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Conserved domains on  [gi|569000227|ref|XP_006524307|]
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ras/Rap GTPase-activating protein SynGAP isoform X13 [Mus musculus]

Protein Classification

RasGAP_DAB2IP and UDM1_RNF168 domain-containing protein( domain architecture ID 11598903)

protein containing domains PH_SynGAP, C2_SynGAP_like, RasGAP_DAB2IP, and UDM1_RNF168

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 ...
 288-611 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: 615.36  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227  288 RYQTMSILPMELYKEFAEYVTNHYRMLCAVLEPALNVKGKEEVASALVHILQSTGKAKDFLSDMAMSEVDRFmEREHLIF 367
Cdd:cd05136     1 RYQSVDILPLEVYKEFLEYLTNNYLDLCEVLEPVLSVKAKEELATALVHILQSTGKAKEFLTDLVMAEVDRL-DDEHLIF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227  368 RENTLATKAIEEYMRLIGQKYLKDAIGEFIRALYESEENCEVDPIKCTAS-SLAEHQANLRMCCELALCKVVNSHCVFPR 446
Cdd:cd05136    80 RGNTLATKAMEAYLKLVGQKYLQETLGEFIRALYESEEDCEVDPSKCPPSaSLSRNQANLRRSVELAWCKILSSHCVFPR 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227  447 ELKEVFASWRLRCAERGREDIADRLISASLFLRFLCPAIMSPSLFGLMQEYPDEQTSRTLTLIAKVIQNLANFSKFTSKE 526
Cdd:cd05136   160 ELREVFSSWRERLEERGREDIADRLISASLFLRFLCPAILSPSLFNLTQEYPSERAARNLTLIAKVIQNLANFTRFGGKE 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227  527 DFLGFMNEFLELEWGSMQQFLYEISNLDTLTNSSSFEGYIDLGRELSTLHALLWEVLPQLSKEALLKLGPLPRLLNDIST 606
Cdd:cd05136   240 EYMEFMNDFVEQEWPNMKQFLQEISSPSPSSNSSDFDGYIDLGRELSLLHSLLVEIISKLNQTTLDKLGPLPRILNDITE 319


                  ....*
gi 569000227  607 ALRNP 611
Cdd:cd05136   320 ALRNP 324
DUF3498 pfam12004
Domain of unknown function (DUF3498); This presumed domain is functionally uncharacterized. ...
 601-1175 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: 565.92  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227   601 LNDISTALRNPN-IQRQPSRQSERTRSQPMVLRGPSAEMQgYMMRDLNSSIdlqsfmarglnssMDMARLPSPTKEKPpp 679
Cdd:pfam12004    1 LRDITTALTNPTpIQQQLRRFSEHSSSPPVPGRSISSGLQ-KMFEDPDDGL-------------SDFTRLPSPTPENK-- 64

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227   680 pppgggkDLFYVSRPPLARSSPAYCTSSSDITEPEQKMLSVNKSVSMLDLQGdgpgGRLNSSSVSNlAAVGDLLHSSQAS 759
Cdd:pfam12004   65 -------DLFFVTRPPLLQPSPARSSSYSDANEPDQQLPNGNKSLSMVDLQD----SRSLQGSPSP-PLHDAPLNLSQAG 132

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227   760 LTAALGLRPAPAGRLSQGSGSSItAAGMRLSQMGVTTdGVPAQQLRIPLSFQNPLFHMAADGPGPPAGHGGSsghgppss 839
Cdd:pfam12004  133 SQASVGLRPAWAARTSQGNPQSA-PQVRRPLQTPVTQ-GTRPQQLLAPLSFQNPVYHMAAGLPVSPRGLGSP-------- 202

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227   840 hhhhhhhhhhrggEPPGDTFAPFHGYSKSEDLSSGVPkpPAASILHSHSYSDEFGPSGTDFTRRQLSLQDSLQHMLSPPQ 919
Cdd:pfam12004  203 -------------DSSSETHSSFSSHSNSEDLSSAAA--NKKSGPSNSSYSEDFARRSTEFTRRQLSLTELQHQPAVPRQ 267

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227   920 ITIGPQRPAPSGPGGGSGggsgggqpppLQRGKSQQLTVSAAQKPRPSSGNLlQSPEPSYGPARPRQQSLSKEGsiggsg 999
Cdd:pfam12004  268 NSAGPQRRIDQQGLGGPP----------LTRGRTPPSLLNSASYPRPSSGSL-MSSSPDWPPARLRQQSSSSKG------ 330

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227  1000 gsgggggggLKPSITK--QHSQTPSTLNP-TMPASERTVAWVSNMPHLSADIESAHIE-REEYKLKEysksmdesrldrv 1075
Cdd:pfam12004  331 ---------DSPETKQrtQHQQVPSPVNPsTLSPVERTAAWVLNMNGQYEEEESSGPEsREELKQAE------------- 388

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227  1076 kEYEEEIHSLKERLHMSNRKLEEYERRLLSQEEQTSKILMQYQARLEQSEKRLRQQQVEKDSQIKSIIGRLMLVEEELRR 1155
Cdd:pfam12004  389 -KYEQEISKLKERLRVSNRKLEEYERRLLAQEEQTQKLLLEYQARLEDSEERLRRQQEEKDSQMKSIISRLMAVEEELKK 467

                          570       580
                   ....*....|....*....|
gi 569000227  1156 DHPAMAEPLpEPKKRLLDAQ 1175
Cdd:pfam12004  468 DHAEMQAVI-DSKQKIIDAQ 486
PH_SynGAP cd13375
Synaptic Ras-GTPase activating protein Pleckstrin homology (PH) domain; SynGAP is a member of ...
 5-196 1.43e-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: 419.49  E-value: 1.43e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227    5 PAAPFRPSQGFLSRRLKSSIKRTKSQPKLDRTSSFRQILPRFRSADHDRARLMQSFKESHSHESLLSPSSAAEALELNLD 84
Cdd:cd13375     1 PTAPFRPSQGFLSRRLKSSIKRTKSQPKLDRTSSFRQILPRFRSADHDRARLMQSFKESHSHESLLSPSSAAEALDLNLD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227   85 EDSIIKPVHSSILGQEFCFEVTTSSGTKCFACRSAAERDKWIENLQRAVKPNKDNSRRVDNVLKLWIIEARELPPKKRYY 164
Cdd:cd13375    81 EDSIIKPVHSSILGQEFCFEVTTASGTKCFACRSAAERDKWIENLQRAVKPNKDNSRRVDNVLKLWIIEARELPPKKRYY 160

                         170       180       190
                  ....*....|....*....|....*....|..
gi 569000227  165 CELCLDDMLYARTTSKPRSasgDTVFWGEHFE 196
Cdd:cd13375   161 CELCLDDMLYARTTSKPRT---DTVFWGEHFE 189
C2_SynGAP_like cd04013
C2 domain present in Ras GTPase activating protein (GAP) family; SynGAP, GAP1, RasGAP, and ...
 135-297 1.39e-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: 1.39e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227  135 PNKDNSRRVDNVLKLWIIEARELPPKKRYYCELCLDDMLYARTTSKPRsasGDTVFWGEHFEFNNLPAVRALRLHLYRDS 214
Cdd:cd04013     1 PNRDNSRRTENSLKLWIIEAKGLPPKKRYYCELCLDKTLYARTTSKLK---TDTLFWGEHFEFSNLPPVSVITVNLYRES 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227  215 DKKRKKDKAGYVGLVTVPVATLAGRHFTEQWYPVTLPTgsggsggmgsggggGSGGGSGGKGKGGCPAVRLKARYQTMSI 294
Cdd:cd04013    78 DKKKKKDKSQLIGTVNIPVTDVSSRQFVEKWYPVSTPK--------------GNGKSGGKEGKGESPSIRIKARYQSTRV 143


                  ...
gi 569000227  295 LPM 297
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 ...
 288-611 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: 615.36  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227  288 RYQTMSILPMELYKEFAEYVTNHYRMLCAVLEPALNVKGKEEVASALVHILQSTGKAKDFLSDMAMSEVDRFmEREHLIF 367
Cdd:cd05136     1 RYQSVDILPLEVYKEFLEYLTNNYLDLCEVLEPVLSVKAKEELATALVHILQSTGKAKEFLTDLVMAEVDRL-DDEHLIF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227  368 RENTLATKAIEEYMRLIGQKYLKDAIGEFIRALYESEENCEVDPIKCTAS-SLAEHQANLRMCCELALCKVVNSHCVFPR 446
Cdd:cd05136    80 RGNTLATKAMEAYLKLVGQKYLQETLGEFIRALYESEEDCEVDPSKCPPSaSLSRNQANLRRSVELAWCKILSSHCVFPR 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227  447 ELKEVFASWRLRCAERGREDIADRLISASLFLRFLCPAIMSPSLFGLMQEYPDEQTSRTLTLIAKVIQNLANFSKFTSKE 526
Cdd:cd05136   160 ELREVFSSWRERLEERGREDIADRLISASLFLRFLCPAILSPSLFNLTQEYPSERAARNLTLIAKVIQNLANFTRFGGKE 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227  527 DFLGFMNEFLELEWGSMQQFLYEISNLDTLTNSSSFEGYIDLGRELSTLHALLWEVLPQLSKEALLKLGPLPRLLNDIST 606
Cdd:cd05136   240 EYMEFMNDFVEQEWPNMKQFLQEISSPSPSSNSSDFDGYIDLGRELSLLHSLLVEIISKLNQTTLDKLGPLPRILNDITE 319


                  ....*
gi 569000227  607 ALRNP 611
Cdd:cd05136   320 ALRNP 324
DUF3498 pfam12004
Domain of unknown function (DUF3498); This presumed domain is functionally uncharacterized. ...
 601-1175 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: 565.92  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227   601 LNDISTALRNPN-IQRQPSRQSERTRSQPMVLRGPSAEMQgYMMRDLNSSIdlqsfmarglnssMDMARLPSPTKEKPpp 679
Cdd:pfam12004    1 LRDITTALTNPTpIQQQLRRFSEHSSSPPVPGRSISSGLQ-KMFEDPDDGL-------------SDFTRLPSPTPENK-- 64

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227   680 pppgggkDLFYVSRPPLARSSPAYCTSSSDITEPEQKMLSVNKSVSMLDLQGdgpgGRLNSSSVSNlAAVGDLLHSSQAS 759
Cdd:pfam12004   65 -------DLFFVTRPPLLQPSPARSSSYSDANEPDQQLPNGNKSLSMVDLQD----SRSLQGSPSP-PLHDAPLNLSQAG 132

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227   760 LTAALGLRPAPAGRLSQGSGSSItAAGMRLSQMGVTTdGVPAQQLRIPLSFQNPLFHMAADGPGPPAGHGGSsghgppss 839
Cdd:pfam12004  133 SQASVGLRPAWAARTSQGNPQSA-PQVRRPLQTPVTQ-GTRPQQLLAPLSFQNPVYHMAAGLPVSPRGLGSP-------- 202

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227   840 hhhhhhhhhhrggEPPGDTFAPFHGYSKSEDLSSGVPkpPAASILHSHSYSDEFGPSGTDFTRRQLSLQDSLQHMLSPPQ 919
Cdd:pfam12004  203 -------------DSSSETHSSFSSHSNSEDLSSAAA--NKKSGPSNSSYSEDFARRSTEFTRRQLSLTELQHQPAVPRQ 267

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227   920 ITIGPQRPAPSGPGGGSGggsgggqpppLQRGKSQQLTVSAAQKPRPSSGNLlQSPEPSYGPARPRQQSLSKEGsiggsg 999
Cdd:pfam12004  268 NSAGPQRRIDQQGLGGPP----------LTRGRTPPSLLNSASYPRPSSGSL-MSSSPDWPPARLRQQSSSSKG------ 330

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227  1000 gsgggggggLKPSITK--QHSQTPSTLNP-TMPASERTVAWVSNMPHLSADIESAHIE-REEYKLKEysksmdesrldrv 1075
Cdd:pfam12004  331 ---------DSPETKQrtQHQQVPSPVNPsTLSPVERTAAWVLNMNGQYEEEESSGPEsREELKQAE------------- 388

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227  1076 kEYEEEIHSLKERLHMSNRKLEEYERRLLSQEEQTSKILMQYQARLEQSEKRLRQQQVEKDSQIKSIIGRLMLVEEELRR 1155
Cdd:pfam12004  389 -KYEQEISKLKERLRVSNRKLEEYERRLLAQEEQTQKLLLEYQARLEDSEERLRRQQEEKDSQMKSIISRLMAVEEELKK 467

                          570       580
                   ....*....|....*....|
gi 569000227  1156 DHPAMAEPLpEPKKRLLDAQ 1175
Cdd:pfam12004  468 DHAEMQAVI-DSKQKIIDAQ 486
PH_SynGAP cd13375
Synaptic Ras-GTPase activating protein Pleckstrin homology (PH) domain; SynGAP is a member of ...
 5-196 1.43e-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: 419.49  E-value: 1.43e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227    5 PAAPFRPSQGFLSRRLKSSIKRTKSQPKLDRTSSFRQILPRFRSADHDRARLMQSFKESHSHESLLSPSSAAEALELNLD 84
Cdd:cd13375     1 PTAPFRPSQGFLSRRLKSSIKRTKSQPKLDRTSSFRQILPRFRSADHDRARLMQSFKESHSHESLLSPSSAAEALDLNLD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227   85 EDSIIKPVHSSILGQEFCFEVTTSSGTKCFACRSAAERDKWIENLQRAVKPNKDNSRRVDNVLKLWIIEARELPPKKRYY 164
Cdd:cd13375    81 EDSIIKPVHSSILGQEFCFEVTTASGTKCFACRSAAERDKWIENLQRAVKPNKDNSRRVDNVLKLWIIEARELPPKKRYY 160

                         170       180       190
                  ....*....|....*....|....*....|..
gi 569000227  165 CELCLDDMLYARTTSKPRSasgDTVFWGEHFE 196
Cdd:cd13375   161 CELCLDDMLYARTTSKPRT---DTVFWGEHFE 189
RasGAP smart00323
GTPase-activator protein for Ras-like GTPases; All alpha-helical domain that accelerates the ...
 284-603 4.82e-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: 330.81  E-value: 4.82e-103
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227    284 RLKARYQTMSILPMELYKEFAEYVTNHY-RMLCAVLEPALNVKGKEEVASALVHILQSTGKAKDFLSDMAMSEVDRfMER 362
Cdd:smart00323   10 RLKTVYTTDFILPSEYYEELLELLLFSLdLSLASALSEVCSGLDKDELATKLVRLFLRRGRGHPFLRALIDPEVER-TDD 88

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227    363 EHLIFRENTLATKAIEEYMRLIGQKYLKDAIGEFIRALYESEENCEVDPIKCTASSLAEHQANLRMCCELALCKVVNSHC 442
Cdd:smart00323   89 PNTIFRGNSLATKSMEVYMKLVGNQYLHTTLKPVLKKIVESKKSCEVDPAKLEGEDLETNLENLLQYVERLFDAIINSSD 168

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227    443 VFPRELKEVFASWRLRCAERGRE-DIADRLISASLFLRFLCPAIMSPSLFGLMQEYPDEQTSRTLTLIAKVIQNLANFSK 521
Cdd:smart00323  169 RLPYGLRDICKQLRQAAEKRFPDaDVIYKAVSSFVFLRFFCPAIVSPKLFNLVDEHPDPTTRRTLTLIAKVLQNLANLSE 248

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227    522 FTSKEDFLGFMNEFLELEWGSMQQFLYEISNLDTLTNSSSFEGYIDLGRELSTLHALLWEVLPQLSKEaLLKLGPLPRLL 601
Cdd:smart00323  249 FGSKEPWMEPLNDFLLSHKDRVKDFLDELSSVPEILVDKVSDSTTISGRELSLLHSLLLENGDALKRE-LNNEDPLGKLL 327


                    ..
gi 569000227    602 ND 603
Cdd:smart00323  328 FK 329
C2_SynGAP_like cd04013
C2 domain present in Ras GTPase activating protein (GAP) family; SynGAP, GAP1, RasGAP, and ...
 135-297 1.39e-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: 1.39e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227  135 PNKDNSRRVDNVLKLWIIEARELPPKKRYYCELCLDDMLYARTTSKPRsasGDTVFWGEHFEFNNLPAVRALRLHLYRDS 214
Cdd:cd04013     1 PNRDNSRRTENSLKLWIIEAKGLPPKKRYYCELCLDKTLYARTTSKLK---TDTLFWGEHFEFSNLPPVSVITVNLYRES 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227  215 DKKRKKDKAGYVGLVTVPVATLAGRHFTEQWYPVTLPTgsggsggmgsggggGSGGGSGGKGKGGCPAVRLKARYQTMSI 294
Cdd:cd04013    78 DKKKKKDKSQLIGTVNIPVTDVSSRQFVEKWYPVSTPK--------------GNGKSGGKEGKGESPSIRIKARYQSTRV 143


                  ...
gi 569000227  295 LPM 297
Cdd:cd04013   144 LPL 146
RasGAP pfam00616
GTPase-activator protein for Ras-like GTPase; All alpha-helical domain that accelerates the ...
 347-518 5.69e-30

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


Pssm-ID: 459871  Cd Length: 207  Bit Score: 118.54  E-value: 5.69e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227   347 FLSDMAMSEVDRFMEREHLiFRENTLATKAIEEYMRL-IGQKYLKDAIGEFIRALYESEE-NCEVDPIK----------- 413
Cdd:pfam00616    1 LISELIEEEIESSDNPNDL-LRGNSLVSKLLETYNRRpRGQEYLKKVLGPLVRKIIEDEDlDLESDPRKiyeslinqeel 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227   414 ---CTASS-----------------LAEHQANLRMCCELALCKVVNSHCVFPREL----KEVFASWRLRCAERGREDIAd 469
Cdd:pfam00616   80 ktgRSDLPrdvspeeaiedpevrqiFEDNLQKLRELADEFLDAIYSSLNQLPYGIryicKQLYELLEEKFPDASEEEIL- 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 569000227   470 RLISASLFLRFLCPAIMSPSLFGLMQEYPDEQTSRTLTLIAKVIQNLAN 518
Cdd:pfam00616  159 NAIGGFLFLRFFCPAIVNPDLFGLVDHQISPKQRRNLTLIAKVLQNLAN 207
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 1053-1180 9.62e-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: 9.62e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227  1053 IEREEYKLKEYSKSMDESRLDRVKEYEEEIHSLKERLHMSNRKLEEYERRLLSQEEQTSKILMQ---YQARLEQSEKRLR 1129
Cdd:TIGR02169  267 LEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEidkLLAEIEELEREIE 346

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 569000227  1130 QQQVEKDsQIKSIIGRLMLVEEELRRDHPAMAEPLPEPKKRLLDAQVEITM 1180
Cdd:TIGR02169  347 EERKRRD-KLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEK 396
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 80-134 1.19e-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: 1.19e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 569000227     80 ELNLDEDSIIKPVHSSILGQEFCFEVTTSSG-TKCFACRSAAERDKWIENLQRAVK 134
Cdd:smart00233   47 SIDLSGCTVREAPDPDSSKKPHCFEIKTSDRkTLLLQAESEEEREKWVEALRKAIA 102
PRK12704 PRK12704
phosphodiesterase; Provisional
 1045-1155 7.66e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 47.08  E-value: 7.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227 1045 SADIESAHIEREEyKLKEYSKSMDESRLDRVKEYEEEIHSLKERLHMS----NRKLEEYERRLLSQEEQTSK---ILMQY 1117
Cdd:PRK12704   30 EAKIKEAEEEAKR-ILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKElrerRNELQKLEKRLLQKEENLDRkleLLEKR 108

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 569000227 1118 QARLEQSEKRLRQQQVEKDSQIKSIIGRLMLVEEELRR 1155
Cdd:PRK12704  109 EEELEKKEKELEQKQQELEKKEEELEELIEEQLQELER 146
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 1053-1174 8.26e-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: 45.69  E-value: 8.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227 1053 IEREEYKLKEYSKSM--DESRLDRV---KEYE---EEIHSLKERLhmsnRKLEEYERRLLSQEEQTSKILMQYQARLEQS 1124
Cdd:COG1579    61 IKRLELEIEEVEARIkkYEEQLGNVrnnKEYEalqKEIESLKRRI----SDLEDEILELMERIEELEEELAELEAELAEL 136

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 569000227 1125 EKRLRQQQVEKDSQIKSIIGRLmlveEELRRDHPAMAEPLPEpkkRLLDA 1174
Cdd:COG1579   137 EAELEEKKAELDEELAELEAEL----EELEAEREELAAKIPP---ELLAL 179
C2 pfam00168
C2 domain;
145-248 8.50e-05

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 43.08  E-value: 8.50e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227   145 NVLKLWIIEARELPPKKRY-----YCELCLDDmLYARTTSKPRSASGDTVfWGEHFEFN-NLPAVRALRLHLYRDSDKKR 218
Cdd:pfam00168    1 GRLTVTVIEAKNLPPKDGNgtsdpYVKVYLLD-GKQKKKTKVVKNTLNPV-WNETFTFSvPDPENAVLEIEVYDYDRFGR 78

                           90       100       110
                   ....*....|....*....|....*....|
gi 569000227   219 KKDkagyVGLVTVPVATLAGRHFTEQWYPV 248
Cdd:pfam00168   79 DDF----IGEVRIPLSELDSGEGLDGWYPL 104
IQG1 COG5261
Protein involved in regulation of cellular morphogenesis/cytokinesis [Cell division and ...
 470-604 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 569000227  470 RLISASLFLRFLCPAIMSPSLFGLMQEYPDEqTSRTLTLIAKVIQNLANFSKFTSkedFLGFMNEFLELEWGSMQQFLYE 549
Cdd:COG5261   613 GLIGGFFFLRFVNEALVSPQTSMLKDSCPSD-NVRKLATLSKILQSVFEITSSDK---FDVPLQPFLKEYKEKVHNLLRK 688

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 569000227  550 ISNLDTLTNSSSFEGYIDLGRELSTLHALLWEVLPQLSK-EALLKLGPLPRLLNDI 604
Cdd:COG5261   689 LGNVGDFEEYFEFDQYIDLVKKSRALEYLVNEIYLTHEIiIEYLDNLYDPDSLVDL 744
UDM1_RNF168 cd22265
UDM1 (ubiquitin-dependent DSB recruitment module 1) domain found in RING finger protein 168; ...
 1076-1127 4.63e-03

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


Pssm-ID: 409018 [Multi-domain]  Cd Length: 73  Bit Score: 37.15  E-value: 4.63e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 569000227 1076 KEYEEEIHSLKERLHM----SNRKLEEYERRLLSQEEQTSKILMQYQARLEQSEKR 1127
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 ...
 288-611 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: 615.36  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227  288 RYQTMSILPMELYKEFAEYVTNHYRMLCAVLEPALNVKGKEEVASALVHILQSTGKAKDFLSDMAMSEVDRFmEREHLIF 367
Cdd:cd05136     1 RYQSVDILPLEVYKEFLEYLTNNYLDLCEVLEPVLSVKAKEELATALVHILQSTGKAKEFLTDLVMAEVDRL-DDEHLIF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227  368 RENTLATKAIEEYMRLIGQKYLKDAIGEFIRALYESEENCEVDPIKCTAS-SLAEHQANLRMCCELALCKVVNSHCVFPR 446
Cdd:cd05136    80 RGNTLATKAMEAYLKLVGQKYLQETLGEFIRALYESEEDCEVDPSKCPPSaSLSRNQANLRRSVELAWCKILSSHCVFPR 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227  447 ELKEVFASWRLRCAERGREDIADRLISASLFLRFLCPAIMSPSLFGLMQEYPDEQTSRTLTLIAKVIQNLANFSKFTSKE 526
Cdd:cd05136   160 ELREVFSSWRERLEERGREDIADRLISASLFLRFLCPAILSPSLFNLTQEYPSERAARNLTLIAKVIQNLANFTRFGGKE 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227  527 DFLGFMNEFLELEWGSMQQFLYEISNLDTLTNSSSFEGYIDLGRELSTLHALLWEVLPQLSKEALLKLGPLPRLLNDIST 606
Cdd:cd05136   240 EYMEFMNDFVEQEWPNMKQFLQEISSPSPSSNSSDFDGYIDLGRELSLLHSLLVEIISKLNQTTLDKLGPLPRILNDITE 319


                  ....*
gi 569000227  607 ALRNP 611
Cdd:cd05136   320 ALRNP 324
DUF3498 pfam12004
Domain of unknown function (DUF3498); This presumed domain is functionally uncharacterized. ...
 601-1175 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: 565.92  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227   601 LNDISTALRNPN-IQRQPSRQSERTRSQPMVLRGPSAEMQgYMMRDLNSSIdlqsfmarglnssMDMARLPSPTKEKPpp 679
Cdd:pfam12004    1 LRDITTALTNPTpIQQQLRRFSEHSSSPPVPGRSISSGLQ-KMFEDPDDGL-------------SDFTRLPSPTPENK-- 64

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227   680 pppgggkDLFYVSRPPLARSSPAYCTSSSDITEPEQKMLSVNKSVSMLDLQGdgpgGRLNSSSVSNlAAVGDLLHSSQAS 759
Cdd:pfam12004   65 -------DLFFVTRPPLLQPSPARSSSYSDANEPDQQLPNGNKSLSMVDLQD----SRSLQGSPSP-PLHDAPLNLSQAG 132

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227   760 LTAALGLRPAPAGRLSQGSGSSItAAGMRLSQMGVTTdGVPAQQLRIPLSFQNPLFHMAADGPGPPAGHGGSsghgppss 839
Cdd:pfam12004  133 SQASVGLRPAWAARTSQGNPQSA-PQVRRPLQTPVTQ-GTRPQQLLAPLSFQNPVYHMAAGLPVSPRGLGSP-------- 202

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227   840 hhhhhhhhhhrggEPPGDTFAPFHGYSKSEDLSSGVPkpPAASILHSHSYSDEFGPSGTDFTRRQLSLQDSLQHMLSPPQ 919
Cdd:pfam12004  203 -------------DSSSETHSSFSSHSNSEDLSSAAA--NKKSGPSNSSYSEDFARRSTEFTRRQLSLTELQHQPAVPRQ 267

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227   920 ITIGPQRPAPSGPGGGSGggsgggqpppLQRGKSQQLTVSAAQKPRPSSGNLlQSPEPSYGPARPRQQSLSKEGsiggsg 999
Cdd:pfam12004  268 NSAGPQRRIDQQGLGGPP----------LTRGRTPPSLLNSASYPRPSSGSL-MSSSPDWPPARLRQQSSSSKG------ 330

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227  1000 gsgggggggLKPSITK--QHSQTPSTLNP-TMPASERTVAWVSNMPHLSADIESAHIE-REEYKLKEysksmdesrldrv 1075
Cdd:pfam12004  331 ---------DSPETKQrtQHQQVPSPVNPsTLSPVERTAAWVLNMNGQYEEEESSGPEsREELKQAE------------- 388

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227  1076 kEYEEEIHSLKERLHMSNRKLEEYERRLLSQEEQTSKILMQYQARLEQSEKRLRQQQVEKDSQIKSIIGRLMLVEEELRR 1155
Cdd:pfam12004  389 -KYEQEISKLKERLRVSNRKLEEYERRLLAQEEQTQKLLLEYQARLEDSEERLRRQQEEKDSQMKSIISRLMAVEEELKK 467

                          570       580
                   ....*....|....*....|
gi 569000227  1156 DHPAMAEPLpEPKKRLLDAQ 1175
Cdd:pfam12004  468 DHAEMQAVI-DSKQKIIDAQ 486
PH_SynGAP cd13375
Synaptic Ras-GTPase activating protein Pleckstrin homology (PH) domain; SynGAP is a member of ...
 5-196 1.43e-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: 419.49  E-value: 1.43e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227    5 PAAPFRPSQGFLSRRLKSSIKRTKSQPKLDRTSSFRQILPRFRSADHDRARLMQSFKESHSHESLLSPSSAAEALELNLD 84
Cdd:cd13375     1 PTAPFRPSQGFLSRRLKSSIKRTKSQPKLDRTSSFRQILPRFRSADHDRARLMQSFKESHSHESLLSPSSAAEALDLNLD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227   85 EDSIIKPVHSSILGQEFCFEVTTSSGTKCFACRSAAERDKWIENLQRAVKPNKDNSRRVDNVLKLWIIEARELPPKKRYY 164
Cdd:cd13375    81 EDSIIKPVHSSILGQEFCFEVTTASGTKCFACRSAAERDKWIENLQRAVKPNKDNSRRVDNVLKLWIIEARELPPKKRYY 160

                         170       180       190
                  ....*....|....*....|....*....|..
gi 569000227  165 CELCLDDMLYARTTSKPRSasgDTVFWGEHFE 196
Cdd:cd13375   161 CELCLDDMLYARTTSKPRT---DTVFWGEHFE 189
RasGAP smart00323
GTPase-activator protein for Ras-like GTPases; All alpha-helical domain that accelerates the ...
 284-603 4.82e-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: 330.81  E-value: 4.82e-103
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227    284 RLKARYQTMSILPMELYKEFAEYVTNHY-RMLCAVLEPALNVKGKEEVASALVHILQSTGKAKDFLSDMAMSEVDRfMER 362
Cdd:smart00323   10 RLKTVYTTDFILPSEYYEELLELLLFSLdLSLASALSEVCSGLDKDELATKLVRLFLRRGRGHPFLRALIDPEVER-TDD 88

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227    363 EHLIFRENTLATKAIEEYMRLIGQKYLKDAIGEFIRALYESEENCEVDPIKCTASSLAEHQANLRMCCELALCKVVNSHC 442
Cdd:smart00323   89 PNTIFRGNSLATKSMEVYMKLVGNQYLHTTLKPVLKKIVESKKSCEVDPAKLEGEDLETNLENLLQYVERLFDAIINSSD 168

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227    443 VFPRELKEVFASWRLRCAERGRE-DIADRLISASLFLRFLCPAIMSPSLFGLMQEYPDEQTSRTLTLIAKVIQNLANFSK 521
Cdd:smart00323  169 RLPYGLRDICKQLRQAAEKRFPDaDVIYKAVSSFVFLRFFCPAIVSPKLFNLVDEHPDPTTRRTLTLIAKVLQNLANLSE 248

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227    522 FTSKEDFLGFMNEFLELEWGSMQQFLYEISNLDTLTNSSSFEGYIDLGRELSTLHALLWEVLPQLSKEaLLKLGPLPRLL 601
Cdd:smart00323  249 FGSKEPWMEPLNDFLLSHKDRVKDFLDELSSVPEILVDKVSDSTTISGRELSLLHSLLLENGDALKRE-LNNEDPLGKLL 327


                    ..
gi 569000227    602 ND 603
Cdd:smart00323  328 FK 329
PH_DAB2IP cd13376
DOC-2/Disabled homolog 2-interacting protein Pleckstrin homology (PH) domain; DAB2IP (also ...
 14-196 1.32e-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: 1.32e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227   14 GFLSRRLKSSIKRTKSQPKLDRTSSFRQILPRFRSADHDRARLMQSFKESHSHESLLSPSSAAEALELNLDEDSIIKPVH 93
Cdd:cd13376     3 GFLSRRLKGSIKRTKSQPKLDRNSSFRHILPGFRSVDNERSHLMPRLKESRSHESLLSPSSAVEALDLSMEEEVVIKPVH 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227   94 SSILGQEFCFEVTTSSGTKCFACRSAAERDKWIENLQRAVKPNKDNSRRVDNVLKLWIIEARELPPKKRYYCELCLDDML 173
Cdd:cd13376    83 SSILGQDYCFEVTTSSGSKCFSCRSAAERDKWMENLRRAVHPNKDNSRRVENMLKLWIIEAKDLPAKKKYLCELCLDDVL 162

                         170       180
                  ....*....|....*....|...
gi 569000227  174 YARTTSKPRSasgDTVFWGEHFE 196
Cdd:cd13376   163 YARTTCKLKT---DNVFWGEHFE 182
RasGAP cd04519
Ras GTPase Activating Domain; RasGAP functions as an enhancer of the hydrolysis of GTP that is ...
 298-552 5.35e-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: 246.63  E-value: 5.35e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227  298 ELYKEFAEYVTNHYRMLCAVLEPALNVKGKEEVASALVHILQSTGKAKDFLSDMAMSEVDRFMErEHLIFRENTLATKAI 377
Cdd:cd04519     1 EEYRLLSLLLTESPLALLRELSQVLPVKDKEEVATALLRIFESRGLALEFLRYLVRSEVKNTKN-PNTLFRGNSLATKLL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227  378 EEYMRLIGQKYLKDAIGEFIRALYESEENCEVDPIKCTASSLAEHQANLRMCCELALCKVVNSHCVFPRELKEVFASWRL 457
Cdd:cd04519    80 DQYMKLVGQEYLKETLSPLIREILESKESCEIDTKLPVGEDLEENLENLLELVNKLVDRILSSLDRLPPELRYVFKILRE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227  458 RCAERGRED--IADRLISASLFLRFLCPAIMSPSLFGLMQEYPDEQTSRTLTLIAKVIQNLANFSKFTSKEDFLGFMNEF 535
Cdd:cd04519   160 FLAERFPEEpdEAYQAVSGFLFLRFICPAIVSPELFGLVPDEPSEQARRNLTLISKVLQSLANGVEFGDKEPFMKPLNDF 239

                         250
                  ....*....|....*..
gi 569000227  536 LELEWGSMQQFLYEISN 552
Cdd:cd04519   240 IKSNKPKLKQFLDELSS 256
C2_SynGAP_like cd04013
C2 domain present in Ras GTPase activating protein (GAP) family; SynGAP, GAP1, RasGAP, and ...
 135-297 1.39e-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: 1.39e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227  135 PNKDNSRRVDNVLKLWIIEARELPPKKRYYCELCLDDMLYARTTSKPRsasGDTVFWGEHFEFNNLPAVRALRLHLYRDS 214
Cdd:cd04013     1 PNRDNSRRTENSLKLWIIEAKGLPPKKRYYCELCLDKTLYARTTSKLK---TDTLFWGEHFEFSNLPPVSVITVNLYRES 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227  215 DKKRKKDKAGYVGLVTVPVATLAGRHFTEQWYPVTLPTgsggsggmgsggggGSGGGSGGKGKGGCPAVRLKARYQTMSI 294
Cdd:cd04013    78 DKKKKKDKSQLIGTVNIPVTDVSSRQFVEKWYPVSTPK--------------GNGKSGGKEGKGESPSIRIKARYQSTRV 143


                  ...
gi 569000227  295 LPM 297
Cdd:cd04013   144 LPL 146
PH_RasSynGAP-like cd13262
Synaptic Ras-GTPase activating protein family Pleckstrin homology (PH) domain; The RasSynGAP ...
 13-143 1.63e-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: 185.71  E-value: 1.63e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227   13 QGFLSRRLKSSIKRTKSQPKLDRTSSFRqiLPRFRSADHDRarlMQSFKESHSHESLLSPSSAAEalELNLDEDSIIKPV 92
Cdd:cd13262     2 SGFFSRRLKGPLKRTKSVTKLERKSSKR--LPRTRLARAPA---GPRLRGSRSHESLLSSSSAAL--DLSADEDVVIRPL 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 569000227   93 HSSILGQEFCFEVTTSSGTKCFACRSAAERDKWIENLQRAVKPNKDNSRRV 143
Cdd:cd13262    75 HSSILGRKHCFQVTTSEGTRCFSCRSAAERDRWIEDLRRAAQPNKDNCRRT 125
RasGAP_CLA2_BUD2 cd05137
Ras-GTPase Activating Domain of CLA2/BUD2; CLA2/BUD2 functions as a GTPase-activating protein ...
 286-567 1.20e-53

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


Pssm-ID: 213339 [Multi-domain]  Cd Length: 356  Bit Score: 192.01  E-value: 1.20e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227  286 KARYQTMSILPMELYKEFAEY---VTNHYRMLCAVLEPALNVkgkEEVASALVHILQSTGKAKDFLSDMAMSEVD----- 357
Cdd:cd05137     1 KVRLDENVVLPSKNYKPLEELlhnFDLGLTLQIAELVPGDKL---ERLSEILLDIFQASGREDEWFMALVEDEIDgidks 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227  358 --------RFMEREH-LIFRENTLATKAIEEYMRLIGQKYLKDAIGEFIRALYESEENCEVDPIKCTASS-------LAE 421
Cdd:cd05137    78 tsknkdmgKSSNNEAnLLFRGNSLLTKSLEKYMRRIGKEYLEKSIGDVIRKICEENKDCEVDPSRVKESDsiekeedLEE 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227  422 HQANLR-MCCELALCKVVNSHCvFPRELKEVFASWR----LRCAERGREDIadrL--ISASLFLRFLCPAIMSPSLFGLM 494
Cdd:cd05137   158 NWENLIsLTEEIWNSIYITSND-CPPELRKILKHIRakveDRYGDFLRTVT---LnsVSGFLFLRFFCPAILNPKLFGLL 233

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569000227  495 QEYPDEQTSRTLTLIAKVIQNLANFSKFTSKEDFLGFMNEFLElewgsmqqflyeisnldtlTNSSSFEGYID 567
Cdd:cd05137   234 KDHPRPRAQRTLTLIAKVLQNLANLTTFGQKEPWMEPMNEFLT-------------------THREELKDYID 287
PH_nGAP cd13373
Neuronal growth-associated proteins Pleckstrin homology (PH) domain; nGAP (also called RASAL2 ...
 8-149 2.27e-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: 2.27e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227    8 PFRPSqGFLSRRLKSSIKRTKSQPKLDRTSSFRqiLPRFRSADhDRARLMQSFKESHSHESLLSPSSAAEALELNLDEDS 87
Cdd:cd13373     1 PFKVS-GFFSKRLKGSIKRTKSQSKLDRNTSFR--LPSLRSAD-DRSRGLPKLKESRSHESLLSPGSAVEALDLGREEKV 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569000227   88 IIKPVHSSILGQEFCFEVTTSSGTKCFACRSAAERDKWIENLQRAVKPNKDNSRRVDNVLKL 149
Cdd:cd13373    77 SVKPLHSSILGQDFCFEVTYSSGSKCFSCSSAAERDKWMENLRRTVQPNKDNCRRAENVLRL 138
RasGAP_GAP1_like cd05128
Ras-GTPase Activating Domain of GAP1 and similar proteins; The GAP1 family of Ras ...
 314-551 1.91e-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: 170.89  E-value: 1.91e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227  314 LCAVLEPALNVkGKEEVASALVHILQSTGKAKDFLSDMAMSEVDRFMErEHLIFRENTLATKAIEEYMRLIGQKYLKDAI 393
Cdd:cd05128    23 AVYLLEELVKV-DKDDVARPLVRIFLHHGQIVPLLRALASREISKTQD-PNTLFRGNSLASKCMDEFMKLVGMQYLHETL 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227  394 GEFIRALYESEENCEVDPIKCTASSLAE-HQANLRMCCELALCKVVNS--HCvfPRELKEVFASWRLRCAER--GREDIA 468
Cdd:cd05128   101 KPVIDEIFSEKKSCEIDPSKLKDGEVLEtNLANLRGYVERVFKAITSSarRC--PTLMCEIFSDLRESAAQRfpDNEDVP 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227  469 DRLISASLFLRFLCPAIMSPSLFGLMQEYPDEQTSRTLTLIAKVIQNLANFSKFTS----KEDFL-GFMNEFLELEW-GS 542
Cdd:cd05128   179 YTAVSGFIFLRFFAPAILNPKLFGLREEHPDPQTARTLTLISKTIQTLGNLGSSSSglgvKEAYMsPLYERFTDEQHvDA 258


                  ....*....
gi 569000227  543 MQQFLYEIS 551
Cdd:cd05128   259 VKKFLDRIS 267
RasGAP_Neurofibromin_like cd05392
Ras-GTPase Activating Domain of proteins similar to neurofibromin; Neurofibromin-like proteins ...
 296-589 8.74e-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: 156.29  E-value: 8.74e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227  296 PMELYKEFAEYVTNHYRMLCAVLE--PALNVkgkEEVASALVHILQSTGKAKDFLSDMAMSEVDRfMEREHLIFRENTLA 373
Cdd:cd05392     2 KSEAYDELLELLIEDPQLLLAIAEvcPSSEV---DLLAQSLLNLFETRNRLLPLISWLIEDEISH-TSRAADLFRRNSVA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227  374 TKAIEEYMRLIGQKYLKDAIGEFIRALYESEENCEVDPIKCTASSLAEHQANLRMCCELALCKVVNSHCVFPRELKEVFA 453
Cdd:cd05392    78 TRLLTLYAKSVGNKYLRKVLRPLLTEIVDNKDYFEVEKIKPDDENLEENADLLMKYAQMLLDSITDSVDQLPPSFRYICN 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227  454 SWRlRCAERGREDIADRLISASLFLRFLCPAIMSPSLFGLMQEYPDEQTSRTLTLIAKVIQNLANFSKFTSKEDFLGFMN 533
Cdd:cd05392   158 TIY-ESVSKKFPDAALIAVGGFLFLRFICPAIVSPESENLLDPPPTPEARRSLILIAKVLQNIANGVLFSLKEPYLESLN 236

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 569000227  534 EFLELEWGSMQQFLYEISNLDTLTNSSSFEGYIDLGRELSTLHALLWEVLPQLSKE 589
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 ...
 327-552 1.70e-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: 1.70e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227  327 KEEVASALVHILQSTGKAKDFLSDMAMSEVDRfMEREHLIFRENTLATKAIEEYMRLIGQKYLKDAIGEFIRALYESEEN 406
Cdd:cd05134    35 KQEAAIPLVRLFLHYGKIVPFISAIASAEVNR-TQDPNTIFRGNSLTSKCIDETMKLAGMHYLQVTLKPIIDEICQEHKP 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227  407 CEVDPIKCTAS-SLAEHQANLRMCCELALCKVVNSHCVFPRELKEVFASWRLRCAERGREDIADRL--ISASLFLRFLCP 483
Cdd:cd05134   114 CEIDPVKLKDGeNLENNRENLRQYVDRIFRVITKSGVSCPTVMCDIFFSLRESAAKRFQVDPDVRYtaVSSFIFLRFFAP 193

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569000227  484 AIMSPSLFGLMQEYPDEQTSRTLTLIAKVIQNLANFSKFTS---KEDFLG-FMNEFLELEWG-SMQQFLYEISN 552
Cdd:cd05134   194 AILSPNLFQLTPHHPDPQTSRTLTLISKTIQTLGSLSKSKSanfKESYMAaFYDYFNEQKYAdAVKNFLDLISS 267
RasGAP_p120GAP cd05391
Ras-GTPase Activating Domain of p120; p120GAP is a negative regulator of Ras that stimulates ...
 294-601 2.22e-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: 132.23  E-value: 2.22e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227  294 ILPMELYKEFAEYVTNhyRMLCAVLEPAlNVKGKEEV--ASALVHILQSTGKAKDFLSDMAMSEVDRFMEREHLiFRENT 371
Cdd:cd05391     4 IMPEEEYSELKELILQ--KELHVVYALA-HVCGQDRTllASILLRIFRHEKLESLLLRTLNDREISMEDEATTL-FRATT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227  372 LATKAIEEYMRLIGQKYLKDAIGEFIRALYESEENCEVDPIKCT----ASSLAEHQANLRMCcelALCKVVNSHCVFPRE 447
Cdd:cd05391    80 LASTLMEQYMKATATPFVHHALKDTILKILESKQSCELNPSKLEknedVNTNLEHLLNILSE---LVEKIFMAAEILPPT 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227  448 LKEVFASWRLRCAERGRED--IADRLISASLFLRFLCPAIMSPSLFGLMQEYPDEQTSRTLTLIAKVIQNLANFSKFTSK 525
Cdd:cd05391   157 LRYIYGCLQKSVQQKWPTNttVRTRVVSGFVFLRLICPAILNPRMFNIISETPSPTAARTLTLVAKSLQNLANLVEFGAK 236

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569000227  526 EDFLGFMNEFLELEWGSMQQFLYEISNLDTLtNSSSFEGYIDLGRELSTLHALLWEVLPQLsKEALLKLGPLPRLL 601
Cdd:cd05391   237 EPYMEGVNPFIKKNKERMIMFLDELGNVPEL-PDTTEHSRTDLSRDLAALHEICVAHSDEL-RTLSNERGALKKLL 310
RasGAP pfam00616
GTPase-activator protein for Ras-like GTPase; All alpha-helical domain that accelerates the ...
 347-518 5.69e-30

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


Pssm-ID: 459871  Cd Length: 207  Bit Score: 118.54  E-value: 5.69e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227   347 FLSDMAMSEVDRFMEREHLiFRENTLATKAIEEYMRL-IGQKYLKDAIGEFIRALYESEE-NCEVDPIK----------- 413
Cdd:pfam00616    1 LISELIEEEIESSDNPNDL-LRGNSLVSKLLETYNRRpRGQEYLKKVLGPLVRKIIEDEDlDLESDPRKiyeslinqeel 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227   414 ---CTASS-----------------LAEHQANLRMCCELALCKVVNSHCVFPREL----KEVFASWRLRCAERGREDIAd 469
Cdd:pfam00616   80 ktgRSDLPrdvspeeaiedpevrqiFEDNLQKLRELADEFLDAIYSSLNQLPYGIryicKQLYELLEEKFPDASEEEIL- 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 569000227   470 RLISASLFLRFLCPAIMSPSLFGLMQEYPDEQTSRTLTLIAKVIQNLAN 518
Cdd:pfam00616  159 NAIGGFLFLRFFCPAIVNPDLFGLVDHQISPKQRRNLTLIAKVLQNLAN 207
RasGAP_RASAL cd05135
Ras-GTPase Activating Domain of RASAL1 and similar proteins; Ras GTPase activating-like ...
 316-554 1.18e-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: 1.18e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227  316 AVLEPALNVKGKEEVASALVHILQSTGKAKDFLSDMAMSEVDRFMEREHLiFRENTLATKAIEEYMRLIGQKYLKDAIGE 395
Cdd:cd05135    29 AMLEEVTTGESRQDVATKLVKIFLGQGLVVPFLDYLNTREVGRTTDPNTL-FRSNSLASKSMEQFMKVVGMPYLHEVLKP 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227  396 FIRALYESEENCEVDPIKCTAS---------SLAEHQ------ANLRMCCELALCKVVNSHCVFPRELKEVFASWRLRCA 460
Cdd:cd05135   108 VINRIFEEKKYVELDPCKIDLNrtrrisfkgSLSEAQvresslELLQGYLGSIIDAIVGSVDQCPPVMRVAFKQLHKRVE 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227  461 ER----GREDIADRLISASLFLRFLCPAIMSPSLFGLMQEYPDEQTSRTLTLIAKVIQNLANFSK--FTSKEDFLGFMNE 534
Cdd:cd05135   188 ERfpeaEHQDVKYLAISGFLFLRFFAPAILTPKLFQLREQHADPRTSRTLLLLAKAVQSIGNLGLqlGQGKEQWMAPLHP 267

                         250       260
                  ....*....|....*....|
gi 569000227  535 FLELEWGSMQQFLYEISNLD 554
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 ...
 327-552 2.20e-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: 2.20e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227  327 KEEVASALVHILQSTGKAKDFLSDMAMSEVDRFMErEHLIFRENTLATKAIEEYMRLIGQKYLKDAIGEFIRALYESEEN 406
Cdd:cd05394    35 KYDAVLPLVRLLLHHNKLVPFVAAVAALDLKDTQE-ANTIFRGNSLATRCLDEMMKIVGKHYLKVTLKPVLDEICESPKP 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227  407 CEVDPIKCTASSLAE-HQANLRMCCELALCKVVNSHCVFPRELKEVFASWRLRCAERGRED--IADRLISASLFLRFLCP 483
Cdd:cd05394   114 CEIDPIKLKEGDNVEnNKENLRYYVDKVFFSIVKSSMSCPTLMCDVFRSLRHLAVKRFPNDphVQYSAVSSFVFLRFFAV 193

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569000227  484 AIMSPSLFGLMQEYPDEQTSRTLTLIAKVIQNLANFSKFTS------KEDFL-GFMNEFLELEW-GSMQQFLYEISN 552
Cdd:cd05394   194 AVVSPHTFQLRPHHPDAQTSRTLTLISKTIQTLGSWGSLSKsklssfKETFMcDFFKMFQEEKYiEKVKKFLDEISS 270
PH_RASAL3 cd13374
RAS protein activator like-3 Pleckstrin homology (PH) domain; RASAL3 is thought to be a Ras ...
 40-158 3.13e-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: 3.13e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227   40 RQILPRFRSADHDRARLMQSFKES--HSHESLLSPSSAAEaLELNLDEDSIIKPVHSSILGQEFCFEVTTSSGTKCFACR 117
Cdd:cd13374    23 RGLLKRLKEKKKAKAESTGTGRDGppSALGSRESLATISE-LDLGAERDVRVWPLHPSLLGEPHCFQVTWPGGSRCFSCR 101

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 569000227  118 SAAERDKWIENLQRAVKPNKDNSRRVDNVLKLWIIEARELP 158
Cdd:cd13374   102 SAAERDRWIEDLRRSFQPHQDNVEREETWLSVWVHEAKGLP 142
RasGAP_Neurofibromin cd05130
Ras-GTPase Activating Domain of neurofibromin; Neurofibromin is the product of the ...
 329-581 5.88e-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: 5.88e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227  329 EVASALVHILQSTGKAKDFLSDMAMSEVDRFMEREHLiFRENTLATKAIEEYMRLIGQKYLKDAIGEFIRALYESEE--N 406
Cdd:cd05130    41 ELARVLVTLFDSKHLLYQLLWNMFSKEVELADSMQTL-FRGNSLASKIMTFCFKVYGATYLQSLLEPLLRTMITSSEwvS 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227  407 CEVDPIKC-TASSLAEHQANLRMCCELALCKVVNSHCVFPRELKEVfaswrLRC-----AERGREDIADRLISAsLFLRF 480
Cdd:cd05130   120 YEVDPTRLeGNENLEENQRNLLQLTEKFFHAIISSSDEFPPQLRSV-----CHClyqvvSHRFPNSGLGAVGSA-IFLRF 193

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227  481 LCPAIMSPSLFGLMQEYPDEQTSRTLTLIAKVIQNLANFSKFTsKEDFLGFMNEFLELEWGSMQQFLYEISNLDTLT--N 558
Cdd:cd05130   194 INPAIVSPYEYGILDREPPPRVKRGLKLMSKILQNIANHVLFT-KEAHMLPFNDFLRNHFEAGRRFFSSIASDCGAVdgP 272

                         250       260
                  ....*....|....*....|...
gi 569000227  559 SSSFEGYIDLGRELStLHALLWE 581
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 ...
 368-601 4.81e-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: 99.35  E-value: 4.81e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227  368 RENTLATKAIEEYMRL-IGQKYLKDAIGEFIRALYESEE-NCEVDPIKC----------------------TASSLAEH- 422
Cdd:cd05132    49 RANTAVSRMMTTYTRRgPGQSYLKTVLADRINDLISLKDlNLEINPLKVyeqmindieldtglpsnlprgiTPEEAAENp 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227  423 ------QANLRMCCELA---LCKVVNSHCVFPRELKEVFASWRLRCAER----GREDIADrLISASLFLRFLCPAIMSPS 489
Cdd:cd05132   129 avqniiEPRLEMLEEITnsfLEAIINSLDEVPYGIRWICKQIRSLTRRKfpdaSDETICS-LIGGFFLLRFINPAIVSPQ 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227  490 LFGLMQEYPDEQTSRTLTLIAKVIQNLANFSKFtSKEDFLGFMNEFLELEWGSMQQFLYEISNLDTLTNSSSFEGYIDLG 569
Cdd:cd05132   208 AYMLVDGKPSDNTRRTLTLIAKLLQNLANKPSY-SKEPYMAPLQPFVEENKERLNKFLNDLCEVDDFYESLELDQYIALS 286

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 569000227  570 R----------ELSTLHALLWEVLPQLSKEALLKLGPLPRLL 601
Cdd:cd05132   287 KkdlsinitlnEIYNTHSLLVKHLAELAPDHNDHLRLILQEL 328
RasGAP_RASA4 cd05395
Ras-GTPase Activating Domain of RASA4; Ras GTPase activating-like 4 protein (RASAL4), also ...
 314-525 2.38e-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: 2.38e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227  314 LCAVLEPALNVKGKEEVASALVHILQSTGKAKDFLSDMAMSEVDRFMEREHLiFRENTLATKAIEEYMRLIGQKYLKDAI 393
Cdd:cd05395    27 LISLIDETTTAECRQEVATNLVKLFLGQGLAKEFLDLLFQLELDKTTEPNTL-FRSNSLASKSMESFLKVAGMQYLHSVL 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227  394 GEFIRALYESEENCEVDPIKC--------------TASSLAEHQAN-LRMCCELALCKVVNSHCVFPRELKEVFASWRLR 458
Cdd:cd05395   106 GPTINRVFEEKKYVELDPSKVeikdvgcsglhriqTESEVIEQSAQlLQSYLGELLSAISKSVKYCPAVIRATFRQLFKR 185

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569000227  459 CAERGREDIADRL----ISASLFLRFLCPAIMSPSLFGLMQEYPDEQTSRTLTLIAKVIQNLANFSKFTSK 525
Cdd:cd05395   186 VQERFPENQHQNVkfiaVTSFLCLRFFSPAIMSPKLFHLREKHADARTSRTLLLLAKAVQNVGNMDTLASR 256
RasGAP_IQGAP_like cd05127
Ras-GTPase Activating Domain of IQ motif containing GTPase activating proteins; This family ...
 355-604 4.79e-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: 4.79e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227  355 EVDRFMEREHLIFRENTLATKAIEEYMR-LIGQKYLKDAIGEFIRALYESEE-NCEVDPIKC------------------ 414
Cdd:cd05127    21 EIESKVSLPEDIVTGNPTVIKLVVNYNRgPRGQKYLRELLGPVVKEILDDDDlDLETDPVDIykawinqeesrtgepskl 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227  415 --------------TASSLAEHQANLRMCCELALCKVVNSHCVFPREL----KEVFASWRLRCAERGREDIAdRLISASL 476
Cdd:cd05127   101 pydvtreqalkdpeVRKRLIEHLEKLRAITDKFLTAITESLDKMPYGMryiaKVLKEALREKFPDAPEEEIL-KIVGNLL 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227  477 FLRFLCPAIMSPSLFGLMQEYPDEQTS----RTLTLIAKVIQNLANFSKFTSKEDFLGFMNEFLELEWGSMQQFLYEIS- 551
Cdd:cd05127   180 YYRYMNPAIVAPEAFDIIDLSVGGQLSplqrRNLGSIAKVLQQAASGKLFGGENPYLSPLNPYISESHEKFKKFFLEACt 259

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569000227  552 --------NLDTLTNSSSFEG---YIDLgRELSTLHALLWEVLPQLS-------KEALLKLGPLPRLLNDI 604
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 ...
 147-247 7.47e-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: 7.47e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227  147 LKLWIIEARELPPKKR-----YYCELCLDDMLYARTTSKPRSAsgdTVFWGEHFEFNNL-PAVRALRLHLYRDSDKKRKK 220
Cdd:cd00030     1 LRVTVIEARNLPAKDLngksdPYVKVSLGGKQKFKTKVVKNTL---NPVWNETFEFPVLdPESDTLTVEVWDKDRFSKDD 77

                          90       100
                  ....*....|....*....|....*...
gi 569000227  221 dkagYVGLVTVPVATLAGR-HFTEQWYP 247
Cdd:cd00030    78 ----FLGEVEIPLSELLDSgKEGELWLP 101
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 1053-1180 9.62e-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: 9.62e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227  1053 IEREEYKLKEYSKSMDESRLDRVKEYEEEIHSLKERLHMSNRKLEEYERRLLSQEEQTSKILMQ---YQARLEQSEKRLR 1129
Cdd:TIGR02169  267 LEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEidkLLAEIEELEREIE 346

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 569000227  1130 QQQVEKDsQIKSIIGRLMLVEEELRRDHPAMAEPLPEPKKRLLDAQVEITM 1180
Cdd:TIGR02169  347 EERKRRD-KLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEK 396
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 80-134 1.19e-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: 1.19e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 569000227     80 ELNLDEDSIIKPVHSSILGQEFCFEVTTSSG-TKCFACRSAAERDKWIENLQRAVK 134
Cdd:smart00233   47 SIDLSGCTVREAPDPDSSKKPHCFEIKTSDRkTLLLQAESEEEREKWVEALRKAIA 102
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 146-245 2.16e-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: 2.16e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227    146 VLKLWIIEARELPPKKRY-----YCELCLDDMLY--ARTTSKPRSASgdtVFWGEHFEFN-NLPAVRALRLHLYrdsdKK 217
Cdd:smart00239    1 TLTVKIISARNLPPKDKGgksdpYVKVSLDGDPKekKKTKVVKNTLN---PVWNETFEFEvPPPELAELEIEVY----DK 73

                            90       100
                    ....*....|....*....|....*...
gi 569000227    218 RKKDKAGYVGLVTVPVATLAGRHFTEQW 245
Cdd:smart00239   74 DRFGRDDFIGQVTIPLSDLLLGGRHEKL 101
C2A_RasGAP cd08383
C2 domain (first repeat) of Ras GTPase activating proteins (GAPs); RasGAPs suppress Ras ...
 147-249 5.75e-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: 5.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227  147 LKLWIIEARELPPKK--RYYCELCLDDMLYARTTSKprsaSGDTVFWGEHFEFNNLPAV---RALRLHLYRDSDKKRKkd 221
Cdd:cd08383     2 LRLRILEAKNLPSKGtrDPYCTVSLDQVEVARTKTV----EKLNPFWGEEFVFDDPPPDvtfFTLSFYNKDKRSKDRD-- 75

                          90       100
                  ....*....|....*....|....*...
gi 569000227  222 kagyVGLVTVPVATLAGRHFTEQWYPVT 249
Cdd:cd08383    76 ----IVIGKVALSKLDLGQGKDEWFPLT 99
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1044-1179 1.37e-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: 49.67  E-value: 1.37e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227  1044 LSADIESAHIEREEY--KLKEYSKSMDESRLdRVKEYEEEIHSLKERLHMSNRKLEEYERRLLSQEE---QTSKILMQYQ 1118
Cdd:TIGR02168  244 LQEELKEAEEELEELtaELQELEEKLEELRL-EVSELEEEIEELQKELYALANEISRLEQQKQILRErlaNLERQLEELE 322

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569000227  1119 ARLEQSEKRLRQQQVEKDsQIKSIIGRLMLVEEELRRDHPAMAEPLPEPKKRLLDAQVEIT 1179
Cdd:TIGR02168  323 AQLEELESKLDELAEELA-ELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLE 382
PRK12704 PRK12704
phosphodiesterase; Provisional
 1045-1155 7.66e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 47.08  E-value: 7.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227 1045 SADIESAHIEREEyKLKEYSKSMDESRLDRVKEYEEEIHSLKERLHMS----NRKLEEYERRLLSQEEQTSK---ILMQY 1117
Cdd:PRK12704   30 EAKIKEAEEEAKR-ILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKElrerRNELQKLEKRLLQKEENLDRkleLLEKR 108

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 569000227 1118 QARLEQSEKRLRQQQVEKDSQIKSIIGRLMLVEEELRR 1155
Cdd:PRK12704  109 EEELEKKEKELEQKQQELEKKEEELEELIEEQLQELER 146
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 1053-1174 8.26e-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: 45.69  E-value: 8.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227 1053 IEREEYKLKEYSKSM--DESRLDRV---KEYE---EEIHSLKERLhmsnRKLEEYERRLLSQEEQTSKILMQYQARLEQS 1124
Cdd:COG1579    61 IKRLELEIEEVEARIkkYEEQLGNVrnnKEYEalqKEIESLKRRI----SDLEDEILELMERIEELEEELAELEAELAEL 136

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 569000227 1125 EKRLRQQQVEKDSQIKSIIGRLmlveEELRRDHPAMAEPLPEpkkRLLDA 1174
Cdd:COG1579   137 EAELEEKKAELDEELAELEAEL----EELEAEREELAAKIPP---ELLAL 179
C2_Ras_p21A1 cd08400
C2 domain present in RAS p21 protein activator 1 (RasA1); RasA1 is a GAP1 (GTPase activating ...
 147-249 8.27e-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: 8.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227  147 LKLWIIEARELPPKK--RYYCELCLDDMLYARTTSKprsaSGDTVFWGEHFEFNNLPA-VRALRLHLYRDSDKKRKKDka 223
Cdd:cd08400     6 LQLNVLEAHKLPVKHvpHPYCVISLNEVKVARTKVR----EGPNPVWSEEFVFDDLPPdVNSFTISLSNKAKRSKDSE-- 79

                          90       100
                  ....*....|....*....|....*.
gi 569000227  224 gyVGLVTVPVATLAGRHFTEQWYPVT 249
Cdd:cd08400    80 --IAEVTVQLSKLQNGQETDEWYPLS 103
C2 pfam00168
C2 domain;
145-248 8.50e-05

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 43.08  E-value: 8.50e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227   145 NVLKLWIIEARELPPKKRY-----YCELCLDDmLYARTTSKPRSASGDTVfWGEHFEFN-NLPAVRALRLHLYRDSDKKR 218
Cdd:pfam00168    1 GRLTVTVIEAKNLPPKDGNgtsdpYVKVYLLD-GKQKKKTKVVKNTLNPV-WNETFTFSvPDPENAVLEIEVYDYDRFGR 78

                           90       100       110
                   ....*....|....*....|....*....|
gi 569000227   219 KKDkagyVGLVTVPVATLAGRHFTEQWYPV 248
Cdd:pfam00168   79 DDF----IGEVRIPLSELDSGEGLDGWYPL 104
IQG1 COG5261
Protein involved in regulation of cellular morphogenesis/cytokinesis [Cell division and ...
 470-604 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 569000227  470 RLISASLFLRFLCPAIMSPSLFGLMQEYPDEqTSRTLTLIAKVIQNLANFSKFTSkedFLGFMNEFLELEWGSMQQFLYE 549
Cdd:COG5261   613 GLIGGFFFLRFVNEALVSPQTSMLKDSCPSD-NVRKLATLSKILQSVFEITSSDK---FDVPLQPFLKEYKEKVHNLLRK 688

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 569000227  550 ISNLDTLTNSSSFEGYIDLGRELSTLHALLWEVLPQLSK-EALLKLGPLPRLLNDI 604
Cdd:COG5261   689 LGNVGDFEEYFEFDQYIDLVKKSRALEYLVNEIYLTHEIiIEYLDNLYDPDSLVDL 744
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 1037-1167 1.65e-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: 1.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227  1037 WVSNMPHLSADIESAHIERE--EYKLKEYSKSMDESRlDRVKEYEEEIHSLKERLHMSNRKLEEYERRLLSQEEQTSKIL 1114
Cdd:TIGR02169  810 IEARLREIEQKLNRLTLEKEylEKEIQELQEQRIDLK-EQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLK 888

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 569000227  1115 MQ---YQARLEQSEKRLRQQQVE---KDSQIKSIIGRLMLVEEELRRDHPAMAEPLPEP 1167
Cdd:TIGR02169  889 KErdeLEAQLRELERKIEELEAQiekKRKRLSELKAKLEALEEELSEIEDPKGEDEEIP 947
RasGAP_IQGAP2 cd05131
Ras-GTPase Activating Domain of IQ motif containing GTPase activating protein 2; IQGAP2 is a ...
 356-612 3.77e-04

Ras-GTPase Activating Domain of IQ motif containing GTPase activating protein 2; IQGAP2 is a member of the IQGAP family that contains a calponin-homology (CH) domain which binds F-actin, IQGAP-specific repeat, a single WW domain, four IQ motifs which mediate interactions with calmodulin, and a Ras-GTPase-activating protein (GAP)-related domain that binds Rho family GTPases. IQGAP2 and IQGAP3 play important roles in the regulation of the cytoskeleton for axon outgrowth in hippocampal neurons and are thought to stay in a common regulatory pathway. The results of RNA interference studies indicated that IQGAP3 partially compensates functions of IQGAP2, but has lesser ability than IQGAP2 to promote axon outgrowth in hippocampal neuron. Moreover, IQGAP2 is required for the cadherin-mediated cell-to-cell adhesion in Xenopus laevis embryos.


Pssm-ID: 213333 [Multi-domain]  Cd Length: 359  Bit Score: 44.22  E-value: 3.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227  356 VDRFMEREHLIfrentLATKAIEEYMRLIGQkyLKDAIGEFIRALYE-SEENCEVDPIkcTASSLAEHQANLRMCCELAL 434
Cdd:cd05131    74 VKEIIEDKSLI-----INTNPVEVYKAWVNQ--LETATGEASKLPYDvTTEQALTHPE--VVNKLESSIQSLRSVTDKVL 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227  435 CKVVNSHCVFPRELKEVFASWRLRCAER---GREDIADRLISASLFLRFLCPAIMSPSLFGLMQ-----EYPDEQTsRTL 506
Cdd:cd05131   145 GSIFSSLDLIPYGMRYIAKVLKNSLHEKfpdATEDELLKIVGNLLYYRYMNPAIVAPDGFDIIDmtaggQIHSEQR-RNL 223

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227  507 TLIAKVIQNLANFSKFTSKEDFLGFMNEFLELEWGSMQQFLYEISNLDTLTNSSSFEGYIDLG-----------RELSTL 575
Cdd:cd05131   224 GSVAKVLQHAASNKLFEGENAHLSSMNSYLSQTYQKFRKFFQAACDVPEPEEKFNIDEYSDMVtlskpviyisiEEIINT 303

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 569000227  576 HALLWE----VLPQ---LSKEALLKLGPLPRLLNDISTALRNPN 612
Cdd:cd05131   304 HSLLLEhqdaIAPDqndLLHELLKDLGEVPDVESFLGEGTVDPN 347
RasGAP_IQGAP1 cd05133
Ras-GTPase Activating Domain of IQ motif containing GTPase activating protein 1; IQGAP1 is a ...
 465-614 6.60e-04

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


Pssm-ID: 213335  Cd Length: 380  Bit Score: 43.49  E-value: 6.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227  465 EDIADRLISASLFLRFLCPAIMSPSLFGLMQEYPDEQTS----RTLTLIAKVIQNLANFSKFTSKEDFLGFMNEFLELEW 540
Cdd:cd05133   178 EDELLKIVGNLLYYRYMNPAIVAPDAFDIIDLSAGGQLTtdqrRNLGSIAKMLQHAASNKMFLGDNAHLSPINEYLSQSY 257

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227  541 GSMQQFLY---------------EISNLDTLTNSSSfegYIDLGRELSTlHALLWE----VLPQLSK---EALLKLGPLP 598
Cdd:cd05133   258 QKFRRFFQaacdvpeledkfnvdEYSDLVTLTKPVI---YISIGEIINT-HTLLLDhqdaIAPEHNDpihELLDDLGEVP 333

                         170
                  ....*....|....*....
gi 569000227  599 ---RLLNDISTALRNPNIQ 614
Cdd:cd05133   334 tieSLIGENPGPPGDPNRE 352
DivIVA COG3599
Cell division septum initiation protein DivIVA, interacts with FtsZ and MinD [Cell cycle ...
 1061-1155 1.00e-03

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: 40.61  E-value: 1.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227 1061 KEYSKSM-----DESR--LDRV-KEYE---EEIHSLKERLHMSNRKLEEYERR-------LLSQEEQTSKILMQYQARLE 1122
Cdd:COG3599    11 KEFKKGFrgydeDEVDefLDEVaEDYErliRENKELKEKLEELEEELEEYRELeetlqktLVVAQETAEEVKENAEKEAE 90

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 569000227 1123 Q--SEKRLRQQQVEKDSQIKSIigRLMLVEEELRR 1155
Cdd:COG3599    91 LiiKEAELEAEKIIEEAQEKAR--KIVREIEELKR 123
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1044-1154 1.52e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.00  E-value: 1.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227 1044 LSADIESAHIEREEY--KLKEYSKSMDESRLdRVKEYEEEIHSLKERLHMSNRKLEEYERRLLSQEEQTSKILMQyQARL 1121
Cdd:COG1196   244 LEAELEELEAELEELeaELAELEAELEELRL-ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER-LEEL 321

                          90       100       110
                  ....*....|....*....|....*....|...
gi 569000227 1122 EQSEKRLRQQQVEKDSQIKSIIGRLMLVEEELR 1154
Cdd:COG1196   322 EEELAELEEELEELEEELEELEEELEEAEEELE 354
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1030-1155 1.59e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.58  E-value: 1.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227 1030 ASERTVAWVSNMPHLSADIESAhieREEYKLKEYSKSMDESRLDRVK----EYEEEIHSLKERLHMSNRKLEEYERRLLS 1105
Cdd:COG4372    29 LSEQLRKALFELDKLQEELEQL---REELEQAREELEQLEEELEQARseleQLEEELEELNEQLQAAQAELAQAQEELES 105

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 569000227 1106 QEEQTSKI---LMQYQA---RLEQSEKRLRQQQVEKDSQIKSIIGRLMLVEEELRR 1155
Cdd:COG4372   106 LQEEAEELqeeLEELQKerqDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLES 161
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1043-1178 1.82e-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: 42.74  E-value: 1.82e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227  1043 HLSADIE--SAHIEREEYKLKEYSKSMDESRlDRVKEYEEEIHSLKERLHMSNRKLEEYERR-----------------L 1103
Cdd:TIGR02168  313 NLERQLEelEAQLEELESKLDELAEELAELE-EKLEELKEELESLEAELEELEAELEELESRleeleeqletlrskvaqL 391

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227  1104 LSQEEQTSKILMQYQARLEQSEKRLRQQQVEKDSQIKSI-----------IGRLMLVEEELRRDHPAMAEPLPEPKKRLL 1172
Cdd:TIGR02168  392 ELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLeeaelkelqaeLEELEEELEELQEELERLEEALEELREELE 471


                   ....*.
gi 569000227  1173 DAQVEI 1178
Cdd:TIGR02168  472 EAEQAL 477
MutS2 COG1193
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
1048-1169 3.34e-03

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


Pssm-ID: 440806 [Multi-domain]  Cd Length: 784  Bit Score: 41.67  E-value: 3.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227 1048 IESA--HIEREEYKLKEYSKSMDESRldrvKEYEEEIHSLKERLHMSNRKLEEYERRLLSQEEQTSKILMQY-------- 1117
Cdd:COG1193   502 IERAreLLGEESIDVEKLIEELERER----RELEEEREEAERLREELEKLREELEEKLEELEEEKEEILEKAreeaeeil 577

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 569000227 1118 ---QARLEQSEKRLRQQQVEKDsQIKSIIGRLMLVEEELRRDHPAMAEPLPEPKK 1169
Cdd:COG1193   578 reaRKEAEELIRELREAQAEEE-ELKEARKKLEELKQELEEKLEKPKKKAKPAKP 631
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 1048-1169 3.52e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 41.74  E-value: 3.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227 1048 IESA--HIEREEYKLKEYSKSMDESRLdRVKEYEEEIHSLK---ERLHMS----NRKLEEYERRLLS-QEEQTSKILMQY 1117
Cdd:PRK00409  504 IEEAkkLIGEDKEKLNELIASLEELER-ELEQKAEEAEALLkeaEKLKEEleekKEKLQEEEDKLLEeAEKEAQQAIKEA 582

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 569000227 1118 QARLEQSEKRLRQQQVEKDSQIKSiigrlMLVEEELRRDHPAmAEPLPEPKK 1169
Cdd:PRK00409  583 KKEADEIIKELRQLQKGGYASVKA-----HELIEARKRLNKA-NEKKEKKKK 628
UDM1_RNF168 cd22265
UDM1 (ubiquitin-dependent DSB recruitment module 1) domain found in RING finger protein 168; ...
 1076-1127 4.63e-03

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


Pssm-ID: 409018 [Multi-domain]  Cd Length: 73  Bit Score: 37.15  E-value: 4.63e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 569000227 1076 KEYEEEIHSLKERLHM----SNRKLEEYERRLLSQEEQTSKILMQYQARLEQSEKR 1127
Cdd:cd22265     9 QEYEEEISKLEAERRAleeeENRASEEYIQKLLAEEEEEEKLAEERRRAEEEQLKE 64
RNase_Y_N pfam12072
RNase Y N-terminal region;
1048-1156 4.93e-03

RNase Y N-terminal region;


Pssm-ID: 463456 [Multi-domain]  Cd Length: 201  Bit Score: 39.87  E-value: 4.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227  1048 IESAHIEREEYKLKEYSKSMDESRLDRVkEYEEEIhslKERlhmsNRKLEEYERRLLSQEEQTSK---ILMQYQARLEQS 1124
Cdd:pfam12072   40 IEEAKKEAETKKKEALLEAKEEIHKLRA-EAEREL---KER----RNELQRQERRLLQKEETLDRkdeSLEKKEESLEKK 111

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 569000227  1125 EKRL--RQQQVE-KDSQIKSIIG-----------------RLML---VEEELRRD 1156
Cdd:pfam12072  112 EKELeaQQQQLEeKEEELEELIEeqrqelerisgltseeaKEILldeVEEELRHE 166
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
1034-1189 6.02e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.77  E-value: 6.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227 1034 TVAWVSNMPHLSADIESAHIEreeyklkEYSKSMDESRLDRVKE----YEEEIHSLKERLHMSNRKLEEYERR--LLSQE 1107
Cdd:COG3206   139 EISYTSPDPELAAAVANALAE-------AYLEQNLELRREEARKalefLEEQLPELRKELEEAEAALEEFRQKngLVDLS 211

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227 1108 EQTSkilmQYQARLEQsekrLRQQQVEKDSQIKSIIGRLMLVEEELRRDHPAMAEPLPEP-----KKRLLDAQVEIT-MS 1181
Cdd:COG3206   212 EEAK----LLLQQLSE----LESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPviqqlRAQLAELEAELAeLS 283


                  ....*...
gi 569000227 1182 FIFSVSHP 1189
Cdd:COG3206   284 ARYTPNHP 291
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
1054-1154 6.65e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.82  E-value: 6.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227 1054 EREEYKLKEYSKSMDESRLDR----VKEYEEEIHSLKERLHMSNRKLEEYERRL--LSQEEQTSKILMQYQARLEQSEKR 1127
Cdd:PRK03918  301 FYEEYLDELREIEKRLSRLEEeingIEERIKELEEKEERLEELKKKLKELEKRLeeLEERHELYEEAKAKKEELERLKKR 380

                          90       100
                  ....*....|....*....|....*...
gi 569000227 1128 LRQQQVEK-DSQIKSIIGRLMLVEEELR 1154
Cdd:PRK03918  381 LTGLTPEKlEKELEELEKAKEEIEEEIS 408
MAT1 pfam06391
CDK-activating kinase assembly factor MAT1; MAT1 is an assembly/targeting factor for ...
 1053-1141 8.19e-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: 39.15  E-value: 8.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227  1053 IEREEYKLKEY---SKSMDESRLDRVKEYEEEIHSLKERLHmsnrklEEYERRLLSQEEQTSKILMQYQARLEQSEKRLR 1129
Cdd:pfam06391   88 LSQEEEELEELlelEKREKEERRKEEKQEEEEEKEKKEKAK------QELIDELMTSNKDAEEIIAQHKKTAKKRKSERR 161

                           90
                   ....*....|..
gi 569000227  1130 QQQVEKDSQIKS 1141
Cdd:pfam06391  162 RKLEELNRVLEQ 173
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1043-1155 9.09e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.31  E-value: 9.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227 1043 HLSADIESAHIEREEYKLKEysksmdESRLDRVKEYEEEIHSLKERLHMSNRKLEEYERRLLSQEEQTSKILMQyQARLE 1122
Cdd:COG1196   313 ELEERLEELEEELAELEEEL------EELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE-LEELA 385

                          90       100       110
                  ....*....|....*....|....*....|...
gi 569000227 1123 QSEKRLRQQQVEKDSQIKSIIGRLMLVEEELRR 1155
Cdd:COG1196   386 EELLEALRAAAELAAQLEELEEAEEALLERLER 418
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
1032-1171 9.73e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.43  E-value: 9.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227 1032 ERTVAWVSNMPHLSADIESAHIEREEYKLKEYSKSMDESRLDRvKEYEEEIHSLKERLHMSNRKLEEYE---------RR 1102
Cdd:PRK03918  365 EEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEI-SKITARIGELKKEIKELKKAIEELKkakgkcpvcGR 443

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569000227 1103 LLSqEEQTSKILMQYQARLEQSEKRLrQQQVEKDSQIKSIIGRL---MLVEEELRRDHpAMAEPLPEPKKRL 1171
Cdd:PRK03918  444 ELT-EEHRKELLEEYTAELKRIEKEL-KEIEEKERKLRKELRELekvLKKESELIKLK-ELAEQLKELEEKL 512
ARGLU pfam15346
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ...
 1048-1132 9.91e-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: 38.11  E-value: 9.91e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000227  1048 IESAHIEREEYKLKEYSKSMdESRLDRVKEYEEEIHSLKERL----HMSNRKLEEYERRL----LSQEEQTSKILMQYQA 1119
Cdd:pfam15346   43 VEEARKIMEKQVLEELERER-EAELEEERRKEEEERKKREELerilEENNRKIEEAQRKEaeerLAMLEEQRRMKEERQR 121

                           90
                   ....*....|...
gi 569000227  1120 RLEQSEKRLRQQQ 1132
Cdd:pfam15346  122 REKEEEEREKREQ 134
 
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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