSRLTH 1049
Cdd:cd08869     82 TLDEDTEVYQYVTNSMAPHPTRDYVVLRTWRTDLPKGACVLVETSVEHTEPVPLGGVRAVVLASRYLIEPCGSGKSRVTH 161

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1953103015 1050 ICRADLRGRSPDWYNKVFGHLCAMEVAKIRDSFPTL 1085
Cdd:cd08869    162 ICRVDLRGRSPEWYNKVYGHLCARELLRIRDSFRQL 197
RhoGAP_DLC1 cd04375
RhoGAP_DLC1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 640-854 2.39e-110

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: 342.09  E-value: 2.39e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953103015  640 VFGVPPLIHVQRTGQPLPQSIQQAMRYLRSQCLDQVGIFRKSGVKSRIQNLRQMNEANPDHVCYEGQSAYDVADLLKQYF 719
Cdd:cd04375      4 VFGVPLLVNLQRTGQPLPRSIQQAMRWLRNNALDQVGLFRKSGVKSRIQKLRSMIESSTDNVNYDGQQAYDVADMLKQYF 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953103015  720 RDLPEPIFTSKLTTTFLQIYQLLPKDQWLAAAQAATLLLPDENREVLQTLLYFLSDIAS-AEENQMTAGNLAVCLAPSIF 798
Cdd:cd04375     84 RDLPEPLLTNKLSETFIAIFQYVPKEQRLEAVQCAILLLPDENREVLQTLLYFLSDVAAnSQENQMTATNLAVCLAPSLF 163

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1953103015  799 HLNVSKKD-SPSPRIRSKRSLVGRPGPRDLSENMAATQGLSHMISDCKKLFQVPQDM 854
Cdd:cd04375    164 HLNTSRREnSSPARRMQRKKSLGKPDQKELSENKAAHQCLAYMIEECNTLFMVPKEM 220
START_STARD13-like cd08909
C-terminal lipid-binding START domain of mammalian STARD13 and related proteins, which also ...
 884-1085 1.64e-90

C-terminal lipid-binding START domain of mammalian STARD13 and related proteins, which also have an N-terminal Rho GTPase-activating protein (RhoGAP) domain; This subgroup includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of STARD13 (also known as DLC-2, Arhgap37, and SDCCAG13) and related proteins. It belongs to the START domain family, and in turn to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. Proteins belonging to this subfamily also have a RhoGAP domain. The precise function of the START domain in this subgroup is unclear.


Pssm-ID: 176918  Cd Length: 205  Bit Score: 288.74  E-value: 1.64e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953103015  884 GISLSLYMEESVQELLRDAAERFKGWMSMPGPQHTELACRKAPDGHPLRVWKVSTEVAAPPPVVLHRVLRERALWDEDLL 963
Cdd:cd08909      4 GGTYQTYLESLIQNLQKEAKEKFKGWISCSSSDNTELAYKKVGDGNPLRLWKVSVEVEAPPSVVLNRVLRERHLWDEDFL 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953103015  964 RAQVLEALMPGVELYHYVTDSMAPHPCRDFVVLRMWRSDLPRGGCLLVSQSLDPEQPVPESGVRAMMLTSQYLMEPCGLG 1043
Cdd:cd08909     84 QWKVVETLDKQTEVYQYVLNCMAPHPSRDFVVLRSWRTDLPKGACSLVSVSVEHEEAPLLGGVRAVVLDSQYLIEPCGSG 163

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1953103015 1044 RSRLTHICRADLRGRSPDWYNKVFGHLCAMEVAKIRDSFPTL 1085
Cdd:cd08909    164 KSRLTHICRVDLKGHSPEWYNKGFGHLCAAEAARIRNSFQPL 205
START_STARD12-like cd08908
C-terminal lipid-binding START domain of mammalian STARD12 and related proteins, which also ...
 890-1082 1.45e-74

C-terminal lipid-binding START domain of mammalian STARD12 and related proteins, which also have an N-terminal Rho GTPase-activating protein (RhoGAP) domain; This subgroup includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of STARD12 (also known as DLC-1, Arhgap7, and p122-RhoGAP) and related proteins. It belongs to the START domain family, and in turn to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. Proteins belonging to this subgroup also have an N-terminal SAM (sterile alpha motif) domain and a RhoGAP domain, and have a SAM-RhoGAP-START domain organization. The precise function of the START domain in this subgroup is unclear.


Pssm-ID: 176917  Cd Length: 204  Bit Score: 244.92  E-value: 1.45e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953103015  890 YMEESVQELLRDAAERFKGWMSMPGPQHTELACRKAPDGHPLRVWKVSTEVAAPPPVVLHRVLRERALWDEDLLRAQVLE 969
Cdd:cd08908     10 FLQDCVDGLFKEVKEKFKGWVSYSTSEQAELSYKKVSEGPPLRLWRTTIEVPAAPEEILKRLLKEQHLWDVDLLDSKVIE 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953103015  970 ALMPGVELYHYVTDSMAPHPCRDFVVLRMWRSDLPRGGCLLVSQSLDPEQpVPESGVRAMMLTSQYLMEPCGLGRSRLTH 1049
Cdd:cd08908     90 ILDSQTEIYQYVQNSMAPHPARDYVVLRTWRTNLPKGACALLATSVDHDR-APVAGVRVNVLLSRYLIEPCGSGKSKLTY 168

                          170       180       190
                   ....*....|....*....|....*....|...
gi 1953103015 1050 ICRADLRGRSPDWYNKVFGHLCAMEVAKIRDSF 1082
Cdd:cd08908    169 MCRIDLRGHMPEWYTKSFGHLCAAEVVKIRDSF 201
START smart00234
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ...
 890-1087 9.14e-57

in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and phosphatidylcholine transfer protein


Pssm-ID: 214575  Cd Length: 205  Bit Score: 194.96  E-value: 9.14e-57
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953103015   890 YMEESVQELLRDAAERFKGWMSMPgPQHTELACRKAP-----DGHPLRVWKVSTEVAAPPPVVLHRVLRERALWDEDLLR 964
Cdd:smart00234    1 VAEEAAAELLKMAAASEEGWVLSS-ENENGDEVRSIFspgrkPGEAFRLVGVVPMVCADLVEELMDDLEYRPEWDKNVAK 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953103015   965 AQVLEALMPGVELYHYVTDSMA-PHPCRDFVVLRMWRSDlPRGGCLLVSQSLDPEQPVPESG-VRAMMLTSQYLMEPCGL 1042
Cdd:smart00234   80 AETLEVIDNGTVIYHYVSKFAAgPVSPRDFVFVRYWRED-EDGSYAVVDVSVTHPTSPPESGyVRAENLPSGLLIEPLGN 158

                           170       180       190       200
                    ....*....|....*....|....*....|....*....|....*
gi 1953103015  1043 GRSRLTHICRADLRGRSPDWYNKVFGHLCAMEVAKirDSFPTLQA 1087
Cdd:smart00234  159 GPSKVTWVSHADLKGWLPHWLVRSLIKSGLAEFAK--TLVATLQK 201
START pfam01852
START domain;
889-1082 1.16e-56

START domain;


Pssm-ID: 426476  Cd Length: 205  Bit Score: 194.54  E-value: 1.16e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953103015  889 LYMEESVQELLRDAAERFKGWMSMPGpQHTELACRKAPD---GHPLRVWKVSTEVAAPPP-VVLHRVLReRALWDEDLLR 964
Cdd:pfam01852    1 ELAEEAAQELLKLALSDEPGWVLLSS-NENGDVVLQIVEpdhGEASRASGVVPMVAALLVaELLKDMEY-RAQWDKDVRS 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953103015  965 AQVLEALMPGVELYHYVTDSMA--PHPCRDFVVLRMWRSDlPRGGCLLVSQSLDPEQPVPESG-VRAMMLTSQYLMEPCG 1041
Cdd:pfam01852   79 AETLEVISSGGDLQYYVAALVApsPLSPRDFVFLRYWRRL-GGGVYVIVDRSVTHPQFPPSSGyVRAERLPSGYLIQPCG 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1953103015 1042 LGRSRLTHICRADLRGRSPDWYNKVFGHLCAMEVAKIRDSF 1082
Cdd:pfam01852  158 NGPSKVTWVSHADLKGWLPSWLLRSLYKSGMPEGAKTWVAT 198
RhoGAP smart00324
GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac ...
 654-809 1.49e-43

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: 155.89  E-value: 1.49e-43
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953103015   654 QPLPQSIQQAMRYLRSQCLDQVGIFRKSGVKSRIQNLRQMNEANPD-HVCYEGQSAYDVADLLKQYFRDLPEPIFTSKLT 732
Cdd:smart00324    1 KPIPIIVEKCIEYLEKRGLDTEGIYRVSGSKSRVKELRDAFDSGPDpDLDLSEYDVHDVAGLLKLFLRELPEPLITYELY 80

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1953103015   733 TTFLQIYQLLPKDQWLAAAQAATLLLPDENREVLQTLLYFLSDIAS-AEENQMTAGNLAVCLAPSIFHLNVSKKDSPS 809
Cdd:smart00324   81 EEFIEAAKLEDETERLRALRELLSLLPPANRATLRYLLAHLNRVAEhSEENKMTARNLAIVFGPTLLRPPDGEVASLK 158
RhoGAP cd00159
RhoGAP: GTPase-activator protein (GAP) for Rho-like GTPases; GAPs towards Rho/Rac/Cdc42-like ...
 657-803 1.47e-39

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 [Multi-domain]  Cd Length: 169  Bit Score: 144.37  E-value: 1.47e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953103015  657 PQSIQQAMRYLRSQCLDQVGIFRKSGVKSRIQNLRQMNEANPDHVCYEGQSAYDVADLLKQYFRDLPEPIFTSKLTTTFL 736
Cdd:cd00159      1 PLIIEKCIEYLEKNGLNTEGIFRVSGSASKIEELKKKFDRGEDIDDLEDYDVHDVASLLKLYLRELPEPLIPFELYDEFI 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1953103015  737 QIYQLLPKDQWLAAAQAATLLLPDENREVLQTLLYFLSDIAS-AEENQMTAGNLAVCLAPSIFHLNVS 803
Cdd:cd00159     81 ELAKIEDEEERIEALKELLKSLPPENRDLLKYLLKLLHKISQnSEVNKMTASNLAIVFAPTLLRPPDS 148
RhoGAP pfam00620
RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.
 657-799 1.37e-38

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


Pssm-ID: 459875  Cd Length: 148  Bit Score: 140.76  E-value: 1.37e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953103015  657 PQSIQQAMRYLRSQCLDQVGIFRKSGVKSRIQNLRQMNEANPD-HVCYEGQSAYDVADLLKQYFRDLPEPIFTSKLTTTF 735
Cdd:pfam00620    1 PLIVRKCVEYLEKRGLDTEGIFRVSGSASRIKELREAFDRGPDvDLDLEEEDVHVVASLLKLFLRELPEPLLTFELYEEF 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953103015  736 LQIYQLLPKDQWLAAAQAATLLLPDENREVLQTLLYFLSDIAS-AEENQMTAGNLAVCLAPSIFH 799
Cdd:pfam00620   81 IEAAKLPDEEERLEALRELLRKLPPANRDTLRYLLAHLNRVAQnSDVNKMNAHNLAIVFGPTLLR 145
SAM_DLC1,2-like cd09538
SAM domain of DLC1,2-like subfamily; SAM (sterile alpha motif) domain of DLC-1,2-like (Deleted ...
 18-77 1.15e-32

SAM domain of DLC1,2-like subfamily; SAM (sterile alpha motif) domain of DLC-1,2-like (Deleted in liver cancer) subfamily is a protein-protein interaction domain located at the N-terminus of the protein. Members of this subfamily do not form dimers/oligomers through their SAM domains. They participate in regulation of cell migration and lipid transfer. SAM domain of human DLC1 protein contains the EF1A1 (eukaryotic elongation factor) binding motif, thus SAM facilitates recruitment of EF1A1 to the membrane periphery and suppresses cell migration. Human Dlc2 gene is known as a tumor suppressor gene. It was found underexpressed in hepatocellular carcinoma.


Pssm-ID: 188937  Cd Length: 60  Bit Score: 120.60  E-value: 1.15e-32
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953103015   18 KRACKWLRATGFPQYAQLFEEGLFPLDIGSVKKDHSFLDKDSLGALCRRLMTLNNCASMK 77
Cdd:cd09538      1 KEACKWLRAAGFPQYAQLYEDSQFPIDISAVKRDHDFLDRDSLQALIRRLNTLNKCASMK 60
SAM_DLC2 cd09592
SAM domain of STARD13-like subfamily; SAM (sterile alpha motif) domain of DLC2 (Deleted in ...
 14-77 1.06e-28

SAM domain of STARD13-like subfamily; SAM (sterile alpha motif) domain of DLC2 (Deleted in liver cancer) protein is a lipid-binding and putative protein-protein interaction domain located at the N-terminus of the protein. Members of this subfamily do not form dimers/oligomers through their SAM domains. They participate in lipid transfer. Human Dlc2 gene is known as a tumor suppressor gene. It was found underexpressed in hepatocellular carcinoma.


Pssm-ID: 188991  Cd Length: 64  Bit Score: 109.35  E-value: 1.06e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1953103015   14 KVEAKRACKWLRATGFPQYAQLFEEGLFPLDIGSVKKDHSFLDKDSLGALCRRLMTLNNCASMK 77
Cdd:cd09592      1 EIEAKEACDWLRAAGFPQYAQLYEDSQFPIDIASVKRDHDFLDRDLVEPLCRRLNTLNKCASMK 64
RhoGAP_ARHGAP6 cd04376
RhoGAP_ARHGAP6: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 656-854 5.21e-27

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: 109.84  E-value: 5.21e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953103015  656 LPQSIQQAMRYLRSQCLDQVGIFRKSGVKSRIQNLRQMNEANPDHVCYEGQSAYDVADLLKQYFRDLPEPIFTSKLTTTF 735
Cdd:cd04376      9 VPRLVESCCQHLEKHGLQTVGIFRVGSSKKRVRQLREEFDRGIDVVLDENHSVHDVAALLKEFFRDMPDPLLPRELYTAF 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953103015  736 LQIYQLLPKDQwLAAAQAATLLLPDENREVLQTLLYFLSDIA---------SAEE---NQMTAGNLAVCLAPSIFHlnvs 803
Cdd:cd04376     89 IGTALLEPDEQ-LEALQLLIYLLPPCNCDTLHRLLKFLHTVAehaadsideDGQEvsgNKMTSLNLATIFGPNLLH---- 163

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1953103015  804 kKDSPSPRIRSKRSLvgrpgprDLSENMAATQGLSHMISDCKKLFQVPQDM 854
Cdd:cd04376    164 -KQKSGEREFVQASL-------RIEESTAIINVVQTMIDNYEELFMVSPEL 206
SAM_DLC1 cd09591
SAM domain of DLC1 subfamily; SAM (sterile alpha motif) domain of DLC1 (Deleted in liver ...
 18-77 5.10e-26

SAM domain of DLC1 subfamily; SAM (sterile alpha motif) domain of DLC1 (Deleted in liver cancer) protein is a protein-protein interaction domain located at the N-terminus. Proteins of this subfamily do not form dimers/oligomers through their SAM domains. They participate in regulation of cell migration. SAM domain of human DLC1 protein contains the EF1A1 (eukaryotic elongation factor) binding motif, thus SAM facilitates recruitment of EF1A1 to the membrane periphery and suppresses cell migration.


Pssm-ID: 188990  Cd Length: 60  Bit Score: 101.64  E-value: 5.10e-26
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953103015   18 KRACKWLRATGFPQYAQLFEEGLFPLDIGSVKKDHSFLDKDSLGALCRRLMTLNNCASMK 77
Cdd:cd09591      1 KEACDWLRAAGFPQYAQLYEDLLFPIDIELVKREHDFLDRDAIEALCRRLNTLNKCAVMK 60
RhoGAP_myosin_IX cd04377
RhoGAP_myosin_IX: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 641-797 1.75e-23

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: 99.05  E-value: 1.75e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953103015  641 FGVPpLIHVQRTGQPLPQSIQQAMRYLRSQCLDQVGIFRKSGVKSRIQNLRQMNEANPDHVCYEGQSAYDVADLLKQYFR 720
Cdd:cd04377      1 FGVS-LSSLTSEDRSVPLVLEKLLEHIEMHGLYTEGIYRKSGSANKIKELRQGLDTDPDSVNLEDYPIHVITSVLKQWLR 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1953103015  721 DLPEPIFTSKLTTTFLQIYQLLPKDQWLAAAQAATLLLPDENREVLQTLLYFLSDIASAEE-NQMTAGNLAVCLAPSI 797
Cdd:cd04377     80 ELPEPLMTFELYENFLRAMELEEKQERVRALYSVLEQLPRANLNTLERLIFHLVRVALQEEvNRMSANALAIVFAPCI 157
RhoGAP_ARHGAP18 cd04391
RhoGAP_ARHGAP18: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 640-858 8.92e-23

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: 97.80  E-value: 8.92e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953103015  640 VFGVPPLIHVQRTGQPLPQS-----IQQAMRYLRSQCLDQVGIFRKSGVKSRIQNLRQMNEANpdhvCYEGQ------SA 708
Cdd:cd04391      1 LFGVPLSTLLERDQKKVPGSkvpliFQKLINKLEERGLETEGILRIPGSAQRVKFLCQELEAK----FYEGTflwdqvKQ 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953103015  709 YDVADLLKQYFRDLPEPIFTSKLTTTFLQIYQLLPKDQWLAAAQAATLLLPDENREVLQTLLYFLSD-IASAEENQMTAG 787
Cdd:cd04391     77 HDAASLLKLFIRELPQPLLTVEYLPAFYSVQGLPSKKDQLQALNLLVLLLPEANRDTLKALLEFLQKvVDHEEKNKMNLW 156

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1953103015  788 NLAVCLAPSIFhlnvskkdsPSPRIRSKRSlvgrpgPRDLSE-NMAAT--QGLSHMISDCKKLFQVPQDMVLQL 858
Cdd:cd04391    157 NVAMIMAPNLF---------PPRGKHSKDN------ESLQEEvNMAAGcaNIMRLLIRYQDLLWTVPSFLINQV 215
RhoGAP-ARHGAP11A cd04394
RhoGAP-ARHGAP11A: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 640-801 1.98e-22

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: 96.39  E-value: 1.98e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953103015  640 VFGVP----PLIHVQRTGQpLPQSIQQAMRYLRSQcLDQVGIFRKSGVKSRIQNLRqmNEANPDHVCYEGQSAYDVADLL 715
Cdd:cd04394      1 VFGVPlhslPHSTVPEYGN-VPKFLVDACTFLLDH-LSTEGLFRKSGSVVRQKELK--AKLEGGEACLSSALPCDVAGLL 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953103015  716 KQYFRDLPEPIFTSKLTTTFLQIyQLLPKDQWLAAAQAATL-LLPDENREVLQTLLYFLSDIAS-AEENQMTAGNLAVCL 793
Cdd:cd04394     77 KQFFRELPEPLLPYDLHEALLKA-QELPTDEERKSATLLLTcLLPDEHVNTLRYFFSFLYDVAQrCSENKMDSSNLAVIF 155


                   ....*...
gi 1953103015  794 APSIFHLN 801
Cdd:cd04394    156 APNLFQSE 163
RhoGAP_FAM13A1a cd04393
RhoGAP_FAM13A1a: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 639-800 2.08e-21

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: 92.91  E-value: 2.08e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953103015  639 QVFGVPpLIHVQRTGQP---LPQSIQQAMRYLRSQCLDQVGIFRKSGVKSRIQNLRQMNEANPDHVCYEGQSAYDVADLL 715
Cdd:cd04393      1 KVFGVP-LQELQQAGQPengVPAVVRHIVEYLEQHGLEQEGLFRVNGNAETVEWLRQRLDSGEEVDLSKEADVCSAASLL 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953103015  716 KQYFRDLPEPIFTSKLTTTFLQIYQ-LLPKDQWLAAAQAATLLLPDENREVLQTLLYFLSDIASA-EENQMTAGNLAVCL 793
Cdd:cd04393     80 RLFLQELPEGLIPASLQIRLMQLYQdYNGEDEFGRKLRDLLQQLPPVNYSLLKFLCHFLSNVASQhHENRMTAENLAAVF 159


                   ....*..
gi 1953103015  794 APSIFHL 800
Cdd:cd04393    160 GPDVFHV 166
START cd00177
Lipid-binding START domain of mammalian STARD1-STARD15 and related proteins; This family ...
 923-1082 4.45e-21

Lipid-binding START domain of mammalian STARD1-STARD15 and related proteins; This family includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD1-STARD15, and related domains, such as the START domain of the Arabidopsis homeobox protein GLABRA 2. The mammalian STARDs are grouped into 8 subfamilies. This family belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. For some members of this family, specific lipids that bind in this pocket are known; these include cholesterol (STARD1/STARD3/ STARD4/STARD5), 25-hydroxycholesterol (STARD5), phosphatidylcholine (STARD2/ STARD7/STARD10), phosphatidylethanolamine (STARD10) and ceramides (STARD11). The START domain is found either alone or in association with other domains. Mammalian STARDs participate in the control of various cellular processes including lipid trafficking between intracellular compartments, lipid metabolism, and modulation of signaling events. Mutation or altered expression of STARDs is linked to diseases such as cancer, genetic disorders, and autoimmune disease. The Arabidopsis homeobox protein GLABRA 2 suppresses root hair formation in hairless epidermal root cells.


Pssm-ID: 176851 [Multi-domain]  Cd Length: 193  Bit Score: 92.02  E-value: 4.45e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953103015  923 RKAPDGHPLRVWKVSTEVAAPPPVVLHRV--LRERALWDEDLLRAQVLEALMPGVELYHYVTDSMAPHPCRDFVVLRMWR 1000
Cdd:cd00177     30 TKPYEDSGLKLLKAEGVIPASPEQVFELLmdIDLRKKWDKNFEEFEVIEEIDEHTDIIYYKTKPPWPVSPRDFVYLRRRR 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953103015 1001 sDLPRGGCLLVSQSLD-PEQPVPESGVRAMMLTSQYLMEPCGLGRSRLTHICRADLRGRSPDW-YNKVFGHLCaMEVAKI 1078
Cdd:cd00177    110 -KLDDGTYVIVSKSVDhDSHPKEKGYVRAEIKLSGWIIEPLDPGKTKVTYVLQVDPKGSIPKSlVNSAAKKQL-ASFLKD 187


                   ....
gi 1953103015 1079 RDSF 1082
Cdd:cd00177    188 LRKA 191
RhoGAP_myosin_IXB cd04407
RhoGAP_myosin_IXB: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 655-798 3.25e-20

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: 89.67  E-value: 3.25e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953103015  655 PLPQSIQQAMRYLRSQCLDQVGIFRKSGVKSRIQNLRQMNEANPDHVCYEGQSAYDVADLLKQYFRDLPEPIFTSKLTTT 734
Cdd:cd04407     14 SVPIVLEKLLEHVEMHGLYTEGIYRKSGSANRMKELHQLLQADPENVKLENYPIHAITGLLKQWLRELPEPLMTFAQYND 93

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953103015  735 FLQIYQLLPKDQWLAAAQAATLLLPDENREVLQTLLYFLSDIASAEE-NQMTAGNLAVCLAPSIF 798
Cdd:cd04407     94 FLRAVELPEKQEQLQAIYRVLEQLPTANHNTLERLIFHLVKVALEEDvNRMSPNALAIVFAPCLL 158
RhoGAP_ARAP cd04385
RhoGAP_ARAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
 676-799 1.16e-19

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: 87.75  E-value: 1.16e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953103015  676 GIFRKSGVKSRIQNLRQMNEANPDHV--CYEGQSAYDVADLLKQYFRDLPEPIFTSKLTTTFLQIYQLLPKDQWLAAAQA 753
Cdd:cd04385     35 GIYRKNGKNSSVKKLLEAFRKDARSVqlREGEYTVHDVADVLKRFLRDLPDPLLTSELHAEWIEAAELENKDERIARYKE 114

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1953103015  754 ATLLLPDENREVLQTLLYFLSDIAS-AEENQMTAGNLAVCLAPSIFH 799
Cdd:cd04385    115 LIRRLPPINRATLKVLIGHLYRVQKhSDENQMSVHNLALVFGPTLFQ 161
RhoGAP_fRGD1 cd04398
RhoGAP_fRGD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 641-798 1.41e-19

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: 87.84  E-value: 1.41e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953103015  641 FGVPPLIHVQRTGQPLPQSIQQAMRYLRSQCLDQVGIFRKSGVKSRIQNLRQMNEANPDHVCYEGQSAYD-----VADLL 715
Cdd:cd04398      1 FGVPLEDLILREGDNVPNIVYQCIQAIENFGLNLEGIYRLSGNVSRVNKLKELFDKDPLNVLLISPEDYEsdihsVASLL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953103015  716 KQYFRDLPEPIFTSKLTTTFLQIYQLLPKDQWLAAAQAATLLLPDENREVLQTLLYFLSDIASAE-ENQMTAGNLAVCLA 794
Cdd:cd04398     81 KLFFRELPEPLLTKALSREFIEAAKIEDESRRRDALHGLINDLPDANYATLRALMFHLARIKEHEsVNRMSVNNLAIIWG 160


                   ....
gi 1953103015  795 PSIF 798
Cdd:cd04398    161 PTLM 164
RhoGAP-p50rhoGAP cd04404
RhoGAP-p50rhoGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 639-795 2.16e-19

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 [Multi-domain]  Cd Length: 195  Bit Score: 87.39  E-value: 2.16e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953103015  639 QVFGVPpLIHVQ---RTGQPLPQSIQQAMRYLRSQCLDQVGIFRKSGVKSRIQNLRQM-NEANPDHVcyegQSAYDV--- 711
Cdd:cd04404      4 QQFGVS-LQFLKeknPEQEPIPPVVRETVEYLQAHALTTEGIFRRSANTQVVKEVQQKyNMGEPVDF----DQYEDVhlp 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953103015  712 ADLLKQYFRDLPEPIFTSKLTTTFLQIyQLLPKDQWLAAAQAATLLLPDENREVLQTLLYFLSDIAS-AEENQMTAGNLA 790
Cdd:cd04404     79 AVILKTFLRELPEPLLTFDLYDDIVGF-LNVDKEERVERVKQLLQTLPEENYQVLKYLIKFLVQVSAhSDQNKMTNSNLA 157


                   ....*
gi 1953103015  791 VCLAP 795
Cdd:cd04404    158 VVFGP 162
RhoGAP_nadrin cd04386
RhoGAP_nadrin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 638-797 1.60e-18

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: 85.20  E-value: 1.60e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953103015  638 QQVFGVPPLIHVQRTGQPLPQSIQQAMRYLRSQCLDQVGIFRKSGVKSRIQNLRQMNEANPDHVCY--EGQSAYDVADLL 715
Cdd:cd04386      2 KPVFGTPLEEHLKRTGREIALPIEACVMCLLETGMNEEGLFRVGGGASKLKRLKAALDAGTFSLPLdeFYSDPHAVASAL 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953103015  716 KQYFRDLPEPIFTSKLTTTFLQIYQLLPKDQWLAAAQAATLLLPDENREVLQTLLYFLSDIA-SAEENQMTAGNLAVCLA 794
Cdd:cd04386     82 KSYLRELPDPLLTYNLYEDWVQAANKPDEDERLQAIWRILNKLPRENRDNLRYLIKFLSKLAqKSDENKMSPSNIAIVLA 161


                   ...
gi 1953103015  795 PSI 797
Cdd:cd04386    162 PNL 164
RhoGAP_ARHGAP20 cd04402
RhoGAP_ARHGAP20: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 656-804 1.12e-17

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: 82.35  E-value: 1.12e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953103015  656 LPQSIQQAMRYLRSQCLDQVGIFRKSGVKSRIQNLR-QMNeaNPDHVCYEGQSAYDVADLLKQYFRDLPEPIFTSKLTTT 734
Cdd:cd04402     15 LPKPILDMLSLLYQKGPSTEGIFRRSANAKACKELKeKLN--SGVEVDLKAEPVLLLASVLKDFLRNIPGSLLSSDLYEE 92

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953103015  735 FLQIYQLLPKDQWLAAAQAATLLLPDENREVLQTLLYFLSDIA-SAEENQMTAGNLAVCLAPSIFHLNVSK 804
Cdd:cd04402     93 WMSALDQENEEEKIAELQRLLDKLPRPNVLLLKHLICVLHNISqNSETNKMDAFNLAVCIAPSLLWPPASS 163
RhoGAP_ARHGAP19 cd04392
RhoGAP_ARHGAP19: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 653-852 3.77e-16

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: 78.27  E-value: 3.77e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953103015  653 GQPLPQS----IQQAMRYLrSQCLDQVGIFRKSGVKSRIQNLR-QMNEANPDHVCYEGQSAYDVADLLKQYFRDLPEPIF 727
Cdd:cd04392      2 GAPLTEEgiaqIYQLIEYL-EKNLRVEGLFRKPGNSARQQELRdLLNSGTDLDLESGGFHAHDCATVLKGFLGELPEPLL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953103015  728 TSKLTTTFLQIYQLLPKDQWLAAAQAATLLL------------PDENREVLQTLLYFLSDIASAEE-NQMTAGNLAVCLA 794
Cdd:cd04392     81 THAHYPAHLQIADLCQFDEKGNKTSAPDKERllealqllllllPEENRNLLKLILDLLYQTAKHEDkNKMSADNLALLFT 160

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1953103015  795 PsifHLNVSKKDSPSprirskrslvgrpgprDLSENMAA-TQGLSHMISDCKKLFQVPQ 852
Cdd:cd04392    161 P---HLICPRNLTPE----------------DLHENAQKlNSIVTFMIKHSQKLFKAPA 200
RhoGAP_CdGAP cd04384
RhoGAP_CdGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 640-798 1.43e-15

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: 76.39  E-value: 1.43e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953103015  640 VFGVPPLIHVQRTGQPLPQSIQQAMRYLRSQCLDQvGIFRKSGVKSRIQNLRQM--NEANPDHVCYEG-QSAYDVADLLK 716
Cdd:cd04384      2 VFGCDLTEHLLNSGQDVPQVLKSCTEFIEKHGIVD-GIYRLSGIASNIQRLRHEfdSEQIPDLTKDVYiQDIHSVSSLCK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953103015  717 QYFRDLPEPIFTSKLTTTFLQIYQLLPKDQWLAAAQAATLLLPDENREVLQTLLYFLSDIA-SAEENQMTAGNLAVCLAP 795
Cdd:cd04384     81 LYFRELPNPLLTYQLYEKFSEAVSAASDEERLEKIHDVIQQLPPPHYRTLEFLMRHLSRLAkYCSITNMHAKNLAIVWAP 160


                   ...
gi 1953103015  796 SIF 798
Cdd:cd04384    161 NLL 163
RhoGap_RalBP1 cd04381
RhoGap_RalBP1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 641-797 2.16e-15

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: 75.55  E-value: 2.16e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953103015  641 FGVPPLIHVQRT----GQPLPQSIQQAMRYLRSQCLDQVGIFRKSGVKSRIQNLRQMNEaNPDHVCYEGQSAYDVADLLK 716
Cdd:cd04381      1 FGASLSLAVERSrchdGIDLPLVFRECIDYVEKHGMKCEGIYKVSGIKSKVDELKAAYN-RRESPNLEEYEPPTVASLLK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953103015  717 QYFRDLPEPIFTSKLTTTFLQIYQLLPKDQWLAAAQAATLLLPDENREVLQTLLYFLSDIASAE-ENQMTAGNLAVCLAP 795
Cdd:cd04381     80 QYLRELPEPLLTKELMPRFEEACGRPTEAEREQELQRLLKELPECNRLLLAWLIVHMDHVIAQElETKMNIQNISIVLSP 159


                   ..
gi 1953103015  796 SI 797
Cdd:cd04381    160 TV 161
RhoGAP_fLRG1 cd04397
RhoGAP_fLRG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 641-811 2.44e-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: 2.44e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953103015  641 FGVPPLIHVQRTGQP-----------LPQSIQQAMRYLRSQCLDQVGIFRKSGVKSRIQNLRQMNEANPDHVC-YEGQSA 708
Cdd:cd04397      1 FGVPLEILVEKFGADstlgvgpgklrIPALIDDIISAMRQMDMSVEGVFRKNGNIRRLKELTEEIDKNPTEVPdLSKENP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953103015  709 YDVADLLKQYFRDLPEPIFTSKLTTTFLQIYQLLPKDQWLAAAQAATLLLPDENREVLQTLLYFLSDIAS----AEE--N 782
Cdd:cd04397     81 VQLAALLKKFLRELPDPLLTFKLYRLWISSQKIEDEEERKRVLHLVYCLLPKYHRDTMEVLFSFLKWVSSfshiDEEtgS 160

                          170       180
                   ....*....|....*....|....*....
gi 1953103015  783 QMTAGNLAVCLAPSIFHlnvSKKDSPSPR 811
Cdd:cd04397    161 KMDIHNLATVITPNILY---SKTDNPNTG 186
RhoGAP_srGAP cd04383
RhoGAP_srGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 649-799 7.96e-15

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: 73.99  E-value: 7.96e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953103015  649 VQRTGQPLPQSIQQAMRYLRSQCLDQVGIFRKSGVKSRIQNLRQMNEANPDHVCYEgQSAYD---VADLLKQYFRDLPEP 725
Cdd:cd04383     11 IQDSGQAIPLVVESCIRFINLYGLQHQGIFRVSGSQVEVNDIKNAFERGEDPLADD-QNDHDinsVAGVLKLYFRGLENP 89

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953103015  726 IFTSKLTTTFLQIYQLLPKDQWLAAAQAATLLLPDENREVLQTLLYFLSDIAS-AEENQMTAGNLAVCLAPSIFH 799
Cdd:cd04383     90 LFPKERFEDLMSCVKLENPTERVHQIREILSTLPRSVIIVMRYLFAFLNHLSQfSDENMMDPYNLAICFGPTLMP 164
RhoGAP_GMIP_PARG1 cd04378
RhoGAP_GMIP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 669-797 8.90e-15

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: 74.38  E-value: 8.90e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953103015  669 SQCLDQVGIFRKSGVKSRIQNLRQMNEANPDHVCYEGQSAYDVADLLKQYFRDLPEPIFTSKLTTTFLQI---YQLLPKD 745
Cdd:cd04378     29 NRALGVQGIYRVSGSKARVEKLCQAFENGKDLVELSELSPHDISSVLKLFLRQLPEPLILFRLYNDFIALakeIQRDTEE 108

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1953103015  746 QWLAAAQAATLLL-----------PDENREVLQTLLYFLSDIAS-AEENQMTAGNLAVCLAPSI 797
Cdd:cd04378    109 DKAPNTPIEVNRIirklkdllrqlPASNYNTLQHLIAHLYRVAEqFEENKMSPNNLGIVFGPTL 172
RhoGAP_Bcr cd04387
RhoGAP_Bcr: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of Bcr ...
 641-809 3.76e-14

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: 72.27  E-value: 3.76e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953103015  641 FGVPPLIHVQRTGQPLPQSIQQAMRYLRSQCLDQVGIFRKSGVKSRIQNLRQMNEANPDHVCYEgQSAYDV---ADLLKQ 717
Cdd:cd04387      1 FGVKISTVTKRERSKVPYIVRQCVEEVERRGMEEVGIYRISGVATDIQALKAAFDTNNKDVSVM-LSEMDVnaiAGTLKL 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953103015  718 YFRDLPEPIFTSKLTTTFLQIYQLLPKDQWLAAAQAATLLLPDENREVLQTLLYFLSDIASAEE-NQMTAGNLAVCLAPS 796
Cdd:cd04387     80 YFRELPEPLFTDELYPNFAEGIALSDPVAKESCMLNLLLSLPDPNLVTFLFLLHHLKRVAEREEvNKMSLHNLATVFGPT 159

                          170
                   ....*....|...
gi 1953103015  797 IFHLNVSKKDSPS 809
Cdd:cd04387    160 LLRPSEKESKIPT 172
RhoGAP_myosin_IXA cd04406
RhoGAP_myosin_IXA: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 641-798 2.71e-13

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: 69.64  E-value: 2.71e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953103015  641 FGVPpLIHVQRTGQPLPQSIQQAMRYLRSQCLDQVGIFRKSGVKSRIQNLRQMNEANPDHVCYEGQSAYDVADLLKQYFR 720
Cdd:cd04406      1 FGVE-LSRLTSEDRSVPLVVEKLINYIEMHGLYTEGIYRKSGSTNKIKELRQGLDTDANSVNLDDYNIHVIASVFKQWLR 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1953103015  721 DLPEPIFTSKLTTTFLQIYQLLPKDQWLAAAQAATLLLPDENREVLQTLLYFLSDIASAEE-NQMTAGNLAVCLAPSIF 798
Cdd:cd04406     80 DLPNPLMTFELYEEFLRAMGLQERRETVRGVYSVIDQLSRTHLNTLERLIFHLVRIALQEEtNRMSANALAIVFAPCIL 158
RhoGAP_ARHGAP27_15_12_9 cd04403
RhoGAP_ARHGAP27_15_12_9: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
 650-799 3.13e-13

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: 69.34  E-value: 3.13e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953103015  650 QRTGQPLPQSIQQAMRYLRSQCLDQVGIFRKSGVKSRIQNLRQMneANPDHVCYEGQSAYD----VADLLKQYFRDLPEP 725
Cdd:cd04403     10 QRENSTVPKFVRLCIEAVEKRGLDVDGIYRVSGNLAVIQKLRFA--VDHDEKLDLDDSKWEdihvITGALKLFFRELPEP 87

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953103015  726 IFTSKLTTTFLQIYQLLPKDQWLAAAQAATLLLPDENREVLQTLLYFLSD-IASAEENQMTAGNLAVCLAPSIFH 799
Cdd:cd04403     88 LFPYSLFNDFVAAIKLSDYEQRVSAVKDLIKSLPKPNHDTLKMLFRHLCRvIEHGEKNRMTTQNLAIVFGPTLLR 162
RhoGAP_SYD1 cd04379
RhoGAP_SYD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
 641-817 7.30e-13

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: 68.65  E-value: 7.30e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953103015  641 FGVP--PLIHVQRTGQPLPQSIQQAMRYLRSQCLDQVGIFRKSGVKSRIQNLRQMNEANPDHVCYEGQSAYDV---ADLL 715
Cdd:cd04379      1 FGVPlsRLVEREGESRDVPIVLQKCVQEIERRGLDVIGLYRLCGSAAKKKELRDAFERNSAAVELSEELYPDInviTGVL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953103015  716 KQYFRDLPEPIFTSKLTTTFLQIYQLLPKDQWLAAAQAATLL---LPDENREVLQTLLYFLSDIAS-AEENQMTAGNLAV 791
Cdd:cd04379     81 KDYLRELPEPLITPQLYEMVLEALAVALPNDVQTNTHLTLSIidcLPLSAKATLLLLLDHLSLVLSnSERNKMTPQNLAV 160

                          170       180
                   ....*....|....*....|....*.
gi 1953103015  792 CLAPSIFhlnvSKKDSPSPRIRSKRS 817
Cdd:cd04379    161 CFGPVLM----FCSQEFSRYGISPTS 182
RhoGAP_p190 cd04373
RhoGAP_p190: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 641-798 8.35e-13

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: 67.87  E-value: 8.35e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953103015  641 FGVPpLIHVQRTGQPLPQSIQQAMRYLRSQCLDQVGIFRKSGVKSRIQNL-RQMNEANPDHVCYEGQSAYDVADLLKQYF 719
Cdd:cd04373      1 FGVP-LANVVTSEKPIPIFLEKCVEFIEATGLETEGIYRVSGNKTHLDSLqKQFDQDHNLDLVSKDFTVNAVAGALKSFF 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953103015  720 RDLPEPIFTSKLTTTFLQIYQLLPKDQWLAAAQAATLLLPDENREVLQTLLYFLSDIA-SAEENQMTAGNLAVCLAPSIF 798
Cdd:cd04373     80 SELPDPLIPYSMHLELVEAAKINDREQRLHALKELLKKFPPENFDVFKYVITHLNKVSqNSKVNLMTSENLSICFWPTLM 159
RhoGAP_fSAC7_BAG7 cd04396
RhoGAP_fSAC7_BAG7: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 666-798 1.47e-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: 68.21  E-value: 1.47e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953103015  666 YLRSQCLDQVGIFRKSGVKSRIQNLRQMNEANPDH---VCYEGQSAYDVADLLKQYFRDLPEPIFTSKLTTTFLQIYQLL 742
Cdd:cd04396     42 YLKENATEVEGIFRVAGSSKRIRELQLIFSTPPDYgksFDWDGYTVHDAASVLRRYLNNLPEPLVPLDLYEEFRNPLRKR 121

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1953103015  743 PKDQWLAAAQAATLLL-----------------PDENREVLQTLLYFLSDIAS-AEENQMTAGNLAVCLAPSIF 798
Cdd:cd04396    122 PRILQYMKGRINEPLNtdidqaikeyrdlitrlPNLNRQLLLYLLDLLAVFARnSDKNLMTASNLAAIFQPGIL 195
RhoGAP_Graf cd04374
RhoGAP_Graf: GTPase-activator protein (GAP) domain for Rho-like GTPases found in GRAF (GTPase ...
 660-797 5.85e-12

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: 65.88  E-value: 5.85e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953103015  660 IQQAMRYLRSQCLDQVGIFRKSGVKSRIQNLRQM----NEANPDHV--CYEGQSAYDVADLLKQYFRDLPEPIFTSKLTT 733
Cdd:cd04374     32 VRKCIEAVETRGINEQGLYRVVGVNSKVQKLLSLgldpKTSTPGDVdlDNSEWEIKTITSALKTYLRNLPEPLMTYELHN 111

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953103015  734 TFLQIYQLLPKDQWLAAAQAATLLLPDENREVLQTLLYFLSDIAS-AEENQMTAGNLAVCLAPSI 797
Cdd:cd04374    112 DFINAAKSENLESRVNAIHSLVHKLPEKNREMLELLIKHLTNVSDhSKKNLMTVSNLGVVFGPTL 176
RhoGAP_GMIP cd04408
RhoGAP_GMIP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of GMIP ...
 656-797 1.44e-11

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: 64.84  E-value: 1.44e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953103015  656 LPQSIQQAMRYLRSQC--------LDQVGIFRKSGVKSRIQNLRQMNEANPDHVCYEGQSAYDVADLLKQYFRDLPEPIF 727
Cdd:cd04408      8 LPRDFPEEVPFVVVRCtaeienraLGVQGIYRISGSKARVEKLCQAFENGRDLVDLSGHSPHDITSVLKHFLKELPEPVL 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953103015  728 TSKLTTTFLQIYQLLPKDQWLAAAQAATLLL------------PDENREVLQTLLYFLSDIASA-EENQMTAGNLAVCLA 794
Cdd:cd04408     88 PFQLYDDFIALAKELQRDSEKAAESPSIVENiirslkellgrlPVSNYNTLRHLMAHLYRVAERfEDNKMSPNNLGIVFG 167


                   ...
gi 1953103015  795 PSI 797
Cdd:cd04408    168 PTL 170
RhoGAP_ARHGAP22_24_25 cd04390
RhoGAP_ARHGAP22_24_25: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
 640-848 6.29e-11

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: 62.85  E-value: 6.29e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953103015  640 VFG---VPPLIHVQRTGQPL-PQSIQQAMRYLRSQCLDQVGIFRKSGVKSRIQNLRQMNEANPDHVCYEGQSAYDVADLL 715
Cdd:cd04390      2 VFGqrlEDTVAYERKFGPRLvPILVEQCVDFIREHGLKEEGLFRLPGQANLVKQLQDAFDAGERPSFDSDTDVHTVASLL 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953103015  716 KQYFRDLPEPIFTSKLTTTFLQIYQLLPKDQWLAAA--QAATLLLPDENREVLQTLLYFLSDIAS-AEENQMTAGNLAVC 792
Cdd:cd04390     82 KLYLRELPEPVIPWAQYEDFLSCAQLLSKDEEKGLGelMKQVSILPKVNYNLLSYICRFLDEVQSnSSVNKMSVQNLATV 161

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953103015  793 LAPSIFhlnvskkdspsprirskrslvgRPGPRDLSENMAAT----QGLSHMISDCKKLF 848
Cdd:cd04390    162 FGPNIL----------------------RPKVEDPATIMEGTpqiqQLMTVMISKHEPLF 199
RhoGAP_fBEM3 cd04400
RhoGAP_fBEM3: RhoGAP (GTPase-activator [GAP] protein for Rho-like small GTPases) domain of ...
 640-803 2.91e-10

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: 60.84  E-value: 2.91e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953103015  640 VFGVPPLIHVQRT-----GQPLPQSIQQAMRYLRSQ-CLDQVGIFRKSGVKSRIQNLR-QMNEANPDHVCYEGQSaYD-- 710
Cdd:cd04400      1 IFGSPLEEAVELSshkynGRDLPSVVYRCIEYLDKNrAIYEEGIFRLSGSASVIKQLKeRFNTEYDVDLFSSSLY-PDvh 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953103015  711 -VADLLKQYFRDLPEPIFTSKLTTTFLQIYQLLPKD-QWLAAAQAATLLLPDENREVLQTLLYFLSDI-ASAEENQMTAG 787
Cdd:cd04400     80 tVAGLLKLYLRELPTLILGGELHNDFKRLVEENHDRsQRALELKDLVSQLPQANYDLLYVLFSFLRKIiEHSDVNKMNLR 159

                          170
                   ....*....|....*.
gi 1953103015  788 NLAVCLAPSifhLNVS 803
Cdd:cd04400    160 NVCIVFSPT---LNIP 172
RhoGAP_MgcRacGAP cd04382
RhoGAP_MgcRacGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 672-798 2.96e-10

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: 60.77  E-value: 2.96e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953103015  672 LDQVGIFRKSGVKSRIQNLRQ---MNEANPDHvcyegqSAYDVADL---LKQYFRDLPEPIFTSKLTTTFLQIYQLLPKD 745
Cdd:cd04382     33 LTEEGLYRVSGSEREVKALKEkflRGKTVPNL------SKVDIHVIcgcLKDFLRSLKEPLITFALWKEFMEAAEILDED 106

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1953103015  746 QWLAAAQAATLLLPDENREVLQTLLYFLSDIASAEENQMTAGNLAVCLAPSIF 798
Cdd:cd04382    107 NSRAALYQAISELPQPNRDTLAFLILHLQRVAQSPECKMDINNLARVFGPTIV 159
RhoGAP_ARHGAP21 cd04395
RhoGAP_ARHGAP21: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 640-797 6.25e-10

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: 60.11  E-value: 6.25e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953103015  640 VFGVP----PLIHVQRTgqpLPQSIQQAMRYLRSQCLDQVGIFRKSGVKSRIQNLRQMNEANPDHVCYEGQSAYD---VA 712
Cdd:cd04395      1 TFGVPlddcPPSSENPY---VPLIVEVCCNIVEARGLETVGIYRVPGNNAAISALQEELNRGGFDIDLQDPRWRDvnvVS 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953103015  713 DLLKQYFRDLPEPIFTSKLTTTFLQIYQLLPKDQWLAAAQAATLLLPDENREVLQTLLYFLSDIA-SAEENQMTAGNLAV 791
Cdd:cd04395     78 SLLKSFFRKLPEPLFTNELYPDFIEANRIEDPVERLKELRRLIHSLPDHHYETLKHLIRHLKTVAdNSEVNKMEPRNLAI 157


                   ....*.
gi 1953103015  792 CLAPSI 797
Cdd:cd04395    158 VFGPTL 163
RhoGAP_PARG1 cd04409
RhoGAP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 641-797 1.14e-09

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: 59.44  E-value: 1.14e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953103015  641 FGVPPLIHVQRTGQPLPQSIQQAMRYLRSQCLDQVGIFRKSGVKSRIQNLRQMNEANPDHVCYEGQSAYDVADLLKQYFR 720
Cdd:cd04409      1 FGADFAQVAKKSPDGIPFIIKKCTSEIESRALCLKGIYRVNGAKSRVEKLCQAFENGKDLVELSELSPHDISNVLKLYLR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953103015  721 DLPEPIFTSKLTTTFLQIYQ------------LLPKDQWLAAAQAATL----------LLPDENREVLQTLLYFLSDIAS 778
Cdd:cd04409     81 QLPEPLILFRLYNEFIGLAKesqhvnetqeakKNSDKKWPNMCTELNRillkskdllrQLPAPNYNTLQFLIVHLHRVSE 160

                          170       180
                   ....*....|....*....|
gi 1953103015  779 -AEENQMTAGNLAVCLAPSI 797
Cdd:cd04409    161 qAEENKMSASNLGIIFGPTL 180
RhoGAP_chimaerin cd04372
RhoGAP_chimaerin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 649-819 1.01e-07

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 [Multi-domain]  Cd Length: 194  Bit Score: 53.29  E-value: 1.01e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953103015  649 VQRTGQPLPQSIQQAMRYLRSQCLDQVGIFRKSGVKSRIQNLRQMNEANPDHVCYEgQSAYD----VADLLKQYFRDLPE 724
Cdd:cd04372      9 VKAHNTQRPMVVDMCIREIEARGLQSEGLYRVSGFAEEIEDVKMAFDRDGEKADIS-ATVYPdinvITGALKLYFRDLPI 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953103015  725 PIFTSKLTTTFLQIYQLLPKDQWLAAAQAATLLLPDENREVLQTLLYFLSDIASAE-ENQMTAGNLAVCLAPSIFHLNVS 803
Cdd:cd04372     88 PVITYDTYPKFIDAAKISNPDERLEAVHEALMLLPPAHYETLRYLMEHLKRVTLHEkDNKMNAENLGIVFGPTLMRPPED 167

                          170
                   ....*....|....*.
gi 1953103015  804 KKDSPSPRIRSKRSLV 819
Cdd:cd04372    168 SALTTLNDMRYQILIV 183
START_STARD10-like cd08871
Lipid-binding START domain of mammalian STARD10 and related proteins; This subfamily includes ...
 924-1066 2.91e-07

Lipid-binding START domain of mammalian STARD10 and related proteins; This subfamily includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD10 (also known as CGI-52, PTCP-like, and SDCCAG28). The START domain family belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. STARD10 binds phophatidylcholine and phosphatidylethanolamine. This protein is widely expressed and is synthesized constitutively in many organs. It may function in the liver in the export of phospholipids into bile. It is concentrated in the sperm flagellum, and may play a role in energy metabolism. In the mammary gland it may participate in the enrichment of lipids in milk, and be a potential marker of differentiation. Its expression is induced in this gland during gestation and lactation. It is overexpressed in mammary tumors from Neu/ErbB2 transgenic mice, in several breast carcinoma cell lines, and in 35% of primary human breast cancers, and may cooperate with c-erbB receptor signaling in breast oncogenesis. It is a potential marker of disease outcome in breast cancer; loss of STARD10 expression in breast cancer strongly predicts an aggressive disease course. The lipid transfer activity of STRAD10 is downregulated by phosphorylation of its Ser284 by CK2 (casein kinase 2).


Pssm-ID: 176880  Cd Length: 222  Bit Score: 52.64  E-value: 2.91e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953103015  924 KAPDGHPLRVWKVSTEVAAPPPVVLHRVLRE---RALWDEDLLRAQVLEALMPGVELYHYVTDSMAPHPCRDFVVLRMWr 1000
Cdd:cd08871     39 KNPENSSIKMIKVSAIFPDVPAETLYDVLHDpeyRKTWDSNMIESFDICQLNPNNDIGYYSAKCPKPLKNRDFVNLRSW- 117

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953103015 1001 sdLPRGG-----CLLVSQSLDPeqpvPESG-VRAMMLTSQYLMEPCGLGRSRLTHICRADLRGRSPDWY-NKV 1066
Cdd:cd08871    118 --LEFGGeyiifNHSVKHKKYP----PRKGfVRAISLLTGYLIRPTGPKGCTLTYVTQNDPKGSLPKWVvNKA 184
START_1 cd08876
Uncharacterized subgroup of the steroidogenic acute regulatory protein (StAR)-related lipid ...
 923-1066 4.03e-07

Uncharacterized subgroup of the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domain family; Functionally uncharacterized subgroup of the START domain family. The START domain family belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. For some mammalian members of the START family (STARDs), it is known which lipids bind in this pocket; these include cholesterol (STARD1, -3, -4, and -5), 25-hydroxycholesterol (STARD5), phosphatidylcholine (STARD2, -7, and -10), phosphatidylethanolamine (STARD10) and ceramides (STARD11). Mammalian STARDs participate in the control of various cellular processes, including lipid trafficking between intracellular compartments, lipid metabolism, and modulation of signaling events. Mutation or altered expression of STARDs is linked to diseases such as cancer, genetic disorders, and autoimmune disease.


Pssm-ID: 176885  Cd Length: 195  Bit Score: 51.50  E-value: 4.03e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953103015  923 RKAPDGHPLRVWKVsTEVAAPPPVVLhRVLRERAL---WDEDLLRAQVLEALMPGVELYHYVTDsmAPHPC--RDFVVLR 997
Cdd:cd08876     33 RDVEGSPLKEFKAV-AEVDASIEAFL-ALLRDTESypqWMPNCKESRVLKRTDDNERSVYTVID--LPWPVkdRDMVLRS 108

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953103015  998 MWRSDLPRGGCLLVSQSLDPEQPVPESGVRAMMLTSQYLMEPCGLGRSRLTHICRADLRGRSPDW-YNKV 1066
Cdd:cd08876    109 TTEQDADDGSVTITLEAAPEALPEQKGYVRIKTVEGQWTFTPLGNGKTRVTYQAYADPGGSIPGWlANAF 178
RhoGAP_KIAA1688 cd04389
RhoGAP_KIAA1688: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
 676-812 4.32e-06

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: 48.54  E-value: 4.32e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953103015  676 GIFRKSGVKSRIQNLR-QMNEAnpdHVCYEGQS-AYDVADLLKQYFRDLPEPIF----------TSKLTTTFLQIYQLLp 743
Cdd:cd04389     42 GIFRVPGDIDEVNELKlRVDQW---DYPLSGLEdPHVPASLLKLWLRELEEPLIpdalyqqcisASEDPDKAVEIVQKL- 117

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1953103015  744 kdqwlaaaqaatlllPDENREVLQTLLYFLSDIA---SAEENQMTAGNLAVCLAPsifhlNVSKKDSPSPRI 812
Cdd:cd04389    118 ---------------PIINRLVLCYLINFLQVFAqpeNVAHTKMDVSNLAMVFAP-----NILRCTSDDPRV 169
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
16-77 9.15e-03

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 35.71  E-value: 9.15e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1953103015   16 EAKRACKWLRATGFPQYAQLFEEGLFPLDIGSVKKDHSFLDKDSLGALCRRLMTLNNCASMK 77
Cdd:pfam07647    5 SLESVADWLRSIGLEQYTDNFRDQGITGAELLLRLTLEDLKRLGITSVGHRRKILKKIQELK 66
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
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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