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Conserved domains on  [gi|1207112902|ref|XP_021335891|]
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rho GTPase-activating protein 27 isoform X2 [Danio rerio]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RhoGAP_ARHGAP27_15_12_9 cd04403
RhoGAP_ARHGAP27_15_12_9: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
 784-968 2.59e-122

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: 369.80  E-value: 2.59e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902 784 FGCHLHNLCSQEKTRVPSFVEKCIRAVEKRGLEIDGLYRVSGNLAVIQKLRFKADHED-LDLEEGNW-DIHVITGALKLF 861
Cdd:cd04403     1 FGCHLEALCQRENSTVPKFVRLCIEAVEKRGLDVDGIYRVSGNLAVIQKLRFAVDHDEkLDLDDSKWeDIHVITGALKLF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902 862 FRELQEPLFPYNLFNEFICAIKTPDYYSKISHMRNLVRSLPPPNHDTMEALFSHLRRVIQHGNENRMTVQNVAIVFGPTL 941
Cdd:cd04403    81 FRELPEPLFPYSLFNDFVAAIKLSDYEQRVSAVKDLIKSLPKPNHDTLKMLFRHLCRVIEHGEKNRMTTQNLAIVFGPTL 160

                         170       180
                  ....*....|....*....|....*..
gi 1207112902 942 LKPEEETASIATYMVFQNQIVEFLLSE 968
Cdd:cd04403   161 LRPEQETGNIAVHMVYQNQIVELILLE 187
PH_ARHGAP9-like cd13233
Beta-spectrin pleckstrin homology (PH) domain; ARHGAP family genes encode Rho/Rac/Cdc42-like ...
 590-701 8.97e-44

Beta-spectrin pleckstrin homology (PH) domain; ARHGAP family genes encode Rho/Rac/Cdc42-like GTPase activating proteins with RhoGAP domain. The ARHGAP members here all have a PH domain upstream of their C-terminal RhoGAP domain. Some have additional N-terminal SH3 and WW domains. The members here include: ARHGAP9, ARHGAP12, ARHGAP15, and ARHGAP27. ARHGAP27 and ARHGAP12 shared the common-domain structure, consisting of SH3, WW, PH, and RhoGAP domains. The PH domain of ArhGAP9 employs a non-canonical phosphoinositide binding mechanism, a variation of the spectrin- Ins(4,5)P2-binding mode, that gives rise to a unique PI binding profile, namely a preference for both PI(4,5)P2 and the PI 3-kinase products PI(3,4,5)P3 and PI(3,4)P2. This lipid binding mechanism is also employed by the PH domain of Tiam1 and Slm1. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


:

Pssm-ID: 270053  Cd Length: 110  Bit Score: 153.98  E-value: 8.97e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902 590 EKAGILNKTKVSENGKKVRKNWGHSWTVLHGGKLTFHKDPKSTpagASSKTNQILPEFTVDLKGATINRAPkDKSSKKNV 669
Cdd:cd13233     1 EKQGLLNKTKIAENGKKLRKNWSTSWVVLTSSHLLFYKDAKSA---AKSGNPYSKPESSVDLRGASIEWAK-EKSSRKNV 76

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1207112902 670 LELKTRTGAEYLIQYDTDSIIQDWHKVILDTI 701
Cdd:cd13233    77 FQISTVTGTEFLLQSDNDTEIREWFDAIKAVI 108
SH3 super family cl17036
Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction ...
 22-77 2.11e-24

Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction domains that bind proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. Thus, they are referred to as proline-recognition domains (PRDs). SH3 domains are less selective and show more diverse specificity compared to other PRDs. They have been shown to bind peptide sequences that lack the PxxP motif; examples include the PxxDY motif of Eps8 and the RKxxYxxY sequence in SKAP55. SH3 domain containing proteins play versatile and diverse roles in the cell, including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies, among others. Many members of this superfamily are adaptor proteins that associate with a number of protein partners, facilitating complex formation and signal transduction.


The actual alignment was detected with superfamily member cd12069:

Pssm-ID: 473055  Cd Length: 57  Bit Score: 96.81  E-value: 2.11e-24
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1207112902  22 VLVNYEYTYTARDGRNVSIKPNEHYILVNKTNEEWWHVQKDAADKPFYIPAKYVTE 77
Cdd:cd12069     2 VLVEHAFEYTGKDGRLVSIKPNERYILLRRTNEHWWHVRRDKGTRPFYIPAKYVKE 57
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 382-410 3.50e-05

WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.


:

Pssm-ID: 459800 [Multi-domain]  Cd Length: 30  Bit Score: 41.34  E-value: 3.50e-05
                          10        20
                  ....*....|....*....|....*....
gi 1207112902 382 SDWEKVLDEStGRHYFFNTVSGQSSWDPP 410
Cdd:pfam00397   3 PGWEERWDPD-GRVYYYNHETGETQWEKP 30
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 315-343 1.08e-04

WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.


:

Pssm-ID: 459800 [Multi-domain]  Cd Length: 30  Bit Score: 40.18  E-value: 1.08e-04
                          10        20
                  ....*....|....*....|....*....
gi 1207112902 315 AGWQVHTDDqSGQEFYYQPSTGRSTWENP 343
Cdd:pfam00397   3 PGWEERWDP-DGRVYYYNHETGETQWEKP 30
PHA03307 super family cl33723
transcriptional regulator ICP4; Provisional
 144-525 1.13e-04

transcriptional regulator ICP4; Provisional


The actual alignment was detected with superfamily member PHA03307:

Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 46.32  E-value: 1.13e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902  144 GLDPDPiKTEAEAGPPVSSNTSSPTNGETAFIILPPPVYTVNTTQSTETDTRSVDDPKDSVGRPRVDSST-------IDE 216
Cdd:PHA03307    58 GAAACD-RFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPppspapdLSE 136

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902  217 DIQMLNRAGWSEVLDVMGKEKNVYESLDTVREPESPKDEADMTVNTT----------PVTPDAPMVEDDTAvyvniPRKR 286
Cdd:PHA03307   137 MLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEETArapssppaepPPSTPPAAASPRPP-----RRSS 211

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902  287 QTTINNSSPIASLLQDFPEPPENFLLDSAGWQVHTDDQSGQEFYYQPSTGR----------STWENPLSSRSMESPVGTE 356
Cdd:PHA03307   212 PISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPitlptriweaSGWNGPSSRPGPASSSSSP 291

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902  357 GGRSPPSFPQSPaCSPVAPAPRRWSSDWEKVLDESTGrhyffntvSGQSSWDPPED-VDSPGRlmflDDCPPPLPEEDYP 435
Cdd:PHA03307   292 RERSPSPSPSSP-GSGPAPSSPRASSSSSSSRESSSS--------STSSSSESSRGaAVSPGP----SPSRSPSPSRPPP 358

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902  436 AS--PELEEASPVSIPAEYSLIHVKKVSIPRVsldRSSPAGWSLdiDSEGTWTFTSEYTQEQWIKSLDDQGRTYYYLRDG 513
Cdd:PHA03307   359 PAdpSSPRKRPRPSRAPSSPAASAGRPTRRRA---RAAVAGRAR--RRDATGRFPAGRPRPSPLDAGAASGAFYARYPLL 433

                          410
                   ....*....|..
gi 1207112902  514 SKSQWNLPEINP 525
Cdd:PHA03307   434 TPSGEPWPGSPP 445
 
Name Accession Description Interval E-value
RhoGAP_ARHGAP27_15_12_9 cd04403
RhoGAP_ARHGAP27_15_12_9: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
 784-968 2.59e-122

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: 369.80  E-value: 2.59e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902 784 FGCHLHNLCSQEKTRVPSFVEKCIRAVEKRGLEIDGLYRVSGNLAVIQKLRFKADHED-LDLEEGNW-DIHVITGALKLF 861
Cdd:cd04403     1 FGCHLEALCQRENSTVPKFVRLCIEAVEKRGLDVDGIYRVSGNLAVIQKLRFAVDHDEkLDLDDSKWeDIHVITGALKLF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902 862 FRELQEPLFPYNLFNEFICAIKTPDYYSKISHMRNLVRSLPPPNHDTMEALFSHLRRVIQHGNENRMTVQNVAIVFGPTL 941
Cdd:cd04403    81 FRELPEPLFPYSLFNDFVAAIKLSDYEQRVSAVKDLIKSLPKPNHDTLKMLFRHLCRVIEHGEKNRMTTQNLAIVFGPTL 160

                         170       180
                  ....*....|....*....|....*..
gi 1207112902 942 LKPEEETASIATYMVFQNQIVEFLLSE 968
Cdd:cd04403   161 LRPEQETGNIAVHMVYQNQIVELILLE 187
RhoGAP smart00324
GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac ...
 798-968 2.11e-61

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: 206.35  E-value: 2.11e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902  798 RVPSFVEKCIRAVEKRGLEIDGLYRVSGNLAVIQKLRFKADH-EDLDLEEGNWDIHVITGALKLFFRELQEPLFPYNLFN 876
Cdd:smart00324   2 PIPIIVEKCIEYLEKRGLDTEGIYRVSGSKSRVKELRDAFDSgPDPDLDLSEYDVHDVAGLLKLFLRELPEPLITYELYE 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902  877 EFICAIKTPDYYSKISHMRNLVRSLPPPNHDTMEALFSHLRRVIQHGNENRMTVQNVAIVFGPTLLKPEEETASIATYMV 956
Cdd:smart00324  82 EFIEAAKLEDETERLRALRELLSLLPPANRATLRYLLAHLNRVAEHSEENKMTARNLAIVFGPTLLRPPDGEVASLKDIR 161

                          170
                   ....*....|..
gi 1207112902  957 FQNQIVEFLLSE 968
Cdd:smart00324 162 HQNTVIEFLIEN 173
RhoGAP pfam00620
RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.
 800-944 2.42e-56

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


Pssm-ID: 459875  Cd Length: 148  Bit Score: 191.22  E-value: 2.42e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902 800 PSFVEKCIRAVEKRGLEIDGLYRVSGNLAVIQKLRFKADH-EDLDLEEGNWDIHVITGALKLFFRELQEPLFPYNLFNEF 878
Cdd:pfam00620   1 PLIVRKCVEYLEKRGLDTEGIFRVSGSASRIKELREAFDRgPDVDLDLEEEDVHVVASLLKLFLRELPEPLLTFELYEEF 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207112902 879 ICAIKTPDYYSKISHMRNLVRSLPPPNHDTMEALFSHLRRVIQHGNENRMTVQNVAIVFGPTLLKP 944
Cdd:pfam00620  81 IEAAKLPDEEERLEALRELLRKLPPANRDTLRYLLAHLNRVAQNSDVNKMNAHNLAIVFGPTLLRP 146
PH_ARHGAP9-like cd13233
Beta-spectrin pleckstrin homology (PH) domain; ARHGAP family genes encode Rho/Rac/Cdc42-like ...
 590-701 8.97e-44

Beta-spectrin pleckstrin homology (PH) domain; ARHGAP family genes encode Rho/Rac/Cdc42-like GTPase activating proteins with RhoGAP domain. The ARHGAP members here all have a PH domain upstream of their C-terminal RhoGAP domain. Some have additional N-terminal SH3 and WW domains. The members here include: ARHGAP9, ARHGAP12, ARHGAP15, and ARHGAP27. ARHGAP27 and ARHGAP12 shared the common-domain structure, consisting of SH3, WW, PH, and RhoGAP domains. The PH domain of ArhGAP9 employs a non-canonical phosphoinositide binding mechanism, a variation of the spectrin- Ins(4,5)P2-binding mode, that gives rise to a unique PI binding profile, namely a preference for both PI(4,5)P2 and the PI 3-kinase products PI(3,4,5)P3 and PI(3,4)P2. This lipid binding mechanism is also employed by the PH domain of Tiam1 and Slm1. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270053  Cd Length: 110  Bit Score: 153.98  E-value: 8.97e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902 590 EKAGILNKTKVSENGKKVRKNWGHSWTVLHGGKLTFHKDPKSTpagASSKTNQILPEFTVDLKGATINRAPkDKSSKKNV 669
Cdd:cd13233     1 EKQGLLNKTKIAENGKKLRKNWSTSWVVLTSSHLLFYKDAKSA---AKSGNPYSKPESSVDLRGASIEWAK-EKSSRKNV 76

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1207112902 670 LELKTRTGAEYLIQYDTDSIIQDWHKVILDTI 701
Cdd:cd13233    77 FQISTVTGTEFLLQSDNDTEIREWFDAIKAVI 108
SH3_ARHGAP27 cd12069
Src Homology 3 domain of Rho GTPase-activating protein 27; Rho GTPase-activating proteins ...
 22-77 2.11e-24

Src Homology 3 domain of Rho GTPase-activating protein 27; Rho GTPase-activating proteins (RhoGAPs or ARHGAPs) bind to Rho proteins and enhance the hydrolysis rates of bound GTP. ARHGAP27, also called CAMGAP1, shows GAP activity towards Rac1 and Cdc42. It binds the adaptor protein CIN85 and may play a role in clathrin-mediated endocytosis. It contains SH3, WW, Pleckstin homology (PH), and RhoGAP domains. SH3 domains bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs; they play a role in the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components and mediate multiprotein complex assemblies.


Pssm-ID: 213002  Cd Length: 57  Bit Score: 96.81  E-value: 2.11e-24
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1207112902  22 VLVNYEYTYTARDGRNVSIKPNEHYILVNKTNEEWWHVQKDAADKPFYIPAKYVTE 77
Cdd:cd12069     2 VLVEHAFEYTGKDGRLVSIKPNERYILLRRTNEHWWHVRRDKGTRPFYIPAKYVKE 57
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 589-702 9.08e-09

Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.


Pssm-ID: 214574 [Multi-domain]  Cd Length: 102  Bit Score: 53.71  E-value: 9.08e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902  589 LEKAGILNKtkvseNGKKVRKNWGHSWTVLHGGKLTFHKDPKSTPAGAssktnqilPEFTVDLKGATINRAPKDKSSK-K 667
Cdd:smart00233   1 VIKEGWLYK-----KSGGGKKSWKKRYFVLFNSTLLYYKSKKDKKSYK--------PKGSIDLSGCTVREAPDPDSSKkP 67

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1207112902  668 NVLELKTRTGAEYLIQYDTDSIIQDWHKVILDTIH 702
Cdd:smart00233  68 HCFEIKTSDRKTLLLQAESEEEREKWVEALRKAIA 102
PH pfam00169
PH domain; PH stands for pleckstrin homology.
 589-702 2.27e-07

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 49.87  E-value: 2.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902 589 LEKAGILNKtkvseNGKKVRKNWGHSWTVLHGGKLTFHKDPKSTPAGAssktnqilPEFTVDLKGATINRAPK-DKSSKK 667
Cdd:pfam00169   1 VVKEGWLLK-----KGGGKKKSWKKRYFVLFDGSLLYYKDDKSGKSKE--------PKGSISLSGCEVVEVVAsDSPKRK 67

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1207112902 668 NVLELKT---RTGAEYLIQYDTDSIIQDWHKVILDTIH 702
Cdd:pfam00169  68 FCFELRTgerTGKRTYLLQAESEEERKDWIKAIQSAIR 105
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 382-410 3.50e-05

WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.


Pssm-ID: 459800 [Multi-domain]  Cd Length: 30  Bit Score: 41.34  E-value: 3.50e-05
                          10        20
                  ....*....|....*....|....*....
gi 1207112902 382 SDWEKVLDEStGRHYFFNTVSGQSSWDPP 410
Cdd:pfam00397   3 PGWEERWDPD-GRVYYYNHETGETQWEKP 30
SH3_1 pfam00018
SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal ...
 28-72 3.78e-05

SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal transduction related to cytoskeletal organization. First described in the Src cytoplasmic tyrosine kinase. The structure is a partly opened beta barrel.


Pssm-ID: 394975 [Multi-domain]  Cd Length: 47  Bit Score: 41.81  E-value: 3.78e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1207112902  28 YTYTARDGRNVSIKPNEHYILVNKTNEEWWHVqKDAADKPFYIPA 72
Cdd:pfam00018   4 YDYTAQEPDELSFKKGDIIIVLEKSEDGWWKG-RNKGGKEGLIPS 47
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 382-412 5.45e-05

Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.


Pssm-ID: 238122 [Multi-domain]  Cd Length: 31  Bit Score: 40.97  E-value: 5.45e-05
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1207112902 382 SDWEKVLDEStGRHYFFNTVSGQSSWDPPED 412
Cdd:cd00201     2 PGWEERWDPD-GRVYYYNHNTKETQWEDPRE 31
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 315-343 1.08e-04

WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.


Pssm-ID: 459800 [Multi-domain]  Cd Length: 30  Bit Score: 40.18  E-value: 1.08e-04
                          10        20
                  ....*....|....*....|....*....
gi 1207112902 315 AGWQVHTDDqSGQEFYYQPSTGRSTWENP 343
Cdd:pfam00397   3 PGWEERWDP-DGRVYYYNHETGETQWEKP 30
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 144-525 1.13e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 46.32  E-value: 1.13e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902  144 GLDPDPiKTEAEAGPPVSSNTSSPTNGETAFIILPPPVYTVNTTQSTETDTRSVDDPKDSVGRPRVDSST-------IDE 216
Cdd:PHA03307    58 GAAACD-RFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPppspapdLSE 136

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902  217 DIQMLNRAGWSEVLDVMGKEKNVYESLDTVREPESPKDEADMTVNTT----------PVTPDAPMVEDDTAvyvniPRKR 286
Cdd:PHA03307   137 MLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEETArapssppaepPPSTPPAAASPRPP-----RRSS 211

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902  287 QTTINNSSPIASLLQDFPEPPENFLLDSAGWQVHTDDQSGQEFYYQPSTGR----------STWENPLSSRSMESPVGTE 356
Cdd:PHA03307   212 PISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPitlptriweaSGWNGPSSRPGPASSSSSP 291

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902  357 GGRSPPSFPQSPaCSPVAPAPRRWSSDWEKVLDESTGrhyffntvSGQSSWDPPED-VDSPGRlmflDDCPPPLPEEDYP 435
Cdd:PHA03307   292 RERSPSPSPSSP-GSGPAPSSPRASSSSSSSRESSSS--------STSSSSESSRGaAVSPGP----SPSRSPSPSRPPP 358

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902  436 AS--PELEEASPVSIPAEYSLIHVKKVSIPRVsldRSSPAGWSLdiDSEGTWTFTSEYTQEQWIKSLDDQGRTYYYLRDG 513
Cdd:PHA03307   359 PAdpSSPRKRPRPSRAPSSPAASAGRPTRRRA---RAAVAGRAR--RRDATGRFPAGRPRPSPLDAGAASGAFYARYPLL 433

                          410
                   ....*....|..
gi 1207112902  514 SKSQWNLPEINP 525
Cdd:PHA03307   434 TPSGEPWPGSPP 445
PRP40 COG5104
Splicing factor [RNA processing and modification];
371-413 8.68e-04

Splicing factor [RNA processing and modification];


Pssm-ID: 227435 [Multi-domain]  Cd Length: 590  Bit Score: 43.15  E-value: 8.68e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1207112902 371 SPVAPAPRRWSSDWEKVLDEStGRHYFFNTVSGQSSWDPPEDV 413
Cdd:COG5104     4 ALLGMASGEARSEWEELKAPD-GRIYYYNKRTGKSSWEKPKEL 45
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
 28-76 1.35e-03

Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences containing proline and hydrophobic amino acids. Pro-containing polypeptides may bind to SH3 domains in 2 different binding orientations.


Pssm-ID: 214620 [Multi-domain]  Cd Length: 56  Bit Score: 37.90  E-value: 1.35e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1207112902   28 YTYTARDGRNVSIKPNEHYILVNKTNEEWWHVQKDaADKPFYIPAKYVT 76
Cdd:smart00326   9 YDYTAQDPDELSFKKGDIITVLEKSDDGWWKGRLG-RGKEGLFPSNYVE 56
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 315-343 5.31e-03

Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.


Pssm-ID: 238122 [Multi-domain]  Cd Length: 31  Bit Score: 35.20  E-value: 5.31e-03
                          10        20
                  ....*....|....*....|....*....
gi 1207112902 315 AGWQVHTDDqSGQEFYYQPSTGRSTWENP 343
Cdd:cd00201     2 PGWEERWDP-DGRVYYYNHNTKETQWEDP 29
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 384-412 8.49e-03

Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.


Pssm-ID: 197736 [Multi-domain]  Cd Length: 33  Bit Score: 34.88  E-value: 8.49e-03
                           10        20
                   ....*....|....*....|....*....
gi 1207112902  384 WEKVLDEStGRHYFFNTVSGQSSWDPPED 412
Cdd:smart00456   6 WEERKDPD-GRPYYYNHETKETQWEKPRE 33
 
Name Accession Description Interval E-value
RhoGAP_ARHGAP27_15_12_9 cd04403
RhoGAP_ARHGAP27_15_12_9: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
 784-968 2.59e-122

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: 369.80  E-value: 2.59e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902 784 FGCHLHNLCSQEKTRVPSFVEKCIRAVEKRGLEIDGLYRVSGNLAVIQKLRFKADHED-LDLEEGNW-DIHVITGALKLF 861
Cdd:cd04403     1 FGCHLEALCQRENSTVPKFVRLCIEAVEKRGLDVDGIYRVSGNLAVIQKLRFAVDHDEkLDLDDSKWeDIHVITGALKLF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902 862 FRELQEPLFPYNLFNEFICAIKTPDYYSKISHMRNLVRSLPPPNHDTMEALFSHLRRVIQHGNENRMTVQNVAIVFGPTL 941
Cdd:cd04403    81 FRELPEPLFPYSLFNDFVAAIKLSDYEQRVSAVKDLIKSLPKPNHDTLKMLFRHLCRVIEHGEKNRMTTQNLAIVFGPTL 160

                         170       180
                  ....*....|....*....|....*..
gi 1207112902 942 LKPEEETASIATYMVFQNQIVEFLLSE 968
Cdd:cd04403   161 LRPEQETGNIAVHMVYQNQIVELILLE 187
RhoGAP smart00324
GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac ...
 798-968 2.11e-61

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: 206.35  E-value: 2.11e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902  798 RVPSFVEKCIRAVEKRGLEIDGLYRVSGNLAVIQKLRFKADH-EDLDLEEGNWDIHVITGALKLFFRELQEPLFPYNLFN 876
Cdd:smart00324   2 PIPIIVEKCIEYLEKRGLDTEGIYRVSGSKSRVKELRDAFDSgPDPDLDLSEYDVHDVAGLLKLFLRELPEPLITYELYE 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902  877 EFICAIKTPDYYSKISHMRNLVRSLPPPNHDTMEALFSHLRRVIQHGNENRMTVQNVAIVFGPTLLKPEEETASIATYMV 956
Cdd:smart00324  82 EFIEAAKLEDETERLRALRELLSLLPPANRATLRYLLAHLNRVAEHSEENKMTARNLAIVFGPTLLRPPDGEVASLKDIR 161

                          170
                   ....*....|..
gi 1207112902  957 FQNQIVEFLLSE 968
Cdd:smart00324 162 HQNTVIEFLIEN 173
RhoGAP cd00159
RhoGAP: GTPase-activator protein (GAP) for Rho-like GTPases; GAPs towards Rho/Rac/Cdc42-like ...
 800-968 6.78e-60

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: 201.76  E-value: 6.78e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902 800 PSFVEKCIRAVEKRGLEIDGLYRVSGNLAVIQKLRFKADHEDLDLEEGNWDIHVITGALKLFFRELQEPLFPYNLFNEFI 879
Cdd:cd00159     1 PLIIEKCIEYLEKNGLNTEGIFRVSGSASKIEELKKKFDRGEDIDDLEDYDVHDVASLLKLYLRELPEPLIPFELYDEFI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902 880 CAIKTPDYYSKISHMRNLVRSLPPPNHDTMEALFSHLRRVIQHGNENRMTVQNVAIVFGPTLLKPEEETASIATYMVFQN 959
Cdd:cd00159    81 ELAKIEDEEERIEALKELLKSLPPENRDLLKYLLKLLHKISQNSEVNKMTASNLAIVFAPTLLRPPDSDDELLEDIKKLN 160


                  ....*....
gi 1207112902 960 QIVEFLLSE 968
Cdd:cd00159   161 EIVEFLIEN 169
RhoGAP pfam00620
RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.
 800-944 2.42e-56

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


Pssm-ID: 459875  Cd Length: 148  Bit Score: 191.22  E-value: 2.42e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902 800 PSFVEKCIRAVEKRGLEIDGLYRVSGNLAVIQKLRFKADH-EDLDLEEGNWDIHVITGALKLFFRELQEPLFPYNLFNEF 878
Cdd:pfam00620   1 PLIVRKCVEYLEKRGLDTEGIFRVSGSASRIKELREAFDRgPDVDLDLEEEDVHVVASLLKLFLRELPEPLLTFELYEEF 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207112902 879 ICAIKTPDYYSKISHMRNLVRSLPPPNHDTMEALFSHLRRVIQHGNENRMTVQNVAIVFGPTLLKP 944
Cdd:pfam00620  81 IEAAKLPDEEERLEALRELLRKLPPANRDTLRYLLAHLNRVAQNSDVNKMNAHNLAIVFGPTLLRP 146
RhoGAP_Graf cd04374
RhoGAP_Graf: GTPase-activator protein (GAP) domain for Rho-like GTPases found in GRAF (GTPase ...
 801-967 2.73e-47

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: 167.57  E-value: 2.73e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902 801 SFVEKCIRAVEKRGLEIDGLYRVSGNLAVIQKL------RFKADHEDLDLEEGNWDIHVITGALKLFFRELQEPLFPYNL 874
Cdd:cd04374    30 KFVRKCIEAVETRGINEQGLYRVVGVNSKVQKLlslgldPKTSTPGDVDLDNSEWEIKTITSALKTYLRNLPEPLMTYEL 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902 875 FNEFICAIKTPDYYSKISHMRNLVRSLPPPNHDTMEALFSHLRRVIQHGNENRMTVQNVAIVFGPTLLKPEEETASIATY 954
Cdd:cd04374   110 HNDFINAAKSENLESRVNAIHSLVHKLPEKNREMLELLIKHLTNVSDHSKKNLMTVSNLGVVFGPTLLRPQEETVAAIMD 189

                         170
                  ....*....|...
gi 1207112902 955 MVFQNQIVEFLLS 967
Cdd:cd04374   190 IKFQNIVVEILIE 202
RhoGAP_ARHGAP21 cd04395
RhoGAP_ARHGAP21: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 793-973 1.72e-46

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: 165.27  E-value: 1.72e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902 793 SQEKTRVPSFVEKCIRAVEKRGLEIDGLYRVSGNLAVIQKLR--FKADHEDLDLEEGNW-DIHVITGALKLFFRELQEPL 869
Cdd:cd04395    12 SSENPYVPLIVEVCCNIVEARGLETVGIYRVPGNNAAISALQeeLNRGGFDIDLQDPRWrDVNVVSSLLKSFFRKLPEPL 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902 870 FPYNLFNEFICAIKTPDYYSKISHMRNLVRSLPPPNHDTMEALFSHLRRVIQHGNENRMTVQNVAIVFGPTLLKPEEET- 948
Cdd:cd04395    92 FTNELYPDFIEANRIEDPVERLKELRRLIHSLPDHHYETLKHLIRHLKTVADNSEVNKMEPRNLAIVFGPTLVRTSDDNm 171

                         170       180
                  ....*....|....*....|....*
gi 1207112902 949 ASIATYMVFQNQIVEFLLSEFESIF 973
Cdd:cd04395   172 ETMVTHMPDQCKIVETLIQHYDWFF 196
RhoGAP_fRGD1 cd04398
RhoGAP_fRGD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 784-973 1.99e-46

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: 164.88  E-value: 1.99e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902 784 FGCHLHNLCSQEKTRVPSFVEKCIRAVEKRGLEIDGLYRVSGNLAVIQKLR--FKADHEDLDL---EEGNWDIHVITGAL 858
Cdd:cd04398     1 FGVPLEDLILREGDNVPNIVYQCIQAIENFGLNLEGIYRLSGNVSRVNKLKelFDKDPLNVLLispEDYESDIHSVASLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902 859 KLFFRELQEPLFPYNLFNEFICAIKTPDYYSKISHMRNLVRSLPPPNHDTMEALFSHLRRVIQHGNENRMTVQNVAIVFG 938
Cdd:cd04398    81 KLFFRELPEPLLTKALSREFIEAAKIEDESRRRDALHGLINDLPDANYATLRALMFHLARIKEHESVNRMSVNNLAIIWG 160

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1207112902 939 PTLLKPEEETASiatYMVFQNQIVEFLLSEFESIF 973
Cdd:cd04398   161 PTLMNAAPDNAA---DMSFQSRVIETLLDNAYQIF 192
RhoGAP_chimaerin cd04372
RhoGAP_chimaerin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 784-973 2.14e-46

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: 164.61  E-value: 2.14e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902 784 FGCHLHNLCSQEKTRVPSFVEKCIRAVEKRGLEIDGLYRVSGNLAVIQ--KLRFKADHEDLDLEEGNW-DIHVITGALKL 860
Cdd:cd04372     1 YGCDLTTLVKAHNTQRPMVVDMCIREIEARGLQSEGLYRVSGFAEEIEdvKMAFDRDGEKADISATVYpDINVITGALKL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902 861 FFRELQEPLFPYNLFNEFICAIKTPDYYSKISHMRNLVRSLPPPNHDTMEALFSHLRRVIQHGNENRMTVQNVAIVFGPT 940
Cdd:cd04372    81 YFRDLPIPVITYDTYPKFIDAAKISNPDERLEAVHEALMLLPPAHYETLRYLMEHLKRVTLHEKDNKMNAENLGIVFGPT 160

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1207112902 941 LLKPEEETASIA-TYMVFQNQIVEFLLSEFESIF 973
Cdd:cd04372   161 LMRPPEDSALTTlNDMRYQILIVQLLITNEDVLF 194
PH_ARHGAP9-like cd13233
Beta-spectrin pleckstrin homology (PH) domain; ARHGAP family genes encode Rho/Rac/Cdc42-like ...
 590-701 8.97e-44

Beta-spectrin pleckstrin homology (PH) domain; ARHGAP family genes encode Rho/Rac/Cdc42-like GTPase activating proteins with RhoGAP domain. The ARHGAP members here all have a PH domain upstream of their C-terminal RhoGAP domain. Some have additional N-terminal SH3 and WW domains. The members here include: ARHGAP9, ARHGAP12, ARHGAP15, and ARHGAP27. ARHGAP27 and ARHGAP12 shared the common-domain structure, consisting of SH3, WW, PH, and RhoGAP domains. The PH domain of ArhGAP9 employs a non-canonical phosphoinositide binding mechanism, a variation of the spectrin- Ins(4,5)P2-binding mode, that gives rise to a unique PI binding profile, namely a preference for both PI(4,5)P2 and the PI 3-kinase products PI(3,4,5)P3 and PI(3,4)P2. This lipid binding mechanism is also employed by the PH domain of Tiam1 and Slm1. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270053  Cd Length: 110  Bit Score: 153.98  E-value: 8.97e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902 590 EKAGILNKTKVSENGKKVRKNWGHSWTVLHGGKLTFHKDPKSTpagASSKTNQILPEFTVDLKGATINRAPkDKSSKKNV 669
Cdd:cd13233     1 EKQGLLNKTKIAENGKKLRKNWSTSWVVLTSSHLLFYKDAKSA---AKSGNPYSKPESSVDLRGASIEWAK-EKSSRKNV 76

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1207112902 670 LELKTRTGAEYLIQYDTDSIIQDWHKVILDTI 701
Cdd:cd13233    77 FQISTVTGTEFLLQSDNDTEIREWFDAIKAVI 108
RhoGAP_Bcr cd04387
RhoGAP_Bcr: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of Bcr ...
 784-963 1.95e-41

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: 150.85  E-value: 1.95e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902 784 FGCHLHNLCSQEKTRVPSFVEKCIRAVEKRGLEIDGLYRVSGNLAVIQKLR--FKADHEDLDLEEGNWDIHVITGALKLF 861
Cdd:cd04387     1 FGVKISTVTKRERSKVPYIVRQCVEEVERRGMEEVGIYRISGVATDIQALKaaFDTNNKDVSVMLSEMDVNAIAGTLKLY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902 862 FRELQEPLFPYNLFNEFICAIKTPDYYSKISHMRNLVRSLPPPNHDTMEALFSHLRRVIQHGNENRMTVQNVAIVFGPTL 941
Cdd:cd04387    81 FRELPEPLFTDELYPNFAEGIALSDPVAKESCMLNLLLSLPDPNLVTFLFLLHHLKRVAEREEVNKMSLHNLATVFGPTL 160

                         170       180
                  ....*....|....*....|..
gi 1207112902 942 LKPEEETASIATYMVFQNQIVE 963
Cdd:cd04387   161 LRPSEKESKIPTNTMTDSWSLE 182
RhoGAP_p190 cd04373
RhoGAP_p190: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 784-948 7.67e-40

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: 145.68  E-value: 7.67e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902 784 FGCHLHNLCSQEKtRVPSFVEKCIRAVEKRGLEIDGLYRVSGN---LAVIQKlRFKADHEdLDLEEGNWDIHVITGALKL 860
Cdd:cd04373     1 FGVPLANVVTSEK-PIPIFLEKCVEFIEATGLETEGIYRVSGNkthLDSLQK-QFDQDHN-LDLVSKDFTVNAVAGALKS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902 861 FFRELQEPLFPYNLFNEFICAIKTPDYYSKISHMRNLVRSLPPPNHDTMEALFSHLRRVIQHGNENRMTVQNVAIVFGPT 940
Cdd:cd04373    78 FFSELPDPLIPYSMHLELVEAAKINDREQRLHALKELLKKFPPENFDVFKYVITHLNKVSQNSKVNLMTSENLSICFWPT 157


                  ....*...
gi 1207112902 941 LLKPEEET 948
Cdd:cd04373   158 LMRPDFTS 165
RhoGAP_MgcRacGAP cd04382
RhoGAP_MgcRacGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 798-967 7.29e-38

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: 140.12  E-value: 7.29e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902 798 RVPSFVEKCIRAVEKRGLEIDGLYRVSGNLAVIQKLRFKADHEDLDLEEGNWDIHVITGALKLFFRELQEPLFPYNLFNE 877
Cdd:cd04382    16 MIPALIVHCVNEIEARGLTEEGLYRVSGSEREVKALKEKFLRGKTVPNLSKVDIHVICGCLKDFLRSLKEPLITFALWKE 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902 878 FICAIKTPDYYSKISHMRNLVRSLPPPNHDTMEALFSHLRRVIQhGNENRMTVQNVAIVFGPTL---LKPEEETASIATY 954
Cdd:cd04382    96 FMEAAEILDEDNSRAALYQAISELPQPNRDTLAFLILHLQRVAQ-SPECKMDINNLARVFGPTIvgySVPNPDPMTILQD 174

                         170
                  ....*....|...
gi 1207112902 955 MVFQNQIVEFLLS 967
Cdd:cd04382   175 TVRQPRVVERLLE 187
RhoGAP_myosin_IX cd04377
RhoGAP_myosin_IX: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 784-968 1.01e-37

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: 139.50  E-value: 1.01e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902 784 FGCHLHNLCSqEKTRVPSFVEKCIRAVEKRGLEIDGLYRVSGNLAVIQKLR--FKADHEDLDLEegNWDIHVITGALKLF 861
Cdd:cd04377     1 FGVSLSSLTS-EDRSVPLVLEKLLEHIEMHGLYTEGIYRKSGSANKIKELRqgLDTDPDSVNLE--DYPIHVITSVLKQW 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902 862 FRELQEPLFPYNLFNEFICAIKTPDYYSKISHMRNLVRSLPPPNHDTMEALFSHLRRVIQHGNENRMTVQNVAIVFGPTL 941
Cdd:cd04377    78 LRELPEPLMTFELYENFLRAMELEEKQERVRALYSVLEQLPRANLNTLERLIFHLVRVALQEEVNRMSANALAIVFAPCI 157

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1207112902 942 LK------PEEETASIATymvfQNQIVEFLLSE 968
Cdd:cd04377   158 LRcpdtadPLQSLQDVSK----TTTCVETLIKE 186
RhoGAP_GMIP_PARG1 cd04378
RhoGAP_GMIP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 784-967 3.50e-36

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: 135.63  E-value: 3.50e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902 784 FGCHLHNLCSQEKTRVPSFVEKCIRAVEKRGLEIDGLYRVSGNLAVIQKL--RFKADHEDLDLEEGNwdIHVITGALKLF 861
Cdd:cd04378     1 FGVDFSQVPRDFPDEVPFIIKKCTSEIENRALGVQGIYRVSGSKARVEKLcqAFENGKDLVELSELS--PHDISSVLKLF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902 862 FRELQEPLFPYNLFNEFI-------------CAIKTPDYYSKISH-MRNLVRSLPPPNHDTMEALFSHLRRVIQHGNENR 927
Cdd:cd04378    79 LRQLPEPLILFRLYNDFIalakeiqrdteedKAPNTPIEVNRIIRkLKDLLRQLPASNYNTLQHLIAHLYRVAEQFEENK 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1207112902 928 MTVQNVAIVFGPTLLKPEEETASIA-TYMV---FQNQIVEFLLS 967
Cdd:cd04378   159 MSPNNLGIVFGPTLIRPRPGDADVSlSSLVdygYQARLVEFLIT 202
RhoGAP_ARAP cd04385
RhoGAP_ARAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
 799-946 2.42e-35

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: 132.82  E-value: 2.42e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902 799 VPSFVEKCIRAVEKRGLEIDGLYRVSGNLAVIQKL--RFKADHEDLDLEEGNWDIHVITGALKLFFRELQEPLFPYNLFN 876
Cdd:cd04385    15 IPVIVDKCIDFITQHGLMSEGIYRKNGKNSSVKKLleAFRKDARSVQLREGEYTVHDVADVLKRFLRDLPDPLLTSELHA 94

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902 877 EFICAIKTPDYYSKISHMRNLVRSLPPPNHDTMEALFSHLRRVIQHGNENRMTVQNVAIVFGPTLLKPEE 946
Cdd:cd04385    95 EWIEAAELENKDERIARYKELIRRLPPINRATLKVLIGHLYRVQKHSDENQMSVHNLALVFGPTLFQTDE 164
RhoGAP_nadrin cd04386
RhoGAP_nadrin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 783-973 3.67e-35

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: 132.97  E-value: 3.67e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902 783 VFGCHLHNLCSQEKTRVPSFVEKCIRAVEKRGLEIDGLYRVSGNLAVIQKLR--FKADHEDLDLEEGNWDIHVITGALKL 860
Cdd:cd04386     4 VFGTPLEEHLKRTGREIALPIEACVMCLLETGMNEEGLFRVGGGASKLKRLKaaLDAGTFSLPLDEFYSDPHAVASALKS 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902 861 FFRELQEPLFPYNLFNEFICAIKTPDYYSKISHMRNLVRSLPPPNHDTMEALFSHLRRVIQHGNENRMTVQNVAIVFGPT 940
Cdd:cd04386    84 YLRELPDPLLTYNLYEDWVQAANKPDEDERLQAIWRILNKLPRENRDNLRYLIKFLSKLAQKSDENKMSPSNIAIVLAPN 163

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1207112902 941 LLKPEEETASIATYM---VFQNQIVEFLLSEFESIF 973
Cdd:cd04386   164 LLWAKNEGSLAEMAAgtsVHVVAIVELIISHADWFF 199
RhoGAP_CdGAP cd04384
RhoGAP_CdGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 783-966 4.85e-35

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: 132.24  E-value: 4.85e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902 783 VFGCHLHNLCSQEKTRVPSFVEKCIRAVEKRGLeIDGLYRVSGNLAVIQKLRFKADHE---DLDLEEGNWDIHVITGALK 859
Cdd:cd04384     2 VFGCDLTEHLLNSGQDVPQVLKSCTEFIEKHGI-VDGIYRLSGIASNIQRLRHEFDSEqipDLTKDVYIQDIHSVSSLCK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902 860 LFFRELQEPLFPYNLFNEFICAIKTPDYYSKISHMRNLVRSLPPPNHDTMEALFSHLRRVIQHGNENRMTVQNVAIVFGP 939
Cdd:cd04384    81 LYFRELPNPLLTYQLYEKFSEAVSAASDEERLEKIHDVIQQLPPPHYRTLEFLMRHLSRLAKYCSITNMHAKNLAIVWAP 160

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1207112902 940 TLLKPEEETASI----ATYMV--FQNQIVEFLL 966
Cdd:cd04384   161 NLLRSKQIESACfsgtAAFMEvrIQSVVVEFIL 193
RhoGAP_fBEM3 cd04400
RhoGAP_fBEM3: RhoGAP (GTPase-activator [GAP] protein for Rho-like small GTPases) domain of ...
 783-973 4.70e-32

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: 123.62  E-value: 4.70e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902 783 VFGCHLH---NLCSQEKTR--VPSFVEKCIRAVEKRGLEID-GLYRVSGNLAVIQKL--RFKaDHEDLDLEEGN--WDIH 852
Cdd:cd04400     1 IFGSPLEeavELSSHKYNGrdLPSVVYRCIEYLDKNRAIYEeGIFRLSGSASVIKQLkeRFN-TEYDVDLFSSSlyPDVH 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902 853 VITGALKLFFRELQEPLFPYNLFNEFICAIKTP-DYYSKISHMRNLVRSLPPPNHDTMEALFSHLRRVIQHGNENRMTVQ 931
Cdd:cd04400    80 TVAGLLKLYLRELPTLILGGELHNDFKRLVEENhDRSQRALELKDLVSQLPQANYDLLYVLFSFLRKIIEHSDVNKMNLR 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1207112902 932 NVAIVFGPTLLKPEEetasiatymVFQnqiveFLLSEFESIF 973
Cdd:cd04400   160 NVCIVFSPTLNIPAG---------IFV-----LFLTDFDCIF 187
RhoGAP_myosin_IXB cd04407
RhoGAP_myosin_IXB: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 784-943 4.49e-31

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: 120.48  E-value: 4.49e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902 784 FGCHLHNLCSqEKTRVPSFVEKCIRAVEKRGLEIDGLYRVSGNLAVIQKLR--FKADHEDLDLEegNWDIHVITGALKLF 861
Cdd:cd04407     1 FGVRVGSLTS-NKTSVPIVLEKLLEHVEMHGLYTEGIYRKSGSANRMKELHqlLQADPENVKLE--NYPIHAITGLLKQW 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902 862 FRELQEPLFPYNLFNEFICAIKTPDYYSKISHMRNLVRSLPPPNHDTMEALFSHLRRVIQHGNENRMTVQNVAIVFGPTL 941
Cdd:cd04407    78 LRELPEPLMTFAQYNDFLRAVELPEKQEQLQAIYRVLEQLPTANHNTLERLIFHLVKVALEEDVNRMSPNALAIVFAPCL 157


                  ..
gi 1207112902 942 LK 943
Cdd:cd04407   158 LR 159
RhoGAP_GMIP cd04408
RhoGAP_GMIP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of GMIP ...
 784-967 5.41e-31

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: 120.69  E-value: 5.41e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902 784 FGCHLHNLCSQEKTRVPSFVEKCIRAVEKRGLEIDGLYRVSGNLAVIQKL--RFKADHEDLDLEEGNwdIHVITGALKLF 861
Cdd:cd04408     1 FGVDFSQLPRDFPEEVPFVVVRCTAEIENRALGVQGIYRISGSKARVEKLcqAFENGRDLVDLSGHS--PHDITSVLKHF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902 862 FRELQEPLFPYNLFNEFIC-----------AIKTPDYYSKISH-MRNLVRSLPPPNHDTMEALFSHLRRVIQHGNENRMT 929
Cdd:cd04408    79 LKELPEPVLPFQLYDDFIAlakelqrdsekAAESPSIVENIIRsLKELLGRLPVSNYNTLRHLMAHLYRVAERFEDNKMS 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1207112902 930 VQNVAIVFGPTLLKPEEETASIATYMV---FQNQIVEFLLS 967
Cdd:cd04408   159 PNNLGIVFGPTLLRPLVGGDVSMICLLdtgYQAQLVEFLIS 199
RhoGAP_PARG1 cd04409
RhoGAP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 784-966 1.66e-29

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: 116.83  E-value: 1.66e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902 784 FGCHLHNLCSQEKTRVPSFVEKCIRAVEKRGLEIDGLYRVSGNLAVIQKL--RFKADHEDLDLEEgnWDIHVITGALKLF 861
Cdd:cd04409     1 FGADFAQVAKKSPDGIPFIIKKCTSEIESRALCLKGIYRVNGAKSRVEKLcqAFENGKDLVELSE--LSPHDISNVLKLY 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902 862 FRELQEPLFPYNLFNEFICAIK----------TPDYYSK------------ISHMRNLVRSLPPPNHDTMEALFSHLRRV 919
Cdd:cd04409    79 LRQLPEPLILFRLYNEFIGLAKesqhvnetqeAKKNSDKkwpnmctelnriLLKSKDLLRQLPAPNYNTLQFLIVHLHRV 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1207112902 920 IQHGNENRMTVQNVAIVFGPTLLKPEEETA--SIATYMVFQNQ--IVEFLL 966
Cdd:cd04409   159 SEQAEENKMSASNLGIIFGPTLIRPRPTDAtvSLSSLVDYPHQarLVELLI 209
RhoGAP_srGAP cd04383
RhoGAP_srGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 799-942 1.95e-29

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: 115.98  E-value: 1.95e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902 799 VPSFVEKCIRAVEKRGLEIDGLYRVSGNLAVIQKLR--FKADHEDLDLEEGNWDIHVITGALKLFFRELQEPLFPYNLFN 876
Cdd:cd04383    18 IPLVVESCIRFINLYGLQHQGIFRVSGSQVEVNDIKnaFERGEDPLADDQNDHDINSVAGVLKLYFRGLENPLFPKERFE 97

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207112902 877 EFICAIKTPDYYSKISHMRNLVRSLPPPNHDTMEALFSHLRRVIQHGNENRMTVQNVAIVFGPTLL 942
Cdd:cd04383    98 DLMSCVKLENPTERVHQIREILSTLPRSVIIVMRYLFAFLNHLSQFSDENMMDPYNLAICFGPTLM 163
RhoGAP-p50rhoGAP cd04404
RhoGAP-p50rhoGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 799-973 3.91e-29

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: 115.13  E-value: 3.91e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902 799 VPSFVEKCIRAVEKRGLEIDGLYRVSGNLAVIQKLRFK---ADHEDLDLEEgnwDIHVITGALKLFFRELQEPLFPYNLF 875
Cdd:cd04404    23 IPPVVRETVEYLQAHALTTEGIFRRSANTQVVKEVQQKynmGEPVDFDQYE---DVHLPAVILKTFLRELPEPLLTFDLY 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902 876 NEfICAIKTPDYYSKISHMRNLVRSLPPPNHDTMEALFSHLRRVIQHGNENRMTVQNVAIVFGPTLLKPEEETASIATyM 955
Cdd:cd04404   100 DD-IVGFLNVDKEERVERVKQLLQTLPEENYQVLKYLIKFLVQVSAHSDQNKMTNSNLAVVFGPNLLWAKDASMSLSA-I 177

                         170
                  ....*....|....*...
gi 1207112902 956 VFQNQIVEFLLSEFESIF 973
Cdd:cd04404   178 NPINTFTKFLLDHQDEIF 195
RhoGAP_SYD1 cd04379
RhoGAP_SYD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
 784-947 1.73e-28

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: 113.72  E-value: 1.73e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902 784 FGCHLHNLCSQEKTR--VPSFVEKCIRAVEKRGLEIDGLYRVSGNLAVIQKLR--FKADHEDLDLEEGNW-DIHVITGAL 858
Cdd:cd04379     1 FGVPLSRLVEREGESrdVPIVLQKCVQEIERRGLDVIGLYRLCGSAAKKKELRdaFERNSAAVELSEELYpDINVITGVL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902 859 KLFFRELQEPLFPYNLFNEFI--CAIKTPDYYS-KISHMRNLVRSLPPPNHDTMEALFSHLRRVIQHGNENRMTVQNVAI 935
Cdd:cd04379    81 KDYLRELPEPLITPQLYEMVLeaLAVALPNDVQtNTHLTLSIIDCLPLSAKATLLLLLDHLSLVLSNSERNKMTPQNLAV 160

                         170
                  ....*....|..
gi 1207112902 936 VFGPTLLKPEEE 947
Cdd:cd04379   161 CFGPVLMFCSQE 172
RhoGAP_ARHGAP18 cd04391
RhoGAP_ARHGAP18: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 783-944 9.15e-28

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: 112.05  E-value: 9.15e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902 783 VFGCHLHNLCSQEK-----TRVPSFVEKCIRAVEKRGLEIDGLYRVSGnlaviQKLRFKADHEDLDLE----EGNWD--- 850
Cdd:cd04391     1 LFGVPLSTLLERDQkkvpgSKVPLIFQKLINKLEERGLETEGILRIPG-----SAQRVKFLCQELEAKfyegTFLWDqvk 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902 851 IHVITGALKLFFRELQEPLFPYNLFNEFICAIKTPDYYSKISHMRNLVRSLPPPNHDTMEALFSHLRRVIQHGNENRMTV 930
Cdd:cd04391    76 QHDAASLLKLFIRELPQPLLTVEYLPAFYSVQGLPSKKDQLQALNLLVLLLPEANRDTLKALLEFLQKVVDHEEKNKMNL 155

                         170
                  ....*....|....
gi 1207112902 931 QNVAIVFGPTLLKP 944
Cdd:cd04391   156 WNVAMIMAPNLFPP 169
RhoGAP_ARHGAP6 cd04376
RhoGAP_ARHGAP6: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 799-973 6.00e-26

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: 106.37  E-value: 6.00e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902 799 VPSFVEKCIRAVEKRGLEIDGLYRVSGNLAVIQKLRfkadhEDLD------LEEgNWDIHVITGALKLFFRELQEPLFPY 872
Cdd:cd04376     9 VPRLVESCCQHLEKHGLQTVGIFRVGSSKKRVRQLR-----EEFDrgidvvLDE-NHSVHDVAALLKEFFRDMPDPLLPR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902 873 NLFNEFICAIK-TPDyySKISHMRNLVRSLPPPNHDTMEALFSHLRRVIQHGNE-----------NRMTVQNVAIVFGPT 940
Cdd:cd04376    83 ELYTAFIGTALlEPD--EQLEALQLLIYLLPPCNCDTLHRLLKFLHTVAEHAADsidedgqevsgNKMTSLNLATIFGPN 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1207112902 941 LLK---------------PEEETASIatymvfqnQIVEFLLSEFESIF 973
Cdd:cd04376   161 LLHkqksgerefvqaslrIEESTAII--------NVVQTMIDNYEELF 200
RhoGAP_ARHGAP22_24_25 cd04390
RhoGAP_ARHGAP22_24_25: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
 783-973 1.48e-25

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: 105.22  E-value: 1.48e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902 783 VFGCHLHNLCSQEKT----RVPSFVEKCIRAVEKRGLEIDGLYRVSGNLAVIQKLRFKADHEDLDLEEGNWDIHVITGAL 858
Cdd:cd04390     2 VFGQRLEDTVAYERKfgprLVPILVEQCVDFIREHGLKEEGLFRLPGQANLVKQLQDAFDAGERPSFDSDTDVHTVASLL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902 859 KLFFRELQEPLFPYNLFNEFICAIKTPDYYSKISH--MRNLVRSLPPPNHDTMEALFSHLRRVIQHGNENRMTVQNVAIV 936
Cdd:cd04390    82 KLYLRELPEPVIPWAQYEDFLSCAQLLSKDEEKGLgeLMKQVSILPKVNYNLLSYICRFLDEVQSNSSVNKMSVQNLATV 161

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1207112902 937 FGPTLLKPE-EETASIATYMVFQNQIVEFLLSEFESIF 973
Cdd:cd04390   162 FGPNILRPKvEDPATIMEGTPQIQQLMTVMISKHEPLF 199
SH3_ARHGAP27 cd12069
Src Homology 3 domain of Rho GTPase-activating protein 27; Rho GTPase-activating proteins ...
 22-77 2.11e-24

Src Homology 3 domain of Rho GTPase-activating protein 27; Rho GTPase-activating proteins (RhoGAPs or ARHGAPs) bind to Rho proteins and enhance the hydrolysis rates of bound GTP. ARHGAP27, also called CAMGAP1, shows GAP activity towards Rac1 and Cdc42. It binds the adaptor protein CIN85 and may play a role in clathrin-mediated endocytosis. It contains SH3, WW, Pleckstin homology (PH), and RhoGAP domains. SH3 domains bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs; they play a role in the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components and mediate multiprotein complex assemblies.


Pssm-ID: 213002  Cd Length: 57  Bit Score: 96.81  E-value: 2.11e-24
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1207112902  22 VLVNYEYTYTARDGRNVSIKPNEHYILVNKTNEEWWHVQKDAADKPFYIPAKYVTE 77
Cdd:cd12069     2 VLVEHAFEYTGKDGRLVSIKPNERYILLRRTNEHWWHVRRDKGTRPFYIPAKYVKE 57
RhoGAP_FAM13A1a cd04393
RhoGAP_FAM13A1a: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 783-939 2.24e-23

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


Pssm-ID: 239858 [Multi-domain]  Cd Length: 189  Bit Score: 98.69  E-value: 2.24e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902 783 VFGCHLHNLCSQEKTR--VPSFVEKCIRAVEKRGLEIDGLYRVSGNLAVIQKLRFKADH-EDLDLEEGNwDIHVITGALK 859
Cdd:cd04393     2 VFGVPLQELQQAGQPEngVPAVVRHIVEYLEQHGLEQEGLFRVNGNAETVEWLRQRLDSgEEVDLSKEA-DVCSAASLLR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902 860 LFFRELQEPLFPYNLFNEFI-CAIKTPDYYSKISHMRNLVRSLPPPNHDTMEALFSHLRRVIQHGNENRMTVQNVAIVFG 938
Cdd:cd04393    81 LFLQELPEGLIPASLQIRLMqLYQDYNGEDEFGRKLRDLLQQLPPVNYSLLKFLCHFLSNVASQHHENRMTAENLAAVFG 160


                  .
gi 1207112902 939 P 939
Cdd:cd04393   161 P 161
RhoGap_RalBP1 cd04381
RhoGap_RalBP1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 798-941 3.14e-23

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: 97.89  E-value: 3.14e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902 798 RVPSFVEKCIRAVEKRGLEIDGLYRVSGNLAVIQKLRFKADHED-LDLEEgnWDIHVITGALKLFFRELQEPLFPYNLFN 876
Cdd:cd04381    19 DLPLVFRECIDYVEKHGMKCEGIYKVSGIKSKVDELKAAYNRREsPNLEE--YEPPTVASLLKQYLRELPEPLLTKELMP 96

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207112902 877 EFICAIKTPDYYSKISHMRNLVRSLPPPNHDTMEALFSHLRRVIQHGNENRMTVQNVAIVFGPTL 941
Cdd:cd04381    97 RFEEACGRPTEAEREQELQRLLKELPECNRLLLAWLIVHMDHVIAQELETKMNIQNISIVLSPTV 161
RhoGAP_myosin_IXA cd04406
RhoGAP_myosin_IXA: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 784-948 4.43e-21

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


Pssm-ID: 239871  Cd Length: 186  Bit Score: 91.99  E-value: 4.43e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902 784 FGCHLHNLCSQEKTrVPSFVEKCIRAVEKRGLEIDGLYRVSGNLAVIQKLRFKADHEDLDLEEGNWDIHVITGALKLFFR 863
Cdd:cd04406     1 FGVELSRLTSEDRS-VPLVVEKLINYIEMHGLYTEGIYRKSGSTNKIKELRQGLDTDANSVNLDDYNIHVIASVFKQWLR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902 864 ELQEPLFPYNLFNEFICAIKTPDYYSKISHMRNLVRSLPPPNHDTMEALFSHLRRVIQHGNENRMTVQNVAIVFGPTLLK 943
Cdd:cd04406    80 DLPNPLMTFELYEEFLRAMGLQERRETVRGVYSVIDQLSRTHLNTLERLIFHLVRIALQEETNRMSANALAIVFAPCILR 159


                  ....*
gi 1207112902 944 PEEET 948
Cdd:cd04406   160 CPDTT 164
SH3_ARHGAP9_like cd11888
Src Homology 3 domain of Rho GTPase-activating protein 9 and similar proteins; This subfamily ...
 21-74 5.30e-21

Src Homology 3 domain of Rho GTPase-activating protein 9 and similar proteins; This subfamily is composed of Rho GTPase-activating proteins including mammalian ARHGAP9, and vertebrate ARHGAPs 12 and 27. RhoGAPs (or ARHGAPs) bind to Rho proteins and enhance the hydrolysis rates of bound GTP. ARHGAP9 functions as a GAP for Rac and Cdc42, but not for RhoA. It negatively regulates cell migration and adhesion. It also acts as a docking protein for the MAP kinases Erk2 and p38alpha, and may facilitate cross-talk between the Rho GTPase and MAPK pathways to control actin remodeling. ARHGAP27, also called CAMGAP1, shows GAP activity towards Rac1 and Cdc42. It binds the adaptor protein CIN85 and may play a role in clathrin-mediated endocytosis. ARHGAP12 has been shown to display GAP activity towards Rac1. It plays a role in regulating HFG-driven cell growth and invasiveness. ARHGAPs in this subfamily contain SH3, WW, Pleckstin homology (PH), and RhoGAP domains. SH3 domains bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs; they play a role in the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components and mediate multiprotein complex assemblies.


Pssm-ID: 212821 [Multi-domain]  Cd Length: 54  Bit Score: 87.04  E-value: 5.30e-21
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1207112902  21 QVLVNYEYTYTARDGRNVSIKPNEHYILVNKTNEEWWHVQKDAADKPFYIPAKY 74
Cdd:cd11888     1 YVVVLYPFEYTGKDGRKVSIKEGERFLLLKKSNDDWWQVRRPGDSKPFYVPAQY 54
RhoGAP-ARHGAP11A cd04394
RhoGAP-ARHGAP11A: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 783-966 6.46e-21

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: 91.76  E-value: 6.46e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902 783 VFGCHLHNLCSQ---EKTRVPSFVEKCIRAVEKRgLEIDGLYRVSGNLAVIQKLRFKADHEDLDLEegNWDIHVITGALK 859
Cdd:cd04394     1 VFGVPLHSLPHStvpEYGNVPKFLVDACTFLLDH-LSTEGLFRKSGSVVRQKELKAKLEGGEACLS--SALPCDVAGLLK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902 860 LFFRELQEPLFPYNLFNEFICAIKTPDYYSKISHMRNLVRSLPPPNHDTMEALFSHLRRVIQHGNENRMTVQNVAIVFGP 939
Cdd:cd04394    78 QFFRELPEPLLPYDLHEALLKAQELPTDEERKSATLLLTCLLPDEHVNTLRYFFSFLYDVAQRCSENKMDSSNLAVIFAP 157

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1207112902 940 TLLKPEE--ETASIATYMVFQNQ--IVEFLL 966
Cdd:cd04394   158 NLFQSEEggEKMSSSTEKRLRLQaaVVQTLI 188
RhoGAP_ARHGAP20 cd04402
RhoGAP_ARHGAP20: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 784-973 4.77e-18

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: 83.12  E-value: 4.77e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902 784 FGCHLHNLCsqEKTRVPSFVEKCIRAVEKRGLEIDGLYRVSGNLAVIQKLRFKAD---HEDLDLEegnwDIHVITGALKL 860
Cdd:cd04402     2 FGQPLSNIC--EDDNLPKPILDMLSLLYQKGPSTEGIFRRSANAKACKELKEKLNsgvEVDLKAE----PVLLLASVLKD 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902 861 FFRELQEPLFPYNLFNEFICAIKTPDYYSKISHMRNLVRSLPPPNHDTMEALFSHLRRVIQHGNENRMTVQNVAIVFGPT 940
Cdd:cd04402    76 FLRNIPGSLLSSDLYEEWMSALDQENEEEKIAELQRLLDKLPRPNVLLLKHLICVLHNISQNSETNKMDAFNLAVCIAPS 155

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1207112902 941 LLKPEEETASIATYMVFQNQIVEFLLSEFESIF 973
Cdd:cd04402   156 LLWPPASSELQNEDLKKVTSLVQFLIENCQEIF 188
SH3_ARHGAP12 cd12070
Src Homology 3 domain of Rho GTPase-activating protein 12; Rho GTPase-activating proteins ...
 24-78 1.99e-17

Src Homology 3 domain of Rho GTPase-activating protein 12; Rho GTPase-activating proteins (RhoGAPs or ARHGAPs) bind to Rho proteins and enhance the hydrolysis rates of bound GTP. ARHGAP12 has been shown to display GAP activity towards Rac1. It plays a role in regulating hepatocyte growth factor (HGF)-driven cell growth and invasiveness. It contains SH3, WW, Pleckstin homology (PH), and RhoGAP domains. SH3 domains bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs; they play a role in the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components and mediate multiprotein complex assemblies.


Pssm-ID: 213003  Cd Length: 60  Bit Score: 76.94  E-value: 1.99e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1207112902  24 VNYEYTYTARDgRNVSIKPNEHYILVNKTNEEWWHVQKDAADKPFYIPAKYVTEL 78
Cdd:cd12070     5 VEYDYDYEAKD-RKIVIKQGERYILVKKTNDDWWQVKKDENSKPFYVPAQYVKEV 58
RhoGAP_ARHGAP19 cd04392
RhoGAP_ARHGAP19: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 812-974 3.74e-17

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


Pssm-ID: 239857  Cd Length: 208  Bit Score: 80.97  E-value: 3.74e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902 812 KRGLEIDGLYRVSGNLAVIQKLRFKADH-EDLDLEEGNWDIHVITGALKLFFRELQEPL-----FPYNL-------FNEF 878
Cdd:cd04392    21 EKNLRVEGLFRKPGNSARQQELRDLLNSgTDLDLESGGFHAHDCATVLKGFLGELPEPLlthahYPAHLqiadlcqFDEK 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902 879 ICAIKTPDYYSKISHMRNLVRSLPPPNHDTMEALFSHLRRVIQHGNENRMTVQNVAIVFGPTLLKPEEETASIATYMVFQ 958
Cdd:cd04392   101 GNKTSAPDKERLLEALQLLLLLLPEENRNLLKLILDLLYQTAKHEDKNKMSADNLALLFTPHLICPRNLTPEDLHENAQK 180

                         170
                  ....*....|....*..
gi 1207112902 959 -NQIVEFLLSEFESIFH 974
Cdd:cd04392   181 lNSIVTFMIKHSQKLFK 197
RhoGAP_fLRG1 cd04397
RhoGAP_fLRG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 796-972 5.73e-16

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: 77.79  E-value: 5.73e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902 796 KTRVPSFVEKCIRAVEKRGLEIDGLYRVSGNLAVIQKLRFKADH---EDLDLEEGNwdiHVITGAL-KLFFRELQEPLFP 871
Cdd:cd04397    24 KLRIPALIDDIISAMRQMDMSVEGVFRKNGNIRRLKELTEEIDKnptEVPDLSKEN---PVQLAALlKKFLRELPDPLLT 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902 872 YNLFNEFICA--IKTPDYYSKISHMrnLVRSLPPPNHDTMEALFSHLRRV--IQHGNE---NRMTVQNVAIVFGPTLLKP 944
Cdd:cd04397   101 FKLYRLWISSqkIEDEEERKRVLHL--VYCLLPKYHRDTMEVLFSFLKWVssFSHIDEetgSKMDIHNLATVITPNILYS 178

                         170       180
                  ....*....|....*....|....*...
gi 1207112902 945 EEETASIATYMVFQNQIVEFLLSEFESI 972
Cdd:cd04397   179 KTDNPNTGDEYFLAIEAVNYLIENNEEF 206
RhoGAP_KIAA1688 cd04389
RhoGAP_KIAA1688: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
 784-959 5.98e-15

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: 73.96  E-value: 5.98e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902 784 FGCHLHNLCSQEKTRVP--------SFVEKCIRAVEkrGLEIDGLYRVSGNLAVIQKLRFKADHEDLDLEeGNWDIHVIT 855
Cdd:cd04389     1 FGSSLEEIMDRQKEKYPelklpwilTFLSEKVLALG--GFQTEGIFRVPGDIDEVNELKLRVDQWDYPLS-GLEDPHVPA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902 856 GALKLFFRELQEPLFPYNLFNEFICAIKTPDyyskisHMRNLVRSLPPPNHDTMEALFSHLRRVIQHGN--ENRMTVQNV 933
Cdd:cd04389    78 SLLKLWLRELEEPLIPDALYQQCISASEDPD------KAVEIVQKLPIINRLVLCYLINFLQVFAQPENvaHTKMDVSNL 151

                         170       180
                  ....*....|....*....|....*.
gi 1207112902 934 AIVFGPTLLKPEEETASIatymVFQN 959
Cdd:cd04389   152 AMVFAPNILRCTSDDPRV----IFEN 173
RhoGAP_p85 cd04388
RhoGAP_p85: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
 800-968 6.79e-14

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


Pssm-ID: 239853  Cd Length: 200  Bit Score: 71.44  E-value: 6.79e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902 800 PSFVEKCIRAVEKRGLEIDGLYR--VSGNLAVIQKLrFKADHEDLDLEEgnWDIHVITGALKLFFRELQEPLFPYNLFNE 877
Cdd:cd04388    16 PPLLIKLVEAIEKKGLESSTLYRtqSSSSLTELRQI-LDCDAASVDLEQ--FDVAALADALKRYLLDLPNPVIPAPVYSE 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902 878 FI-CAIKTPDYYSKISHMRNLVRS--LPPPNHDTMEALFSHLRRVIQHGNENRMTVQNVAIVFGPTLLK---PEEETASi 951
Cdd:cd04388    93 MIsRAQEVQSSDEYAQLLRKLIRSpnLPHQYWLTLQYLLKHFFRLCQSSSKNLLSARALAEIFSPLLFRfqpASSDSPE- 171

                         170
                  ....*....|....*..
gi 1207112902 952 atymvFQNQIVEFLLSE 968
Cdd:cd04388   172 -----FHIRIIEVLITS 183
PH_beta_spectrin cd10571
Beta-spectrin pleckstrin homology (PH) domain; Beta spectrin binds actin and functions as a ...
 593-697 1.30e-12

Beta-spectrin pleckstrin homology (PH) domain; Beta spectrin binds actin and functions as a major component of the cytoskeleton underlying cellular membranes. Beta spectrin consists of multiple spectrin repeats followed by a PH domain, which binds to inositol-1,4,5-trisphosphate. The PH domain of beta-spectrin is thought to play a role in the association of spectrin with the plasma membrane of cells. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 269975  Cd Length: 106  Bit Score: 64.94  E-value: 1.30e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902 593 GILN-KTKVSENGKK-VRKNWGHSWTVLHGGKLTFHKDPKSTPAGaSSKTNqilpEFTVDLKGATINRAPkDKSSKKNVL 670
Cdd:cd10571     3 GFLErKHEWESGGKKaSNRSWKNVYTVLRGQELSFYKDQKAAKSG-ITYAA----EPPLNLYNAVCEVAS-DYTKKKHVF 76

                          90       100
                  ....*....|....*....|....*..
gi 1207112902 671 ELKTRTGAEYLIQYDTDSIIQDWHKVI 697
Cdd:cd10571    77 RLKLSDGAEFLFQAKDEEEMNQWVKKI 103
RhoGAP_DLC1 cd04375
RhoGAP_DLC1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 782-941 9.65e-11

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: 62.82  E-value: 9.65e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902 782 NVFGCHLhnLCSQEKT--RVPSFVEKCIRAVEKRGLEIDGLYRVSGNLAVIQKLR--FKADHEDLDLEEgnWDIHVITGA 857
Cdd:cd04375     3 NVFGVPL--LVNLQRTgqPLPRSIQQAMRWLRNNALDQVGLFRKSGVKSRIQKLRsmIESSTDNVNYDG--QQAYDVADM 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902 858 LKLFFRELQEPLFPYNLFNEFICAIKTPDYYSKISHMRNLVRSLPPPNHDTMEALFSHLRRVIQHGNENRMTVQNVAIVF 937
Cdd:cd04375    79 LKQYFRDLPEPLLTNKLSETFIAIFQYVPKEQRLEAVQCAILLLPDENREVLQTLLYFLSDVAANSQENQMTATNLAVCL 158


                  ....
gi 1207112902 938 GPTL 941
Cdd:cd04375   159 APSL 162
SH3_ARHGAP9 cd12143
Src Homology 3 domain of Rho GTPase-activating protein 9 and similar proteins; Rho ...
 26-74 1.00e-10

Src Homology 3 domain of Rho GTPase-activating protein 9 and similar proteins; Rho GTPase-activating proteins (RhoGAPs or ARHGAPs) bind to Rho proteins and enhance the hydrolysis rates of bound GTP. ARHGAP9 functions as a GAP for Rac and Cdc42, but not for RhoA. It negatively regulates cell migration and adhesion. It also acts as a docking protein for the MAP kinases Erk2 and p38alpha, and may facilitate cross-talk between the Rho GTPase and MAPK pathways to control actin remodeling. It contains SH3, WW, Pleckstin homology (PH), and RhoGAP domains. SH3 domains bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs; they play a role in the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components and mediate multiprotein complex assemblies.


Pssm-ID: 213019  Cd Length: 57  Bit Score: 58.01  E-value: 1.00e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1207112902  26 YEYTYTARDGRNVSIKPNEHYILVNKTNEEWWHVQKDAA---DKPFYIPAKY 74
Cdd:cd12143     6 YAYQYTGADGRQVSIAEGERFLLLRKTNSDWWQVRRLEApstSRPLFVPATY 57
RhoGAP_fSAC7_BAG7 cd04396
RhoGAP_fSAC7_BAG7: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 798-966 1.29e-10

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: 62.43  E-value: 1.29e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902 798 RVPSFVEKCIRAVEKRGLEIDGLYRVSGNLAVIQKLRFKADHEDLDLEEGNWD---IHVITGALKLFFRELQEPLFPYNL 874
Cdd:cd04396    31 YIPVVVAKCGVYLKENATEVEGIFRVAGSSKRIRELQLIFSTPPDYGKSFDWDgytVHDAASVLRRYLNNLPEPLVPLDL 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902 875 FNEF----------ICAIKTPDYYSKISHM-------RNLVRSLPPPNHDTMEALFSHLRRVIQHGNENRMTVQNVAIVF 937
Cdd:cd04396   111 YEEFrnplrkrpriLQYMKGRINEPLNTDIdqaikeyRDLITRLPNLNRQLLLYLLDLLAVFARNSDKNLMTASNLAAIF 190

                         170       180
                  ....*....|....*....|....*....
gi 1207112902 938 GPTLLKPEEETASIATYMVFQnQIVEFLL 966
Cdd:cd04396   191 QPGILSHPDHEMDPKEYKLSR-LVVEFLI 218
PH_ARHGAP21-like cd01253
ARHGAP21 and related proteins pleckstrin homology (PH) domain; ARHGAP family genes encode Rho ...
 590-714 9.83e-10

ARHGAP21 and related proteins pleckstrin homology (PH) domain; ARHGAP family genes encode Rho/Rac/Cdc42-like GTPase activating proteins with a RhoGAP domain. These proteins functions as a GTPase-activating protein (GAP) for RHOA and CDC42. ARHGAP21 controls the Arp2/3 complex and F-actin dynamics at the Golgi complex by regulating the activity of the small GTPase Cdc42. It is recruited to the Golgi by to GTPase, ARF1, through its PH domain and its helical motif. It is also required for CTNNA1 recruitment to adherens junctions. ARHGAP21 and it related proteins all contains a PH domain and a RhoGAP domain. Some of the members have additional N-terminal domains including PDZ, SH3, and SPEC. The ARHGAP21 PH domain interacts with the GTPbound forms of both ARF1 and ARF6 ARF-binding domain/ArfBD. The members here include: ARHGAP15, ARHGAP21, and ARHGAP23. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 269955  Cd Length: 113  Bit Score: 57.00  E-value: 9.83e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902 590 EKAGILN-KTKVSENGKKV-RKNWGHSWTVLHGGKLTFHKDPKSTPAGASSKTNQILPeftVDLKGATINRApKDKSSKK 667
Cdd:cd01253     1 AREGWLHyKQIVTDKGKRVsDRSWKQAWAVLRGHSLYLYKDKREQTPALSIELGSEQR---ISIRGCIVDIA-YSYTKRK 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1207112902 668 NVLELKTRTGAEYLIQYDTDSIIQDWHKVIldtihqlngdQHHSEEE 714
Cdd:cd01253    77 HVFRLTTSDFSEYLFQAEDRDDMLGWIKAI----------QENSNAE 113
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 589-702 9.08e-09

Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.


Pssm-ID: 214574 [Multi-domain]  Cd Length: 102  Bit Score: 53.71  E-value: 9.08e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902  589 LEKAGILNKtkvseNGKKVRKNWGHSWTVLHGGKLTFHKDPKSTPAGAssktnqilPEFTVDLKGATINRAPKDKSSK-K 667
Cdd:smart00233   1 VIKEGWLYK-----KSGGGKKSWKKRYFVLFNSTLLYYKSKKDKKSYK--------PKGSIDLSGCTVREAPDPDSSKkP 67

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1207112902  668 NVLELKTRTGAEYLIQYDTDSIIQDWHKVILDTIH 702
Cdd:smart00233  68 HCFEIKTSDRKTLLLQAESEEEREKWVEALRKAIA 102
PH pfam00169
PH domain; PH stands for pleckstrin homology.
 589-702 2.27e-07

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 49.87  E-value: 2.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902 589 LEKAGILNKtkvseNGKKVRKNWGHSWTVLHGGKLTFHKDPKSTPAGAssktnqilPEFTVDLKGATINRAPK-DKSSKK 667
Cdd:pfam00169   1 VVKEGWLLK-----KGGGKKKSWKKRYFVLFDGSLLYYKDDKSGKSKE--------PKGSISLSGCEVVEVVAsDSPKRK 67

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1207112902 668 NVLELKT---RTGAEYLIQYDTDSIIQDWHKVILDTIH 702
Cdd:pfam00169  68 FCFELRTgerTGKRTYLLQAESEEERKDWIKAIQSAIR 105
RhoGAP_OCRL1 cd04380
RhoGAP_OCRL1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 850-968 1.29e-06

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


Pssm-ID: 239845  Cd Length: 220  Bit Score: 50.42  E-value: 1.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902 850 DIHVITGALKLFFRELQEPLFPYNLFNEFICAIKTPdyYSKISHmrnLVR-SLPPPNHDTMEALFSHLRRVIQHGNENRM 928
Cdd:cd04380   103 SAESVAEALLLFLESLPDPIIPYSLYERLLEAVANN--EEDKRQ---VIRiSLPPVHRNVFVYLCSFLRELLSESADRGL 177

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1207112902 929 TVQNVAIVFGPTLL--KPEEETASIATYMVFQNQIVE-FLLSE 968
Cdd:cd04380   178 DENTLATIFGRVLLrdPPRAGGKERRAERDRKRAFIEqFLLND 220
PH1_Pleckstrin_2 cd13301
Pleckstrin 2 Pleckstrin homology (PH) domain, repeat 1; Pleckstrin is a protein found in ...
 607-711 1.82e-06

Pleckstrin 2 Pleckstrin homology (PH) domain, repeat 1; Pleckstrin is a protein found in platelets. This name is derived from platelet and leukocyte C kinase substrate and the KSTR string of amino acids. Pleckstrin 2 contains two PH domains and a DEP (dishvelled, egl-10, and pleckstrin) domain. Unlike pleckstrin 1, pleckstrin 2 does not contain obvious sites of PKC phosphorylation. Pleckstrin 2 plays a role in actin rearrangement, large lamellipodia and peripheral ruffle formation, and may help orchestrate cytoskeletal arrangement. The PH domains of pleckstrin 2 are thought to contribute to lamellipodia formation. This cd contains the first PH domain repeat. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270113  Cd Length: 108  Bit Score: 47.37  E-value: 1.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902 607 VRKNWGHSWTVLHGGKLTFHKDPK-STPAGassktnqilpefTVDLKGATINRAPKDKSSKKNVLELKTRTGAEYLIQYD 685
Cdd:cd13301    15 VVNNWKARWFVLKEDGLEYYKKKTdSSPKG------------MIPLKGCTITSPCLEYGKRPLVFKLTTAKGQEHFFQAC 82

                          90       100
                  ....*....|....*....|....*.
gi 1207112902 686 TDSIIQDWHKVILDTIHQLNGDQHHS 711
Cdd:cd13301    83 SREERDAWAKDITKAITCLEGGKRFA 108
SH3_Tec_like cd11768
Src Homology 3 domain of Tec-like Protein Tyrosine Kinases; The Tec (Tyrosine kinase expressed ...
 28-77 3.86e-06

Src Homology 3 domain of Tec-like Protein Tyrosine Kinases; The Tec (Tyrosine kinase expressed in hepatocellular carcinoma) subfamily is composed of Tec, Btk, Bmx (Etk), Itk (Tsk, Emt), Rlk (Txk), and similar proteins. They are cytoplasmic (or nonreceptor) tyr kinases containing Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Most Tec subfamily members (except Rlk) also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, some members contain the Tec homology (TH) domain, which contains proline-rich and zinc-binding regions. Tec kinases are expressed mainly by haematopoietic cells, although Tec and Bmx are also found in endothelial cells. B-cells express Btk and Tec, while T-cells express Itk, Txk, and Tec. Collectively, Tec kinases are expressed in a variety of myeloid cells such as mast cells, platelets, macrophages, and dendritic cells. Each Tec kinase shows a distinct cell-type pattern of expression. The function of Tec kinases in lymphoid cells have been studied extensively. They play important roles in the development, differentiation, maturation, regulation, survival, and function of B-cells and T-cells. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212702 [Multi-domain]  Cd Length: 54  Bit Score: 44.96  E-value: 3.86e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1207112902  28 YTYTARDGRNVSIKPNEHYILVNKTNEEWWHVqKDAADKPFYIPAKYVTE 77
Cdd:cd11768     6 YDFQPIEPGDLPLEKGEEYVVLDDSNEHWWRA-RDKNGNEGYIPSNYVTE 54
SH3_Alpha_Spectrin cd11808
Src homology 3 domain of Alpha Spectrin; Spectrin is a major structural component of the red ...
 28-75 8.02e-06

Src homology 3 domain of Alpha Spectrin; Spectrin is a major structural component of the red blood cell membrane skeleton and is important in erythropoiesis and membrane biogenesis. It is a flexible, rope-like molecule composed of two subunits, alpha and beta, which consist of many spectrin-type repeats. Alpha and beta spectrin associate to form heterodimers and tetramers; spectrin tetramer formation is critical for red cell shape and deformability. Defects in alpha spectrin have been associated with inherited hemolytic anemias including hereditary spherocytosis (HSp), hereditary elliptocytosis (HE), and hereditary pyropoikilocytosis (HPP). Alpha spectrin contains a middle SH3 domain and a C-terminal EF-hand binding motif in addition to multiple spectrin repeats. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212742 [Multi-domain]  Cd Length: 53  Bit Score: 44.01  E-value: 8.02e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1207112902  28 YTYTARDGRNVSIKPNEHYILVNKTNEEWWHVQKDaaDKPFYIPAKYV 75
Cdd:cd11808     6 YDYQEKSPREVSMKKGDILTLLNSSNKDWWKVEVN--DRQGFVPAAYV 51
SH3_Yes cd12007
Src homology 3 domain of Yes Protein Tyrosine Kinase; Yes (or c-Yes) is a member of the Src ...
 28-75 2.12e-05

Src homology 3 domain of Yes Protein Tyrosine Kinase; Yes (or c-Yes) is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. c-Yes kinase is the cellular homolog of the oncogenic protein (v-Yes) encoded by the Yamaguchi 73 and Esh sarcoma viruses. It displays functional overlap with other Src subfamily members, particularly Src. It also shows some unique functions such as binding to occludins, transmembrane proteins that regulate extracellular interactions in tight junctions. Yes also associates with a number of proteins in different cell types that Src does not interact with, like JAK2 and gp130 in pre-adipocytes, and Pyk2 in treated pulmonary vein endothelial cells. Although the biological function of Yes remains unclear, it appears to have a role in regulating cell-cell interactions and vesicle trafficking in polarized cells. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The SH3 domain of Src kinases contributes to substrate recruitment by binding adaptor proteins/substrates, and regulation of kinase activity through an intramolecular interaction. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212940 [Multi-domain]  Cd Length: 58  Bit Score: 43.10  E-value: 2.12e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1207112902  28 YTYTARDGRNVSIKPNEHYILVNKTNEEWWHVQKDAADKPFYIPAKYV 75
Cdd:cd12007     7 YDYEARTTEDLSFKKGERFQIINNTEGDWWEARSIATGKNGYIPSNYV 54
PH cd00821
Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are ...
 591-697 2.19e-05

Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 275388 [Multi-domain]  Cd Length: 92  Bit Score: 44.07  E-value: 2.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902 591 KAGILNKTkvsenGKKVRKNWGHSWTVLHGGKLTFHKDPKSTPAGassktnqilPEFTVDLKGaTINRAPKDKSSKKNVL 670
Cdd:cd00821     1 KEGYLLKR-----GGGGLKSWKKRWFVLFEGVLLYYKSKKDSSYK---------PKGSIPLSG-ILEVEEVSPKERPHCF 65

                          90       100
                  ....*....|....*....|....*..
gi 1207112902 671 ELKTRTGAEYLIQYDTDSIIQDWHKVI 697
Cdd:cd00821    66 ELVTPDGRTYYLQADSEEERQEWLKAL 92
SH3_ITK cd11908
Src Homology 3 domain of Interleukin-2-inducible T-cell Kinase; ITK (also known as Tsk or Emt) ...
 28-77 3.34e-05

Src Homology 3 domain of Interleukin-2-inducible T-cell Kinase; ITK (also known as Tsk or Emt) is a cytoplasmic (or nonreceptor) tyr kinase containing Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. It also contains an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation, and the Tec homology (TH) domain, which contains proline-rich and zinc-binding regions. ITK is expressed in T-cells and mast cells, and is important in their development and differentiation. Of the three Tec kinases expressed in T-cells, ITK plays the predominant role in T-cell receptor (TCR) signaling. It is activated by phosphorylation upon TCR crosslinking and is involved in the pathway resulting in phospholipase C-gamma1 activation and actin polymerization. It also plays a role in the downstream signaling of the T-cell costimulatory receptor CD28, the T-cell surface receptor CD2, and the chemokine receptor CXCR4. In addition, ITK is crucial for the development of T-helper(Th)2 effector responses. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212841 [Multi-domain]  Cd Length: 56  Bit Score: 42.31  E-value: 3.34e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1207112902  28 YTYTARDGRNVSIKPNEHYILVNKTNEEWWHVQkDAADKPFYIPAKYVTE 77
Cdd:cd11908     7 YDYQTNDPQELALRYNEEYHLLDSSEIHWWRVQ-DKNGHEGYVPSSYLVE 55
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 382-410 3.50e-05

WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.


Pssm-ID: 459800 [Multi-domain]  Cd Length: 30  Bit Score: 41.34  E-value: 3.50e-05
                          10        20
                  ....*....|....*....|....*....
gi 1207112902 382 SDWEKVLDEStGRHYFFNTVSGQSSWDPP 410
Cdd:pfam00397   3 PGWEERWDPD-GRVYYYNHETGETQWEKP 30
SH3_1 pfam00018
SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal ...
 28-72 3.78e-05

SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal transduction related to cytoskeletal organization. First described in the Src cytoplasmic tyrosine kinase. The structure is a partly opened beta barrel.


Pssm-ID: 394975 [Multi-domain]  Cd Length: 47  Bit Score: 41.81  E-value: 3.78e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1207112902  28 YTYTARDGRNVSIKPNEHYILVNKTNEEWWHVqKDAADKPFYIPA 72
Cdd:pfam00018   4 YDYTAQEPDELSFKKGDIIIVLEKSEDGWWKG-RNKGGKEGLIPS 47
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 382-412 5.45e-05

Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.


Pssm-ID: 238122 [Multi-domain]  Cd Length: 31  Bit Score: 40.97  E-value: 5.45e-05
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1207112902 382 SDWEKVLDEStGRHYFFNTVSGQSSWDPPED 412
Cdd:cd00201     2 PGWEERWDPD-GRVYYYNHNTKETQWEDPRE 31
RhoGAP_fRGD2 cd04399
RhoGAP_fRGD2: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 784-974 7.20e-05

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


Pssm-ID: 239864  Cd Length: 212  Bit Score: 45.02  E-value: 7.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902 784 FGCHLHNLCSQEKTRVPSFVEKCIRAVEKRGLEIDG--------LYRVSgnLAVIQKLRFKADH----EDLDLEEGNWDI 851
Cdd:cd04399     1 FGVDLETRCRLDKKVVPLIVSAILSYLDQLYPDLINdevrrnvwTDPVS--LKETHQLRNLLNKpkkpDKEVIILKKFEP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902 852 HVITGALKLFFRELQEPLFPYNLFnEFICAI-------KTPDYYSKISHMRNLVRSLPPPNHDTMEALFSHLRRVIQ--H 922
Cdd:cd04399    79 STVASVLKLYLLELPDSLIPHDIY-DLIRSLysayppsQEDSDTARIQGLQSTLSQLPKSHIATLDAIITHFYRLIEitK 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1207112902 923 GNENRMTVQ-NVAIVFGPTLLKPEEETasiATYM--VFQNQIVEFLLSEFESIFH 974
Cdd:cd04399   158 MGESEEEYAdKLATSLSREILRPIIES---LLTIgdKHGYKFFRDLLTHKDQIFS 209
PH_AtPH1 cd13276
Arabidopsis thaliana Pleckstrin homolog (PH) 1 (AtPH1) PH domain; AtPH1 is expressed in all ...
 591-693 9.80e-05

Arabidopsis thaliana Pleckstrin homolog (PH) 1 (AtPH1) PH domain; AtPH1 is expressed in all plant tissue and is proposed to be the plant homolog of human pleckstrin. Pleckstrin consists of two PH domains separated by a linker region, while AtPH has a single PH domain with a short N-terminal extension. AtPH1 binds PtdIns3P specifically and is thought to be an adaptor molecule since it has no obvious catalytic functions. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270095  Cd Length: 106  Bit Score: 42.30  E-value: 9.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902 591 KAGILnkTKVSEngkkVRKNWGHSWTVLHGGKLTFHKDPKSTPagaSSKTNQIlpeftVDLKGATINRAPKDKSSKKNVL 670
Cdd:cd13276     1 KAGWL--EKQGE----FIKTWRRRWFVLKQGKLFWFKEPDVTP---YSKPRGV-----IDLSKCLTVKSAEDATNKENAF 66

                          90       100
                  ....*....|....*....|...
gi 1207112902 671 ELKTRTGAEYLIQyDTDSIIQDW 693
Cdd:cd13276    67 ELSTPEETFYFIA-DNEKEKEEW 88
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 315-343 1.08e-04

WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.


Pssm-ID: 459800 [Multi-domain]  Cd Length: 30  Bit Score: 40.18  E-value: 1.08e-04
                          10        20
                  ....*....|....*....|....*....
gi 1207112902 315 AGWQVHTDDqSGQEFYYQPSTGRSTWENP 343
Cdd:pfam00397   3 PGWEERWDP-DGRVYYYNHETGETQWEKP 30
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 144-525 1.13e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 46.32  E-value: 1.13e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902  144 GLDPDPiKTEAEAGPPVSSNTSSPTNGETAFIILPPPVYTVNTTQSTETDTRSVDDPKDSVGRPRVDSST-------IDE 216
Cdd:PHA03307    58 GAAACD-RFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPppspapdLSE 136

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902  217 DIQMLNRAGWSEVLDVMGKEKNVYESLDTVREPESPKDEADMTVNTT----------PVTPDAPMVEDDTAvyvniPRKR 286
Cdd:PHA03307   137 MLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEETArapssppaepPPSTPPAAASPRPP-----RRSS 211

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902  287 QTTINNSSPIASLLQDFPEPPENFLLDSAGWQVHTDDQSGQEFYYQPSTGR----------STWENPLSSRSMESPVGTE 356
Cdd:PHA03307   212 PISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPitlptriweaSGWNGPSSRPGPASSSSSP 291

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902  357 GGRSPPSFPQSPaCSPVAPAPRRWSSDWEKVLDESTGrhyffntvSGQSSWDPPED-VDSPGRlmflDDCPPPLPEEDYP 435
Cdd:PHA03307   292 RERSPSPSPSSP-GSGPAPSSPRASSSSSSSRESSSS--------STSSSSESSRGaAVSPGP----SPSRSPSPSRPPP 358

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902  436 AS--PELEEASPVSIPAEYSLIHVKKVSIPRVsldRSSPAGWSLdiDSEGTWTFTSEYTQEQWIKSLDDQGRTYYYLRDG 513
Cdd:PHA03307   359 PAdpSSPRKRPRPSRAPSSPAASAGRPTRRRA---RAAVAGRAR--RRDATGRFPAGRPRPSPLDAGAASGAFYARYPLL 433

                          410
                   ....*....|..
gi 1207112902  514 SKSQWNLPEINP 525
Cdd:PHA03307   434 TPSGEPWPGSPP 445
PH_EFA6 cd13295
Exchange Factor for ARF6 Pleckstrin homology (PH) domain; EFA6 (also called PSD/pleckstrin and ...
 583-693 3.34e-04

Exchange Factor for ARF6 Pleckstrin homology (PH) domain; EFA6 (also called PSD/pleckstrin and Sec7 domain containing) is an guanine nucleotide exchange factor for ADP ribosylation factor 6 (ARF6), which is involved in membrane recycling. EFA6 has four structurally related polypeptides: EFA6A, EFA6B, EFA6C and EFA6D. It consists of a N-terminal proline rich region (PR), a SEC7 domain, a PH domain, a PR, a coiled-coil region, and a C-terminal PR. The EFA6 PH domain regulates its association with the plasma membrane. EFA6 activates Arf6 through its Sec7 catalytic domain and modulates this activity through its C-terminal domain, which rearranges the actin cytoskeleton in fibroblastic cell lines. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270107  Cd Length: 126  Bit Score: 41.55  E-value: 3.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902 583 PDDVSNLEKAGILNKTKVSENGKKV---RKNWGHSWTVLHGGKLTFHKDPKSTPAGASSKTnqilPEFTVDLKGATINRA 659
Cdd:cd13295     1 DPNAVEYKKGYLMRKCCADPDGKKTpfgKRGWKMFYATLKGLVLYLHKDEYGCKKALRYES----LRNAISVHHSLATKA 76

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1207112902 660 PkDKSSKKNVLELKTRTGAEYLIQYDTDSIIQDW 693
Cdd:cd13295    77 T-DYTKKPHVFRLRTADWREYLFQASDTKEMQSW 109
PH1_PLEKHH1_PLEKHH2 cd13282
Pleckstrin homology (PH) domain containing, family H (with MyTH4 domain) members 1 and 2 ...
 591-697 3.40e-04

Pleckstrin homology (PH) domain containing, family H (with MyTH4 domain) members 1 and 2 (PLEKHH1) PH domain, repeat 1; PLEKHH1 and PLEKHH2 (also called PLEKHH1L) are thought to function in phospholipid binding and signal transduction. There are 3 Human PLEKHH genes: PLEKHH1, PLEKHH2, and PLEKHH3. There are many isoforms, the longest of which contain a FERM domain, a MyTH4 domain, two PH domains, a peroximal domain, a vacuolar domain, and a coiled coil stretch. The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C/N, alpha-, and C-lobe/A-lobe, B-lobe, C-lobe/F1, F2, F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 241436  Cd Length: 96  Bit Score: 40.74  E-value: 3.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902 591 KAGILNKTkvsenGKKVrKNWGHSWTVLHGGKLTFHKDPKSTpagaSSKtnqilPEFTVDLKGAT-INRAPKDKSskknv 669
Cdd:cd13282     1 KAGYLTKL-----GGKV-KTWKRRWFVLKNGELFYYKSPNDV----IRK-----PQGQIALDGSCeIARAEGAQT----- 60

                          90       100       110
                  ....*....|....*....|....*....|
gi 1207112902 670 LELKT--RTgaeYLIQYDTDSIIQDWHKVI 697
Cdd:cd13282    61 FEIVTekRT---YYLTADSENDLDEWIRVI 87
PH_9 pfam15410
Pleckstrin homology domain; This Pleckstrin homology domain is found in some fungal species.
 591-693 3.88e-04

Pleckstrin homology domain; This Pleckstrin homology domain is found in some fungal species.


Pssm-ID: 434701  Cd Length: 118  Bit Score: 41.26  E-value: 3.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207112902 591 KAGIL-NKTKVSENGKKV---RKNWGHSWTVLHGGKLTFHKD--PKSTPAGASSKTNQILPEFTVDLKGATINRAPkDKS 664
Cdd:pfam15410   2 KKGIVmRKCCFESKGKKTprgKRSWKMVYAVLKDLVLYLYKDehPPESSQFEDKKSLKNAPVGKIRLHHALATPAP-DYT 80

                          90       100
                  ....*....|....*....|....*....
gi 1207112902 665 SKKNVLELKTRTGAEYLIQYDTDSIIQDW 693
Cdd:pfam15410  81 KKSHVFRLQTADGAEYLFQTGSPKELQEW 109
SH3_SPIN90 cd11849
Src homology 3 domain of SH3 protein interacting with Nck, 90 kDa (SPIN90); SPIN90 is also ...
 28-76 3.97e-04

Src homology 3 domain of SH3 protein interacting with Nck, 90 kDa (SPIN90); SPIN90 is also called NCK interacting protein with SH3 domain (NCKIPSD), Dia-interacting protein (DIP), 54 kDa vimentin-interacting protein (VIP54), or WASP-interacting SH3-domain protein (WISH). It is an F-actin binding protein that regulates actin polymerization and endocytosis. It associates with the Arp2/3 complex near actin filaments and determines filament localization at the leading edge of lamellipodia. SPIN90 is expressed in the early stages of neuronal differentiation and plays a role in regulating growth cone dynamics and neurite outgrowth. It also interacts with IRSp53 and regulates cell motility by playing a role in the formation of membrane protrusions. SPIN90 contains an N-terminal SH3 domain, a proline-rich domain, and a C-terminal VCA (verprolin-homology and cofilin-like acidic) domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212783 [Multi-domain]  Cd Length: 53  Bit Score: 39.22  E-value: 3.97e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1207112902  28 YTYTARDGRNVSIKPNEHYILVNKTNEEWWHVQKDAADKPfYIPAKYVT 76
Cdd:cd11849     6 YDFKSAEPNTLSFSEGETFLLLERSNAHWWLVTNHSGETG-YVPANYVK 53
SH3_TXK cd11907
Src Homology 3 domain of TXK, also called Resting lymphocyte kinase (Rlk); TXK is a ...
 28-77 7.52e-04

Src Homology 3 domain of TXK, also called Resting lymphocyte kinase (Rlk); TXK is a cytoplasmic (or nonreceptor) tyr kinase containing Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. It also contains an N-terminal cysteine-rich region. Rlk is expressed in T-cells and mast cell lines, and is a key component of T-cell receptor (TCR) signaling. It is important in TCR-stimulated proliferation, IL-2 production and phospholipase C-gamma1 activation. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212840 [Multi-domain]  Cd Length: 55  Bit Score: 38.40  E-value: 7.52e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1207112902  28 YTYTARDGRNVSIKPNEHYILVNKTNEEWWHVqKDAADKPFYIPAKYVTE 77
Cdd:cd11907     7 YDFLPREPSNLALKRAEEYLILEQYDPHWWKA-RDRYGNEGLIPSNYVTE 55
PRP40 COG5104
Splicing factor [RNA processing and modification];
371-413 8.68e-04

Splicing factor [RNA processing and modification];


Pssm-ID: 227435 [Multi-domain]  Cd Length: 590  Bit Score: 43.15  E-value: 8.68e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1207112902 371 SPVAPAPRRWSSDWEKVLDEStGRHYFFNTVSGQSSWDPPEDV 413
Cdd:COG5104     4 ALLGMASGEARSEWEELKAPD-GRIYYYNKRTGKSSWEKPKEL 45
SH3_Src_like cd11845
Src homology 3 domain of Src kinase-like Protein Tyrosine Kinases; Src subfamily members ...
 28-74 1.04e-03

Src homology 3 domain of Src kinase-like Protein Tyrosine Kinases; Src subfamily members include Src, Lck, Hck, Blk, Lyn, Fgr, Fyn, Yrk, Yes, and Brk. Src (or c-Src) proteins are cytoplasmic (or non-receptor) PTKs which are anchored to the plasma membrane. They contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). However, Brk lacks the N-terminal myristoylation sites. Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. They were identified as the first proto-oncogene products, and they regulate cell adhesion, invasion, and motility in cancer cells, and tumor vasculature, contributing to cancer progression and metastasis. Src kinases are overexpressed in a variety of human cancers, making them attractive targets for therapy. They are also implicated in acute inflammatory responses and osteoclast function. Src, Fyn, Yes, and Yrk are widely expressed, while Blk, Lck, Hck, Fgr, Lyn, and Brk show a limited expression pattern. This subfamily also includes Drosophila Src42A, Src oncogene at 42A (also known as Dsrc41) which accumulates at sites of cell-cell or cell-matrix adhesion, and participates in Drosphila development and wound healing. It has been shown to promote tube elongation in the tracheal system, is essential for proper cell-cell matching during dorsal closure, and regulates cell-cell contacts in developing Drosophila eyes. The SH3 domain of Src kinases contributes to substrate recruitment by binding adaptor proteins/substrates, and regulation of kinase activity through an intramolecular interaction. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212779 [Multi-domain]  Cd Length: 52  Bit Score: 37.95  E-value: 1.04e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1207112902  28 YTYTARDGRNVSIKPNEHYILVNKTNEEWWHVQKDAADKPFYIPAKY 74
Cdd:cd11845     6 YDYEARTDDDLSFKKGDRLQILDDSDGDWWLARHLSTGKEGYIPSNY 52
SH3_BTK cd11906
Src Homology 3 domain of Bruton's tyrosine kinase; BTK is a cytoplasmic (or nonreceptor) tyr ...
 27-77 1.09e-03

Src Homology 3 domain of Bruton's tyrosine kinase; BTK is a cytoplasmic (or nonreceptor) tyr kinase containing Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. It also contains an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation, and the Tec homology (TH) domain with proline-rich and zinc-binding regions. Btk is expressed in B-cells, and a variety of myeloid cells including mast cells, platelets, neutrophils, and dendrictic cells. It interacts with a variety of partners, from cytosolic proteins to nuclear transcription factors, suggesting a diversity of functions. Stimulation of a diverse array of cell surface receptors, including antigen engagement of the B-cell receptor (BCR), leads to PH-mediated membrane translocation of Btk and subsequent phosphorylation by Src kinase and activation. Btk plays an important role in the life cycle of B-cells including their development, differentiation, proliferation, survival, and apoptosis. Mutations in Btk cause the primary immunodeficiency disease, X-linked agammaglobulinaemia (XLA) in humans. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212839 [Multi-domain]  Cd Length: 55  Bit Score: 37.88  E-value: 1.09e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1207112902  27 EYTYTARDGRNVSIKPNEHYILVNKTNEEWWHVqKDAADKPFYIPAKYVTE 77
Cdd:cd11906     6 LYDYTPMNAQDLQLRKGEEYVILEESNLPWWRA-RDKNGREGYIPSNYVTE 55
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
 28-76 1.35e-03

Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences containing proline and hydrophobic amino acids. Pro-containing polypeptides may bind to SH3 domains in 2 different binding orientations.


Pssm-ID: 214620 [Multi-domain]  Cd Length: 56  Bit Score: 37.90  E-value: 1.35e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1207112902   28 YTYTARDGRNVSIKPNEHYILVNKTNEEWWHVQKDaADKPFYIPAKYVT 76
Cdd:smart00326   9 YDYTAQDPDELSFKKGDIITVLEKSDDGWWKGRLG-RGKEGLFPSNYVE 56
SH3_Nck2_1 cd11899
First Src Homology 3 domain of Nck2 adaptor protein; Nck2 (also called Nckbeta or Growth ...
 19-75 3.76e-03

First Src Homology 3 domain of Nck2 adaptor protein; Nck2 (also called Nckbeta or Growth factor receptor-bound protein 4, Grb4) plays a crucial role in connecting signaling pathways of tyrosine kinase receptors and important effectors in actin dynamics and cytoskeletal remodeling. It binds neuronal signaling proteins such as ephrinB and Disabled-1 (Dab-1) exclusively. Nck adaptor proteins regulate actin cytoskeleton dynamics by linking proline-rich effector molecules to protein tyrosine kinases and phosphorylated signaling intermediates. They contain three SH3 domains and a C-terminal SH2 domain. They function downstream of the PDGFbeta receptor and are involved in Rho GTPase signaling and actin dynamics. Vertebrates contain two Nck adaptor proteins: Nck1 (also called Nckalpha) and Nck2, which show partly overlapping functions but also bind distinct targets. The first SH3 domain of Nck2 binds the PxxDY sequence in the CD3e cytoplasmic tail; this binding inhibits phosphorylation by Src kinases, resulting in the downregulation of TCR surface expression. SH3 domains are protein interaction domains that usually bind to proline-rich ligands with moderate affinity and selectivity, preferentially a PxxP motif. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212832 [Multi-domain]  Cd Length: 58  Bit Score: 36.65  E-value: 3.76e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1207112902  19 SQQVLVNYEYTYTARDGRNVSIKPNEHYILVNKTnEEWWHVqKDAADKPFYIPAKYV 75
Cdd:cd11899     1 TEEVIVIAKWDYTAQQDQELDIKKNERLWLLDDS-KTWWRV-RNAANRTGYVPSNYV 55
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 315-343 5.31e-03

Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.


Pssm-ID: 238122 [Multi-domain]  Cd Length: 31  Bit Score: 35.20  E-value: 5.31e-03
                          10        20
                  ....*....|....*....|....*....
gi 1207112902 315 AGWQVHTDDqSGQEFYYQPSTGRSTWENP 343
Cdd:cd00201     2 PGWEERWDP-DGRVYYYNHNTKETQWEDP 29
SH3_Stac_1 cd11833
First C-terminal Src homology 3 domain of SH3 and cysteine-rich domain-containing (Stac) ...
 28-75 5.84e-03

First C-terminal Src homology 3 domain of SH3 and cysteine-rich domain-containing (Stac) proteins; Stac proteins are putative adaptor proteins that contain a cysteine-rich C1 domain and one or two SH3 domains at the C-terminus. There are three mammalian members (Stac1, Stac2, and Stac3) of this family. Stac1 and Stac3 contain two SH3 domains while Stac2 contains a single SH3 domain at the C-terminus. This model represents the first C-terminal SH3 domain of Stac1 and Stac3, and the single C-terminal SH3 domain of Stac2. Stac1 and Stac2 have been found to be expressed differently in mature dorsal root ganglia (DRG) neurons. Stac1 is mainly expressed in peptidergic neurons while Stac2 is found in a subset of nonpeptidergic and all trkB+ neurons. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212767 [Multi-domain]  Cd Length: 53  Bit Score: 35.94  E-value: 5.84e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1207112902  28 YTYTARDGRNVSIKPNEHYILVNKTNEEWWHVQKDaaDKPFYIPAKYV 75
Cdd:cd11833     6 YKFKPQENEDLEMRPGDKITLLDDSNEDWWKGKIE--DRVGFFPANFV 51
SH3_Tec cd11905
Src Homology 3 domain of Tec (Tyrosine kinase expressed in hepatocellular carcinoma); Tec is a ...
 28-77 7.07e-03

Src Homology 3 domain of Tec (Tyrosine kinase expressed in hepatocellular carcinoma); Tec is a cytoplasmic (or nonreceptor) tyr kinase containing Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. It also contains an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation, and the Tec homology (TH) domain, which contains proline-rich and zinc-binding regions. It is more widely-expressed than other Tec subfamily kinases. Tec is found in endothelial cells, both B- and T-cells, and a variety of myeloid cells including mast cells, erythroid cells, platelets, macrophages and neutrophils. Tec is a key component of T-cell receptor (TCR) signaling, and is important in TCR-stimulated proliferation, IL-2 production and phospholipase C-gamma1 activation. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212838 [Multi-domain]  Cd Length: 56  Bit Score: 35.56  E-value: 7.07e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1207112902  28 YTYTARDGRNVSIKPNEHYILVNKTNEEWWHVqKDAADKPFYIPAKYVTE 77
Cdd:cd11905     7 YDFQPTEPHDLRLETGEEYVILEKNDVHWWKA-RDKYGKEGYIPSNYVTG 55
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 384-412 8.49e-03

Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.


Pssm-ID: 197736 [Multi-domain]  Cd Length: 33  Bit Score: 34.88  E-value: 8.49e-03
                           10        20
                   ....*....|....*....|....*....
gi 1207112902  384 WEKVLDEStGRHYFFNTVSGQSSWDPPED 412
Cdd:smart00456   6 WEERKDPD-GRPYYYNHETKETQWEKPRE 33
SH3_Nck_1 cd11765
First Src Homology 3 domain of Nck adaptor proteins; Nck adaptor proteins regulate actin ...
 28-75 8.65e-03

First Src Homology 3 domain of Nck adaptor proteins; Nck adaptor proteins regulate actin cytoskeleton dynamics by linking proline-rich effector molecules to protein tyrosine kinases and phosphorylated signaling intermediates. They contain three SH3 domains and a C-terminal SH2 domain. They function downstream of the PDGFbeta receptor and are involved in Rho GTPase signaling and actin dynamics. Vertebrates contain two Nck adaptor proteins: Nck1 (also called Nckalpha) and Nck2 (also called Nckbeta or Growth factor receptor-bound protein 4, Grb4), which show partly overlapping functions but also bind distinct targets. Their SH3 domains are involved in recruiting downstream effector molecules, such as the N-WASP/Arp2/3 complex, which when activated induces actin polymerization that results in the production of pedestals, or protrusions of the plasma membrane. The first SH3 domain of Nck proteins preferentially binds the PxxDY sequence, which is present in the CD3e cytoplasmic tail. This binding inhibits phosphorylation by Src kinases, resulting in the downregulation of TCR surface expression. SH3 domains are protein interaction domains that usually bind to proline-rich ligands with moderate affinity and selectivity, preferentially a PxxP motif. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212699 [Multi-domain]  Cd Length: 51  Bit Score: 35.47  E-value: 8.65e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1207112902  28 YTYTARDGRNVSIKPNEHYILVNKTnEEWWHVQKDaADKPFYIPAKYV 75
Cdd:cd11765     6 YDYTAQGDQELSIKKNEKLTLLDDS-KHWWKVQNS-SNQTGYVPSNYV 51
 
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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