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Conserved domains on  [gi|569000222|ref|XP_006524305|]
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ras/Rap GTPase-activating protein SynGAP isoform X10 [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 ...
319-642 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: 616.52  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222  319 RYQTMSILPMELYKEFAEYVTNHYRMLCAVLEPALNVKGKEEVASALVHILQSTGKAKDFLSDMAMSEVDRFmEREHLIF 398
Cdd:cd05136     1 RYQSVDILPLEVYKEFLEYLTNNYLDLCEVLEPVLSVKAKEELATALVHILQSTGKAKEFLTDLVMAEVDRL-DDEHLIF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222  399 RENTLATKAIEEYMRLIGQKYLKDAIGEFIRALYESEENCEVDPIKCTAS-SLAEHQANLRMCCELALCKVVNSHCVFPR 477
Cdd:cd05136    80 RGNTLATKAMEAYLKLVGQKYLQETLGEFIRALYESEEDCEVDPSKCPPSaSLSRNQANLRRSVELAWCKILSSHCVFPR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222  478 ELKEVFASWRLRCAERGREDIADRLISASLFLRFLCPAIMSPSLFGLMQEYPDEQTSRTLTLIAKVIQNLANFSKFTSKE 557
Cdd:cd05136   160 ELREVFSSWRERLEERGREDIADRLISASLFLRFLCPAILSPSLFNLTQEYPSERAARNLTLIAKVIQNLANFTRFGGKE 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222  558 DFLGFMNEFLELEWGSMQQFLYEISNLDTLTNSSSFEGYIDLGRELSTLHALLWEVLPQLSKEALLKLGPLPRLLNDIST 637
Cdd:cd05136   240 EYMEFMNDFVEQEWPNMKQFLQEISSPSPSSNSSDFDGYIDLGRELSLLHSLLVEIISKLNQTTLDKLGPLPRILNDITE 319

                  ....*
gi 569000222  638 ALRNP 642
Cdd:cd05136   320 ALRNP 324
DUF3498 pfam12004
Domain of unknown function (DUF3498); This presumed domain is functionally uncharacterized. ...
632-1206 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: 565.54  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222   632 LNDISTALRNPN-IQRQPSRQSERTRSQPMVLRGPSAEMQgYMMRDLNSSIdlqsfmarglnssMDMARLPSPTKEKPpp 710
Cdd:pfam12004    1 LRDITTALTNPTpIQQQLRRFSEHSSSPPVPGRSISSGLQ-KMFEDPDDGL-------------SDFTRLPSPTPENK-- 64
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222   711 pppgggkDLFYVSRPPLARSSPAYCTSSSDITEPEQKMLSVNKSVSMLDLQGdgpgGRLNSSSVSNlAAVGDLLHSSQAS 790
Cdd:pfam12004   65 -------DLFFVTRPPLLQPSPARSSSYSDANEPDQQLPNGNKSLSMVDLQD----SRSLQGSPSP-PLHDAPLNLSQAG 132
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222   791 LTAALGLRPAPAGRLSQGSGSSItAAGMRLSQMGVTTdGVPAQQLRIPLSFQNPLFHMAADGPGPPAGHGGSsghgppss 870
Cdd:pfam12004  133 SQASVGLRPAWAARTSQGNPQSA-PQVRRPLQTPVTQ-GTRPQQLLAPLSFQNPVYHMAAGLPVSPRGLGSP-------- 202
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222   871 hhhhhhhhhhrggEPPGDTFAPFHGYSKSEDLSSGVPkpPAASILHSHSYSDEFGPSGTDFTRRQLSLQDSLQHMLSPPQ 950
Cdd:pfam12004  203 -------------DSSSETHSSFSSHSNSEDLSSAAA--NKKSGPSNSSYSEDFARRSTEFTRRQLSLTELQHQPAVPRQ 267
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222   951 ITIGPQRPAPSGPGGGSGggsgggqpppLQRGKSQQLTVSAAQKPRPSSGNLlQSPEPSYGPARPRQQSLSKEGsiggsg 1030
Cdd:pfam12004  268 NSAGPQRRIDQQGLGGPP----------LTRGRTPPSLLNSASYPRPSSGSL-MSSSPDWPPARLRQQSSSSKG------ 330
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222  1031 gsgggggggLKPSITK--QHSQTPSTLNP-TMPASERTVAWVSNMPHLSADIESAHIE-REEYKLKEysksmdesrldrv 1106
Cdd:pfam12004  331 ---------DSPETKQrtQHQQVPSPVNPsTLSPVERTAAWVLNMNGQYEEEESSGPEsREELKQAE------------- 388
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222  1107 kEYEEEIHSLKERLHMSNRKLEEYERRLLSQEEQTSKILMQYQARLEQSEKRLRQQQVEKDSQIKSIIGRLMLVEEELRR 1186
Cdd:pfam12004  389 -KYEQEISKLKERLRVSNRKLEEYERRLLAQEEQTQKLLLEYQARLEDSEERLRRQQEEKDSQMKSIISRLMAVEEELKK 467
                          570       580
                   ....*....|....*....|
gi 569000222  1187 DHPAMAEPLpEPKKRLLDAQ 1206
Cdd:pfam12004  468 DHAEMQAVI-DSKQKIIDAQ 486
PH_SynGAP cd13375
Synaptic Ras-GTPase activating protein Pleckstrin homology (PH) domain; SynGAP is a member of ...
36-227 1.50e-138

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: 420.26  E-value: 1.50e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222   36 PAAPFRPSQGFLSRRLKSSIKRTKSQPKLDRTSSFRQILPRFRSADHDRARLMQSFKESHSHESLLSPSSAAEALELNLD 115
Cdd:cd13375     1 PTAPFRPSQGFLSRRLKSSIKRTKSQPKLDRTSSFRQILPRFRSADHDRARLMQSFKESHSHESLLSPSSAAEALDLNLD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222  116 EDSIIKPVHSSILGQEFCFEVTTSSGTKCFACRSAAERDKWIENLQRAVKPNKDNSRRVDNVLKLWIIEARELPPKKRYY 195
Cdd:cd13375    81 EDSIIKPVHSSILGQEFCFEVTTASGTKCFACRSAAERDKWIENLQRAVKPNKDNSRRVDNVLKLWIIEARELPPKKRYY 160
                         170       180       190
                  ....*....|....*....|....*....|..
gi 569000222  196 CELCLDDMLYARTTSKPRSasgDTVFWGEHFE 227
Cdd:cd13375   161 CELCLDDMLYARTTSKPRT---DTVFWGEHFE 189
C2_SynGAP_like cd04013
C2 domain present in Ras GTPase activating protein (GAP) family; SynGAP, GAP1, RasGAP, and ...
166-328 1.28e-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: 226.80  E-value: 1.28e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222  166 PNKDNSRRVDNVLKLWIIEARELPPKKRYYCELCLDDMLYARTTSKPRsasGDTVFWGEHFEFNNLPAVRALRLHLYRDS 245
Cdd:cd04013     1 PNRDNSRRTENSLKLWIIEAKGLPPKKRYYCELCLDKTLYARTTSKLK---TDTLFWGEHFEFSNLPPVSVITVNLYRES 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222  246 DKKRKKDKAGYVGLVTVPVATLAGRHFTEQWYPVTLPTgsggsggmgsggggGSGGGSGGKGKGGCPAVRLKARYQTMSI 325
Cdd:cd04013    78 DKKKKKDKSQLIGTVNIPVTDVSSRQFVEKWYPVSTPK--------------GNGKSGGKEGKGESPSIRIKARYQSTRV 143

                  ...
gi 569000222  326 LPM 328
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 ...
319-642 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: 616.52  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222  319 RYQTMSILPMELYKEFAEYVTNHYRMLCAVLEPALNVKGKEEVASALVHILQSTGKAKDFLSDMAMSEVDRFmEREHLIF 398
Cdd:cd05136     1 RYQSVDILPLEVYKEFLEYLTNNYLDLCEVLEPVLSVKAKEELATALVHILQSTGKAKEFLTDLVMAEVDRL-DDEHLIF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222  399 RENTLATKAIEEYMRLIGQKYLKDAIGEFIRALYESEENCEVDPIKCTAS-SLAEHQANLRMCCELALCKVVNSHCVFPR 477
Cdd:cd05136    80 RGNTLATKAMEAYLKLVGQKYLQETLGEFIRALYESEEDCEVDPSKCPPSaSLSRNQANLRRSVELAWCKILSSHCVFPR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222  478 ELKEVFASWRLRCAERGREDIADRLISASLFLRFLCPAIMSPSLFGLMQEYPDEQTSRTLTLIAKVIQNLANFSKFTSKE 557
Cdd:cd05136   160 ELREVFSSWRERLEERGREDIADRLISASLFLRFLCPAILSPSLFNLTQEYPSERAARNLTLIAKVIQNLANFTRFGGKE 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222  558 DFLGFMNEFLELEWGSMQQFLYEISNLDTLTNSSSFEGYIDLGRELSTLHALLWEVLPQLSKEALLKLGPLPRLLNDIST 637
Cdd:cd05136   240 EYMEFMNDFVEQEWPNMKQFLQEISSPSPSSNSSDFDGYIDLGRELSLLHSLLVEIISKLNQTTLDKLGPLPRILNDITE 319

                  ....*
gi 569000222  638 ALRNP 642
Cdd:cd05136   320 ALRNP 324
DUF3498 pfam12004
Domain of unknown function (DUF3498); This presumed domain is functionally uncharacterized. ...
632-1206 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: 565.54  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222   632 LNDISTALRNPN-IQRQPSRQSERTRSQPMVLRGPSAEMQgYMMRDLNSSIdlqsfmarglnssMDMARLPSPTKEKPpp 710
Cdd:pfam12004    1 LRDITTALTNPTpIQQQLRRFSEHSSSPPVPGRSISSGLQ-KMFEDPDDGL-------------SDFTRLPSPTPENK-- 64
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222   711 pppgggkDLFYVSRPPLARSSPAYCTSSSDITEPEQKMLSVNKSVSMLDLQGdgpgGRLNSSSVSNlAAVGDLLHSSQAS 790
Cdd:pfam12004   65 -------DLFFVTRPPLLQPSPARSSSYSDANEPDQQLPNGNKSLSMVDLQD----SRSLQGSPSP-PLHDAPLNLSQAG 132
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222   791 LTAALGLRPAPAGRLSQGSGSSItAAGMRLSQMGVTTdGVPAQQLRIPLSFQNPLFHMAADGPGPPAGHGGSsghgppss 870
Cdd:pfam12004  133 SQASVGLRPAWAARTSQGNPQSA-PQVRRPLQTPVTQ-GTRPQQLLAPLSFQNPVYHMAAGLPVSPRGLGSP-------- 202
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222   871 hhhhhhhhhhrggEPPGDTFAPFHGYSKSEDLSSGVPkpPAASILHSHSYSDEFGPSGTDFTRRQLSLQDSLQHMLSPPQ 950
Cdd:pfam12004  203 -------------DSSSETHSSFSSHSNSEDLSSAAA--NKKSGPSNSSYSEDFARRSTEFTRRQLSLTELQHQPAVPRQ 267
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222   951 ITIGPQRPAPSGPGGGSGggsgggqpppLQRGKSQQLTVSAAQKPRPSSGNLlQSPEPSYGPARPRQQSLSKEGsiggsg 1030
Cdd:pfam12004  268 NSAGPQRRIDQQGLGGPP----------LTRGRTPPSLLNSASYPRPSSGSL-MSSSPDWPPARLRQQSSSSKG------ 330
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222  1031 gsgggggggLKPSITK--QHSQTPSTLNP-TMPASERTVAWVSNMPHLSADIESAHIE-REEYKLKEysksmdesrldrv 1106
Cdd:pfam12004  331 ---------DSPETKQrtQHQQVPSPVNPsTLSPVERTAAWVLNMNGQYEEEESSGPEsREELKQAE------------- 388
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222  1107 kEYEEEIHSLKERLHMSNRKLEEYERRLLSQEEQTSKILMQYQARLEQSEKRLRQQQVEKDSQIKSIIGRLMLVEEELRR 1186
Cdd:pfam12004  389 -KYEQEISKLKERLRVSNRKLEEYERRLLAQEEQTQKLLLEYQARLEDSEERLRRQQEEKDSQMKSIISRLMAVEEELKK 467
                          570       580
                   ....*....|....*....|
gi 569000222  1187 DHPAMAEPLpEPKKRLLDAQ 1206
Cdd:pfam12004  468 DHAEMQAVI-DSKQKIIDAQ 486
PH_SynGAP cd13375
Synaptic Ras-GTPase activating protein Pleckstrin homology (PH) domain; SynGAP is a member of ...
36-227 1.50e-138

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: 420.26  E-value: 1.50e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222   36 PAAPFRPSQGFLSRRLKSSIKRTKSQPKLDRTSSFRQILPRFRSADHDRARLMQSFKESHSHESLLSPSSAAEALELNLD 115
Cdd:cd13375     1 PTAPFRPSQGFLSRRLKSSIKRTKSQPKLDRTSSFRQILPRFRSADHDRARLMQSFKESHSHESLLSPSSAAEALDLNLD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222  116 EDSIIKPVHSSILGQEFCFEVTTSSGTKCFACRSAAERDKWIENLQRAVKPNKDNSRRVDNVLKLWIIEARELPPKKRYY 195
Cdd:cd13375    81 EDSIIKPVHSSILGQEFCFEVTTASGTKCFACRSAAERDKWIENLQRAVKPNKDNSRRVDNVLKLWIIEARELPPKKRYY 160
                         170       180       190
                  ....*....|....*....|....*....|..
gi 569000222  196 CELCLDDMLYARTTSKPRSasgDTVFWGEHFE 227
Cdd:cd13375   161 CELCLDDMLYARTTSKPRT---DTVFWGEHFE 189
RasGAP smart00323
GTPase-activator protein for Ras-like GTPases; All alpha-helical domain that accelerates the ...
315-634 3.41e-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: 331.58  E-value: 3.41e-103
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222    315 RLKARYQTMSILPMELYKEFAEYVTNHY-RMLCAVLEPALNVKGKEEVASALVHILQSTGKAKDFLSDMAMSEVDRfMER 393
Cdd:smart00323   10 RLKTVYTTDFILPSEYYEELLELLLFSLdLSLASALSEVCSGLDKDELATKLVRLFLRRGRGHPFLRALIDPEVER-TDD 88
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222    394 EHLIFRENTLATKAIEEYMRLIGQKYLKDAIGEFIRALYESEENCEVDPIKCTASSLAEHQANLRMCCELALCKVVNSHC 473
Cdd:smart00323   89 PNTIFRGNSLATKSMEVYMKLVGNQYLHTTLKPVLKKIVESKKSCEVDPAKLEGEDLETNLENLLQYVERLFDAIINSSD 168
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222    474 VFPRELKEVFASWRLRCAERGRE-DIADRLISASLFLRFLCPAIMSPSLFGLMQEYPDEQTSRTLTLIAKVIQNLANFSK 552
Cdd:smart00323  169 RLPYGLRDICKQLRQAAEKRFPDaDVIYKAVSSFVFLRFFCPAIVSPKLFNLVDEHPDPTTRRTLTLIAKVLQNLANLSE 248
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222    553 FTSKEDFLGFMNEFLELEWGSMQQFLYEISNLDTLTNSSSFEGYIDLGRELSTLHALLWEVLPQLSKEaLLKLGPLPRLL 632
Cdd:smart00323  249 FGSKEPWMEPLNDFLLSHKDRVKDFLDELSSVPEILVDKVSDSTTISGRELSLLHSLLLENGDALKRE-LNNEDPLGKLL 327

                    ..
gi 569000222    633 ND 634
Cdd:smart00323  328 FK 329
C2_SynGAP_like cd04013
C2 domain present in Ras GTPase activating protein (GAP) family; SynGAP, GAP1, RasGAP, and ...
166-328 1.28e-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: 226.80  E-value: 1.28e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222  166 PNKDNSRRVDNVLKLWIIEARELPPKKRYYCELCLDDMLYARTTSKPRsasGDTVFWGEHFEFNNLPAVRALRLHLYRDS 245
Cdd:cd04013     1 PNRDNSRRTENSLKLWIIEAKGLPPKKRYYCELCLDKTLYARTTSKLK---TDTLFWGEHFEFSNLPPVSVITVNLYRES 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222  246 DKKRKKDKAGYVGLVTVPVATLAGRHFTEQWYPVTLPTgsggsggmgsggggGSGGGSGGKGKGGCPAVRLKARYQTMSI 325
Cdd:cd04013    78 DKKKKKDKSQLIGTVNIPVTDVSSRQFVEKWYPVSTPK--------------GNGKSGGKEGKGESPSIRIKARYQSTRV 143

                  ...
gi 569000222  326 LPM 328
Cdd:cd04013   144 LPL 146
RasGAP pfam00616
GTPase-activator protein for Ras-like GTPase; All alpha-helical domain that accelerates the ...
378-549 4.09e-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: 118.93  E-value: 4.09e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222   378 FLSDMAMSEVDRFMEREHLiFRENTLATKAIEEYMRL-IGQKYLKDAIGEFIRALYESEE-NCEVDPIK----------- 444
Cdd:pfam00616    1 LISELIEEEIESSDNPNDL-LRGNSLVSKLLETYNRRpRGQEYLKKVLGPLVRKIIEDEDlDLESDPRKiyeslinqeel 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222   445 ---CTASS-----------------LAEHQANLRMCCELALCKVVNSHCVFPREL----KEVFASWRLRCAERGREDIAd 500
Cdd:pfam00616   80 ktgRSDLPrdvspeeaiedpevrqiFEDNLQKLRELADEFLDAIYSSLNQLPYGIryicKQLYELLEEKFPDASEEEIL- 158
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 569000222   501 RLISASLFLRFLCPAIMSPSLFGLMQEYPDEQTSRTLTLIAKVIQNLAN 549
Cdd:pfam00616  159 NAIGGFLFLRFFCPAIVNPDLFGLVDHQISPKQRRNLTLIAKVLQNLAN 207
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
1084-1211 8.57e-07

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: 53.53  E-value: 8.57e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222  1084 IEREEYKLKEYSKSMDESRLDRVKEYEEEIHSLKERLHMSNRKLEEYERRLLSQEEQTSKILMQ---YQARLEQSEKRLR 1160
Cdd:TIGR02169  267 LEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEidkLLAEIEELEREIE 346
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 569000222  1161 QQQVEKDsQIKSIIGRLMLVEEELRRDHPAMAEPLPEPKKRLLDAQVEITM 1211
Cdd:TIGR02169  347 EERKRRD-KLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEK 396
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
111-165 1.25e-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: 1.25e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 569000222    111 ELNLDEDSIIKPVHSSILGQEFCFEVTTSSG-TKCFACRSAAERDKWIENLQRAVK 165
Cdd:smart00233   47 SIDLSGCTVREAPDPDSSKKPHCFEIKTSDRkTLLLQAESEEEREKWVEALRKAIA 102
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
1084-1205 6.16e-05

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: 46.07  E-value: 6.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222 1084 IEREEYKLKEYSKSM--DESRLDRV---KEYE---EEIHSLKERLhmsnRKLEEYERRLLSQEEQTSKILMQYQARLEQS 1155
Cdd:COG1579    61 IKRLELEIEEVEARIkkYEEQLGNVrnnKEYEalqKEIESLKRRI----SDLEDEILELMERIEELEEELAELEAELAEL 136
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 569000222 1156 EKRLRQQQVEKDSQIKSIIGRLmlveEELRRDHPAMAEPLPEpkkRLLDA 1205
Cdd:COG1579   137 EAELEEKKAELDEELAELEAEL----EELEAEREELAAKIPP---ELLAL 179
PRK12704 PRK12704
phosphodiesterase; Provisional
1076-1186 7.05e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 47.08  E-value: 7.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222 1076 SADIESAHIEREEyKLKEYSKSMDESRLDRVKEYEEEIHSLKERLHMS----NRKLEEYERRLLSQEEQTSK---ILMQY 1148
Cdd:PRK12704   30 EAKIKEAEEEAKR-ILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKElrerRNELQKLEKRLLQKEENLDRkleLLEKR 108
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 569000222 1149 QARLEQSEKRLRQQQVEKDSQIKSIIGRLMLVEEELRR 1186
Cdd:PRK12704  109 EEELEKKEKELEQKQQELEKKEEELEELIEEQLQELER 146
C2 pfam00168
C2 domain;
176-279 8.46e-05

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 43.08  E-value: 8.46e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222   176 NVLKLWIIEARELPPKKRY-----YCELCLDDmLYARTTSKPRSASGDTVfWGEHFEFN-NLPAVRALRLHLYRDSDKKR 249
Cdd:pfam00168    1 GRLTVTVIEAKNLPPKDGNgtsdpYVKVYLLD-GKQKKKTKVVKNTLNPV-WNETFTFSvPDPENAVLEIEVYDYDRFGR 78
                           90       100       110
                   ....*....|....*....|....*....|
gi 569000222   250 KKDkagyVGLVTVPVATLAGRHFTEQWYPV 279
Cdd:pfam00168   79 DDF----IGEVRIPLSELDSGEGLDGWYPL 104
IQG1 COG5261
Protein involved in regulation of cellular morphogenesis/cytokinesis [Cell division and ...
501-635 1.58e-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: 46.42  E-value: 1.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222  501 RLISASLFLRFLCPAIMSPSLFGLMQEYPDEqTSRTLTLIAKVIQNLANFSKFTSkedFLGFMNEFLELEWGSMQQFLYE 580
Cdd:COG5261   613 GLIGGFFFLRFVNEALVSPQTSMLKDSCPSD-NVRKLATLSKILQSVFEITSSDK---FDVPLQPFLKEYKEKVHNLLRK 688
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 569000222  581 ISNLDTLTNSSSFEGYIDLGRELSTLHALLWEVLPQLSK-EALLKLGPLPRLLNDI 635
Cdd:COG5261   689 LGNVGDFEEYFEFDQYIDLVKKSRALEYLVNEIYLTHEIiIEYLDNLYDPDSLVDL 744
UDM1_RNF168 cd22265
UDM1 (ubiquitin-dependent DSB recruitment module 1) domain found in RING finger protein 168; ...
1107-1158 3.86e-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: 37.53  E-value: 3.86e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 569000222 1107 KEYEEEIHSLKERLHM----SNRKLEEYERRLLSQEEQTSKILMQYQARLEQSEKR 1158
Cdd:cd22265     9 QEYEEEISKLEAERRAleeeENRASEEYIQKLLAEEEEEEKLAEERRRAEEEQLKE 64
 
Name Accession Description Interval E-value
RasGAP_DAB2IP cd05136
Ras-GTPase Activating Domain of DAB2IP and similar proteins; The DAB2IP family of Ras ...
319-642 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: 616.52  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222  319 RYQTMSILPMELYKEFAEYVTNHYRMLCAVLEPALNVKGKEEVASALVHILQSTGKAKDFLSDMAMSEVDRFmEREHLIF 398
Cdd:cd05136     1 RYQSVDILPLEVYKEFLEYLTNNYLDLCEVLEPVLSVKAKEELATALVHILQSTGKAKEFLTDLVMAEVDRL-DDEHLIF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222  399 RENTLATKAIEEYMRLIGQKYLKDAIGEFIRALYESEENCEVDPIKCTAS-SLAEHQANLRMCCELALCKVVNSHCVFPR 477
Cdd:cd05136    80 RGNTLATKAMEAYLKLVGQKYLQETLGEFIRALYESEEDCEVDPSKCPPSaSLSRNQANLRRSVELAWCKILSSHCVFPR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222  478 ELKEVFASWRLRCAERGREDIADRLISASLFLRFLCPAIMSPSLFGLMQEYPDEQTSRTLTLIAKVIQNLANFSKFTSKE 557
Cdd:cd05136   160 ELREVFSSWRERLEERGREDIADRLISASLFLRFLCPAILSPSLFNLTQEYPSERAARNLTLIAKVIQNLANFTRFGGKE 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222  558 DFLGFMNEFLELEWGSMQQFLYEISNLDTLTNSSSFEGYIDLGRELSTLHALLWEVLPQLSKEALLKLGPLPRLLNDIST 637
Cdd:cd05136   240 EYMEFMNDFVEQEWPNMKQFLQEISSPSPSSNSSDFDGYIDLGRELSLLHSLLVEIISKLNQTTLDKLGPLPRILNDITE 319

                  ....*
gi 569000222  638 ALRNP 642
Cdd:cd05136   320 ALRNP 324
DUF3498 pfam12004
Domain of unknown function (DUF3498); This presumed domain is functionally uncharacterized. ...
632-1206 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: 565.54  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222   632 LNDISTALRNPN-IQRQPSRQSERTRSQPMVLRGPSAEMQgYMMRDLNSSIdlqsfmarglnssMDMARLPSPTKEKPpp 710
Cdd:pfam12004    1 LRDITTALTNPTpIQQQLRRFSEHSSSPPVPGRSISSGLQ-KMFEDPDDGL-------------SDFTRLPSPTPENK-- 64
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222   711 pppgggkDLFYVSRPPLARSSPAYCTSSSDITEPEQKMLSVNKSVSMLDLQGdgpgGRLNSSSVSNlAAVGDLLHSSQAS 790
Cdd:pfam12004   65 -------DLFFVTRPPLLQPSPARSSSYSDANEPDQQLPNGNKSLSMVDLQD----SRSLQGSPSP-PLHDAPLNLSQAG 132
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222   791 LTAALGLRPAPAGRLSQGSGSSItAAGMRLSQMGVTTdGVPAQQLRIPLSFQNPLFHMAADGPGPPAGHGGSsghgppss 870
Cdd:pfam12004  133 SQASVGLRPAWAARTSQGNPQSA-PQVRRPLQTPVTQ-GTRPQQLLAPLSFQNPVYHMAAGLPVSPRGLGSP-------- 202
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222   871 hhhhhhhhhhrggEPPGDTFAPFHGYSKSEDLSSGVPkpPAASILHSHSYSDEFGPSGTDFTRRQLSLQDSLQHMLSPPQ 950
Cdd:pfam12004  203 -------------DSSSETHSSFSSHSNSEDLSSAAA--NKKSGPSNSSYSEDFARRSTEFTRRQLSLTELQHQPAVPRQ 267
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222   951 ITIGPQRPAPSGPGGGSGggsgggqpppLQRGKSQQLTVSAAQKPRPSSGNLlQSPEPSYGPARPRQQSLSKEGsiggsg 1030
Cdd:pfam12004  268 NSAGPQRRIDQQGLGGPP----------LTRGRTPPSLLNSASYPRPSSGSL-MSSSPDWPPARLRQQSSSSKG------ 330
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222  1031 gsgggggggLKPSITK--QHSQTPSTLNP-TMPASERTVAWVSNMPHLSADIESAHIE-REEYKLKEysksmdesrldrv 1106
Cdd:pfam12004  331 ---------DSPETKQrtQHQQVPSPVNPsTLSPVERTAAWVLNMNGQYEEEESSGPEsREELKQAE------------- 388
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222  1107 kEYEEEIHSLKERLHMSNRKLEEYERRLLSQEEQTSKILMQYQARLEQSEKRLRQQQVEKDSQIKSIIGRLMLVEEELRR 1186
Cdd:pfam12004  389 -KYEQEISKLKERLRVSNRKLEEYERRLLAQEEQTQKLLLEYQARLEDSEERLRRQQEEKDSQMKSIISRLMAVEEELKK 467
                          570       580
                   ....*....|....*....|
gi 569000222  1187 DHPAMAEPLpEPKKRLLDAQ 1206
Cdd:pfam12004  468 DHAEMQAVI-DSKQKIIDAQ 486
PH_SynGAP cd13375
Synaptic Ras-GTPase activating protein Pleckstrin homology (PH) domain; SynGAP is a member of ...
36-227 1.50e-138

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: 420.26  E-value: 1.50e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222   36 PAAPFRPSQGFLSRRLKSSIKRTKSQPKLDRTSSFRQILPRFRSADHDRARLMQSFKESHSHESLLSPSSAAEALELNLD 115
Cdd:cd13375     1 PTAPFRPSQGFLSRRLKSSIKRTKSQPKLDRTSSFRQILPRFRSADHDRARLMQSFKESHSHESLLSPSSAAEALDLNLD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222  116 EDSIIKPVHSSILGQEFCFEVTTSSGTKCFACRSAAERDKWIENLQRAVKPNKDNSRRVDNVLKLWIIEARELPPKKRYY 195
Cdd:cd13375    81 EDSIIKPVHSSILGQEFCFEVTTASGTKCFACRSAAERDKWIENLQRAVKPNKDNSRRVDNVLKLWIIEARELPPKKRYY 160
                         170       180       190
                  ....*....|....*....|....*....|..
gi 569000222  196 CELCLDDMLYARTTSKPRSasgDTVFWGEHFE 227
Cdd:cd13375   161 CELCLDDMLYARTTSKPRT---DTVFWGEHFE 189
RasGAP smart00323
GTPase-activator protein for Ras-like GTPases; All alpha-helical domain that accelerates the ...
315-634 3.41e-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: 331.58  E-value: 3.41e-103
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222    315 RLKARYQTMSILPMELYKEFAEYVTNHY-RMLCAVLEPALNVKGKEEVASALVHILQSTGKAKDFLSDMAMSEVDRfMER 393
Cdd:smart00323   10 RLKTVYTTDFILPSEYYEELLELLLFSLdLSLASALSEVCSGLDKDELATKLVRLFLRRGRGHPFLRALIDPEVER-TDD 88
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222    394 EHLIFRENTLATKAIEEYMRLIGQKYLKDAIGEFIRALYESEENCEVDPIKCTASSLAEHQANLRMCCELALCKVVNSHC 473
Cdd:smart00323   89 PNTIFRGNSLATKSMEVYMKLVGNQYLHTTLKPVLKKIVESKKSCEVDPAKLEGEDLETNLENLLQYVERLFDAIINSSD 168
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222    474 VFPRELKEVFASWRLRCAERGRE-DIADRLISASLFLRFLCPAIMSPSLFGLMQEYPDEQTSRTLTLIAKVIQNLANFSK 552
Cdd:smart00323  169 RLPYGLRDICKQLRQAAEKRFPDaDVIYKAVSSFVFLRFFCPAIVSPKLFNLVDEHPDPTTRRTLTLIAKVLQNLANLSE 248
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222    553 FTSKEDFLGFMNEFLELEWGSMQQFLYEISNLDTLTNSSSFEGYIDLGRELSTLHALLWEVLPQLSKEaLLKLGPLPRLL 632
Cdd:smart00323  249 FGSKEPWMEPLNDFLLSHKDRVKDFLDELSSVPEILVDKVSDSTTISGRELSLLHSLLLENGDALKRE-LNNEDPLGKLL 327

                    ..
gi 569000222    633 ND 634
Cdd:smart00323  328 FK 329
PH_DAB2IP cd13376
DOC-2/Disabled homolog 2-interacting protein Pleckstrin homology (PH) domain; DAB2IP (also ...
45-227 1.35e-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: 281.98  E-value: 1.35e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222   45 GFLSRRLKSSIKRTKSQPKLDRTSSFRQILPRFRSADHDRARLMQSFKESHSHESLLSPSSAAEALELNLDEDSIIKPVH 124
Cdd:cd13376     3 GFLSRRLKGSIKRTKSQPKLDRNSSFRHILPGFRSVDNERSHLMPRLKESRSHESLLSPSSAVEALDLSMEEEVVIKPVH 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222  125 SSILGQEFCFEVTTSSGTKCFACRSAAERDKWIENLQRAVKPNKDNSRRVDNVLKLWIIEARELPPKKRYYCELCLDDML 204
Cdd:cd13376    83 SSILGQDYCFEVTTSSGSKCFSCRSAAERDKWMENLRRAVHPNKDNSRRVENMLKLWIIEAKDLPAKKKYLCELCLDDVL 162
                         170       180
                  ....*....|....*....|...
gi 569000222  205 YARTTSKPRSasgDTVFWGEHFE 227
Cdd:cd13376   163 YARTTCKLKT---DNVFWGEHFE 182
RasGAP cd04519
Ras GTPase Activating Domain; RasGAP functions as an enhancer of the hydrolysis of GTP that is ...
329-583 2.88e-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: 247.40  E-value: 2.88e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222  329 ELYKEFAEYVTNHYRMLCAVLEPALNVKGKEEVASALVHILQSTGKAKDFLSDMAMSEVDRFMErEHLIFRENTLATKAI 408
Cdd:cd04519     1 EEYRLLSLLLTESPLALLRELSQVLPVKDKEEVATALLRIFESRGLALEFLRYLVRSEVKNTKN-PNTLFRGNSLATKLL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222  409 EEYMRLIGQKYLKDAIGEFIRALYESEENCEVDPIKCTASSLAEHQANLRMCCELALCKVVNSHCVFPRELKEVFASWRL 488
Cdd:cd04519    80 DQYMKLVGQEYLKETLSPLIREILESKESCEIDTKLPVGEDLEENLENLLELVNKLVDRILSSLDRLPPELRYVFKILRE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222  489 RCAERGRED--IADRLISASLFLRFLCPAIMSPSLFGLMQEYPDEQTSRTLTLIAKVIQNLANFSKFTSKEDFLGFMNEF 566
Cdd:cd04519   160 FLAERFPEEpdEAYQAVSGFLFLRFICPAIVSPELFGLVPDEPSEQARRNLTLISKVLQSLANGVEFGDKEPFMKPLNDF 239
                         250
                  ....*....|....*..
gi 569000222  567 LELEWGSMQQFLYEISN 583
Cdd:cd04519   240 IKSNKPKLKQFLDELSS 256
C2_SynGAP_like cd04013
C2 domain present in Ras GTPase activating protein (GAP) family; SynGAP, GAP1, RasGAP, and ...
166-328 1.28e-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: 226.80  E-value: 1.28e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222  166 PNKDNSRRVDNVLKLWIIEARELPPKKRYYCELCLDDMLYARTTSKPRsasGDTVFWGEHFEFNNLPAVRALRLHLYRDS 245
Cdd:cd04013     1 PNRDNSRRTENSLKLWIIEAKGLPPKKRYYCELCLDKTLYARTTSKLK---TDTLFWGEHFEFSNLPPVSVITVNLYRES 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222  246 DKKRKKDKAGYVGLVTVPVATLAGRHFTEQWYPVTLPTgsggsggmgsggggGSGGGSGGKGKGGCPAVRLKARYQTMSI 325
Cdd:cd04013    78 DKKKKKDKSQLIGTVNIPVTDVSSRQFVEKWYPVSTPK--------------GNGKSGGKEGKGESPSIRIKARYQSTRV 143

                  ...
gi 569000222  326 LPM 328
Cdd:cd04013   144 LPL 146
PH_RasSynGAP-like cd13262
Synaptic Ras-GTPase activating protein family Pleckstrin homology (PH) domain; The RasSynGAP ...
44-174 2.26e-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: 185.33  E-value: 2.26e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222   44 QGFLSRRLKSSIKRTKSQPKLDRTSSFRqiLPRFRSADHDRarlMQSFKESHSHESLLSPSSAAEalELNLDEDSIIKPV 123
Cdd:cd13262     2 SGFFSRRLKGPLKRTKSVTKLERKSSKR--LPRTRLARAPA---GPRLRGSRSHESLLSSSSAAL--DLSADEDVVIRPL 74
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 569000222  124 HSSILGQEFCFEVTTSSGTKCFACRSAAERDKWIENLQRAVKPNKDNSRRV 174
Cdd:cd13262    75 HSSILGRKHCFQVTTSEGTRCFSCRSAAERDRWIEDLRRAAQPNKDNCRRT 125
RasGAP_CLA2_BUD2 cd05137
Ras-GTPase Activating Domain of CLA2/BUD2; CLA2/BUD2 functions as a GTPase-activating protein ...
317-598 9.29e-54

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: 192.39  E-value: 9.29e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222  317 KARYQTMSILPMELYKEFAEY---VTNHYRMLCAVLEPALNVkgkEEVASALVHILQSTGKAKDFLSDMAMSEVD----- 388
Cdd:cd05137     1 KVRLDENVVLPSKNYKPLEELlhnFDLGLTLQIAELVPGDKL---ERLSEILLDIFQASGREDEWFMALVEDEIDgidks 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222  389 --------RFMEREH-LIFRENTLATKAIEEYMRLIGQKYLKDAIGEFIRALYESEENCEVDPIKCTASS-------LAE 452
Cdd:cd05137    78 tsknkdmgKSSNNEAnLLFRGNSLLTKSLEKYMRRIGKEYLEKSIGDVIRKICEENKDCEVDPSRVKESDsiekeedLEE 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222  453 HQANLR-MCCELALCKVVNSHCvFPRELKEVFASWR----LRCAERGREDIadrL--ISASLFLRFLCPAIMSPSLFGLM 525
Cdd:cd05137   158 NWENLIsLTEEIWNSIYITSND-CPPELRKILKHIRakveDRYGDFLRTVT---LnsVSGFLFLRFFCPAILNPKLFGLL 233
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569000222  526 QEYPDEQTSRTLTLIAKVIQNLANFSKFTSKEDFLGFMNEFLElewgsmqqflyeisnldtlTNSSSFEGYID 598
Cdd:cd05137   234 KDHPRPRAQRTLTLIAKVLQNLANLTTFGQKEPWMEPMNEFLT-------------------THREELKDYID 287
PH_nGAP cd13373
Neuronal growth-associated proteins Pleckstrin homology (PH) domain; nGAP (also called RASAL2 ...
39-180 2.33e-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: 183.01  E-value: 2.33e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222   39 PFRPSqGFLSRRLKSSIKRTKSQPKLDRTSSFRqiLPRFRSADhDRARLMQSFKESHSHESLLSPSSAAEALELNLDEDS 118
Cdd:cd13373     1 PFKVS-GFFSKRLKGSIKRTKSQSKLDRNTSFR--LPSLRSAD-DRSRGLPKLKESRSHESLLSPGSAVEALDLGREEKV 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569000222  119 IIKPVHSSILGQEFCFEVTTSSGTKCFACRSAAERDKWIENLQRAVKPNKDNSRRVDNVLKL 180
Cdd:cd13373    77 SVKPLHSSILGQDFCFEVTYSSGSKCFSCSSAAERDKWMENLRRTVQPNKDNCRRAENVLRL 138
RasGAP_GAP1_like cd05128
Ras-GTPase Activating Domain of GAP1 and similar proteins; The GAP1 family of Ras ...
345-582 1.30e-47

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: 171.66  E-value: 1.30e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222  345 LCAVLEPALNVkGKEEVASALVHILQSTGKAKDFLSDMAMSEVDRFMErEHLIFRENTLATKAIEEYMRLIGQKYLKDAI 424
Cdd:cd05128    23 AVYLLEELVKV-DKDDVARPLVRIFLHHGQIVPLLRALASREISKTQD-PNTLFRGNSLASKCMDEFMKLVGMQYLHETL 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222  425 GEFIRALYESEENCEVDPIKCTASSLAE-HQANLRMCCELALCKVVNS--HCvfPRELKEVFASWRLRCAER--GREDIA 499
Cdd:cd05128   101 KPVIDEIFSEKKSCEIDPSKLKDGEVLEtNLANLRGYVERVFKAITSSarRC--PTLMCEIFSDLRESAAQRfpDNEDVP 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222  500 DRLISASLFLRFLCPAIMSPSLFGLMQEYPDEQTSRTLTLIAKVIQNLANFSKFTS----KEDFL-GFMNEFLELEW-GS 573
Cdd:cd05128   179 YTAVSGFIFLRFFAPAILNPKLFGLREEHPDPQTARTLTLISKTIQTLGNLGSSSSglgvKEAYMsPLYERFTDEQHvDA 258

                  ....*....
gi 569000222  574 MQQFLYEIS 582
Cdd:cd05128   259 VKKFLDRIS 267
RasGAP_Neurofibromin_like cd05392
Ras-GTPase Activating Domain of proteins similar to neurofibromin; Neurofibromin-like proteins ...
327-620 5.42e-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: 157.06  E-value: 5.42e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222  327 PMELYKEFAEYVTNHYRMLCAVLE--PALNVkgkEEVASALVHILQSTGKAKDFLSDMAMSEVDRfMEREHLIFRENTLA 404
Cdd:cd05392     2 KSEAYDELLELLIEDPQLLLAIAEvcPSSEV---DLLAQSLLNLFETRNRLLPLISWLIEDEISH-TSRAADLFRRNSVA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222  405 TKAIEEYMRLIGQKYLKDAIGEFIRALYESEENCEVDPIKCTASSLAEHQANLRMCCELALCKVVNSHCVFPRELKEVFA 484
Cdd:cd05392    78 TRLLTLYAKSVGNKYLRKVLRPLLTEIVDNKDYFEVEKIKPDDENLEENADLLMKYAQMLLDSITDSVDQLPPSFRYICN 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222  485 SWRlRCAERGREDIADRLISASLFLRFLCPAIMSPSLFGLMQEYPDEQTSRTLTLIAKVIQNLANFSKFTSKEDFLGFMN 564
Cdd:cd05392   158 TIY-ESVSKKFPDAALIAVGGFLFLRFICPAIVSPESENLLDPPPTPEARRSLILIAKVLQNIANGVLFSLKEPYLESLN 236
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 569000222  565 EFLELEWGSMQQFLYEISNLDTLTNSSSFEGYIDLGRELSTLHALLWEVLPQLSKE 620
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 ...
358-583 1.75e-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: 1.75e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222  358 KEEVASALVHILQSTGKAKDFLSDMAMSEVDRfMEREHLIFRENTLATKAIEEYMRLIGQKYLKDAIGEFIRALYESEEN 437
Cdd:cd05134    35 KQEAAIPLVRLFLHYGKIVPFISAIASAEVNR-TQDPNTIFRGNSLTSKCIDETMKLAGMHYLQVTLKPIIDEICQEHKP 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222  438 CEVDPIKCTAS-SLAEHQANLRMCCELALCKVVNSHCVFPRELKEVFASWRLRCAERGREDIADRL--ISASLFLRFLCP 514
Cdd:cd05134   114 CEIDPVKLKDGeNLENNRENLRQYVDRIFRVITKSGVSCPTVMCDIFFSLRESAAKRFQVDPDVRYtaVSSFIFLRFFAP 193
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569000222  515 AIMSPSLFGLMQEYPDEQTSRTLTLIAKVIQNLANFSKFTS---KEDFLG-FMNEFLELEWG-SMQQFLYEISN 583
Cdd:cd05134   194 AILSPNLFQLTPHHPDPQTSRTLTLISKTIQTLGSLSKSKSanfKESYMAaFYDYFNEQKYAdAVKNFLDLISS 267
RasGAP_p120GAP cd05391
Ras-GTPase Activating Domain of p120; p120GAP is a negative regulator of Ras that stimulates ...
325-632 1.61e-33

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: 132.61  E-value: 1.61e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222  325 ILPMELYKEFAEYVTNhyRMLCAVLEPAlNVKGKEEV--ASALVHILQSTGKAKDFLSDMAMSEVDRFMEREHLiFRENT 402
Cdd:cd05391     4 IMPEEEYSELKELILQ--KELHVVYALA-HVCGQDRTllASILLRIFRHEKLESLLLRTLNDREISMEDEATTL-FRATT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222  403 LATKAIEEYMRLIGQKYLKDAIGEFIRALYESEENCEVDPIKCT----ASSLAEHQANLRMCcelALCKVVNSHCVFPRE 478
Cdd:cd05391    80 LASTLMEQYMKATATPFVHHALKDTILKILESKQSCELNPSKLEknedVNTNLEHLLNILSE---LVEKIFMAAEILPPT 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222  479 LKEVFASWRLRCAERGRED--IADRLISASLFLRFLCPAIMSPSLFGLMQEYPDEQTSRTLTLIAKVIQNLANFSKFTSK 556
Cdd:cd05391   157 LRYIYGCLQKSVQQKWPTNttVRTRVVSGFVFLRLICPAILNPRMFNIISETPSPTAARTLTLVAKSLQNLANLVEFGAK 236
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569000222  557 EDFLGFMNEFLELEWGSMQQFLYEISNLDTLtNSSSFEGYIDLGRELSTLHALLWEVLPQLsKEALLKLGPLPRLL 632
Cdd:cd05391   237 EPYMEGVNPFIKKNKERMIMFLDELGNVPEL-PDTTEHSRTDLSRDLAALHEICVAHSDEL-RTLSNERGALKKLL 310
RasGAP pfam00616
GTPase-activator protein for Ras-like GTPase; All alpha-helical domain that accelerates the ...
378-549 4.09e-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: 118.93  E-value: 4.09e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222   378 FLSDMAMSEVDRFMEREHLiFRENTLATKAIEEYMRL-IGQKYLKDAIGEFIRALYESEE-NCEVDPIK----------- 444
Cdd:pfam00616    1 LISELIEEEIESSDNPNDL-LRGNSLVSKLLETYNRRpRGQEYLKKVLGPLVRKIIEDEDlDLESDPRKiyeslinqeel 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222   445 ---CTASS-----------------LAEHQANLRMCCELALCKVVNSHCVFPREL----KEVFASWRLRCAERGREDIAd 500
Cdd:pfam00616   80 ktgRSDLPrdvspeeaiedpevrqiFEDNLQKLRELADEFLDAIYSSLNQLPYGIryicKQLYELLEEKFPDASEEEIL- 158
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 569000222   501 RLISASLFLRFLCPAIMSPSLFGLMQEYPDEQTSRTLTLIAKVIQNLAN 549
Cdd:pfam00616  159 NAIGGFLFLRFFCPAIVNPDLFGLVDHQISPKQRRNLTLIAKVLQNLAN 207
RasGAP_RASAL cd05135
Ras-GTPase Activating Domain of RASAL1 and similar proteins; Ras GTPase activating-like ...
347-585 1.16e-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: 1.16e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222  347 AVLEPALNVKGKEEVASALVHILQSTGKAKDFLSDMAMSEVDRFMEREHLiFRENTLATKAIEEYMRLIGQKYLKDAIGE 426
Cdd:cd05135    29 AMLEEVTTGESRQDVATKLVKIFLGQGLVVPFLDYLNTREVGRTTDPNTL-FRSNSLASKSMEQFMKVVGMPYLHEVLKP 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222  427 FIRALYESEENCEVDPIKCTAS---------SLAEHQ------ANLRMCCELALCKVVNSHCVFPRELKEVFASWRLRCA 491
Cdd:cd05135   108 VINRIFEEKKYVELDPCKIDLNrtrrisfkgSLSEAQvresslELLQGYLGSIIDAIVGSVDQCPPVMRVAFKQLHKRVE 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222  492 ER----GREDIADRLISASLFLRFLCPAIMSPSLFGLMQEYPDEQTSRTLTLIAKVIQNLANFSK--FTSKEDFLGFMNE 565
Cdd:cd05135   188 ERfpeaEHQDVKYLAISGFLFLRFFAPAILTPKLFQLREQHADPRTSRTLLLLAKAVQSIGNLGLqlGQGKEQWMAPLHP 267
                         250       260
                  ....*....|....*....|
gi 569000222  566 FLELEWGSMQQFLYEISNLD 585
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 ...
358-583 2.03e-27

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: 113.06  E-value: 2.03e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222  358 KEEVASALVHILQSTGKAKDFLSDMAMSEVDRFMErEHLIFRENTLATKAIEEYMRLIGQKYLKDAIGEFIRALYESEEN 437
Cdd:cd05394    35 KYDAVLPLVRLLLHHNKLVPFVAAVAALDLKDTQE-ANTIFRGNSLATRCLDEMMKIVGKHYLKVTLKPVLDEICESPKP 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222  438 CEVDPIKCTASSLAE-HQANLRMCCELALCKVVNSHCVFPRELKEVFASWRLRCAERGRED--IADRLISASLFLRFLCP 514
Cdd:cd05394   114 CEIDPIKLKEGDNVEnNKENLRYYVDKVFFSIVKSSMSCPTLMCDVFRSLRHLAVKRFPNDphVQYSAVSSFVFLRFFAV 193
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569000222  515 AIMSPSLFGLMQEYPDEQTSRTLTLIAKVIQNLANFSKFTS------KEDFL-GFMNEFLELEW-GSMQQFLYEISN 583
Cdd:cd05394   194 AVVSPHTFQLRPHHPDAQTSRTLTLISKTIQTLGSWGSLSKsklssfKETFMcDFFKMFQEEKYiEKVKKFLDEISS 270
PH_RASAL3 cd13374
RAS protein activator like-3 Pleckstrin homology (PH) domain; RASAL3 is thought to be a Ras ...
71-189 3.40e-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: 105.48  E-value: 3.40e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222   71 RQILPRFRSADHDRARLMQSFKES--HSHESLLSPSSAAEaLELNLDEDSIIKPVHSSILGQEFCFEVTTSSGTKCFACR 148
Cdd:cd13374    23 RGLLKRLKEKKKAKAESTGTGRDGppSALGSRESLATISE-LDLGAERDVRVWPLHPSLLGEPHCFQVTWPGGSRCFSCR 101
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 569000222  149 SAAERDKWIENLQRAVKPNKDNSRRVDNVLKLWIIEARELP 189
Cdd:cd13374   102 SAAERDRWIEDLRRSFQPHQDNVEREETWLSVWVHEAKGLP 142
RasGAP_Neurofibromin cd05130
Ras-GTPase Activating Domain of neurofibromin; Neurofibromin is the product of the ...
360-612 5.21e-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: 101.63  E-value: 5.21e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222  360 EVASALVHILQSTGKAKDFLSDMAMSEVDRFMEREHLiFRENTLATKAIEEYMRLIGQKYLKDAIGEFIRALYESEE--N 437
Cdd:cd05130    41 ELARVLVTLFDSKHLLYQLLWNMFSKEVELADSMQTL-FRGNSLASKIMTFCFKVYGATYLQSLLEPLLRTMITSSEwvS 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222  438 CEVDPIKC-TASSLAEHQANLRMCCELALCKVVNSHCVFPRELKEVfaswrLRC-----AERGREDIADRLISAsLFLRF 511
Cdd:cd05130   120 YEVDPTRLeGNENLEENQRNLLQLTEKFFHAIISSSDEFPPQLRSV-----CHClyqvvSHRFPNSGLGAVGSA-IFLRF 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222  512 LCPAIMSPSLFGLMQEYPDEQTSRTLTLIAKVIQNLANFSKFTsKEDFLGFMNEFLELEWGSMQQFLYEISNLDTLT--N 589
Cdd:cd05130   194 INPAIVSPYEYGILDREPPPRVKRGLKLMSKILQNIANHVLFT-KEAHMLPFNDFLRNHFEAGRRFFSSIASDCGAVdgP 272
                         250       260
                  ....*....|....*....|...
gi 569000222  590 SSSFEGYIDLGRELStLHALLWE 612
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 ...
399-632 3.82e-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: 99.73  E-value: 3.82e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222  399 RENTLATKAIEEYMRL-IGQKYLKDAIGEFIRALYESEE-NCEVDPIKC----------------------TASSLAEH- 453
Cdd:cd05132    49 RANTAVSRMMTTYTRRgPGQSYLKTVLADRINDLISLKDlNLEINPLKVyeqmindieldtglpsnlprgiTPEEAAENp 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222  454 ------QANLRMCCELA---LCKVVNSHCVFPRELKEVFASWRLRCAER----GREDIADrLISASLFLRFLCPAIMSPS 520
Cdd:cd05132   129 avqniiEPRLEMLEEITnsfLEAIINSLDEVPYGIRWICKQIRSLTRRKfpdaSDETICS-LIGGFFLLRFINPAIVSPQ 207
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222  521 LFGLMQEYPDEQTSRTLTLIAKVIQNLANFSKFtSKEDFLGFMNEFLELEWGSMQQFLYEISNLDTLTNSSSFEGYIDLG 600
Cdd:cd05132   208 AYMLVDGKPSDNTRRTLTLIAKLLQNLANKPSY-SKEPYMAPLQPFVEENKERLNKFLNDLCEVDDFYESLELDQYIALS 286
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 569000222  601 R----------ELSTLHALLWEVLPQLSKEALLKLGPLPRLL 632
Cdd:cd05132   287 KkdlsinitlnEIYNTHSLLVKHLAELAPDHNDHLRLILQEL 328
RasGAP_RASA4 cd05395
Ras-GTPase Activating Domain of RASA4; Ras GTPase activating-like 4 protein (RASAL4), also ...
345-556 2.47e-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: 95.71  E-value: 2.47e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222  345 LCAVLEPALNVKGKEEVASALVHILQSTGKAKDFLSDMAMSEVDRFMEREHLiFRENTLATKAIEEYMRLIGQKYLKDAI 424
Cdd:cd05395    27 LISLIDETTTAECRQEVATNLVKLFLGQGLAKEFLDLLFQLELDKTTEPNTL-FRSNSLASKSMESFLKVAGMQYLHSVL 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222  425 GEFIRALYESEENCEVDPIKC--------------TASSLAEHQAN-LRMCCELALCKVVNSHCVFPRELKEVFASWRLR 489
Cdd:cd05395   106 GPTINRVFEEKKYVELDPSKVeikdvgcsglhriqTESEVIEQSAQlLQSYLGELLSAISKSVKYCPAVIRATFRQLFKR 185
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569000222  490 CAERGREDIADRL----ISASLFLRFLCPAIMSPSLFGLMQEYPDEQTSRTLTLIAKVIQNLANFSKFTSK 556
Cdd:cd05395   186 VQERFPENQHQNVkfiaVTSFLCLRFFSPAIMSPKLFHLREKHADARTSRTLLLLAKAVQNVGNMDTLASR 256
RasGAP_IQGAP_like cd05127
Ras-GTPase Activating Domain of IQ motif containing GTPase activating proteins; This family ...
386-635 4.43e-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: 53.36  E-value: 4.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222  386 EVDRFMEREHLIFRENTLATKAIEEYMR-LIGQKYLKDAIGEFIRALYESEE-NCEVDPIKC------------------ 445
Cdd:cd05127    21 EIESKVSLPEDIVTGNPTVIKLVVNYNRgPRGQKYLRELLGPVVKEILDDDDlDLETDPVDIykawinqeesrtgepskl 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222  446 --------------TASSLAEHQANLRMCCELALCKVVNSHCVFPREL----KEVFASWRLRCAERGREDIAdRLISASL 507
Cdd:cd05127   101 pydvtreqalkdpeVRKRLIEHLEKLRAITDKFLTAITESLDKMPYGMryiaKVLKEALREKFPDAPEEEIL-KIVGNLL 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222  508 FLRFLCPAIMSPSLFGLMQEYPDEQTS----RTLTLIAKVIQNLANFSKFTSKEDFLGFMNEFLELEWGSMQQFLYEIS- 582
Cdd:cd05127   180 YYRYMNPAIVAPEAFDIIDLSVGGQLSplqrRNLGSIAKVLQQAASGKLFGGENPYLSPLNPYISESHEKFKKFFLEACt 259
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569000222  583 --------NLDTLTNSSSFEG---YIDLgRELSTLHALLWEVLPQLS-------KEALLKLGPLPRLLNDI 635
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 ...
178-278 7.66e-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: 48.60  E-value: 7.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222  178 LKLWIIEARELPPKKR-----YYCELCLDDMLYARTTSKPRSAsgdTVFWGEHFEFNNL-PAVRALRLHLYRDSDKKRKK 251
Cdd:cd00030     1 LRVTVIEARNLPAKDLngksdPYVKVSLGGKQKFKTKVVKNTL---NPVWNETFEFPVLdPESDTLTVEVWDKDRFSKDD 77
                          90       100
                  ....*....|....*....|....*...
gi 569000222  252 dkagYVGLVTVPVATLAGR-HFTEQWYP 278
Cdd:cd00030    78 ----FLGEVEIPLSELLDSgKEGELWLP 101
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
1084-1211 8.57e-07

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: 53.53  E-value: 8.57e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222  1084 IEREEYKLKEYSKSMDESRLDRVKEYEEEIHSLKERLHMSNRKLEEYERRLLSQEEQTSKILMQ---YQARLEQSEKRLR 1160
Cdd:TIGR02169  267 LEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEidkLLAEIEELEREIE 346
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 569000222  1161 QQQVEKDsQIKSIIGRLMLVEEELRRDHPAMAEPLPEPKKRLLDAQVEITM 1211
Cdd:TIGR02169  347 EERKRRD-KLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEK 396
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
111-165 1.25e-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: 1.25e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 569000222    111 ELNLDEDSIIKPVHSSILGQEFCFEVTTSSG-TKCFACRSAAERDKWIENLQRAVK 165
Cdd:smart00233   47 SIDLSGCTVREAPDPDSSKKPHCFEIKTSDRkTLLLQAESEEEREKWVEALRKAIA 102
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
177-276 2.15e-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: 2.15e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222    177 VLKLWIIEARELPPKKRY-----YCELCLDDMLY--ARTTSKPRSASgdtVFWGEHFEFN-NLPAVRALRLHLYrdsdKK 248
Cdd:smart00239    1 TLTVKIISARNLPPKDKGgksdpYVKVSLDGDPKekKKTKVVKNTLN---PVWNETFEFEvPPPELAELEIEVY----DK 73
                            90       100
                    ....*....|....*....|....*...
gi 569000222    249 RKKDKAGYVGLVTVPVATLAGRHFTEQW 276
Cdd:smart00239   74 DRFGRDDFIGQVTIPLSDLLLGGRHEKL 101
C2A_RasGAP cd08383
C2 domain (first repeat) of Ras GTPase activating proteins (GAPs); RasGAPs suppress Ras ...
178-280 5.90e-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: 46.49  E-value: 5.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222  178 LKLWIIEARELPPKK--RYYCELCLDDMLYARTTSKprsaSGDTVFWGEHFEFNNLPAV---RALRLHLYRDSDKKRKkd 252
Cdd:cd08383     2 LRLRILEAKNLPSKGtrDPYCTVSLDQVEVARTKTV----EKLNPFWGEEFVFDDPPPDvtfFTLSFYNKDKRSKDRD-- 75
                          90       100
                  ....*....|....*....|....*...
gi 569000222  253 kagyVGLVTVPVATLAGRHFTEQWYPVT 280
Cdd:cd08383    76 ----IVIGKVALSKLDLGQGKDEWFPLT 99
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1075-1210 1.18e-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: 50.06  E-value: 1.18e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222  1075 LSADIESAHIEREEY--KLKEYSKSMDESRLdRVKEYEEEIHSLKERLHMSNRKLEEYERRLLSQEE---QTSKILMQYQ 1149
Cdd:TIGR02168  244 LQEELKEAEEELEELtaELQELEEKLEELRL-EVSELEEEIEELQKELYALANEISRLEQQKQILRErlaNLERQLEELE 322
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569000222  1150 ARLEQSEKRLRQQQVEKDsQIKSIIGRLMLVEEELRRDHPAMAEPLPEPKKRLLDAQVEIT 1210
Cdd:TIGR02168  323 AQLEELESKLDELAEELA-ELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLE 382
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
1084-1205 6.16e-05

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: 46.07  E-value: 6.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222 1084 IEREEYKLKEYSKSM--DESRLDRV---KEYE---EEIHSLKERLhmsnRKLEEYERRLLSQEEQTSKILMQYQARLEQS 1155
Cdd:COG1579    61 IKRLELEIEEVEARIkkYEEQLGNVrnnKEYEalqKEIESLKRRI----SDLEDEILELMERIEELEEELAELEAELAEL 136
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 569000222 1156 EKRLRQQQVEKDSQIKSIIGRLmlveEELRRDHPAMAEPLPEpkkRLLDA 1205
Cdd:COG1579   137 EAELEEKKAELDEELAELEAEL----EELEAEREELAAKIPP---ELLAL 179
PRK12704 PRK12704
phosphodiesterase; Provisional
1076-1186 7.05e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 47.08  E-value: 7.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222 1076 SADIESAHIEREEyKLKEYSKSMDESRLDRVKEYEEEIHSLKERLHMS----NRKLEEYERRLLSQEEQTSK---ILMQY 1148
Cdd:PRK12704   30 EAKIKEAEEEAKR-ILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKElrerRNELQKLEKRLLQKEENLDRkleLLEKR 108
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 569000222 1149 QARLEQSEKRLRQQQVEKDSQIKSIIGRLMLVEEELRR 1186
Cdd:PRK12704  109 EEELEKKEKELEQKQQELEKKEEELEELIEEQLQELER 146
C2_Ras_p21A1 cd08400
C2 domain present in RAS p21 protein activator 1 (RasA1); RasA1 is a GAP1 (GTPase activating ...
178-280 7.85e-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: 43.51  E-value: 7.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222  178 LKLWIIEARELPPKK--RYYCELCLDDMLYARTTSKprsaSGDTVFWGEHFEFNNLPA-VRALRLHLYRDSDKKRKKDka 254
Cdd:cd08400     6 LQLNVLEAHKLPVKHvpHPYCVISLNEVKVARTKVR----EGPNPVWSEEFVFDDLPPdVNSFTISLSNKAKRSKDSE-- 79
                          90       100
                  ....*....|....*....|....*.
gi 569000222  255 gyVGLVTVPVATLAGRHFTEQWYPVT 280
Cdd:cd08400    80 --IAEVTVQLSKLQNGQETDEWYPLS 103
C2 pfam00168
C2 domain;
176-279 8.46e-05

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 43.08  E-value: 8.46e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222   176 NVLKLWIIEARELPPKKRY-----YCELCLDDmLYARTTSKPRSASGDTVfWGEHFEFN-NLPAVRALRLHLYRDSDKKR 249
Cdd:pfam00168    1 GRLTVTVIEAKNLPPKDGNgtsdpYVKVYLLD-GKQKKKTKVVKNTLNPV-WNETFTFSvPDPENAVLEIEVYDYDRFGR 78
                           90       100       110
                   ....*....|....*....|....*....|
gi 569000222   250 KKDkagyVGLVTVPVATLAGRHFTEQWYPV 279
Cdd:pfam00168   79 DDF----IGEVRIPLSELDSGEGLDGWYPL 104
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
1068-1198 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 569000222  1068 WVSNMPHLSADIESAHIERE--EYKLKEYSKSMDESRlDRVKEYEEEIHSLKERLHMSNRKLEEYERRLLSQEEQTSKIL 1145
Cdd:TIGR02169  810 IEARLREIEQKLNRLTLEKEylEKEIQELQEQRIDLK-EQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLK 888
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 569000222  1146 MQ---YQARLEQSEKRLRQQQVE---KDSQIKSIIGRLMLVEEELRRDHPAMAEPLPEP 1198
Cdd:TIGR02169  889 KErdeLEAQLRELERKIEELEAQiekKRKRLSELKAKLEALEEELSEIEDPKGEDEEIP 947
IQG1 COG5261
Protein involved in regulation of cellular morphogenesis/cytokinesis [Cell division and ...
501-635 1.58e-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: 46.42  E-value: 1.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222  501 RLISASLFLRFLCPAIMSPSLFGLMQEYPDEqTSRTLTLIAKVIQNLANFSKFTSkedFLGFMNEFLELEWGSMQQFLYE 580
Cdd:COG5261   613 GLIGGFFFLRFVNEALVSPQTSMLKDSCPSD-NVRKLATLSKILQSVFEITSSDK---FDVPLQPFLKEYKEKVHNLLRK 688
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 569000222  581 ISNLDTLTNSSSFEGYIDLGRELSTLHALLWEVLPQLSK-EALLKLGPLPRLLNDI 635
Cdd:COG5261   689 LGNVGDFEEYFEFDQYIDLVKKSRALEYLVNEIYLTHEIiIEYLDNLYDPDSLVDL 744
RasGAP_IQGAP1 cd05133
Ras-GTPase Activating Domain of IQ motif containing GTPase activating protein 1; IQGAP1 is a ...
496-645 5.18e-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: 43.88  E-value: 5.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222  496 EDIADRLISASLFLRFLCPAIMSPSLFGLMQEYPDEQTS----RTLTLIAKVIQNLANFSKFTSKEDFLGFMNEFLELEW 571
Cdd:cd05133   178 EDELLKIVGNLLYYRYMNPAIVAPDAFDIIDLSAGGQLTtdqrRNLGSIAKMLQHAASNKMFLGDNAHLSPINEYLSQSY 257
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222  572 GSMQQFLY---------------EISNLDTLTNSSSfegYIDLGRELSTlHALLWE----VLPQLSK---EALLKLGPLP 629
Cdd:cd05133   258 QKFRRFFQaacdvpeledkfnvdEYSDLVTLTKPVI---YISIGEIINT-HTLLLDhqdaIAPEHNDpihELLDDLGEVP 333
                         170
                  ....*....|....*....
gi 569000222  630 ---RLLNDISTALRNPNIQ 645
Cdd:cd05133   334 tieSLIGENPGPPGDPNRE 352
DivIVA COG3599
Cell division septum initiation protein DivIVA, interacts with FtsZ and MinD [Cell cycle ...
1092-1186 7.32e-04

Cell division septum initiation protein DivIVA, interacts with FtsZ and MinD [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442818 [Multi-domain]  Cd Length: 125  Bit Score: 40.99  E-value: 7.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222 1092 KEYSKSM-----DESR--LDRV-KEYE---EEIHSLKERLHMSNRKLEEYERR-------LLSQEEQTSKILMQYQARLE 1153
Cdd:COG3599    11 KEFKKGFrgydeDEVDefLDEVaEDYErliRENKELKEKLEELEEELEEYRELeetlqktLVVAQETAEEVKENAEKEAE 90
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 569000222 1154 Q--SEKRLRQQQVEKDSQIKSIigRLMLVEEELRR 1186
Cdd:COG3599    91 LiiKEAELEAEKIIEEAQEKAR--KIVREIEELKR 123
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1061-1186 1.07e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.97  E-value: 1.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222 1061 ASERTVAWVSNMPHLSADIESAhieREEYKLKEYSKSMDESRLDRVK----EYEEEIHSLKERLHMSNRKLEEYERRLLS 1136
Cdd:COG4372    29 LSEQLRKALFELDKLQEELEQL---REELEQAREELEQLEEELEQARseleQLEEELEELNEQLQAAQAELAQAQEELES 105
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 569000222 1137 QEEQTSKI---LMQYQA---RLEQSEKRLRQQQVEKDSQIKSIIGRLMLVEEELRR 1186
Cdd:COG4372   106 LQEEAEELqeeLEELQKerqDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLES 161
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
1075-1185 1.34e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.39  E-value: 1.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222 1075 LSADIESAHIEREEY--KLKEYSKSMDESRLdRVKEYEEEIHSLKERLHMSNRKLEEYERRLLSQEEQTSKILMQyQARL 1152
Cdd:COG1196   244 LEAELEELEAELEELeaELAELEAELEELRL-ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER-LEEL 321
                          90       100       110
                  ....*....|....*....|....*....|...
gi 569000222 1153 EQSEKRLRQQQVEKDSQIKSIIGRLMLVEEELR 1185
Cdd:COG1196   322 EEELAELEEELEELEEELEELEEELEEAEEELE 354
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1074-1209 1.46e-03

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: 43.12  E-value: 1.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222  1074 HLSADIE--SAHIEREEYKLKEYSKSMDESRlDRVKEYEEEIHSLKERLHMSNRKLEEYERR-----------------L 1134
Cdd:TIGR02168  313 NLERQLEelEAQLEELESKLDELAEELAELE-EKLEELKEELESLEAELEELEAELEELESRleeleeqletlrskvaqL 391
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222  1135 LSQEEQTSKILMQYQARLEQSEKRLRQQQVEKDSQIKSI-----------IGRLMLVEEELRRDHPAMAEPLPEPKKRLL 1203
Cdd:TIGR02168  392 ELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLeeaelkelqaeLEELEEELEELQEELERLEEALEELREELE 471

                   ....*.
gi 569000222  1204 DAQVEI 1209
Cdd:TIGR02168  472 EAEQAL 477
MutS2 COG1193
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
1079-1200 3.18e-03

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


Pssm-ID: 440806 [Multi-domain]  Cd Length: 784  Bit Score: 42.05  E-value: 3.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222 1079 IESA--HIEREEYKLKEYSKSMDESRldrvKEYEEEIHSLKERLHMSNRKLEEYERRLLSQEEQTSKILMQY-------- 1148
Cdd:COG1193   502 IERAreLLGEESIDVEKLIEELERER----RELEEEREEAERLREELEKLREELEEKLEELEEEKEEILEKAreeaeeil 577
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 569000222 1149 ---QARLEQSEKRLRQQQVEKDsQIKSIIGRLMLVEEELRRDHPAMAEPLPEPKK 1200
Cdd:COG1193   578 reaRKEAEELIRELREAQAEEE-ELKEARKKLEELKQELEEKLEKPKKKAKPAKP 631
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
1079-1200 3.30e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 41.74  E-value: 3.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222 1079 IESA--HIEREEYKLKEYSKSMDESRLdRVKEYEEEIHSLK---ERLHMS----NRKLEEYERRLLS-QEEQTSKILMQY 1148
Cdd:PRK00409  504 IEEAkkLIGEDKEKLNELIASLEELER-ELEQKAEEAEALLkeaEKLKEEleekKEKLQEEEDKLLEeAEKEAQQAIKEA 582
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 569000222 1149 QARLEQSEKRLRQQQVEKDSQIKSiigrlMLVEEELRRDHPAmAEPLPEPKK 1200
Cdd:PRK00409  583 KKEADEIIKELRQLQKGGYASVKA-----HELIEARKRLNKA-NEKKEKKKK 628
RNase_Y_N pfam12072
RNase Y N-terminal region;
1079-1187 3.60e-03

RNase Y N-terminal region;


Pssm-ID: 463456 [Multi-domain]  Cd Length: 201  Bit Score: 40.25  E-value: 3.60e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222  1079 IESAHIEREEYKLKEYSKSMDESRLDRVkEYEEEIhslKERlhmsNRKLEEYERRLLSQEEQTSK---ILMQYQARLEQS 1155
Cdd:pfam12072   40 IEEAKKEAETKKKEALLEAKEEIHKLRA-EAEREL---KER----RNELQRQERRLLQKEETLDRkdeSLEKKEESLEKK 111
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 569000222  1156 EKRL--RQQQVE-KDSQIKSIIG-----------------RLML---VEEELRRD 1187
Cdd:pfam12072  112 EKELeaQQQQLEeKEEELEELIEeqrqelerisgltseeaKEILldeVEEELRHE 166
UDM1_RNF168 cd22265
UDM1 (ubiquitin-dependent DSB recruitment module 1) domain found in RING finger protein 168; ...
1107-1158 3.86e-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: 37.53  E-value: 3.86e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 569000222 1107 KEYEEEIHSLKERLHM----SNRKLEEYERRLLSQEEQTSKILMQYQARLEQSEKR 1158
Cdd:cd22265     9 QEYEEEISKLEAERRAleeeENRASEEYIQKLLAEEEEEEKLAEERRRAEEEQLKE 64
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
1065-1220 4.59e-03

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.16  E-value: 4.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222 1065 TVAWVSNMPHLSADIESAHIEreeyklkEYSKSMDESRLDRVKE----YEEEIHSLKERLHMSNRKLEEYERR--LLSQE 1138
Cdd:COG3206   139 EISYTSPDPELAAAVANALAE-------AYLEQNLELRREEARKalefLEEQLPELRKELEEAEAALEEFRQKngLVDLS 211
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222 1139 EQTSkilmQYQARLEQsekrLRQQQVEKDSQIKSIIGRLMLVEEELRRDHPAMAEPLPEP-----KKRLLDAQVEIT-MS 1212
Cdd:COG3206   212 EEAK----LLLQQLSE----LESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPviqqlRAQLAELEAELAeLS 283

                  ....*...
gi 569000222 1213 FIFSVSHP 1220
Cdd:COG3206   284 ARYTPNHP 291
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
1085-1185 6.22e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.82  E-value: 6.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222 1085 EREEYKLKEYSKSMDESRLDR----VKEYEEEIHSLKERLHMSNRKLEEYERRL--LSQEEQTSKILMQYQARLEQSEKR 1158
Cdd:PRK03918  301 FYEEYLDELREIEKRLSRLEEeingIEERIKELEEKEERLEELKKKLKELEKRLeeLEERHELYEEAKAKKEELERLKKR 380
                          90       100
                  ....*....|....*....|....*...
gi 569000222 1159 LRQQQVEK-DSQIKSIIGRLMLVEEELR 1185
Cdd:PRK03918  381 LTGLTPEKlEKELEELEKAKEEIEEEIS 408
MAT1 pfam06391
CDK-activating kinase assembly factor MAT1; MAT1 is an assembly/targeting factor for ...
1084-1172 6.87e-03

CDK-activating kinase assembly factor MAT1; MAT1 is an assembly/targeting factor for cyclin-dependent kinase-activating kinase (CAK), which interacts with the transcription factor TFIIH. The domain found to the N-terminal side of this domain is a C3HC4 RING finger.


Pssm-ID: 461894 [Multi-domain]  Cd Length: 202  Bit Score: 39.53  E-value: 6.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222  1084 IEREEYKLKEY---SKSMDESRLDRVKEYEEEIHSLKERLHmsnrklEEYERRLLSQEEQTSKILMQYQARLEQSEKRLR 1160
Cdd:pfam06391   88 LSQEEEELEELlelEKREKEERRKEEKQEEEEEKEKKEKAK------QELIDELMTSNKDAEEIIAQHKKTAKKRKSERR 161
                           90
                   ....*....|..
gi 569000222  1161 QQQVEKDSQIKS 1172
Cdd:pfam06391  162 RKLEELNRVLEQ 173
ARGLU pfam15346
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ...
1079-1163 7.88e-03

Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is required for the oestrogen-dependent expression of ESR1 target genes. It functions in cooperation with MED1. The family of proteins is found in eukaryotes.


Pssm-ID: 405931 [Multi-domain]  Cd Length: 151  Bit Score: 38.49  E-value: 7.88e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222  1079 IESAHIEREEYKLKEYSKSMdESRLDRVKEYEEEIHSLKERL----HMSNRKLEEYERRL----LSQEEQTSKILMQYQA 1150
Cdd:pfam15346   43 VEEARKIMEKQVLEELERER-EAELEEERRKEEEERKKREELerilEENNRKIEEAQRKEaeerLAMLEEQRRMKEERQR 121
                           90
                   ....*....|...
gi 569000222  1151 RLEQSEKRLRQQQ 1163
Cdd:pfam15346  122 REKEEEEREKREQ 134
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
1074-1186 7.89e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.69  E-value: 7.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222 1074 HLSADIESAHIEREEYKLKEysksmdESRLDRVKEYEEEIHSLKERLHMSNRKLEEYERRLLSQEEQTSKILMQyQARLE 1153
Cdd:COG1196   313 ELEERLEELEEELAELEEEL------EELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE-LEELA 385
                          90       100       110
                  ....*....|....*....|....*....|...
gi 569000222 1154 QSEKRLRQQQVEKDSQIKSIIGRLMLVEEELRR 1186
Cdd:COG1196   386 EELLEALRAAAELAAQLEELEEAEEALLERLER 418
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
1075-1192 8.94e-03

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: 39.52  E-value: 8.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222 1075 LSADIES--AHIEREEYKL------KEY---SKSMDESRLdRVKEYEEEIHSLKERLHMSNRKLEEYERRLLSQEEQTSK 1143
Cdd:COG1579    64 LELEIEEveARIKKYEEQLgnvrnnKEYealQKEIESLKR-RISDLEDEILELMERIEELEEELAELEAELAELEAELEE 142
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 569000222 1144 ILMQYQARLEQSEKRLRQQQVEKDSQIKSIIGRLMLVEEELRRDHPAMA 1192
Cdd:COG1579   143 KKAELDEELAELEAELEELEAEREELAAKIPPELLALYERIRKRKNGLA 191
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
1063-1202 9.19e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.43  E-value: 9.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000222 1063 ERTVAWVSNMPHLSADIESAHIEREEYKLKEYSKSMDESRLDRvKEYEEEIHSLKERLHMSNRKLEEYE---------RR 1133
Cdd:PRK03918  365 EEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEI-SKITARIGELKKEIKELKKAIEELKkakgkcpvcGR 443
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569000222 1134 LLSqEEQTSKILMQYQARLEQSEKRLrQQQVEKDSQIKSIIGRL---MLVEEELRRDHpAMAEPLPEPKKRL 1202
Cdd:PRK03918  444 ELT-EEHRKELLEEYTAELKRIEKEL-KEIEEKERKLRKELRELekvLKKESELIKLK-ELAEQLKELEEKL 512
 
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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