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Conserved domains on  [gi|1693744514|ref|NP_001357962|]
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ras/Rap GTPase-activating protein SynGAP isoform 2 [Mus musculus]

Protein Classification

Ras GTPase-activating protein( domain architecture ID 11598903)

Ras GTPase-activating protein similar to Caenorhabditis elegans Ras GTPase-activating protein gap-2 that acts as a negative regulator of LET-60 Ras

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RasGAP_DAB2IP cd05136
Ras-GTPase Activating Domain of DAB2IP and similar proteins; The DAB2IP family of Ras ...
405-728 0e+00

Ras-GTPase Activating Domain of DAB2IP and similar proteins; The DAB2IP family of Ras GTPase-activating proteins includes DAB2IP, nGAP, and Syn GAP. Disabled 2 interactive protein, (DAB2IP; also known as ASK-interacting protein 1 (AIP1)), is a member of the GTPase-activating proteins, down-regulates Ras-mediated signal pathways, and mediates TNF-induced activation of ASK1-JNK signaling pathways. The mechanism by which TNF signaling is coupled to DAB2IP is not known.


:

Pssm-ID: 213338  Cd Length: 324  Bit Score: 619.21  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514  405 RYQTMSILPMELYKEFAEYVTNHYRMLCAVLEPALNVKGKEEVASALVHILQSTGKAKDFLSDMAMSEVDRFmEREHLIF 484
Cdd:cd05136      1 RYQSVDILPLEVYKEFLEYLTNNYLDLCEVLEPVLSVKAKEELATALVHILQSTGKAKEFLTDLVMAEVDRL-DDEHLIF 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514  485 RENTLATKAIEEYMRLIGQKYLKDAIGEFIRALYESEENCEVDPIKCTAS-SLAEHQANLRMCCELALCKVVNSHCVFPR 563
Cdd:cd05136     80 RGNTLATKAMEAYLKLVGQKYLQETLGEFIRALYESEEDCEVDPSKCPPSaSLSRNQANLRRSVELAWCKILSSHCVFPR 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514  564 ELKEVFASWRLRCAERGREDIADRLISASLFLRFLCPAIMSPSLFGLMQEYPDEQTSRTLTLIAKVIQNLANFSKFTSKE 643
Cdd:cd05136    160 ELREVFSSWRERLEERGREDIADRLISASLFLRFLCPAILSPSLFNLTQEYPSERAARNLTLIAKVIQNLANFTRFGGKE 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514  644 DFLGFMNEFLELEWGSMQQFLYEISNLDTLTNSSSFEGYIDLGRELSTLHALLWEVLPQLSKEALLKLGPLPRLLNDIST 723
Cdd:cd05136    240 EYMEFMNDFVEQEWPNMKQFLQEISSPSPSSNSSDFDGYIDLGRELSLLHSLLVEIISKLNQTTLDKLGPLPRILNDITE 319

                   ....*
gi 1693744514  724 ALRNP 728
Cdd:cd05136    320 ALRNP 324
DUF3498 pfam12004
Domain of unknown function (DUF3498); This presumed domain is functionally uncharacterized. ...
718-1311 0e+00

Domain of unknown function (DUF3498); This presumed domain is functionally uncharacterized. This domain is found in eukaryotes. This domain is typically between 433 to 538 amino acids in length. This domain is found associated with pfam00616, pfam00168. This domain has two conserved sequence motifs: DLQ and PLSFQNP.


:

Pssm-ID: 463427 [Multi-domain]  Cd Length: 511  Bit Score: 585.18  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514  718 LNDISTALRNPN-IQRQPSRQSERTRSQPMVLRGPSAEMQgYMMRDLNSSIdlqsfmarglnssMDMARLPSPTKEKPpp 796
Cdd:pfam12004    1 LRDITTALTNPTpIQQQLRRFSEHSSSPPVPGRSISSGLQ-KMFEDPDDGL-------------SDFTRLPSPTPENK-- 64
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514  797 pppgggkDLFYVSRPPLARSSPAYCTSSSDITEPEQKMLSVNKSVSMLDLQGdgpgGRLNSSSVSNlAAVGDLLHSSQAS 876
Cdd:pfam12004   65 -------DLFFVTRPPLLQPSPARSSSYSDANEPDQQLPNGNKSLSMVDLQD----SRSLQGSPSP-PLHDAPLNLSQAG 132
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514  877 LTAALGLRPAPAGRLSQGSGSSItAAGMRLSQMGVTTdGVPAQQLRIPLSFQNPLFHMAADGPGPPAGHGGSsghgppss 956
Cdd:pfam12004  133 SQASVGLRPAWAARTSQGNPQSA-PQVRRPLQTPVTQ-GTRPQQLLAPLSFQNPVYHMAAGLPVSPRGLGSP-------- 202
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514  957 hhhhhhhhhhrggEPPGDTFAPFHGYSKSEDLSSGVPkpPAASILHSHSYSDEFGPSGTDFTRRQLSLQDSLQHMLSPPQ 1036
Cdd:pfam12004  203 -------------DSSSETHSSFSSHSNSEDLSSAAA--NKKSGPSNSSYSEDFARRSTEFTRRQLSLTELQHQPAVPRQ 267
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514 1037 ITIGPQRPAPSGPGGGSGggsgggqpppLQRGKSQQLTVSAAQKPRPSSGNLlQSPEPSYGPARPRQQSLSKEGsiggsg 1116
Cdd:pfam12004  268 NSAGPQRRIDQQGLGGPP----------LTRGRTPPSLLNSASYPRPSSGSL-MSSSPDWPPARLRQQSSSSKG------ 330
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514 1117 gsgggggggLKPSITK--QHSQTPSTLNP-TMPASERTVAWVSNMPHLSADIESAHIE-REEYKLKEysksmdesrldrE 1192
Cdd:pfam12004  331 ---------DSPETKQrtQHQQVPSPVNPsTLSPVERTAAWVLNMNGQYEEEESSGPEsREELKQAE------------K 389
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514 1193 YEEEIHSLKERLHMSNRKLEEYERRLLSQEEQTSKILMQYQARLEQSEKRLRQQQVEKDSQIKSIIGRLMLVEEELRRDH 1272
Cdd:pfam12004  390 YEQEISKLKERLRVSNRKLEEYERRLLAQEEQTQKLLLEYQARLEDSEERLRRQQEEKDSQMKSIISRLMAVEEELKKDH 469
                          570       580       590
                   ....*....|....*....|....*....|....*....
gi 1693744514 1273 PAMAEPLpEPKKRLLDAQERQLPPLGPTNPRVTLAPPWN 1311
Cdd:pfam12004  470 AEMQAVI-DSKQKIIDAQEKRIASLDAANARLMSALTQL 507
PH_SynGAP cd13375
Synaptic Ras-GTPase activating protein Pleckstrin homology (PH) domain; SynGAP is a member of ...
122-313 1.17e-137

Synaptic Ras-GTPase activating protein Pleckstrin homology (PH) domain; SynGAP is a member of the RasSynGAP family along with DOC-2/DAB2-interacting protein (DAB2IP) and neuronal growth-associated protein (nGAP/RASAL2). SynGAP, a neuronal Ras-GAP, has been shown display both Ras-GAP activity and Ras-related protein (Rap)-GAP activity. Saccharomyces cerevisiae Bud2 and GAP1 members CAPRI (Ca2+-promoted Ras inactivator) and RASAL (Ras-GTPase-activating-like protein) also possess this dual activity. Human DOC-2/DAB2-interacting protein (DAB2IP) is encoded by a tumor suppressor gene and a newly recognized member of the Ras-GTPase-activating family. Members here include mammals, amphibians, and bony fish. 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: 270178  Cd Length: 189  Bit Score: 417.95  E-value: 1.17e-137
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514  122 PAAPFRPSQGFLSRRLKSSIKRTKSQPKLDRTSSFRQILPRFRSADHDRARLMQSFKESHSHESLLSPSSAAEALELNLD 201
Cdd:cd13375      1 PTAPFRPSQGFLSRRLKSSIKRTKSQPKLDRTSSFRQILPRFRSADHDRARLMQSFKESHSHESLLSPSSAAEALDLNLD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514  202 EDSIIKPVHSSILGQEFCFEVTTSSGTKCFACRSAAERDKWIENLQRAVKPNKDNSRRVDNVLKLWIIEARELPPKKRYY 281
Cdd:cd13375     81 EDSIIKPVHSSILGQEFCFEVTTASGTKCFACRSAAERDKWIENLQRAVKPNKDNSRRVDNVLKLWIIEARELPPKKRYY 160
                          170       180       190
                   ....*....|....*....|....*....|..
gi 1693744514  282 CELCLDDMLYARTTSKPRSasgDTVFWGEHFE 313
Cdd:cd13375    161 CELCLDDMLYARTTSKPRT---DTVFWGEHFE 189
C2_SynGAP_like cd04013
C2 domain present in Ras GTPase activating protein (GAP) family; SynGAP, GAP1, RasGAP, and ...
252-414 2.41e-68

C2 domain present in Ras GTPase activating protein (GAP) family; SynGAP, GAP1, RasGAP, and neurofibromin are all members of the Ras-specific GAP (GTPase-activating protein) family. SynGAP regulates the MAP kinase signaling pathway and is critical for cognition and synapse function. Mutations in this gene causes mental retardation in humans. SynGAP contains a PH-like domain, a C2 domain, and a Ras-GAP domain. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


:

Pssm-ID: 175980 [Multi-domain]  Cd Length: 146  Bit Score: 226.03  E-value: 2.41e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514  252 PNKDNSRRVDNVLKLWIIEARELPPKKRYYCELCLDDMLYARTTSKPRsasGDTVFWGEHFEFNNLPAVRALRLHLYRDS 331
Cdd:cd04013      1 PNRDNSRRTENSLKLWIIEAKGLPPKKRYYCELCLDKTLYARTTSKLK---TDTLFWGEHFEFSNLPPVSVITVNLYRES 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514  332 DKKRKKDKAGYVGLVTVPVATLAGRHFTEQWYPVTLPTgsggsggmgsggggGSGGGSGGKGKGGCPAVRLKARYQTMSI 411
Cdd:cd04013     78 DKKKKKDKSQLIGTVNIPVTDVSSRQFVEKWYPVSTPK--------------GNGKSGGKEGKGESPSIRIKARYQSTRV 143

                   ...
gi 1693744514  412 LPM 414
Cdd:cd04013    144 LPL 146
 
Name Accession Description Interval E-value
RasGAP_DAB2IP cd05136
Ras-GTPase Activating Domain of DAB2IP and similar proteins; The DAB2IP family of Ras ...
405-728 0e+00

Ras-GTPase Activating Domain of DAB2IP and similar proteins; The DAB2IP family of Ras GTPase-activating proteins includes DAB2IP, nGAP, and Syn GAP. Disabled 2 interactive protein, (DAB2IP; also known as ASK-interacting protein 1 (AIP1)), is a member of the GTPase-activating proteins, down-regulates Ras-mediated signal pathways, and mediates TNF-induced activation of ASK1-JNK signaling pathways. The mechanism by which TNF signaling is coupled to DAB2IP is not known.


Pssm-ID: 213338  Cd Length: 324  Bit Score: 619.21  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514  405 RYQTMSILPMELYKEFAEYVTNHYRMLCAVLEPALNVKGKEEVASALVHILQSTGKAKDFLSDMAMSEVDRFmEREHLIF 484
Cdd:cd05136      1 RYQSVDILPLEVYKEFLEYLTNNYLDLCEVLEPVLSVKAKEELATALVHILQSTGKAKEFLTDLVMAEVDRL-DDEHLIF 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514  485 RENTLATKAIEEYMRLIGQKYLKDAIGEFIRALYESEENCEVDPIKCTAS-SLAEHQANLRMCCELALCKVVNSHCVFPR 563
Cdd:cd05136     80 RGNTLATKAMEAYLKLVGQKYLQETLGEFIRALYESEEDCEVDPSKCPPSaSLSRNQANLRRSVELAWCKILSSHCVFPR 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514  564 ELKEVFASWRLRCAERGREDIADRLISASLFLRFLCPAIMSPSLFGLMQEYPDEQTSRTLTLIAKVIQNLANFSKFTSKE 643
Cdd:cd05136    160 ELREVFSSWRERLEERGREDIADRLISASLFLRFLCPAILSPSLFNLTQEYPSERAARNLTLIAKVIQNLANFTRFGGKE 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514  644 DFLGFMNEFLELEWGSMQQFLYEISNLDTLTNSSSFEGYIDLGRELSTLHALLWEVLPQLSKEALLKLGPLPRLLNDIST 723
Cdd:cd05136    240 EYMEFMNDFVEQEWPNMKQFLQEISSPSPSSNSSDFDGYIDLGRELSLLHSLLVEIISKLNQTTLDKLGPLPRILNDITE 319

                   ....*
gi 1693744514  724 ALRNP 728
Cdd:cd05136    320 ALRNP 324
DUF3498 pfam12004
Domain of unknown function (DUF3498); This presumed domain is functionally uncharacterized. ...
718-1311 0e+00

Domain of unknown function (DUF3498); This presumed domain is functionally uncharacterized. This domain is found in eukaryotes. This domain is typically between 433 to 538 amino acids in length. This domain is found associated with pfam00616, pfam00168. This domain has two conserved sequence motifs: DLQ and PLSFQNP.


Pssm-ID: 463427 [Multi-domain]  Cd Length: 511  Bit Score: 585.18  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514  718 LNDISTALRNPN-IQRQPSRQSERTRSQPMVLRGPSAEMQgYMMRDLNSSIdlqsfmarglnssMDMARLPSPTKEKPpp 796
Cdd:pfam12004    1 LRDITTALTNPTpIQQQLRRFSEHSSSPPVPGRSISSGLQ-KMFEDPDDGL-------------SDFTRLPSPTPENK-- 64
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514  797 pppgggkDLFYVSRPPLARSSPAYCTSSSDITEPEQKMLSVNKSVSMLDLQGdgpgGRLNSSSVSNlAAVGDLLHSSQAS 876
Cdd:pfam12004   65 -------DLFFVTRPPLLQPSPARSSSYSDANEPDQQLPNGNKSLSMVDLQD----SRSLQGSPSP-PLHDAPLNLSQAG 132
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514  877 LTAALGLRPAPAGRLSQGSGSSItAAGMRLSQMGVTTdGVPAQQLRIPLSFQNPLFHMAADGPGPPAGHGGSsghgppss 956
Cdd:pfam12004  133 SQASVGLRPAWAARTSQGNPQSA-PQVRRPLQTPVTQ-GTRPQQLLAPLSFQNPVYHMAAGLPVSPRGLGSP-------- 202
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514  957 hhhhhhhhhhrggEPPGDTFAPFHGYSKSEDLSSGVPkpPAASILHSHSYSDEFGPSGTDFTRRQLSLQDSLQHMLSPPQ 1036
Cdd:pfam12004  203 -------------DSSSETHSSFSSHSNSEDLSSAAA--NKKSGPSNSSYSEDFARRSTEFTRRQLSLTELQHQPAVPRQ 267
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514 1037 ITIGPQRPAPSGPGGGSGggsgggqpppLQRGKSQQLTVSAAQKPRPSSGNLlQSPEPSYGPARPRQQSLSKEGsiggsg 1116
Cdd:pfam12004  268 NSAGPQRRIDQQGLGGPP----------LTRGRTPPSLLNSASYPRPSSGSL-MSSSPDWPPARLRQQSSSSKG------ 330
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514 1117 gsgggggggLKPSITK--QHSQTPSTLNP-TMPASERTVAWVSNMPHLSADIESAHIE-REEYKLKEysksmdesrldrE 1192
Cdd:pfam12004  331 ---------DSPETKQrtQHQQVPSPVNPsTLSPVERTAAWVLNMNGQYEEEESSGPEsREELKQAE------------K 389
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514 1193 YEEEIHSLKERLHMSNRKLEEYERRLLSQEEQTSKILMQYQARLEQSEKRLRQQQVEKDSQIKSIIGRLMLVEEELRRDH 1272
Cdd:pfam12004  390 YEQEISKLKERLRVSNRKLEEYERRLLAQEEQTQKLLLEYQARLEDSEERLRRQQEEKDSQMKSIISRLMAVEEELKKDH 469
                          570       580       590
                   ....*....|....*....|....*....|....*....
gi 1693744514 1273 PAMAEPLpEPKKRLLDAQERQLPPLGPTNPRVTLAPPWN 1311
Cdd:pfam12004  470 AEMQAVI-DSKQKIIDAQEKRIASLDAANARLMSALTQL 507
PH_SynGAP cd13375
Synaptic Ras-GTPase activating protein Pleckstrin homology (PH) domain; SynGAP is a member of ...
122-313 1.17e-137

Synaptic Ras-GTPase activating protein Pleckstrin homology (PH) domain; SynGAP is a member of the RasSynGAP family along with DOC-2/DAB2-interacting protein (DAB2IP) and neuronal growth-associated protein (nGAP/RASAL2). SynGAP, a neuronal Ras-GAP, has been shown display both Ras-GAP activity and Ras-related protein (Rap)-GAP activity. Saccharomyces cerevisiae Bud2 and GAP1 members CAPRI (Ca2+-promoted Ras inactivator) and RASAL (Ras-GTPase-activating-like protein) also possess this dual activity. Human DOC-2/DAB2-interacting protein (DAB2IP) is encoded by a tumor suppressor gene and a newly recognized member of the Ras-GTPase-activating family. Members here include mammals, amphibians, and bony fish. 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: 270178  Cd Length: 189  Bit Score: 417.95  E-value: 1.17e-137
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514  122 PAAPFRPSQGFLSRRLKSSIKRTKSQPKLDRTSSFRQILPRFRSADHDRARLMQSFKESHSHESLLSPSSAAEALELNLD 201
Cdd:cd13375      1 PTAPFRPSQGFLSRRLKSSIKRTKSQPKLDRTSSFRQILPRFRSADHDRARLMQSFKESHSHESLLSPSSAAEALDLNLD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514  202 EDSIIKPVHSSILGQEFCFEVTTSSGTKCFACRSAAERDKWIENLQRAVKPNKDNSRRVDNVLKLWIIEARELPPKKRYY 281
Cdd:cd13375     81 EDSIIKPVHSSILGQEFCFEVTTASGTKCFACRSAAERDKWIENLQRAVKPNKDNSRRVDNVLKLWIIEARELPPKKRYY 160
                          170       180       190
                   ....*....|....*....|....*....|..
gi 1693744514  282 CELCLDDMLYARTTSKPRSasgDTVFWGEHFE 313
Cdd:cd13375    161 CELCLDDMLYARTTSKPRT---DTVFWGEHFE 189
RasGAP smart00323
GTPase-activator protein for Ras-like GTPases; All alpha-helical domain that accelerates the ...
401-720 1.92e-103

GTPase-activator protein for Ras-like GTPases; All alpha-helical domain that accelerates the GTPase activity of Ras, thereby "switching" it into an "off" position. Improved domain limits from structure.


Pssm-ID: 214617  Cd Length: 344  Bit Score: 332.35  E-value: 1.92e-103
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514   401 RLKARYQTMSILPMELYKEFAEYVTNHY-RMLCAVLEPALNVKGKEEVASALVHILQSTGKAKDFLSDMAMSEVDRfMER 479
Cdd:smart00323   10 RLKTVYTTDFILPSEYYEELLELLLFSLdLSLASALSEVCSGLDKDELATKLVRLFLRRGRGHPFLRALIDPEVER-TDD 88
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514   480 EHLIFRENTLATKAIEEYMRLIGQKYLKDAIGEFIRALYESEENCEVDPIKCTASSLAEHQANLRMCCELALCKVVNSHC 559
Cdd:smart00323   89 PNTIFRGNSLATKSMEVYMKLVGNQYLHTTLKPVLKKIVESKKSCEVDPAKLEGEDLETNLENLLQYVERLFDAIINSSD 168
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514   560 VFPRELKEVFASWRLRCAERGRE-DIADRLISASLFLRFLCPAIMSPSLFGLMQEYPDEQTSRTLTLIAKVIQNLANFSK 638
Cdd:smart00323  169 RLPYGLRDICKQLRQAAEKRFPDaDVIYKAVSSFVFLRFFCPAIVSPKLFNLVDEHPDPTTRRTLTLIAKVLQNLANLSE 248
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514   639 FTSKEDFLGFMNEFLELEWGSMQQFLYEISNLDTLTNSSSFEGYIDLGRELSTLHALLWEVLPQLSKEaLLKLGPLPRLL 718
Cdd:smart00323  249 FGSKEPWMEPLNDFLLSHKDRVKDFLDELSSVPEILVDKVSDSTTISGRELSLLHSLLLENGDALKRE-LNNEDPLGKLL 327

                    ..
gi 1693744514   719 ND 720
Cdd:smart00323  328 FK 329
C2_SynGAP_like cd04013
C2 domain present in Ras GTPase activating protein (GAP) family; SynGAP, GAP1, RasGAP, and ...
252-414 2.41e-68

C2 domain present in Ras GTPase activating protein (GAP) family; SynGAP, GAP1, RasGAP, and neurofibromin are all members of the Ras-specific GAP (GTPase-activating protein) family. SynGAP regulates the MAP kinase signaling pathway and is critical for cognition and synapse function. Mutations in this gene causes mental retardation in humans. SynGAP contains a PH-like domain, a C2 domain, and a Ras-GAP domain. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


Pssm-ID: 175980 [Multi-domain]  Cd Length: 146  Bit Score: 226.03  E-value: 2.41e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514  252 PNKDNSRRVDNVLKLWIIEARELPPKKRYYCELCLDDMLYARTTSKPRsasGDTVFWGEHFEFNNLPAVRALRLHLYRDS 331
Cdd:cd04013      1 PNRDNSRRTENSLKLWIIEAKGLPPKKRYYCELCLDKTLYARTTSKLK---TDTLFWGEHFEFSNLPPVSVITVNLYRES 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514  332 DKKRKKDKAGYVGLVTVPVATLAGRHFTEQWYPVTLPTgsggsggmgsggggGSGGGSGGKGKGGCPAVRLKARYQTMSI 411
Cdd:cd04013     78 DKKKKKDKSQLIGTVNIPVTDVSSRQFVEKWYPVSTPK--------------GNGKSGGKEGKGESPSIRIKARYQSTRV 143

                   ...
gi 1693744514  412 LPM 414
Cdd:cd04013    144 LPL 146
RasGAP pfam00616
GTPase-activator protein for Ras-like GTPase; All alpha-helical domain that accelerates the ...
464-635 5.76e-30

GTPase-activator protein for Ras-like GTPase; All alpha-helical domain that accelerates the GTPase activity of Ras, thereby "switching" it into an "off" position.


Pssm-ID: 459871  Cd Length: 207  Bit Score: 118.54  E-value: 5.76e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514  464 FLSDMAMSEVDRFMEREHLiFRENTLATKAIEEYMRL-IGQKYLKDAIGEFIRALYESEE-NCEVDPIK----------- 530
Cdd:pfam00616    1 LISELIEEEIESSDNPNDL-LRGNSLVSKLLETYNRRpRGQEYLKKVLGPLVRKIIEDEDlDLESDPRKiyeslinqeel 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514  531 ---CTASS-----------------LAEHQANLRMCCELALCKVVNSHCVFPREL----KEVFASWRLRCAERGREDIAd 586
Cdd:pfam00616   80 ktgRSDLPrdvspeeaiedpevrqiFEDNLQKLRELADEFLDAIYSSLNQLPYGIryicKQLYELLEEKFPDASEEEIL- 158
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1693744514  587 RLISASLFLRFLCPAIMSPSLFGLMQEYPDEQTSRTLTLIAKVIQNLAN 635
Cdd:pfam00616  159 NAIGGFLFLRFFCPAIVNPDLFGLVDHQISPKQRRNLTLIAKVLQNLAN 207
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
197-251 1.28e-06

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: 48.31  E-value: 1.28e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 1693744514   197 ELNLDEDSIIKPVHSSILGQEFCFEVTTSSG-TKCFACRSAAERDKWIENLQRAVK 251
Cdd:smart00233   47 SIDLSGCTVREAPDPDSSKKPHCFEIKTSDRkTLLLQAESEEEREKWVEALRKAIA 102
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
1168-1293 4.93e-06

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 49.15  E-value: 4.93e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514 1168 AHIEREEYKLKEYSKSMDESRLDREYE---EEIHSLKERLhmsnRKLEEYERRLLSQEEQTSKILMQYQARLEQSEKRLR 1244
Cdd:COG1579     66 LEIEEVEARIKKYEEQLGNVRNNKEYEalqKEIESLKRRI----SDLEDEILELMERIEELEEELAELEAELAELEAELE 141
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1693744514 1245 QQQVEKDSQIKSIIGRLmlveEELRRDHPAMAEPLPEpkkRLLDAQERQ 1293
Cdd:COG1579    142 EKKAELDEELAELEAEL----EELEAEREELAAKIPP---ELLALYERI 183
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
1159-1292 1.17e-05

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 50.07  E-value: 1.17e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514 1159 PHLSADIESAHIEREEYKLKEYSKSMDESRldrEYEEEIHSLKERLHMSNRKLEEYERRLLSQEEQTSKILMQ---YQAR 1235
Cdd:TIGR02169  261 SELEKRLEEIEQLLEELNKKIKDLGEEEQL---RVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEidkLLAE 337
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1693744514 1236 LEQSEKRLRQQQVEKDsQIKSIIGRLMLVEEELRRDHPAMAEPLPEPKKRLLDAQER 1292
Cdd:TIGR02169  338 IEELEREIEEERKRRD-KLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREK 393
C2 pfam00168
C2 domain;
262-365 7.27e-05

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 43.08  E-value: 7.27e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514  262 NVLKLWIIEARELPPKKRY-----YCELCLDDmLYARTTSKPRSASGDTVfWGEHFEFN-NLPAVRALRLHLYRDSDKKR 335
Cdd:pfam00168    1 GRLTVTVIEAKNLPPKDGNgtsdpYVKVYLLD-GKQKKKTKVVKNTLNPV-WNETFTFSvPDPENAVLEIEVYDYDRFGR 78
                           90       100       110
                   ....*....|....*....|....*....|
gi 1693744514  336 KKdkagYVGLVTVPVATLAGRHFTEQWYPV 365
Cdd:pfam00168   79 DD----FIGEVRIPLSELDSGEGLDGWYPL 104
IQG1 COG5261
Protein involved in regulation of cellular morphogenesis/cytokinesis [Cell division and ...
587-721 1.89e-04

Protein involved in regulation of cellular morphogenesis/cytokinesis [Cell division and chromosome partitioning / Signal transduction mechanisms];


Pssm-ID: 227586 [Multi-domain]  Cd Length: 1054  Bit Score: 46.03  E-value: 1.89e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514  587 RLISASLFLRFLCPAIMSPSLFGLMQEYPDEqTSRTLTLIAKVIQNLANFSKFTSkedFLGFMNEFLELEWGSMQQFLYE 666
Cdd:COG5261    613 GLIGGFFFLRFVNEALVSPQTSMLKDSCPSD-NVRKLATLSKILQSVFEITSSDK---FDVPLQPFLKEYKEKVHNLLRK 688
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1693744514  667 ISNLDTLTNSSSFEGYIDLGRELSTLHALLWEVLPQLSK-EALLKLGPLPRLLNDI 721
Cdd:COG5261    689 LGNVGDFEEYFEFDQYIDLVKKSRALEYLVNEIYLTHEIiIEYLDNLYDPDSLVDL 744
PRK12704 PRK12704
phosphodiesterase; Provisional
1162-1294 7.16e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 44.00  E-value: 7.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514 1162 SADIESAHIEREEyKLKEYSKSMDESRLDREYE--EEIHSLKERLHMS----NRKLEEYERRLLSQEEQTSK---ILMQY 1232
Cdd:PRK12704    30 EAKIKEAEEEAKR-ILEEAKKEAEAIKKEALLEakEEIHKLRNEFEKElrerRNELQKLEKRLLQKEENLDRkleLLEKR 108
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1693744514 1233 QARLEQSEKRLRQQQVEKDSQIKSIIGRLMLVEEELRRdhpAMAEPLPEPKKRLLDAQERQL 1294
Cdd:PRK12704   109 EEELEKKEKELEQKQQELEKKEEELEELIEEQLQELER---ISGLTAEEAKEILLEKVEEEA 167
UDM1_RNF168 cd22265
UDM1 (ubiquitin-dependent DSB recruitment module 1) domain found in RING finger protein 168; ...
1189-1242 5.41e-03

UDM1 (ubiquitin-dependent DSB recruitment module 1) domain found in RING finger protein 168; RING finger protein 168 (RNF168) is an E3 ubiquitin-protein ligase that promotes noncanonical K27 ubiquitination to signal DNA damage. Together with RNF8, RNF168 functions as a DNA damage response (DDR) factor that promotes a series of ubiquitylation events on substrates such as H2A and H2AX. With H2AK13/15 ubiquitylation, it facilitates recruitment of repair factors p53-binding protein 1 (53BP1) or the RAP80-BRCA1 complex to sites of double-strand breaks (DSBs), and inhibits homologous recombination (HR) in cells deficient in the tumor suppressor BRCA1. RNF168 also promotes H2A neddylation, which antagonizes ubiquitylation of H2A and regulates DNA damage repair. In addition, RNF168 forms a functional complex with RAD6A or RAD6B during the DNA damage response. This model corresponds to the UDM1 (ubiquitin-dependent double-strand break [DSB] recruitment module 1) domain of RNF168, which comprises LRM1 (LR motif 1), UMI (ubiquitin-interacting motif [UIM]- and MIU-related UBD) and MIU1 (motif interacting with ubiquitin 1). Mutations of Ub-interacting residues in UDM1 have little effect on the accumulation of RNF168 to DSB sites, suggesting that it may not be the main site of binding ubiquitylated and polyubiquitylated targets.


Pssm-ID: 409018 [Multi-domain]  Cd Length: 73  Bit Score: 37.15  E-value: 5.41e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1693744514 1189 LDREYEEEIHSLKERLHM----SNRKLEEYERRLLSQEEQTSKILMQYQARLEQSEKR 1242
Cdd:cd22265      7 LRQEYEEEISKLEAERRAleeeENRASEEYIQKLLAEEEEEEKLAEERRRAEEEQLKE 64
 
Name Accession Description Interval E-value
RasGAP_DAB2IP cd05136
Ras-GTPase Activating Domain of DAB2IP and similar proteins; The DAB2IP family of Ras ...
405-728 0e+00

Ras-GTPase Activating Domain of DAB2IP and similar proteins; The DAB2IP family of Ras GTPase-activating proteins includes DAB2IP, nGAP, and Syn GAP. Disabled 2 interactive protein, (DAB2IP; also known as ASK-interacting protein 1 (AIP1)), is a member of the GTPase-activating proteins, down-regulates Ras-mediated signal pathways, and mediates TNF-induced activation of ASK1-JNK signaling pathways. The mechanism by which TNF signaling is coupled to DAB2IP is not known.


Pssm-ID: 213338  Cd Length: 324  Bit Score: 619.21  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514  405 RYQTMSILPMELYKEFAEYVTNHYRMLCAVLEPALNVKGKEEVASALVHILQSTGKAKDFLSDMAMSEVDRFmEREHLIF 484
Cdd:cd05136      1 RYQSVDILPLEVYKEFLEYLTNNYLDLCEVLEPVLSVKAKEELATALVHILQSTGKAKEFLTDLVMAEVDRL-DDEHLIF 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514  485 RENTLATKAIEEYMRLIGQKYLKDAIGEFIRALYESEENCEVDPIKCTAS-SLAEHQANLRMCCELALCKVVNSHCVFPR 563
Cdd:cd05136     80 RGNTLATKAMEAYLKLVGQKYLQETLGEFIRALYESEEDCEVDPSKCPPSaSLSRNQANLRRSVELAWCKILSSHCVFPR 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514  564 ELKEVFASWRLRCAERGREDIADRLISASLFLRFLCPAIMSPSLFGLMQEYPDEQTSRTLTLIAKVIQNLANFSKFTSKE 643
Cdd:cd05136    160 ELREVFSSWRERLEERGREDIADRLISASLFLRFLCPAILSPSLFNLTQEYPSERAARNLTLIAKVIQNLANFTRFGGKE 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514  644 DFLGFMNEFLELEWGSMQQFLYEISNLDTLTNSSSFEGYIDLGRELSTLHALLWEVLPQLSKEALLKLGPLPRLLNDIST 723
Cdd:cd05136    240 EYMEFMNDFVEQEWPNMKQFLQEISSPSPSSNSSDFDGYIDLGRELSLLHSLLVEIISKLNQTTLDKLGPLPRILNDITE 319

                   ....*
gi 1693744514  724 ALRNP 728
Cdd:cd05136    320 ALRNP 324
DUF3498 pfam12004
Domain of unknown function (DUF3498); This presumed domain is functionally uncharacterized. ...
718-1311 0e+00

Domain of unknown function (DUF3498); This presumed domain is functionally uncharacterized. This domain is found in eukaryotes. This domain is typically between 433 to 538 amino acids in length. This domain is found associated with pfam00616, pfam00168. This domain has two conserved sequence motifs: DLQ and PLSFQNP.


Pssm-ID: 463427 [Multi-domain]  Cd Length: 511  Bit Score: 585.18  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514  718 LNDISTALRNPN-IQRQPSRQSERTRSQPMVLRGPSAEMQgYMMRDLNSSIdlqsfmarglnssMDMARLPSPTKEKPpp 796
Cdd:pfam12004    1 LRDITTALTNPTpIQQQLRRFSEHSSSPPVPGRSISSGLQ-KMFEDPDDGL-------------SDFTRLPSPTPENK-- 64
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514  797 pppgggkDLFYVSRPPLARSSPAYCTSSSDITEPEQKMLSVNKSVSMLDLQGdgpgGRLNSSSVSNlAAVGDLLHSSQAS 876
Cdd:pfam12004   65 -------DLFFVTRPPLLQPSPARSSSYSDANEPDQQLPNGNKSLSMVDLQD----SRSLQGSPSP-PLHDAPLNLSQAG 132
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514  877 LTAALGLRPAPAGRLSQGSGSSItAAGMRLSQMGVTTdGVPAQQLRIPLSFQNPLFHMAADGPGPPAGHGGSsghgppss 956
Cdd:pfam12004  133 SQASVGLRPAWAARTSQGNPQSA-PQVRRPLQTPVTQ-GTRPQQLLAPLSFQNPVYHMAAGLPVSPRGLGSP-------- 202
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514  957 hhhhhhhhhhrggEPPGDTFAPFHGYSKSEDLSSGVPkpPAASILHSHSYSDEFGPSGTDFTRRQLSLQDSLQHMLSPPQ 1036
Cdd:pfam12004  203 -------------DSSSETHSSFSSHSNSEDLSSAAA--NKKSGPSNSSYSEDFARRSTEFTRRQLSLTELQHQPAVPRQ 267
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514 1037 ITIGPQRPAPSGPGGGSGggsgggqpppLQRGKSQQLTVSAAQKPRPSSGNLlQSPEPSYGPARPRQQSLSKEGsiggsg 1116
Cdd:pfam12004  268 NSAGPQRRIDQQGLGGPP----------LTRGRTPPSLLNSASYPRPSSGSL-MSSSPDWPPARLRQQSSSSKG------ 330
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514 1117 gsgggggggLKPSITK--QHSQTPSTLNP-TMPASERTVAWVSNMPHLSADIESAHIE-REEYKLKEysksmdesrldrE 1192
Cdd:pfam12004  331 ---------DSPETKQrtQHQQVPSPVNPsTLSPVERTAAWVLNMNGQYEEEESSGPEsREELKQAE------------K 389
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514 1193 YEEEIHSLKERLHMSNRKLEEYERRLLSQEEQTSKILMQYQARLEQSEKRLRQQQVEKDSQIKSIIGRLMLVEEELRRDH 1272
Cdd:pfam12004  390 YEQEISKLKERLRVSNRKLEEYERRLLAQEEQTQKLLLEYQARLEDSEERLRRQQEEKDSQMKSIISRLMAVEEELKKDH 469
                          570       580       590
                   ....*....|....*....|....*....|....*....
gi 1693744514 1273 PAMAEPLpEPKKRLLDAQERQLPPLGPTNPRVTLAPPWN 1311
Cdd:pfam12004  470 AEMQAVI-DSKQKIIDAQEKRIASLDAANARLMSALTQL 507
PH_SynGAP cd13375
Synaptic Ras-GTPase activating protein Pleckstrin homology (PH) domain; SynGAP is a member of ...
122-313 1.17e-137

Synaptic Ras-GTPase activating protein Pleckstrin homology (PH) domain; SynGAP is a member of the RasSynGAP family along with DOC-2/DAB2-interacting protein (DAB2IP) and neuronal growth-associated protein (nGAP/RASAL2). SynGAP, a neuronal Ras-GAP, has been shown display both Ras-GAP activity and Ras-related protein (Rap)-GAP activity. Saccharomyces cerevisiae Bud2 and GAP1 members CAPRI (Ca2+-promoted Ras inactivator) and RASAL (Ras-GTPase-activating-like protein) also possess this dual activity. Human DOC-2/DAB2-interacting protein (DAB2IP) is encoded by a tumor suppressor gene and a newly recognized member of the Ras-GTPase-activating family. Members here include mammals, amphibians, and bony fish. 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: 270178  Cd Length: 189  Bit Score: 417.95  E-value: 1.17e-137
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514  122 PAAPFRPSQGFLSRRLKSSIKRTKSQPKLDRTSSFRQILPRFRSADHDRARLMQSFKESHSHESLLSPSSAAEALELNLD 201
Cdd:cd13375      1 PTAPFRPSQGFLSRRLKSSIKRTKSQPKLDRTSSFRQILPRFRSADHDRARLMQSFKESHSHESLLSPSSAAEALDLNLD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514  202 EDSIIKPVHSSILGQEFCFEVTTSSGTKCFACRSAAERDKWIENLQRAVKPNKDNSRRVDNVLKLWIIEARELPPKKRYY 281
Cdd:cd13375     81 EDSIIKPVHSSILGQEFCFEVTTASGTKCFACRSAAERDKWIENLQRAVKPNKDNSRRVDNVLKLWIIEARELPPKKRYY 160
                          170       180       190
                   ....*....|....*....|....*....|..
gi 1693744514  282 CELCLDDMLYARTTSKPRSasgDTVFWGEHFE 313
Cdd:cd13375    161 CELCLDDMLYARTTSKPRT---DTVFWGEHFE 189
RasGAP smart00323
GTPase-activator protein for Ras-like GTPases; All alpha-helical domain that accelerates the ...
401-720 1.92e-103

GTPase-activator protein for Ras-like GTPases; All alpha-helical domain that accelerates the GTPase activity of Ras, thereby "switching" it into an "off" position. Improved domain limits from structure.


Pssm-ID: 214617  Cd Length: 344  Bit Score: 332.35  E-value: 1.92e-103
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514   401 RLKARYQTMSILPMELYKEFAEYVTNHY-RMLCAVLEPALNVKGKEEVASALVHILQSTGKAKDFLSDMAMSEVDRfMER 479
Cdd:smart00323   10 RLKTVYTTDFILPSEYYEELLELLLFSLdLSLASALSEVCSGLDKDELATKLVRLFLRRGRGHPFLRALIDPEVER-TDD 88
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514   480 EHLIFRENTLATKAIEEYMRLIGQKYLKDAIGEFIRALYESEENCEVDPIKCTASSLAEHQANLRMCCELALCKVVNSHC 559
Cdd:smart00323   89 PNTIFRGNSLATKSMEVYMKLVGNQYLHTTLKPVLKKIVESKKSCEVDPAKLEGEDLETNLENLLQYVERLFDAIINSSD 168
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514   560 VFPRELKEVFASWRLRCAERGRE-DIADRLISASLFLRFLCPAIMSPSLFGLMQEYPDEQTSRTLTLIAKVIQNLANFSK 638
Cdd:smart00323  169 RLPYGLRDICKQLRQAAEKRFPDaDVIYKAVSSFVFLRFFCPAIVSPKLFNLVDEHPDPTTRRTLTLIAKVLQNLANLSE 248
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514   639 FTSKEDFLGFMNEFLELEWGSMQQFLYEISNLDTLTNSSSFEGYIDLGRELSTLHALLWEVLPQLSKEaLLKLGPLPRLL 718
Cdd:smart00323  249 FGSKEPWMEPLNDFLLSHKDRVKDFLDELSSVPEILVDKVSDSTTISGRELSLLHSLLLENGDALKRE-LNNEDPLGKLL 327

                    ..
gi 1693744514   719 ND 720
Cdd:smart00323  328 FK 329
PH_DAB2IP cd13376
DOC-2/Disabled homolog 2-interacting protein Pleckstrin homology (PH) domain; DAB2IP (also ...
131-313 2.68e-87

DOC-2/Disabled homolog 2-interacting protein Pleckstrin homology (PH) domain; DAB2IP (also called AIP1/ASK1-interacting protein-1 and DIP1/2) is a member of the RasSynGAP family along with Synaptic Ras-GTPase activating protein (SynGAP) and neuronal growth-associated protein (nGAP/RASAL2). DAB2IP is a critical component of many signal transduction pathways mediated by Ras and tumor necrosis factors including apoptosis pathways, and it is involved in the formation of many types of tumors. DAB2IP participates in regulation of gene expression and pluripotency of cells. Human DAB2IP is expressed in the adrenal gland, pancreas, endocardium, stomach, kidney, testis, small intestine, liver, trachea, skin, ovary, endometrium, lung, esophagus and bladder. No expression was observed in the cerebrum, parotid gland, thymus, thyroid gland and spleen. 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: 270179  Cd Length: 182  Bit Score: 281.21  E-value: 2.68e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514  131 GFLSRRLKSSIKRTKSQPKLDRTSSFRQILPRFRSADHDRARLMQSFKESHSHESLLSPSSAAEALELNLDEDSIIKPVH 210
Cdd:cd13376      3 GFLSRRLKGSIKRTKSQPKLDRNSSFRHILPGFRSVDNERSHLMPRLKESRSHESLLSPSSAVEALDLSMEEEVVIKPVH 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514  211 SSILGQEFCFEVTTSSGTKCFACRSAAERDKWIENLQRAVKPNKDNSRRVDNVLKLWIIEARELPPKKRYYCELCLDDML 290
Cdd:cd13376     83 SSILGQDYCFEVTTSSGSKCFSCRSAAERDKWMENLRRAVHPNKDNSRRVENMLKLWIIEAKDLPAKKKYLCELCLDDVL 162
                          170       180
                   ....*....|....*....|...
gi 1693744514  291 YARTTSKPRSasgDTVFWGEHFE 313
Cdd:cd13376    163 YARTTCKLKT---DNVFWGEHFE 182
RasGAP cd04519
Ras GTPase Activating Domain; RasGAP functions as an enhancer of the hydrolysis of GTP that is ...
415-669 1.59e-74

Ras GTPase Activating Domain; RasGAP functions as an enhancer of the hydrolysis of GTP that is bound to Ras-GTPases. Proteins having a RasGAP domain include p120GAP, IQGAP, Rab5-activating protein 6, and Neurofibromin, among others. Although the Rho (Ras homolog) GTPases are most closely related to members of the Ras family, RhoGAP and RasGAP exhibit no similarity at their amino acid sequence level. RasGTPases function as molecular switches in a large number of signaling pathways. They are in the on state when bound to GTP, and in the off state when bound to GDP. The RasGAP domain speeds up the hydrolysis of GTP in Ras-like proteins acting as a negative regulator.


Pssm-ID: 213328  Cd Length: 256  Bit Score: 248.18  E-value: 1.59e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514  415 ELYKEFAEYVTNHYRMLCAVLEPALNVKGKEEVASALVHILQSTGKAKDFLSDMAMSEVDRFMErEHLIFRENTLATKAI 494
Cdd:cd04519      1 EEYRLLSLLLTESPLALLRELSQVLPVKDKEEVATALLRIFESRGLALEFLRYLVRSEVKNTKN-PNTLFRGNSLATKLL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514  495 EEYMRLIGQKYLKDAIGEFIRALYESEENCEVDPIKCTASSLAEHQANLRMCCELALCKVVNSHCVFPRELKEVFASWRL 574
Cdd:cd04519     80 DQYMKLVGQEYLKETLSPLIREILESKESCEIDTKLPVGEDLEENLENLLELVNKLVDRILSSLDRLPPELRYVFKILRE 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514  575 RCAERGRED--IADRLISASLFLRFLCPAIMSPSLFGLMQEYPDEQTSRTLTLIAKVIQNLANFSKFTSKEDFLGFMNEF 652
Cdd:cd04519    160 FLAERFPEEpdEAYQAVSGFLFLRFICPAIVSPELFGLVPDEPSEQARRNLTLISKVLQSLANGVEFGDKEPFMKPLNDF 239
                          250
                   ....*....|....*..
gi 1693744514  653 LELEWGSMQQFLYEISN 669
Cdd:cd04519    240 IKSNKPKLKQFLDELSS 256
C2_SynGAP_like cd04013
C2 domain present in Ras GTPase activating protein (GAP) family; SynGAP, GAP1, RasGAP, and ...
252-414 2.41e-68

C2 domain present in Ras GTPase activating protein (GAP) family; SynGAP, GAP1, RasGAP, and neurofibromin are all members of the Ras-specific GAP (GTPase-activating protein) family. SynGAP regulates the MAP kinase signaling pathway and is critical for cognition and synapse function. Mutations in this gene causes mental retardation in humans. SynGAP contains a PH-like domain, a C2 domain, and a Ras-GAP domain. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


Pssm-ID: 175980 [Multi-domain]  Cd Length: 146  Bit Score: 226.03  E-value: 2.41e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514  252 PNKDNSRRVDNVLKLWIIEARELPPKKRYYCELCLDDMLYARTTSKPRsasGDTVFWGEHFEFNNLPAVRALRLHLYRDS 331
Cdd:cd04013      1 PNRDNSRRTENSLKLWIIEAKGLPPKKRYYCELCLDKTLYARTTSKLK---TDTLFWGEHFEFSNLPPVSVITVNLYRES 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514  332 DKKRKKDKAGYVGLVTVPVATLAGRHFTEQWYPVTLPTgsggsggmgsggggGSGGGSGGKGKGGCPAVRLKARYQTMSI 411
Cdd:cd04013     78 DKKKKKDKSQLIGTVNIPVTDVSSRQFVEKWYPVSTPK--------------GNGKSGGKEGKGESPSIRIKARYQSTRV 143

                   ...
gi 1693744514  412 LPM 414
Cdd:cd04013    144 LPL 146
PH_RasSynGAP-like cd13262
Synaptic Ras-GTPase activating protein family Pleckstrin homology (PH) domain; The RasSynGAP ...
130-260 5.81e-54

Synaptic Ras-GTPase activating protein family Pleckstrin homology (PH) domain; The RasSynGAP family is composed of members: DAB2IP, nGAP, and SynGAP. Neuronal growth-associated proteins (nGAPs) are growth cone markers found in multiple types of neurons. There are many nGAPs including Cap1 (Adenylate cyclase-associated protein 1), Capzb (Capping protein (actin filament) muscle Z-line, beta), Clptm1 (Cleft lip and palate associated transmembrane protein 1), Cotl1 (Coactosin-like 1), Crmp1 (Collapsin response mediator protein 1), Cyfip1 (Cytoplasmic FMR1 interacting protein 1), Fabp7 (Fatty acid binding protein 7, brain), Farp2 (FERM, RhoGEF and pleckstrin domain protein 2), Gap43 (Growth associated protein 43), Gnao1 (Guanine nucleotide binding protein (G protein), alpha activating activity polypeptide O), Gnai2 (Guanine nucleotide binding protein (G protein), alpha inhibiting 2), Pacs1 (Phosphofurin acidic cluster sorting protein 1), Rtn1 (Reticulon 1), Sept2 (Septin 2), Snap25 (Synaptosomal-associated protein 25), Strap (Serine/threonine kinase receptor associated protein), Stx7 (Syntaxin 7), and Tmod2 (Tropomodulin 2). SynGAP, a neuronal Ras-GAP, has been shown display both Ras-GAP activity and Ras-related protein (Rap)-GAP activity. Saccharomyces cerevisiae Bud2 and GAP1 members CAPRI (Ca2+-promoted Ras inactivator) and RASAL (Ras-GTPase-activating-like protein) also possess this dual activity. Human DOC-2/DAB2-interacting protein (DAB2IP) is encoded by a tumor suppressor gene and a newly recognized member of the Ras-GTPase-activating family. DAB2IP is a critical component of many signal transduction pathways mediated by Ras and tumor necrosis factors including apoptosis pathways, and it is involved in the formation of many types of tumors. DAB2IP participates in regulation of gene expression and pluripotency of cells. It has been reported that DAB2IP was expressed in different tumor tissues. Little information is available concerning the expression levels of DAB2IP in normal tissues and cells, however, and no studies of its expression patterns during the development of human embryos have been reported. DAB2IP was expressed primarily in cell cytoplasm throughout the fetal development. The expression levels varied among tissues and different gestational ages. 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: 270082  Cd Length: 125  Bit Score: 184.17  E-value: 5.81e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514  130 QGFLSRRLKSSIKRTKSQPKLDRTSSFRqiLPRFRSADHDRarlMQSFKESHSHESLLSPSSAAEalELNLDEDSIIKPV 209
Cdd:cd13262      2 SGFFSRRLKGPLKRTKSVTKLERKSSKR--LPRTRLARAPA---GPRLRGSRSHESLLSSSSAAL--DLSADEDVVIRPL 74
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1693744514  210 HSSILGQEFCFEVTTSSGTKCFACRSAAERDKWIENLQRAVKPNKDNSRRV 260
Cdd:cd13262     75 HSSILGRKHCFQVTTSEGTRCFSCRSAAERDRWIEDLRRAAQPNKDNCRRT 125
RasGAP_CLA2_BUD2 cd05137
Ras-GTPase Activating Domain of CLA2/BUD2; CLA2/BUD2 functions as a GTPase-activating protein ...
403-684 1.12e-53

Ras-GTPase Activating Domain of CLA2/BUD2; CLA2/BUD2 functions as a GTPase-activating protein (GAP) for BUD1/RSR1 and is necessary for proper bud-site selection in yeast. BUD2 has sequence similarity to the catalytic domain of RasGAPs, and stimulates the hydrolysis of BUD1-GTP to BUD1-GDP. Elimination of Bud2p activity by mutation causes a random budding pattern with no growth defect. Overproduction of Bud2p also alters the budding pattern.


Pssm-ID: 213339 [Multi-domain]  Cd Length: 356  Bit Score: 192.01  E-value: 1.12e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514  403 KARYQTMSILPMELYKEFAEY---VTNHYRMLCAVLEPALNVkgkEEVASALVHILQSTGKAKDFLSDMAMSEVD----- 474
Cdd:cd05137      1 KVRLDENVVLPSKNYKPLEELlhnFDLGLTLQIAELVPGDKL---ERLSEILLDIFQASGREDEWFMALVEDEIDgidks 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514  475 --------RFMEREH-LIFRENTLATKAIEEYMRLIGQKYLKDAIGEFIRALYESEENCEVDPIKCTASS-------LAE 538
Cdd:cd05137     78 tsknkdmgKSSNNEAnLLFRGNSLLTKSLEKYMRRIGKEYLEKSIGDVIRKICEENKDCEVDPSRVKESDsiekeedLEE 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514  539 HQANLR-MCCELALCKVVNSHCvFPRELKEVFASWR----LRCAERGREDIadrL--ISASLFLRFLCPAIMSPSLFGLM 611
Cdd:cd05137    158 NWENLIsLTEEIWNSIYITSND-CPPELRKILKHIRakveDRYGDFLRTVT---LnsVSGFLFLRFFCPAILNPKLFGLL 233
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1693744514  612 QEYPDEQTSRTLTLIAKVIQNLANFSKFTSKEDFLGFMNEFLElewgsmqqflyeisnldtlTNSSSFEGYID 684
Cdd:cd05137    234 KDHPRPRAQRTLTLIAKVLQNLANLTTFGQKEPWMEPMNEFLT-------------------THREELKDYID 287
PH_nGAP cd13373
Neuronal growth-associated proteins Pleckstrin homology (PH) domain; nGAP (also called RASAL2 ...
125-266 4.93e-53

Neuronal growth-associated proteins Pleckstrin homology (PH) domain; nGAP (also called RASAL2/RAS protein activator like-3) is a member of the RasSynGAP family along with DOC-2/DAB2-interacting protein (DAB2IP) and synaptic RasGAP (SynGAP). nGAPs are growth cone markers found in multiple types of neurons. There are many nGAPs including Cap1 (Adenylate cyclase-associated protein 1), Capzb (Capping protein (actin filament) muscle Z-line, beta), Clptm1 (Cleft lip and palate associated transmembrane protein 1), Cotl1 (Coactosin-like 1), Crmp1 (Collapsin response mediator protein 1), Cyfip1 (Cytoplasmic FMR1 interacting protein 1), Fabp7 (Fatty acid binding protein 7, brain), Farp2 (FERM, RhoGEF and pleckstrin domain protein 2), Gap43 (Growth associated protein 43), Gnao1 (Guanine nucleotide binding protein (G protein), alpha activating activity polypeptide O), Gnai2 (Guanine nucleotide binding protein (G protein), alpha inhibiting 2), Pacs1 (Phosphofurin acidic cluster sorting protein 1), Rtn1 (Reticulon 1), Sept2 (Septin 2), Snap25 (Synaptosomal-associated protein 25), Strap (Serine/threonine kinase receptor associated protein), Stx7 (Syntaxin 7), and Tmod2 (Tropomodulin 2). PH domains are only found in eukaryotes. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. 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: 270176  Cd Length: 138  Bit Score: 182.23  E-value: 4.93e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514  125 PFRPSqGFLSRRLKSSIKRTKSQPKLDRTSSFRqiLPRFRSADhDRARLMQSFKESHSHESLLSPSSAAEALELNLDEDS 204
Cdd:cd13373      1 PFKVS-GFFSKRLKGSIKRTKSQSKLDRNTSFR--LPSLRSAD-DRSRGLPKLKESRSHESLLSPGSAVEALDLGREEKV 76
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1693744514  205 IIKPVHSSILGQEFCFEVTTSSGTKCFACRSAAERDKWIENLQRAVKPNKDNSRRVDNVLKL 266
Cdd:cd13373     77 SVKPLHSSILGQDFCFEVTYSSGSKCFSCSSAAERDKWMENLRRTVQPNKDNCRRAENVLRL 138
RasGAP_GAP1_like cd05128
Ras-GTPase Activating Domain of GAP1 and similar proteins; The GAP1 family of Ras ...
431-668 4.81e-48

Ras-GTPase Activating Domain of GAP1 and similar proteins; The GAP1 family of Ras GTPase-activating proteins includes GAP1(m) (or RASA2), GAP1_IP4BP (or RASA3), Ca2+ -promoted Ras inactivator (CAPRI, or RASAL4), and Ras GTPase activating-like proteins (RASAL) or RASAL1. The members are characterized by a conserved domain structure comprising N-terminal tandem C2 domains, a highly conserved central RasGAP domain, and a C-terminal pleckstrin homology domain that is associated with a Bruton's tyrosine kinase motif. While this domain structure is conserved, a small change in the function of each individual domain and the interaction between domains has a marked effect on the regulation of each protein.


Pssm-ID: 213330  Cd Length: 269  Bit Score: 172.82  E-value: 4.81e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514  431 LCAVLEPALNVkGKEEVASALVHILQSTGKAKDFLSDMAMSEVDRFMErEHLIFRENTLATKAIEEYMRLIGQKYLKDAI 510
Cdd:cd05128     23 AVYLLEELVKV-DKDDVARPLVRIFLHHGQIVPLLRALASREISKTQD-PNTLFRGNSLASKCMDEFMKLVGMQYLHETL 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514  511 GEFIRALYESEENCEVDPIKCTASSLAE-HQANLRMCCELALCKVVNS--HCvfPRELKEVFASWRLRCAER--GREDIA 585
Cdd:cd05128    101 KPVIDEIFSEKKSCEIDPSKLKDGEVLEtNLANLRGYVERVFKAITSSarRC--PTLMCEIFSDLRESAAQRfpDNEDVP 178
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514  586 DRLISASLFLRFLCPAIMSPSLFGLMQEYPDEQTSRTLTLIAKVIQNLANFSKFTS----KEDFL-GFMNEFLELEW-GS 659
Cdd:cd05128    179 YTAVSGFIFLRFFAPAILNPKLFGLREEHPDPQTARTLTLISKTIQTLGNLGSSSSglgvKEAYMsPLYERFTDEQHvDA 258

                   ....*....
gi 1693744514  660 MQQFLYEIS 668
Cdd:cd05128    259 VKKFLDRIS 267
RasGAP_Neurofibromin_like cd05392
Ras-GTPase Activating Domain of proteins similar to neurofibromin; Neurofibromin-like proteins ...
413-706 3.51e-42

Ras-GTPase Activating Domain of proteins similar to neurofibromin; Neurofibromin-like proteins include the Saccharomyces cerevisiae RasGAP proteins Ira1 and Ira2, the closest homolog of neurofibromin, which is responsible for the human autosomal dominant disease neurofibromatosis type I (NF1). The RasGAP Ira1/2 proteins are negative regulators of the Ras-cAMP signaling pathway and conserved from yeast to human. In yeast Ras proteins are activated by GEFs, and inhibited by two GAPs, Ira1 and Ira2. Ras proteins activate the cAMP/protein kinase A (PKA) pathway, which controls metabolism, stress resistance, growth, and meiosis. Recent studies showed that the kelch proteins Gpb1 and Gpb2 inhibit Ras activity via association with Ira1 and Ira2. Gpb1/2 bind to a conserved C-terminal domain of Ira1/2, and loss of Gpb1/2 results in a destabilization of Ira1 and Ira2, leading to elevated levels of Ras2-GTP and uninhibited cAMP-PKA signaling. Since the Gpb1/2 binding domain on Ira1/2 is conserved in the human neurofibromin protein, the studies suggest that an analogous signaling mechanism may contribute to the neoplastic development of NF1.


Pssm-ID: 213341  Cd Length: 317  Bit Score: 157.45  E-value: 3.51e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514  413 PMELYKEFAEYVTNHYRMLCAVLE--PALNVkgkEEVASALVHILQSTGKAKDFLSDMAMSEVDRfMEREHLIFRENTLA 490
Cdd:cd05392      2 KSEAYDELLELLIEDPQLLLAIAEvcPSSEV---DLLAQSLLNLFETRNRLLPLISWLIEDEISH-TSRAADLFRRNSVA 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514  491 TKAIEEYMRLIGQKYLKDAIGEFIRALYESEENCEVDPIKCTASSLAEHQANLRMCCELALCKVVNSHCVFPRELKEVFA 570
Cdd:cd05392     78 TRLLTLYAKSVGNKYLRKVLRPLLTEIVDNKDYFEVEKIKPDDENLEENADLLMKYAQMLLDSITDSVDQLPPSFRYICN 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514  571 SWRlRCAERGREDIADRLISASLFLRFLCPAIMSPSLFGLMQEYPDEQTSRTLTLIAKVIQNLANFSKFTSKEDFLGFMN 650
Cdd:cd05392    158 TIY-ESVSKKFPDAALIAVGGFLFLRFICPAIVSPESENLLDPPPTPEARRSLILIAKVLQNIANGVLFSLKEPYLESLN 236
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1693744514  651 EFLELEWGSMQQFLYEISNLDTLTNSSSFEGYIDLGRELSTLHALLWEVLPQLSKE 706
Cdd:cd05392    237 EFLKKNSDRIQQFLSEVSTIPPTDPIFDESDEEPITADLRYLHKFLYLHFLEIRKE 292
RasGAP_RASA3 cd05134
Ras-GTPase Activating Domain of RASA3; RASA3 (or GAP1_IP4BP) is a member of the GAP1 family ...
444-669 1.78e-36

Ras-GTPase Activating Domain of RASA3; RASA3 (or GAP1_IP4BP) is a member of the GAP1 family and has been shown to specifically bind 1,3,4,5-tetrakisphosphate (IP4). Thus, RASA3 may function as an IP4 receptor. The members of GAP1 family are characterized by a conserved domain structure comprising N-terminal tandem C2 domains, a highly conserved central RasGAP domain, and a C-terminal pleckstrin-homology domain that is associated with a Bruton's tyrosine kinase motif. Purified RASA3 stimulates GAP activity on Ras with about a five-fold lower potency than p120RasGAP, but shows no GAP-stimulating activity at all against Rac or Rab3A.


Pssm-ID: 213336  Cd Length: 269  Bit Score: 139.39  E-value: 1.78e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514  444 KEEVASALVHILQSTGKAKDFLSDMAMSEVDRfMEREHLIFRENTLATKAIEEYMRLIGQKYLKDAIGEFIRALYESEEN 523
Cdd:cd05134     35 KQEAAIPLVRLFLHYGKIVPFISAIASAEVNR-TQDPNTIFRGNSLTSKCIDETMKLAGMHYLQVTLKPIIDEICQEHKP 113
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514  524 CEVDPIKCTAS-SLAEHQANLRMCCELALCKVVNSHCVFPRELKEVFASWRLRCAERGREDIADRL--ISASLFLRFLCP 600
Cdd:cd05134    114 CEIDPVKLKDGeNLENNRENLRQYVDRIFRVITKSGVSCPTVMCDIFFSLRESAAKRFQVDPDVRYtaVSSFIFLRFFAP 193
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1693744514  601 AIMSPSLFGLMQEYPDEQTSRTLTLIAKVIQNLANFSKFTS---KEDFLG-FMNEFLELEWG-SMQQFLYEISN 669
Cdd:cd05134    194 AILSPNLFQLTPHHPDPQTSRTLTLISKTIQTLGSLSKSKSanfKESYMAaFYDYFNEQKYAdAVKNFLDLISS 267
RasGAP_p120GAP cd05391
Ras-GTPase Activating Domain of p120; p120GAP is a negative regulator of Ras that stimulates ...
411-718 9.17e-34

Ras-GTPase Activating Domain of p120; p120GAP is a negative regulator of Ras that stimulates hydrolysis of bound GTP to GDP. Once the Ras regulator p120GAP, a member of the GAP protein family, is recruited to the membrane, it is transiently immobilized to interact with Ras-GTP. The down-regulation of Ras by p120GAP is a critical step in the regulation of many cellular processes, which is disrupted in approximately 30% of human cancers. p120GAP contains SH2, SH3, PH, calcium- and lipid-binding domains, suggesting its involvement in a complex network of cellular interactions in vivo.


Pssm-ID: 213340  Cd Length: 328  Bit Score: 133.38  E-value: 9.17e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514  411 ILPMELYKEFAEYVTNhyRMLCAVLEPAlNVKGKEEV--ASALVHILQSTGKAKDFLSDMAMSEVDRFMEREHLiFRENT 488
Cdd:cd05391      4 IMPEEEYSELKELILQ--KELHVVYALA-HVCGQDRTllASILLRIFRHEKLESLLLRTLNDREISMEDEATTL-FRATT 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514  489 LATKAIEEYMRLIGQKYLKDAIGEFIRALYESEENCEVDPIKCT----ASSLAEHQANLRMCcelALCKVVNSHCVFPRE 564
Cdd:cd05391     80 LASTLMEQYMKATATPFVHHALKDTILKILESKQSCELNPSKLEknedVNTNLEHLLNILSE---LVEKIFMAAEILPPT 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514  565 LKEVFASWRLRCAERGRED--IADRLISASLFLRFLCPAIMSPSLFGLMQEYPDEQTSRTLTLIAKVIQNLANFSKFTSK 642
Cdd:cd05391    157 LRYIYGCLQKSVQQKWPTNttVRTRVVSGFVFLRLICPAILNPRMFNIISETPSPTAARTLTLVAKSLQNLANLVEFGAK 236
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1693744514  643 EDFLGFMNEFLELEWGSMQQFLYEISNLDTLtNSSSFEGYIDLGRELSTLHALLWEVLPQLsKEALLKLGPLPRLL 718
Cdd:cd05391    237 EPYMEGVNPFIKKNKERMIMFLDELGNVPEL-PDTTEHSRTDLSRDLAALHEICVAHSDEL-RTLSNERGALKKLL 310
RasGAP pfam00616
GTPase-activator protein for Ras-like GTPase; All alpha-helical domain that accelerates the ...
464-635 5.76e-30

GTPase-activator protein for Ras-like GTPase; All alpha-helical domain that accelerates the GTPase activity of Ras, thereby "switching" it into an "off" position.


Pssm-ID: 459871  Cd Length: 207  Bit Score: 118.54  E-value: 5.76e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514  464 FLSDMAMSEVDRFMEREHLiFRENTLATKAIEEYMRL-IGQKYLKDAIGEFIRALYESEE-NCEVDPIK----------- 530
Cdd:pfam00616    1 LISELIEEEIESSDNPNDL-LRGNSLVSKLLETYNRRpRGQEYLKKVLGPLVRKIIEDEDlDLESDPRKiyeslinqeel 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514  531 ---CTASS-----------------LAEHQANLRMCCELALCKVVNSHCVFPREL----KEVFASWRLRCAERGREDIAd 586
Cdd:pfam00616   80 ktgRSDLPrdvspeeaiedpevrqiFEDNLQKLRELADEFLDAIYSSLNQLPYGIryicKQLYELLEEKFPDASEEEIL- 158
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1693744514  587 RLISASLFLRFLCPAIMSPSLFGLMQEYPDEQTSRTLTLIAKVIQNLAN 635
Cdd:pfam00616  159 NAIGGFLFLRFFCPAIVNPDLFGLVDHQISPKQRRNLTLIAKVLQNLAN 207
RasGAP_RASAL cd05135
Ras-GTPase Activating Domain of RASAL1 and similar proteins; Ras GTPase activating-like ...
433-671 1.00e-29

Ras-GTPase Activating Domain of RASAL1 and similar proteins; Ras GTPase activating-like protein (RASAL) or RASAL1 is a member of the GAP1 family, and a Ca2+ sensor responding in-phase to repetitive Ca2+ signals by associating with the plasma membrane and deactivating Ras. It contains a conserved domain structure comprising N-terminal tandem C2 domains, a highly conserved central RasGAP domain, and a C-terminal pleckstrin-homology domain that is associated with a Bruton's tyrosine kinase motif. RASAL, like Ca2+ -promoted Ras inactivator (CAPRI, or RASAL4), is a cytosolic protein that undergoes a rapid translocation to the plasma membrane in response to receptor-mediated elevation in the concentration of intracellular free Ca2+, a translocation that activates its ability to function as a RasGAP. However, unlike RASAL4, RASAL undergoes an oscillatory translocation to the plasma membrane that occurs in synchrony with repetitive Ca2+ spikes.


Pssm-ID: 213337  Cd Length: 287  Bit Score: 120.30  E-value: 1.00e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514  433 AVLEPALNVKGKEEVASALVHILQSTGKAKDFLSDMAMSEVDRFMEREHLiFRENTLATKAIEEYMRLIGQKYLKDAIGE 512
Cdd:cd05135     29 AMLEEVTTGESRQDVATKLVKIFLGQGLVVPFLDYLNTREVGRTTDPNTL-FRSNSLASKSMEQFMKVVGMPYLHEVLKP 107
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514  513 FIRALYESEENCEVDPIKCTAS---------SLAEHQ------ANLRMCCELALCKVVNSHCVFPRELKEVFASWRLRCA 577
Cdd:cd05135    108 VINRIFEEKKYVELDPCKIDLNrtrrisfkgSLSEAQvresslELLQGYLGSIIDAIVGSVDQCPPVMRVAFKQLHKRVE 187
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514  578 ER----GREDIADRLISASLFLRFLCPAIMSPSLFGLMQEYPDEQTSRTLTLIAKVIQNLANFSK--FTSKEDFLGFMNE 651
Cdd:cd05135    188 ERfpeaEHQDVKYLAISGFLFLRFFAPAILTPKLFQLREQHADPRTSRTLLLLAKAVQSIGNLGLqlGQGKEQWMAPLHP 267
                          250       260
                   ....*....|....*....|
gi 1693744514  652 FLELEWGSMQQFLYEISNLD 671
Cdd:cd05135    268 FILQSVARVKDFLDRLIDID 287
RasGAP_RASA2 cd05394
Ras-GTPase Activating Domain of RASA2; RASA2 (or GAP1(m)) is a member of the GAP1 family of ...
444-669 8.60e-28

Ras-GTPase Activating Domain of RASA2; RASA2 (or GAP1(m)) is a member of the GAP1 family of Ras GTPase-activating proteins that includes GAP1_IP4BP (or RASA3), CAPRI, and RASAL. In vitro, RASA2 has been shown to bind inositol 1,3,4,5-tetrakisphosphate (IP4), the water soluble inositol head group of the lipid second messenger phosphatidylinositol 3,4,5-trisphosphate (PIP3). In vivo studies also demonstrated that RASA2 binds PIP3, and it is recruited to the plasma membrane following agonist stimulation of PI 3-kinase. Furthermore, the membrane translocation is a consequence of the ability of its pleckstrin homology (PH) domain to bind PIP3.


Pssm-ID: 213342  Cd Length: 272  Bit Score: 114.22  E-value: 8.60e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514  444 KEEVASALVHILQSTGKAKDFLSDMAMSEVDRFMErEHLIFRENTLATKAIEEYMRLIGQKYLKDAIGEFIRALYESEEN 523
Cdd:cd05394     35 KYDAVLPLVRLLLHHNKLVPFVAAVAALDLKDTQE-ANTIFRGNSLATRCLDEMMKIVGKHYLKVTLKPVLDEICESPKP 113
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514  524 CEVDPIKCTASSLAE-HQANLRMCCELALCKVVNSHCVFPRELKEVFASWRLRCAERGRED--IADRLISASLFLRFLCP 600
Cdd:cd05394    114 CEIDPIKLKEGDNVEnNKENLRYYVDKVFFSIVKSSMSCPTLMCDVFRSLRHLAVKRFPNDphVQYSAVSSFVFLRFFAV 193
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1693744514  601 AIMSPSLFGLMQEYPDEQTSRTLTLIAKVIQNLANFSKFTS------KEDFL-GFMNEFLELEW-GSMQQFLYEISN 669
Cdd:cd05394    194 AVVSPHTFQLRPHHPDAQTSRTLTLISKTIQTLGSWGSLSKsklssfKETFMcDFFKMFQEEKYiEKVKKFLDEISS 270
PH_RASAL3 cd13374
RAS protein activator like-3 Pleckstrin homology (PH) domain; RASAL3 is thought to be a Ras ...
157-275 8.00e-26

RAS protein activator like-3 Pleckstrin homology (PH) domain; RASAL3 is thought to be a Ras GTPase-activating protein. It is involved in positive regulation of Ras GTPase activity and of small GTPase mediated signal transduction as well as negative regulation of Ras protein signal transduction. It contains a PH domain, a C2 domain, and a Ras-GAP 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: 270177  Cd Length: 146  Bit Score: 104.71  E-value: 8.00e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514  157 RQILPRFRSADHDRARLMQSFKES--HSHESLLSPSSAAEaLELNLDEDSIIKPVHSSILGQEFCFEVTTSSGTKCFACR 234
Cdd:cd13374     23 RGLLKRLKEKKKAKAESTGTGRDGppSALGSRESLATISE-LDLGAERDVRVWPLHPSLLGEPHCFQVTWPGGSRCFSCR 101
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1693744514  235 SAAERDKWIENLQRAVKPNKDNSRRVDNVLKLWIIEARELP 275
Cdd:cd13374    102 SAAERDRWIEDLRRSFQPHQDNVEREETWLSVWVHEAKGLP 142
RasGAP_Neurofibromin cd05130
Ras-GTPase Activating Domain of neurofibromin; Neurofibromin is the product of the ...
446-698 3.22e-23

Ras-GTPase Activating Domain of neurofibromin; Neurofibromin is the product of the neurofibromatosis type 1 gene (NF1) and shares a region of similarity with catalytic domain of the mammalian p120RasGAP protein and an extended similarity with the Saccharomyces cerevisiae RasGAP proteins Ira1 and Ira2. Neurofibromin has been shown to function as a GAP (GTPase-activating protein) which inhibits low molecular weight G proteins such as Ras by stimulating their intrinsic GTPase activity. NF1 is a common genetic disorder characterized by various symptoms ranging from predisposition for the development of tumors to learning disability or mental retardation. Loss of neurofibromin activity can be correlated to the increase in Ras-GTP concentration in neurofibromas of NF1 of patients, supporting the notion that unregulated Ras signaling may contribute to their development.


Pssm-ID: 213332 [Multi-domain]  Cd Length: 332  Bit Score: 102.40  E-value: 3.22e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514  446 EVASALVHILQSTGKAKDFLSDMAMSEVDRFMEREHLiFRENTLATKAIEEYMRLIGQKYLKDAIGEFIRALYESEE--N 523
Cdd:cd05130     41 ELARVLVTLFDSKHLLYQLLWNMFSKEVELADSMQTL-FRGNSLASKIMTFCFKVYGATYLQSLLEPLLRTMITSSEwvS 119
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514  524 CEVDPIKC-TASSLAEHQANLRMCCELALCKVVNSHCVFPRELKEVfaswrLRC-----AERGREDIADRLISAsLFLRF 597
Cdd:cd05130    120 YEVDPTRLeGNENLEENQRNLLQLTEKFFHAIISSSDEFPPQLRSV-----CHClyqvvSHRFPNSGLGAVGSA-IFLRF 193
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514  598 LCPAIMSPSLFGLMQEYPDEQTSRTLTLIAKVIQNLANFSKFTsKEDFLGFMNEFLELEWGSMQQFLYEISNLDTLT--N 675
Cdd:cd05130    194 INPAIVSPYEYGILDREPPPRVKRGLKLMSKILQNIANHVLFT-KEAHMLPFNDFLRNHFEAGRRFFSSIASDCGAVdgP 272
                          250       260
                   ....*....|....*....|...
gi 1693744514  676 SSSFEGYIDLGRELStLHALLWE 698
Cdd:cd05130    273 SSKYLSFINDANVLA-LHRLLWN 294
RasGAP_GAPA cd05132
Ras-GTPase Activating Domain of GAPA; GAPA is an IQGAP-related protein and is predicted to ...
485-718 6.24e-22

Ras-GTPase Activating Domain of GAPA; GAPA is an IQGAP-related protein and is predicted to bind to small GTPases, which are yet to be identified. IQGAP proteins are integral components of cytoskeletal regulation. Results from truncated GAPAs indicated that almost the entire region of GAPA homologous to IQGAP is required for cytokinesis in Dictyostelium. More members of the IQGAP family are emerging, and evidence suggests that there are both similarities and differences in their function.


Pssm-ID: 213334  Cd Length: 352  Bit Score: 98.96  E-value: 6.24e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514  485 RENTLATKAIEEYMRL-IGQKYLKDAIGEFIRALYESEE-NCEVDPIKC----------------------TASSLAEH- 539
Cdd:cd05132     49 RANTAVSRMMTTYTRRgPGQSYLKTVLADRINDLISLKDlNLEINPLKVyeqmindieldtglpsnlprgiTPEEAAENp 128
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514  540 ------QANLRMCCELA---LCKVVNSHCVFPRELKEVFASWRLRCAER----GREDIADrLISASLFLRFLCPAIMSPS 606
Cdd:cd05132    129 avqniiEPRLEMLEEITnsfLEAIINSLDEVPYGIRWICKQIRSLTRRKfpdaSDETICS-LIGGFFLLRFINPAIVSPQ 207
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514  607 LFGLMQEYPDEQTSRTLTLIAKVIQNLANFSKFtSKEDFLGFMNEFLELEWGSMQQFLYEISNLDTLTNSSSFEGYIDLG 686
Cdd:cd05132    208 AYMLVDGKPSDNTRRTLTLIAKLLQNLANKPSY-SKEPYMAPLQPFVEENKERLNKFLNDLCEVDDFYESLELDQYIALS 286
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1693744514  687 R----------ELSTLHALLWEVLPQLSKEALLKLGPLPRLL 718
Cdd:cd05132    287 KkdlsinitlnEIYNTHSLLVKHLAELAPDHNDHLRLILQEL 328
RasGAP_RASA4 cd05395
Ras-GTPase Activating Domain of RASA4; Ras GTPase activating-like 4 protein (RASAL4), also ...
431-642 1.49e-21

Ras-GTPase Activating Domain of RASA4; Ras GTPase activating-like 4 protein (RASAL4), also known as Ca2+ -promoted Ras inactivator (CAPRI), is a member of the GAP1 family. Members of the GAP1 family are characterized by a conserved domain structure comprising N-terminal tandem C2 domains, a highly conserved central RasGAP domain, and a C-terminal pleckstrin-homology domain that is associated with a Bruton's tyrosine kinase motif. RASAL4, like RASAL, is a cytosolic protein that undergoes a rapid translocation to the plasma membrane in response to a receptor-mediated elevation in the concentration of intracellular free Ca2+ ([Ca2+]i). However, unlike RASAL, RASAL4 does not sense oscillations in [Ca2+]i.


Pssm-ID: 213343 [Multi-domain]  Cd Length: 287  Bit Score: 96.48  E-value: 1.49e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514  431 LCAVLEPALNVKGKEEVASALVHILQSTGKAKDFLSDMAMSEVDRFMEREHLiFRENTLATKAIEEYMRLIGQKYLKDAI 510
Cdd:cd05395     27 LISLIDETTTAECRQEVATNLVKLFLGQGLAKEFLDLLFQLELDKTTEPNTL-FRSNSLASKSMESFLKVAGMQYLHSVL 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514  511 GEFIRALYESEENCEVDPIKC--------------TASSLAEHQAN-LRMCCELALCKVVNSHCVFPRELKEVFASWRLR 575
Cdd:cd05395    106 GPTINRVFEEKKYVELDPSKVeikdvgcsglhriqTESEVIEQSAQlLQSYLGELLSAISKSVKYCPAVIRATFRQLFKR 185
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1693744514  576 CAERGREDIADRL----ISASLFLRFLCPAIMSPSLFGLMQEYPDEQTSRTLTLIAKVIQNLANFSKFTSK 642
Cdd:cd05395    186 VQERFPENQHQNVkfiaVTSFLCLRFFSPAIMSPKLFHLREKHADARTSRTLLLLAKAVQNVGNMDTLASR 256
RasGAP_IQGAP_like cd05127
Ras-GTPase Activating Domain of IQ motif containing GTPase activating proteins; This family ...
472-721 6.07e-07

Ras-GTPase Activating Domain of IQ motif containing GTPase activating proteins; This family represents IQ motif containing GTPase activating protein (IQGAP) which associated with the Ras GTP-binding protein. A primary function of IQGAP proteins is to modulate cytoskeletal architecture. There are three known IQGAP family members: IQGAP1, IQGAP2 and IQGAP3. Human IQGAP1 and IQGAP2 share 62% identity. IQGAPs are multi-domain molecules having a calponin-homology (CH) domain which binds F-actin, IQGAP-specific repeats, a single WW domain, four IQ motifs that mediate interactions with calmodulin, and a RasGAP related domain that binds active Rho family GTPases. IQGAP is an essential regulator of cytoskeletal function. IQGAP1 negatively regulates Ras family GTPases by stimulating their intrinsic GTPase activity, the protein actually lacks GAP activity. Both IQGAP1 and IQGAP2 specifically bind to Cdc42 and Rac1, but not to RhoA. Despite of their similarities to part of the sequence of RasGAP, neither IQGAP1 nor IQGAP2 interacts with Ras. IQGAP3, only present in mammals, regulates the organization of the cytoskeleton under the regulation of Rac1 and Cdc42 in neuronal cells. The depletion of IQGAP3 is shown to impair neurite or axon outgrowth in neuronal cells with disorganized cytoskeleton.


Pssm-ID: 213329 [Multi-domain]  Cd Length: 331  Bit Score: 52.97  E-value: 6.07e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514  472 EVDRFMEREHLIFRENTLATKAIEEYMR-LIGQKYLKDAIGEFIRALYESEE-NCEVDPIKC------------------ 531
Cdd:cd05127     21 EIESKVSLPEDIVTGNPTVIKLVVNYNRgPRGQKYLRELLGPVVKEILDDDDlDLETDPVDIykawinqeesrtgepskl 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514  532 --------------TASSLAEHQANLRMCCELALCKVVNSHCVFPREL----KEVFASWRLRCAERGREDIAdRLISASL 593
Cdd:cd05127    101 pydvtreqalkdpeVRKRLIEHLEKLRAITDKFLTAITESLDKMPYGMryiaKVLKEALREKFPDAPEEEIL-KIVGNLL 179
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514  594 FLRFLCPAIMSPSLFGLMQEYPDEQTS----RTLTLIAKVIQNLANFSKFTSKEDFLGFMNEFLELEWGSMQQFLYEIS- 668
Cdd:cd05127    180 YYRYMNPAIVAPEAFDIIDLSVGGQLSplqrRNLGSIAKVLQQAASGKLFGGENPYLSPLNPYISESHEKFKKFFLEACt 259
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1693744514  669 --------NLDTLTNSSSFEG---YIDLgRELSTLHALLWEVLPQLS-------KEALLKLGPLPRLLNDI 721
Cdd:cd05127    260 vpeaeehfNIDEYSDLTMLTKptiYISL-QEIFATHKLLLEHQDEIApdpddplRELLDDLGPAPTIESLL 329
C2 cd00030
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
264-364 6.71e-07

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


Pssm-ID: 175973 [Multi-domain]  Cd Length: 102  Bit Score: 48.99  E-value: 6.71e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514  264 LKLWIIEARELPPKKR-----YYCELCLDDMLYARTTSKPRSAsgdTVFWGEHFEFNNL-PAVRALRLHLYRDSDKKRKK 337
Cdd:cd00030      1 LRVTVIEARNLPAKDLngksdPYVKVSLGGKQKFKTKVVKNTL---NPVWNETFEFPVLdPESDTLTVEVWDKDRFSKDD 77
                           90       100
                   ....*....|....*....|....*...
gi 1693744514  338 dkagYVGLVTVPVATLAGR-HFTEQWYP 364
Cdd:cd00030     78 ----FLGEVEIPLSELLDSgKEGELWLP 101
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
197-251 1.28e-06

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: 48.31  E-value: 1.28e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 1693744514   197 ELNLDEDSIIKPVHSSILGQEFCFEVTTSSG-TKCFACRSAAERDKWIENLQRAVK 251
Cdd:smart00233   47 SIDLSGCTVREAPDPDSSKKPHCFEIKTSDRkTLLLQAESEEEREKWVEALRKAIA 102
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
263-362 1.98e-06

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


Pssm-ID: 214577 [Multi-domain]  Cd Length: 101  Bit Score: 47.48  E-value: 1.98e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514   263 VLKLWIIEARELPPKKRY-----YCELCLDDMLY--ARTTSKPRSASgdtVFWGEHFEFN-NLPAVRALRLHLYrdsdKK 334
Cdd:smart00239    1 TLTVKIISARNLPPKDKGgksdpYVKVSLDGDPKekKKTKVVKNTLN---PVWNETFEFEvPPPELAELEIEVY----DK 73
                            90       100
                    ....*....|....*....|....*...
gi 1693744514   335 RKKDKAGYVGLVTVPVATLAGRHFTEQW 362
Cdd:smart00239   74 DRFGRDDFIGQVTIPLSDLLLGGRHEKL 101
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
1168-1293 4.93e-06

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 49.15  E-value: 4.93e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514 1168 AHIEREEYKLKEYSKSMDESRLDREYE---EEIHSLKERLhmsnRKLEEYERRLLSQEEQTSKILMQYQARLEQSEKRLR 1244
Cdd:COG1579     66 LEIEEVEARIKKYEEQLGNVRNNKEYEalqKEIESLKRRI----SDLEDEILELMERIEELEEELAELEAELAELEAELE 141
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1693744514 1245 QQQVEKDSQIKSIIGRLmlveEELRRDHPAMAEPLPEpkkRLLDAQERQ 1293
Cdd:COG1579    142 EKKAELDEELAELEAEL----EELEAEREELAAKIPP---ELLALYERI 183
C2A_RasGAP cd08383
C2 domain (first repeat) of Ras GTPase activating proteins (GAPs); RasGAPs suppress Ras ...
264-366 5.81e-06

C2 domain (first repeat) of Ras GTPase activating proteins (GAPs); RasGAPs suppress Ras function by enhancing the GTPase activity of Ras proteins resulting in the inactive GDP-bound form of Ras. In this way it can control cellular proliferation and differentiation. The proteins here all contain either a single C2 domain or two tandem C2 domains, a Ras-GAP domain, and a pleckstrin homology (PH)-like domain. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. Members here have a type-I topology.


Pssm-ID: 176029 [Multi-domain]  Cd Length: 117  Bit Score: 46.87  E-value: 5.81e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514  264 LKLWIIEARELPPKK--RYYCELCLDDMLYARTTSKprsaSGDTVFWGEHFEFNNLPAV---RALRLHLYRDSDKKRKkd 338
Cdd:cd08383      2 LRLRILEAKNLPSKGtrDPYCTVSLDQVEVARTKTV----EKLNPFWGEEFVFDDPPPDvtfFTLSFYNKDKRSKDRD-- 75
                           90       100
                   ....*....|....*....|....*...
gi 1693744514  339 kagyVGLVTVPVATLAGRHFTEQWYPVT 366
Cdd:cd08383     76 ----IVIGKVALSKLDLGQGKDEWFPLT 99
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
1159-1292 1.17e-05

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 50.07  E-value: 1.17e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514 1159 PHLSADIESAHIEREEYKLKEYSKSMDESRldrEYEEEIHSLKERLHMSNRKLEEYERRLLSQEEQTSKILMQ---YQAR 1235
Cdd:TIGR02169  261 SELEKRLEEIEQLLEELNKKIKDLGEEEQL---RVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEidkLLAE 337
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1693744514 1236 LEQSEKRLRQQQVEKDsQIKSIIGRLMLVEEELRRDHPAMAEPLPEPKKRLLDAQER 1292
Cdd:TIGR02169  338 IEELEREIEEERKRRD-KLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREK 393
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
1170-1272 2.57e-05

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 48.81  E-value: 2.57e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514 1170 IEREEYKLKEYSKSMDESRLDREYEEEIHSLKERLHMSNRKLEEYERRLLSQEEQTSKILMQYQARLEQSEKRLRQQQVE 1249
Cdd:pfam02463  169 RKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRD 248
                           90       100
                   ....*....|....*....|...
gi 1693744514 1250 KDSQIKSIIGRLMLVEEELRRDH 1272
Cdd:pfam02463  249 EQEEIESSKQEIEKEEEKLAQVL 271
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1161-1291 2.61e-05

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 48.90  E-value: 2.61e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514 1161 LSADIESAHIEREEY--KLKEYSKSMDESRL-DREYEEEIHSLKERLHMSNRKLEEYERRLLSQEE---QTSKILMQYQA 1234
Cdd:TIGR02168  244 LQEELKEAEEELEELtaELQELEEKLEELRLeVSELEEEIEELQKELYALANEISRLEQQKQILRErlaNLERQLEELEA 323
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1693744514 1235 RLEQSEKRLRQQQVEKDsQIKSIIGRLMLVEEELRRDHPAMAEPLPEPKKRLLDAQE 1291
Cdd:TIGR02168  324 QLEELESKLDELAEELA-ELEEKLEELKEELESLEAELEELEAELEELESRLEELEE 379
RNase_Y_N pfam12072
RNase Y N-terminal region;
1165-1294 7.15e-05

RNase Y N-terminal region;


Pssm-ID: 463456 [Multi-domain]  Cd Length: 201  Bit Score: 45.26  E-value: 7.15e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514 1165 IESAHIEREEYKLKEYSKSMDES-RLDREYEEEIhslKERlhmsNRKLEEYERRLLSQEEQTSK---ILMQYQARLEQSE 1240
Cdd:pfam12072   40 IEEAKKEAETKKKEALLEAKEEIhKLRAEAEREL---KER----RNELQRQERRLLQKEETLDRkdeSLEKKEESLEKKE 112
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1693744514 1241 KRL--RQQQVE-KDSQIKSIIGRLMlveEELRRDHPAMAEplpEPKKRLLDAQERQL 1294
Cdd:pfam12072  113 KELeaQQQQLEeKEEELEELIEEQR---QELERISGLTSE---EAKEILLDEVEEEL 163
C2 pfam00168
C2 domain;
262-365 7.27e-05

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 43.08  E-value: 7.27e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514  262 NVLKLWIIEARELPPKKRY-----YCELCLDDmLYARTTSKPRSASGDTVfWGEHFEFN-NLPAVRALRLHLYRDSDKKR 335
Cdd:pfam00168    1 GRLTVTVIEAKNLPPKDGNgtsdpYVKVYLLD-GKQKKKTKVVKNTLNPV-WNETFTFSvPDPENAVLEIEVYDYDRFGR 78
                           90       100       110
                   ....*....|....*....|....*....|
gi 1693744514  336 KKdkagYVGLVTVPVATLAGRHFTEQWYPV 365
Cdd:pfam00168   79 DD----FIGEVRIPLSELDSGEGLDGWYPL 104
C2_Ras_p21A1 cd08400
C2 domain present in RAS p21 protein activator 1 (RasA1); RasA1 is a GAP1 (GTPase activating ...
264-366 7.30e-05

C2 domain present in RAS p21 protein activator 1 (RasA1); RasA1 is a GAP1 (GTPase activating protein 1), a Ras-specific GAP member, which suppresses Ras function by enhancing the GTPase activity of Ras proteins resulting in the inactive GDP-bound form of Ras. In this way it can control cellular proliferation and differentiation. RasA1 contains a C2 domain, a Ras-GAP domain, a pleckstrin homology (PH)-like domain, a SH3 domain, and 2 SH2 domains. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. Members here have a type-I topology.


Pssm-ID: 176045 [Multi-domain]  Cd Length: 126  Bit Score: 43.90  E-value: 7.30e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514  264 LKLWIIEARELPPKK--RYYCELCLDDMLYARTTSKprsaSGDTVFWGEHFEFNNLPA-VRALRLHLYRDSDKKRKKDka 340
Cdd:cd08400      6 LQLNVLEAHKLPVKHvpHPYCVISLNEVKVARTKVR----EGPNPVWSEEFVFDDLPPdVNSFTISLSNKAKRSKDSE-- 79
                           90       100
                   ....*....|....*....|....*.
gi 1693744514  341 gyVGLVTVPVATLAGRHFTEQWYPVT 366
Cdd:cd08400     80 --IAEVTVQLSKLQNGQETDEWYPLS 103
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
1154-1301 1.54e-04

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 46.21  E-value: 1.54e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514 1154 WVSNMPHLSADIESAHIERE--EYKLKEYSKSMDESRLDR-EYEEEIHSLKERLHMSNRKLEEYERRLLSQEEQTSKILM 1230
Cdd:TIGR02169  810 IEARLREIEQKLNRLTLEKEylEKEIQELQEQRIDLKEQIkSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKK 889
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514 1231 Q---YQARLEQSEKRLRQQQVE---KDSQIKSIIGRLMLVEEELRRDHPAMAEPLPEPKKRL--------LDAQERQLPP 1296
Cdd:TIGR02169  890 ErdeLEAQLRELERKIEELEAQiekKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELsledvqaeLQRVEEEIRA 969

                   ....*
gi 1693744514 1297 LGPTN 1301
Cdd:TIGR02169  970 LEPVN 974
IQG1 COG5261
Protein involved in regulation of cellular morphogenesis/cytokinesis [Cell division and ...
587-721 1.89e-04

Protein involved in regulation of cellular morphogenesis/cytokinesis [Cell division and chromosome partitioning / Signal transduction mechanisms];


Pssm-ID: 227586 [Multi-domain]  Cd Length: 1054  Bit Score: 46.03  E-value: 1.89e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514  587 RLISASLFLRFLCPAIMSPSLFGLMQEYPDEqTSRTLTLIAKVIQNLANFSKFTSkedFLGFMNEFLELEWGSMQQFLYE 666
Cdd:COG5261    613 GLIGGFFFLRFVNEALVSPQTSMLKDSCPSD-NVRKLATLSKILQSVFEITSSDK---FDVPLQPFLKEYKEKVHNLLRK 688
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1693744514  667 ISNLDTLTNSSSFEGYIDLGRELSTLHALLWEVLPQLSK-EALLKLGPLPRLLNDI 721
Cdd:COG5261    689 LGNVGDFEEYFEFDQYIDLVKKSRALEYLVNEIYLTHEIiIEYLDNLYDPDSLVDL 744
PRK12704 PRK12704
phosphodiesterase; Provisional
1162-1294 7.16e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 44.00  E-value: 7.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514 1162 SADIESAHIEREEyKLKEYSKSMDESRLDREYE--EEIHSLKERLHMS----NRKLEEYERRLLSQEEQTSK---ILMQY 1232
Cdd:PRK12704    30 EAKIKEAEEEAKR-ILEEAKKEAEAIKKEALLEakEEIHKLRNEFEKElrerRNELQKLEKRLLQKEENLDRkleLLEKR 108
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1693744514 1233 QARLEQSEKRLRQQQVEKDSQIKSIIGRLMLVEEELRRdhpAMAEPLPEPKKRLLDAQERQL 1294
Cdd:PRK12704   109 EEELEKKEKELEQKQQELEKKEEELEELIEEQLQELER---ISGLTAEEAKEILLEKVEEEA 167
RasGAP_IQGAP1 cd05133
Ras-GTPase Activating Domain of IQ motif containing GTPase activating protein 1; IQGAP1 is a ...
582-731 8.47e-04

Ras-GTPase Activating Domain of IQ motif containing GTPase activating protein 1; IQGAP1 is a homodimeric protein that is widely expressed among vertebrate cell types from early embryogenesis. Mammalian IQGAP1 protein is the best characterized member of the IQGAP family, and contains several protein-interacting domains. Human IQGAP1 is most similar to mouse Iqgap1 (94% identity) and has 62% identity to human IQGAP2. IQGAP1 binds and cross-links actin filaments in vitro and has been implicated in Ca2+/calmodulin signaling, E-cadherin-dependent cell adhesion, cell motility, and invasion. Yeast IQGAP homologs have a role in the recruitment of actin filaments, are components of the spindle pole body, and are required for actomyosin ring assembly and cytokinesis. Furthermore, IQGAP1 over-expression has also been detected in gastric and colorectal carcinomas and gastric cancer cell lines.


Pssm-ID: 213335  Cd Length: 380  Bit Score: 43.49  E-value: 8.47e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514  582 EDIADRLISASLFLRFLCPAIMSPSLFGLMQEYPDEQTS----RTLTLIAKVIQNLANFSKFTSKEDFLGFMNEFLELEW 657
Cdd:cd05133    178 EDELLKIVGNLLYYRYMNPAIVAPDAFDIIDLSAGGQLTtdqrRNLGSIAKMLQHAASNKMFLGDNAHLSPINEYLSQSY 257
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514  658 GSMQQFLY---------------EISNLDTLTNSSSfegYIDLGRELSTlHALLWE----VLPQLS---KEALLKLGPLP 715
Cdd:cd05133    258 QKFRRFFQaacdvpeledkfnvdEYSDLVTLTKPVI---YISIGEIINT-HTLLLDhqdaIAPEHNdpiHELLDDLGEVP 333
                          170
                   ....*....|....*....
gi 1693744514  716 ---RLLNDISTALRNPNIQ 731
Cdd:cd05133    334 tieSLIGENPGPPGDPNRE 352
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
1174-1293 1.08e-03

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 43.40  E-value: 1.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514 1174 EYKLKEYSKSMDESRLDREYEEEIHSLKERLHMSNRKLEEYERRLLSQE------EQTSKILMQYQARLEQSEKRLRQQQ 1247
Cdd:PRK11448   128 DFKPGPFVPPEDPENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQqelvalEGLAAELEEKQQELEAQLEQLQEKA 207
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1693744514 1248 VEKDSQIK--------SIIGRLMLVEEELRrdhpamaeplpepkkRLLDAQERQ 1293
Cdd:PRK11448   208 AETSQERKqkrkeitdQAAKRLELSEEETR---------------ILIDQQLRK 246
MutS2 COG1193
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
1165-1284 1.62e-03

dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];


Pssm-ID: 440806 [Multi-domain]  Cd Length: 784  Bit Score: 42.82  E-value: 1.62e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514 1165 IESA--HIEREEYKLKEYSKSMDESRldREYEEEIHSLKERLHMSNRKLEEYERRLLSQEEQTSKILMQY---------- 1232
Cdd:COG1193    502 IERAreLLGEESIDVEKLIEELERER--RELEEEREEAERLREELEKLREELEEKLEELEEEKEEILEKAreeaeeilre 579
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1693744514 1233 -QARLEQSEKRLRQQQVEKDsQIKSIIGRLMLVEEELRRDHPAMAEPLPEPKK 1284
Cdd:COG1193    580 aRKEAEELIRELREAQAEEE-ELKEARKKLEELKQELEEKLEKPKKKAKPAKP 631
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
1165-1296 2.28e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 42.51  E-value: 2.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514 1165 IESA--HIEREEYKLKEYSKSMDESRldREYEEEIHSLKERLHMSNRKLEEYERRLLSQEEQTSKILMQ----YQARLEQ 1238
Cdd:PRK00409   504 IEEAkkLIGEDKEKLNELIASLEELE--RELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEaekeAQQAIKE 581
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1693744514 1239 SE-------KRLRQQQVEKDSQIKsiigrlmlvEEELRRDHPAMAEPLPEPKKRLLDAQERQLPP 1296
Cdd:PRK00409   582 AKkeadeiiKELRQLQKGGYASVK---------AHELIEARKRLNKANEKKEKKKKKQKEKQEEL 637
UDM1_RNF168 cd22265
UDM1 (ubiquitin-dependent DSB recruitment module 1) domain found in RING finger protein 168; ...
1189-1242 5.41e-03

UDM1 (ubiquitin-dependent DSB recruitment module 1) domain found in RING finger protein 168; RING finger protein 168 (RNF168) is an E3 ubiquitin-protein ligase that promotes noncanonical K27 ubiquitination to signal DNA damage. Together with RNF8, RNF168 functions as a DNA damage response (DDR) factor that promotes a series of ubiquitylation events on substrates such as H2A and H2AX. With H2AK13/15 ubiquitylation, it facilitates recruitment of repair factors p53-binding protein 1 (53BP1) or the RAP80-BRCA1 complex to sites of double-strand breaks (DSBs), and inhibits homologous recombination (HR) in cells deficient in the tumor suppressor BRCA1. RNF168 also promotes H2A neddylation, which antagonizes ubiquitylation of H2A and regulates DNA damage repair. In addition, RNF168 forms a functional complex with RAD6A or RAD6B during the DNA damage response. This model corresponds to the UDM1 (ubiquitin-dependent double-strand break [DSB] recruitment module 1) domain of RNF168, which comprises LRM1 (LR motif 1), UMI (ubiquitin-interacting motif [UIM]- and MIU-related UBD) and MIU1 (motif interacting with ubiquitin 1). Mutations of Ub-interacting residues in UDM1 have little effect on the accumulation of RNF168 to DSB sites, suggesting that it may not be the main site of binding ubiquitylated and polyubiquitylated targets.


Pssm-ID: 409018 [Multi-domain]  Cd Length: 73  Bit Score: 37.15  E-value: 5.41e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1693744514 1189 LDREYEEEIHSLKERLHM----SNRKLEEYERRLLSQEEQTSKILMQYQARLEQSEKR 1242
Cdd:cd22265      7 LRQEYEEEISKLEAERRAleeeENRASEEYIQKLLAEEEEEEKLAEERRRAEEEQLKE 64
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
1161-1294 5.42e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.08  E-value: 5.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514 1161 LSADIESAHIEREEY--KLKEYSKSMDESRLDR-EYEEEIHSLKERLHMSNRKLEEYERRLLSQEEQtskilmqyQARLE 1237
Cdd:COG1196    244 LEAELEELEAELEELeaELAELEAELEELRLELeELELELEEAQAEEYELLAELARLEQDIARLEER--------RRELE 315
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1693744514 1238 QSEKRLRQQQVEKDSQIKSIIGRLMLVEEELRRDHPAMAeplpEPKKRLLDAQERQL 1294
Cdd:COG1196    316 ERLEELEEELAELEEELEELEEELEELEEELEEAEEELE----EAEAELAEAEEALL 368
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1161-1294 6.22e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.66  E-value: 6.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514 1161 LSADIESAHIEREEY--KLKEYSKSMDESRLDREY-EEEIHSLKERLHMSNRKLEEYerrllsQEEQtsKILMQYQARLE 1237
Cdd:COG4372     64 LEEELEQARSELEQLeeELEELNEQLQAAQAELAQaQEELESLQEEAEELQEELEEL------QKER--QDLEQQRKQLE 135
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1693744514 1238 QSEKRLRQQQVEKDSQIKSIIGRLMLVEEELRRDHPAMAEPLPEPKKRLLDAQERQL 1294
Cdd:COG4372    136 AQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEA 192
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
1164-1293 8.33e-03

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 40.32  E-value: 8.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693744514 1164 DIESAHIEREEYKLKEYSKSMDESRLDREYEEEIHSLKERLHMSNRKLEEYERRllsQEEQTSKILMQYQ-----ARLEQ 1238
Cdd:pfam15709  349 EVERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQR---QEEEERKQRLQLQaaqerARQQQ 425
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1693744514 1239 SEKRLRQQQVEKDSQIKSiigrLMLVEEELRRdHPAMAEPLPEPKKRLLDAQERQ 1293
Cdd:pfam15709  426 EEFRRKLQELQRKKQQEE----AERAEAEKQR-QKELEMQLAEEQKRLMEMAEEE 475
 
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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