NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1823433676|ref|XP_032940023|]
View 

ras/Rap GTPase-activating protein SynGAP isoform X2 [Catharus ustulatus]

Protein Classification

PH_SynGAP and RasGAP_DAB2IP domain-containing protein( domain architecture ID 11598901)

protein containing domains PH_SynGAP, C2_SynGAP_like, RasGAP_DAB2IP, and DUF3498

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 369-692 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: 638.09  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  369 RFQTMSILPMELYKEFAEYVTNNYRMLCAVLEPVLSVKSKEEVACALVHILQSTGKAKDFLSDMAMTEVDRFmDREHLIF 448
Cdd:cd05136      1 RYQSVDILPLEVYKEFLEYLTNNYLDLCEVLEPVLSVKAKEELATALVHILQSTGKAKEFLTDLVMAEVDRL-DDEHLIF 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  449 RENTLATKAIEEYLKLIGQKYLKDAIGEFIRALYESEENCEVDPMKCSAS-TLADHQANLRMCCELALCKVVNSHCVFPR 527
Cdd:cd05136     80 RGNTLATKAMEAYLKLVGQKYLQETLGEFIRALYESEEDCEVDPSKCPPSaSLSRNQANLRRSVELAWCKILSSHCVFPR 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  528 ELKEVFASWRLRCAERGREDIADRLISASLFLRFLCPAVMSPSLFGLMQEYPDEQTARTLTLIAKVIQNLANFTKFGSKE 607
Cdd:cd05136    160 ELREVFSSWRERLEERGREDIADRLISASLFLRFLCPAILSPSLFNLTQEYPSERAARNLTLIAKVIQNLANFTRFGGKE 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  608 EYMAFMNEFLELEWASMQQFLYEISNLDTLTNSTSFEGYIDLGRELSTLHALLWEVMSQLSKEALLKLGPLPRLLTDISV 687
Cdd:cd05136    240 EYMEFMNDFVEQEWPNMKQFLQEISSPSPSSNSSDFDGYIDLGRELSLLHSLLVEIISKLNQTTLDKLGPLPRILNDITE 319


                   ....*
gi 1823433676  688 ALRNP 692
Cdd:cd05136    320 ALRNP 324
PH_SynGAP cd13375
Synaptic Ras-GTPase activating protein Pleckstrin homology (PH) domain; SynGAP is a member of ...
 109-297 1.63e-135

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: 411.01  E-value: 1.63e-135
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  109 PAPPFRPSQGFLSRRLKSSIKRTKSQPKLDRTSSFRQILPRFRSADHDRARLMQSFKESHSHESLLSPSSAAEALELNLD 188
Cdd:cd13375      1 PTAPFRPSQGFLSRRLKSSIKRTKSQPKLDRTSSFRQILPRFRSADHDRARLMQSFKESHSHESLLSPSSAAEALDLNLD 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  189 EDSIIKAVHSSILGQEFCFEVTTASGTKCFACRSAAERDKWIENLQRAVKPNKDNSRRVDNVLKLWVIEARDLPPKKRYY 268
Cdd:cd13375     81 EDSIIKPVHSSILGQEFCFEVTTASGTKCFACRSAAERDKWIENLQRAVKPNKDNSRRVDNVLKLWIIEARELPPKKRYY 160

                          170       180
                   ....*....|....*....|....*....
gi 1823433676  269 CELCLDDMLYARTTSKARTDNVFWGEHFE 297
Cdd:cd13375    161 CELCLDDMLYARTTSKPRTDTVFWGEHFE 189
DUF3498 super family cl26404
Domain of unknown function (DUF3498); This presumed domain is functionally uncharacterized. ...
 682-1165 1.35e-123

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.


The actual alignment was detected with superfamily member pfam12004:

Pssm-ID: 463427 [Multi-domain]  Cd Length: 511  Bit Score: 392.20  E-value: 1.35e-123
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  682 LTDISVALRNPH-LQRQPS-QGERLPPKGLVLRGPSADLQpYLVRDLNSSVdlqsymvrglnssMDVPRLPSPPQEKGpp 759
Cdd:pfam12004    1 LRDITTALTNPTpIQQQLRrFSEHSSSPPVPGRSISSGLQ-KMFEDPDDGL-------------SDFTRLPSPTPENK-- 64

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  760 EVLVLSRPPLARSSPAYCTSSSDLTEPEGGRGGALgvgKSVSMLDLQDGRVDSIPSLPA--ELLAGGPAPGGAGQGGLRP 837
Cdd:pfam12004   65 DLFFVTRPPLLQPSPARSSSYSDANEPDQQLPNGN---KSLSMVDLQDSRSLQGSPSPPlhDAPLNLSQAGSQASVGLRP 141

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  838 ---GRLSQGSASSLA----PPRLGV-PEPGGPQLRVPLSFQNPLFHLAADGPLRGPDGGGGGGGRGEggggdgghfggva 909
Cdd:pfam12004  142 awaARTSQGNPQSAPqvrrPLQTPVtQGTRPQQLLAPLSFQNPVYHMAAGLPVSPRGLGSPDSSSET------------- 208

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  910 PPPLHGYSKSEEL--ATPPQKHITHSHSYSDEFGRPGGDFGRRQLSLQDT----LAPPQITIG---------APPPPTPR 974
Cdd:pfam12004  209 HSSFSSHSNSEDLssAAANKKSGPSNSSYSEDFARRSTEFTRRQLSLTELqhqpAVPRQNSAGpqrridqqgLGGPPLTR 288

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  975 GSRagkgggGPSALGVPQKPRPASGNLlASPEPAYGPPRSRQPSLAKEASVAGMKPPVTKQASQTP---STLNPVlpasE 1051
Cdd:pfam12004  289 GRT------PPSLLNSASYPRPSSGSL-MSSSPDWPPARLRQQSSSSKGDSPETKQRTQHQQVPSPvnpSTLSPV----E 357

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676 1052 RTVAWVSNMPHLSADIESSHIE-REEYKLKEysksmdesrldrvkEYEEEIHSLKERLHMSNRKLEEYERRLVTQEEQTS 1130
Cdd:pfam12004  358 RTAAWVLNMNGQYEEEESSGPEsREELKQAE--------------KYEQEISKLKERLRVSNRKLEEYERRLLAQEEQTQ 423

                          490       500       510
                   ....*....|....*....|....*....|....*
gi 1823433676 1131 RILLQYQQRLELSEKRLRQQQQEKDSQIKSIIGSL 1165
Cdd:pfam12004  424 KLLLEYQARLEDSEERLRRQQEEKDSQMKSIISRL 458
C2_SynGAP_like cd04013
C2 domain present in Ras GTPase activating protein (GAP) family; SynGAP, GAP1, RasGAP, and ...
 239-378 1.88e-74

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: 243.37  E-value: 1.88e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  239 PNKDNSRRVDNVLKLWVIEARDLPPKKRYYCELCLDDMLYARTTSKARTDNVFWGEHFEFNNLPAVRTIRLHLYKDTDKK 318
Cdd:cd04013      1 PNRDNSRRTENSLKLWIIEAKGLPPKKRYYCELCLDKTLYARTTSKLKTDTLFWGEHFEFSNLPPVSVITVNLYRESDKK 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1823433676  319 RKKDKSNYVGMVSIPIASVTGRHFAEQWYPLSQPSGSKS------KAGCPALRVKSRFQTMSILPM 378
Cdd:cd04013     81 KKKDKSQLIGTVNIPVTDVSSRQFVEKWYPVSTPKGNGKsggkegKGESPSIRIKARYQSTRVLPL 146
 
Name Accession Description Interval E-value
RasGAP_DAB2IP cd05136
Ras-GTPase Activating Domain of DAB2IP and similar proteins; The DAB2IP family of Ras ...
 369-692 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: 638.09  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  369 RFQTMSILPMELYKEFAEYVTNNYRMLCAVLEPVLSVKSKEEVACALVHILQSTGKAKDFLSDMAMTEVDRFmDREHLIF 448
Cdd:cd05136      1 RYQSVDILPLEVYKEFLEYLTNNYLDLCEVLEPVLSVKAKEELATALVHILQSTGKAKEFLTDLVMAEVDRL-DDEHLIF 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  449 RENTLATKAIEEYLKLIGQKYLKDAIGEFIRALYESEENCEVDPMKCSAS-TLADHQANLRMCCELALCKVVNSHCVFPR 527
Cdd:cd05136     80 RGNTLATKAMEAYLKLVGQKYLQETLGEFIRALYESEEDCEVDPSKCPPSaSLSRNQANLRRSVELAWCKILSSHCVFPR 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  528 ELKEVFASWRLRCAERGREDIADRLISASLFLRFLCPAVMSPSLFGLMQEYPDEQTARTLTLIAKVIQNLANFTKFGSKE 607
Cdd:cd05136    160 ELREVFSSWRERLEERGREDIADRLISASLFLRFLCPAILSPSLFNLTQEYPSERAARNLTLIAKVIQNLANFTRFGGKE 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  608 EYMAFMNEFLELEWASMQQFLYEISNLDTLTNSTSFEGYIDLGRELSTLHALLWEVMSQLSKEALLKLGPLPRLLTDISV 687
Cdd:cd05136    240 EYMEFMNDFVEQEWPNMKQFLQEISSPSPSSNSSDFDGYIDLGRELSLLHSLLVEIISKLNQTTLDKLGPLPRILNDITE 319


                   ....*
gi 1823433676  688 ALRNP 692
Cdd:cd05136    320 ALRNP 324
PH_SynGAP cd13375
Synaptic Ras-GTPase activating protein Pleckstrin homology (PH) domain; SynGAP is a member of ...
 109-297 1.63e-135

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: 411.01  E-value: 1.63e-135
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  109 PAPPFRPSQGFLSRRLKSSIKRTKSQPKLDRTSSFRQILPRFRSADHDRARLMQSFKESHSHESLLSPSSAAEALELNLD 188
Cdd:cd13375      1 PTAPFRPSQGFLSRRLKSSIKRTKSQPKLDRTSSFRQILPRFRSADHDRARLMQSFKESHSHESLLSPSSAAEALDLNLD 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  189 EDSIIKAVHSSILGQEFCFEVTTASGTKCFACRSAAERDKWIENLQRAVKPNKDNSRRVDNVLKLWVIEARDLPPKKRYY 268
Cdd:cd13375     81 EDSIIKPVHSSILGQEFCFEVTTASGTKCFACRSAAERDKWIENLQRAVKPNKDNSRRVDNVLKLWIIEARELPPKKRYY 160

                          170       180
                   ....*....|....*....|....*....
gi 1823433676  269 CELCLDDMLYARTTSKARTDNVFWGEHFE 297
Cdd:cd13375    161 CELCLDDMLYARTTSKPRTDTVFWGEHFE 189
DUF3498 pfam12004
Domain of unknown function (DUF3498); This presumed domain is functionally uncharacterized. ...
 682-1165 1.35e-123

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: 392.20  E-value: 1.35e-123
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  682 LTDISVALRNPH-LQRQPS-QGERLPPKGLVLRGPSADLQpYLVRDLNSSVdlqsymvrglnssMDVPRLPSPPQEKGpp 759
Cdd:pfam12004    1 LRDITTALTNPTpIQQQLRrFSEHSSSPPVPGRSISSGLQ-KMFEDPDDGL-------------SDFTRLPSPTPENK-- 64

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  760 EVLVLSRPPLARSSPAYCTSSSDLTEPEGGRGGALgvgKSVSMLDLQDGRVDSIPSLPA--ELLAGGPAPGGAGQGGLRP 837
Cdd:pfam12004   65 DLFFVTRPPLLQPSPARSSSYSDANEPDQQLPNGN---KSLSMVDLQDSRSLQGSPSPPlhDAPLNLSQAGSQASVGLRP 141

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  838 ---GRLSQGSASSLA----PPRLGV-PEPGGPQLRVPLSFQNPLFHLAADGPLRGPDGGGGGGGRGEggggdgghfggva 909
Cdd:pfam12004  142 awaARTSQGNPQSAPqvrrPLQTPVtQGTRPQQLLAPLSFQNPVYHMAAGLPVSPRGLGSPDSSSET------------- 208

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  910 PPPLHGYSKSEEL--ATPPQKHITHSHSYSDEFGRPGGDFGRRQLSLQDT----LAPPQITIG---------APPPPTPR 974
Cdd:pfam12004  209 HSSFSSHSNSEDLssAAANKKSGPSNSSYSEDFARRSTEFTRRQLSLTELqhqpAVPRQNSAGpqrridqqgLGGPPLTR 288

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  975 GSRagkgggGPSALGVPQKPRPASGNLlASPEPAYGPPRSRQPSLAKEASVAGMKPPVTKQASQTP---STLNPVlpasE 1051
Cdd:pfam12004  289 GRT------PPSLLNSASYPRPSSGSL-MSSSPDWPPARLRQQSSSSKGDSPETKQRTQHQQVPSPvnpSTLSPV----E 357

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676 1052 RTVAWVSNMPHLSADIESSHIE-REEYKLKEysksmdesrldrvkEYEEEIHSLKERLHMSNRKLEEYERRLVTQEEQTS 1130
Cdd:pfam12004  358 RTAAWVLNMNGQYEEEESSGPEsREELKQAE--------------KYEQEISKLKERLRVSNRKLEEYERRLLAQEEQTQ 423

                          490       500       510
                   ....*....|....*....|....*....|....*
gi 1823433676 1131 RILLQYQQRLELSEKRLRQQQQEKDSQIKSIIGSL 1165
Cdd:pfam12004  424 KLLLEYQARLEDSEERLRRQQEEKDSQMKSIISRL 458
RasGAP smart00323
GTPase-activator protein for Ras-like GTPases; All alpha-helical domain that accelerates the ...
 362-684 7.98e-108

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: 343.14  E-value: 7.98e-108
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676   362 PALRVKSRFQTMSILPMELYKEFAEYVTNNY-RMLCAVLEPVLSVKSKEEVACALVHILQSTGKAKDFLSDMAMTEVDRf 440
Cdd:smart00323    7 GSLRLKTVYTTDFILPSEYYEELLELLLFSLdLSLASALSEVCSGLDKDELATKLVRLFLRRGRGHPFLRALIDPEVER- 85

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676   441 MDREHLIFRENTLATKAIEEYLKLIGQKYLKDAIGEFIRALYESEENCEVDPMKCSASTLADHQANLRMCCELALCKVVN 520
Cdd:smart00323   86 TDDPNTIFRGNSLATKSMEVYMKLVGNQYLHTTLKPVLKKIVESKKSCEVDPAKLEGEDLETNLENLLQYVERLFDAIIN 165

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676   521 SHCVFPRELKEVFASWRLRCAERGRE-DIADRLISASLFLRFLCPAVMSPSLFGLMQEYPDEQTARTLTLIAKVIQNLAN 599
Cdd:smart00323  166 SSDRLPYGLRDICKQLRQAAEKRFPDaDVIYKAVSSFVFLRFFCPAIVSPKLFNLVDEHPDPTTRRTLTLIAKVLQNLAN 245

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676   600 FTKFGSKEEYMAFMNEFLELEWASMQQFLYEISNLDTLTNSTSFEGYIDLGRELSTLHALLWEVMSQLSKEaLLKLGPLP 679
Cdd:smart00323  246 LSEFGSKEPWMEPLNDFLLSHKDRVKDFLDELSSVPEILVDKVSDSTTISGRELSLLHSLLLENGDALKRE-LNNEDPLG 324


                    ....*
gi 1823433676   680 RLLTD 684
Cdd:smart00323  325 KLLFK 329
C2_SynGAP_like cd04013
C2 domain present in Ras GTPase activating protein (GAP) family; SynGAP, GAP1, RasGAP, and ...
 239-378 1.88e-74

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: 243.37  E-value: 1.88e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  239 PNKDNSRRVDNVLKLWVIEARDLPPKKRYYCELCLDDMLYARTTSKARTDNVFWGEHFEFNNLPAVRTIRLHLYKDTDKK 318
Cdd:cd04013      1 PNRDNSRRTENSLKLWIIEAKGLPPKKRYYCELCLDKTLYARTTSKLKTDTLFWGEHFEFSNLPPVSVITVNLYRESDKK 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1823433676  319 RKKDKSNYVGMVSIPIASVTGRHFAEQWYPLSQPSGSKS------KAGCPALRVKSRFQTMSILPM 378
Cdd:cd04013     81 KKKDKSQLIGTVNIPVTDVSSRQFVEKWYPVSTPKGNGKsggkegKGESPSIRIKARYQSTRVLPL 146
RasGAP pfam00616
GTPase-activator protein for Ras-like GTPase; All alpha-helical domain that accelerates the ...
 428-599 1.74e-31

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: 122.78  E-value: 1.74e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  428 FLSDMAMTEVDRFMDREHLiFRENTLATKAIEEYLKL-IGQKYLKDAIGEFIRALYESEE-NCEVDPMKCSAS------- 498
Cdd:pfam00616    1 LISELIEEEIESSDNPNDL-LRGNSLVSKLLETYNRRpRGQEYLKKVLGPLVRKIIEDEDlDLESDPRKIYESlinqeel 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  499 ------------------------TLADHQANLRMCCELALCKVVNSHCVFPREL----KEVFASWRLRCAERGREDIAd 550
Cdd:pfam00616   80 ktgrsdlprdvspeeaiedpevrqIFEDNLQKLRELADEFLDAIYSSLNQLPYGIryicKQLYELLEEKFPDASEEEIL- 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1823433676  551 RLISASLFLRFLCPAVMSPSLFGLMQEYPDEQTARTLTLIAKVIQNLAN 599
Cdd:pfam00616  159 NAIGGFLFLRFFCPAIVNPDLFGLVDHQISPKQRRNLTLIAKVLQNLAN 207
C2 pfam00168
C2 domain;
249-349 1.82e-09

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 56.17  E-value: 1.82e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  249 NVLKLWVIEARDLPPKKRY-----YCELCL-DDMLYARTTSKARTDNVFWGEHFEFN-NLPAVRTIRLHLYKDTDKKRkk 321
Cdd:pfam00168    1 GRLTVTVIEAKNLPPKDGNgtsdpYVKVYLlDGKQKKKTKVVKNTLNPVWNETFTFSvPDPENAVLEIEVYDYDRFGR-- 78

                           90       100
                   ....*....|....*....|....*...
gi 1823433676  322 dkSNYVGMVSIPIASVTGRHFAEQWYPL 349
Cdd:pfam00168   79 --DDFIGEVRIPLSELDSGEGLDGWYPL 104
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 250-346 7.68e-09

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: 54.42  E-value: 7.68e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676   250 VLKLWVIEARDLPPKKRY-----YCELCLDDMLY--ARTTSKARTDNVFWGEHFEFN-NLPAVRTIRLHLYkdtdKKRKK 321
Cdd:smart00239    1 TLTVKIISARNLPPKDKGgksdpYVKVSLDGDPKekKKTKVVKNTLNPVWNETFEFEvPPPELAELEIEVY----DKDRF 76

                            90       100
                    ....*....|....*....|....*
gi 1823433676   322 DKSNYVGMVSIPIASVTGRHFAEQW 346
Cdd:smart00239   77 GRDDFIGQVTIPLSDLLLGGRHEKL 101
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 184-238 1.38e-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: 47.93  E-value: 1.38e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 1823433676   184 ELNLDEDSIIKAVHSSILGQEFCFEVTTASG-TKCFACRSAAERDKWIENLQRAVK 238
Cdd:smart00233   47 SIDLSGCTVREAPDPDSSKKPHCFEIKTSDRkTLLLQAESEEEREKWVEALRKAIA 102
PRK12704 PRK12704
phosphodiesterase; Provisional
 1079-1161 1.75e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 45.54  E-value: 1.75e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676 1079 LKEYSKSMDESRLDRVKEYEEEIHSLKERLHMS----NRKLEEYERRLVTQEEQTSR---ILLQYQQRLELSEKRLRQQQ 1151
Cdd:PRK12704    44 LEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKElrerRNELQKLEKRLLQKEENLDRkleLLEKREEELEKKEKELEQKQ 123

                           90
                   ....*....|
gi 1823433676 1152 QEKDSQIKSI 1161
Cdd:PRK12704   124 QELEKKEEEL 133
DivIVA COG3599
Cell division septum initiation protein DivIVA, interacts with FtsZ and MinD [Cell cycle ...
 1080-1159 2.97e-04

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


Pssm-ID: 442818 [Multi-domain]  Cd Length: 125  Bit Score: 41.76  E-value: 2.97e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676 1080 KEYSKSM-----DESR--LDRV-KEYE---EEIHSLKERLHMSNRKLEEYERRlvtqEEQTSRILLQYQqrlELSEKRLR 1148
Cdd:COG3599     11 KEFKKGFrgydeDEVDefLDEVaEDYErliRENKELKEKLEELEEELEEYREL----EETLQKTLVVAQ---ETAEEVKE 83

                           90
                   ....*....|.
gi 1823433676 1149 QQQQEKDSQIK 1159
Cdd:COG3599     84 NAEKEAELIIK 94
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 1056-1157 4.51e-03

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: 41.59  E-value: 4.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676 1056 WVSNMPHLSADIESSHIERE--EYKLKEYSKSMDESRlDRVKEYEEEIHSLKERLHMSNRKLEEYERRLVTQEEQTSRIl 1133
Cdd:TIGR02169  810 IEARLREIEQKLNRLTLEKEylEKEIQELQEQRIDLK-EQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDL- 887

                           90       100
                   ....*....|....*....|....
gi 1823433676 1134 lqYQQRLELsEKRLRQQQQEKDSQ 1157
Cdd:TIGR02169  888 --KKERDEL-EAQLRELERKIEEL 908
IQG1 COG5261
Protein involved in regulation of cellular morphogenesis/cytokinesis [Cell division and ...
 551-651 5.69e-03

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: 41.02  E-value: 5.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  551 RLISASLFLRFLCPAVMSPSLFGLMQEYPDEQTaRTLTLIAKVIQNLANFTKFGSkeeYMAFMNEFLELEWASMQQFLYE 630
Cdd:COG5261    613 GLIGGFFFLRFVNEALVSPQTSMLKDSCPSDNV-RKLATLSKILQSVFEITSSDK---FDVPLQPFLKEYKEKVHNLLRK 688

                           90       100
                   ....*....|....*....|.
gi 1823433676  631 ISNLDTLTNSTSFEGYIDLGR 651
Cdd:COG5261    689 LGNVGDFEEYFEFDQYIDLVK 709
 
Name Accession Description Interval E-value
RasGAP_DAB2IP cd05136
Ras-GTPase Activating Domain of DAB2IP and similar proteins; The DAB2IP family of Ras ...
 369-692 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: 638.09  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  369 RFQTMSILPMELYKEFAEYVTNNYRMLCAVLEPVLSVKSKEEVACALVHILQSTGKAKDFLSDMAMTEVDRFmDREHLIF 448
Cdd:cd05136      1 RYQSVDILPLEVYKEFLEYLTNNYLDLCEVLEPVLSVKAKEELATALVHILQSTGKAKEFLTDLVMAEVDRL-DDEHLIF 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  449 RENTLATKAIEEYLKLIGQKYLKDAIGEFIRALYESEENCEVDPMKCSAS-TLADHQANLRMCCELALCKVVNSHCVFPR 527
Cdd:cd05136     80 RGNTLATKAMEAYLKLVGQKYLQETLGEFIRALYESEEDCEVDPSKCPPSaSLSRNQANLRRSVELAWCKILSSHCVFPR 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  528 ELKEVFASWRLRCAERGREDIADRLISASLFLRFLCPAVMSPSLFGLMQEYPDEQTARTLTLIAKVIQNLANFTKFGSKE 607
Cdd:cd05136    160 ELREVFSSWRERLEERGREDIADRLISASLFLRFLCPAILSPSLFNLTQEYPSERAARNLTLIAKVIQNLANFTRFGGKE 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  608 EYMAFMNEFLELEWASMQQFLYEISNLDTLTNSTSFEGYIDLGRELSTLHALLWEVMSQLSKEALLKLGPLPRLLTDISV 687
Cdd:cd05136    240 EYMEFMNDFVEQEWPNMKQFLQEISSPSPSSNSSDFDGYIDLGRELSLLHSLLVEIISKLNQTTLDKLGPLPRILNDITE 319


                   ....*
gi 1823433676  688 ALRNP 692
Cdd:cd05136    320 ALRNP 324
PH_SynGAP cd13375
Synaptic Ras-GTPase activating protein Pleckstrin homology (PH) domain; SynGAP is a member of ...
 109-297 1.63e-135

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: 411.01  E-value: 1.63e-135
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  109 PAPPFRPSQGFLSRRLKSSIKRTKSQPKLDRTSSFRQILPRFRSADHDRARLMQSFKESHSHESLLSPSSAAEALELNLD 188
Cdd:cd13375      1 PTAPFRPSQGFLSRRLKSSIKRTKSQPKLDRTSSFRQILPRFRSADHDRARLMQSFKESHSHESLLSPSSAAEALDLNLD 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  189 EDSIIKAVHSSILGQEFCFEVTTASGTKCFACRSAAERDKWIENLQRAVKPNKDNSRRVDNVLKLWVIEARDLPPKKRYY 268
Cdd:cd13375     81 EDSIIKPVHSSILGQEFCFEVTTASGTKCFACRSAAERDKWIENLQRAVKPNKDNSRRVDNVLKLWIIEARELPPKKRYY 160

                          170       180
                   ....*....|....*....|....*....
gi 1823433676  269 CELCLDDMLYARTTSKARTDNVFWGEHFE 297
Cdd:cd13375    161 CELCLDDMLYARTTSKPRTDTVFWGEHFE 189
DUF3498 pfam12004
Domain of unknown function (DUF3498); This presumed domain is functionally uncharacterized. ...
 682-1165 1.35e-123

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: 392.20  E-value: 1.35e-123
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  682 LTDISVALRNPH-LQRQPS-QGERLPPKGLVLRGPSADLQpYLVRDLNSSVdlqsymvrglnssMDVPRLPSPPQEKGpp 759
Cdd:pfam12004    1 LRDITTALTNPTpIQQQLRrFSEHSSSPPVPGRSISSGLQ-KMFEDPDDGL-------------SDFTRLPSPTPENK-- 64

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  760 EVLVLSRPPLARSSPAYCTSSSDLTEPEGGRGGALgvgKSVSMLDLQDGRVDSIPSLPA--ELLAGGPAPGGAGQGGLRP 837
Cdd:pfam12004   65 DLFFVTRPPLLQPSPARSSSYSDANEPDQQLPNGN---KSLSMVDLQDSRSLQGSPSPPlhDAPLNLSQAGSQASVGLRP 141

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  838 ---GRLSQGSASSLA----PPRLGV-PEPGGPQLRVPLSFQNPLFHLAADGPLRGPDGGGGGGGRGEggggdgghfggva 909
Cdd:pfam12004  142 awaARTSQGNPQSAPqvrrPLQTPVtQGTRPQQLLAPLSFQNPVYHMAAGLPVSPRGLGSPDSSSET------------- 208

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  910 PPPLHGYSKSEEL--ATPPQKHITHSHSYSDEFGRPGGDFGRRQLSLQDT----LAPPQITIG---------APPPPTPR 974
Cdd:pfam12004  209 HSSFSSHSNSEDLssAAANKKSGPSNSSYSEDFARRSTEFTRRQLSLTELqhqpAVPRQNSAGpqrridqqgLGGPPLTR 288

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  975 GSRagkgggGPSALGVPQKPRPASGNLlASPEPAYGPPRSRQPSLAKEASVAGMKPPVTKQASQTP---STLNPVlpasE 1051
Cdd:pfam12004  289 GRT------PPSLLNSASYPRPSSGSL-MSSSPDWPPARLRQQSSSSKGDSPETKQRTQHQQVPSPvnpSTLSPV----E 357

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676 1052 RTVAWVSNMPHLSADIESSHIE-REEYKLKEysksmdesrldrvkEYEEEIHSLKERLHMSNRKLEEYERRLVTQEEQTS 1130
Cdd:pfam12004  358 RTAAWVLNMNGQYEEEESSGPEsREELKQAE--------------KYEQEISKLKERLRVSNRKLEEYERRLLAQEEQTQ 423

                          490       500       510
                   ....*....|....*....|....*....|....*
gi 1823433676 1131 RILLQYQQRLELSEKRLRQQQQEKDSQIKSIIGSL 1165
Cdd:pfam12004  424 KLLLEYQARLEDSEERLRRQQEEKDSQMKSIISRL 458
RasGAP smart00323
GTPase-activator protein for Ras-like GTPases; All alpha-helical domain that accelerates the ...
 362-684 7.98e-108

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: 343.14  E-value: 7.98e-108
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676   362 PALRVKSRFQTMSILPMELYKEFAEYVTNNY-RMLCAVLEPVLSVKSKEEVACALVHILQSTGKAKDFLSDMAMTEVDRf 440
Cdd:smart00323    7 GSLRLKTVYTTDFILPSEYYEELLELLLFSLdLSLASALSEVCSGLDKDELATKLVRLFLRRGRGHPFLRALIDPEVER- 85

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676   441 MDREHLIFRENTLATKAIEEYLKLIGQKYLKDAIGEFIRALYESEENCEVDPMKCSASTLADHQANLRMCCELALCKVVN 520
Cdd:smart00323   86 TDDPNTIFRGNSLATKSMEVYMKLVGNQYLHTTLKPVLKKIVESKKSCEVDPAKLEGEDLETNLENLLQYVERLFDAIIN 165

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676   521 SHCVFPRELKEVFASWRLRCAERGRE-DIADRLISASLFLRFLCPAVMSPSLFGLMQEYPDEQTARTLTLIAKVIQNLAN 599
Cdd:smart00323  166 SSDRLPYGLRDICKQLRQAAEKRFPDaDVIYKAVSSFVFLRFFCPAIVSPKLFNLVDEHPDPTTRRTLTLIAKVLQNLAN 245

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676   600 FTKFGSKEEYMAFMNEFLELEWASMQQFLYEISNLDTLTNSTSFEGYIDLGRELSTLHALLWEVMSQLSKEaLLKLGPLP 679
Cdd:smart00323  246 LSEFGSKEPWMEPLNDFLLSHKDRVKDFLDELSSVPEILVDKVSDSTTISGRELSLLHSLLLENGDALKRE-LNNEDPLG 324


                    ....*
gi 1823433676   680 RLLTD 684
Cdd:smart00323  325 KLLFK 329
PH_DAB2IP cd13376
DOC-2/Disabled homolog 2-interacting protein Pleckstrin homology (PH) domain; DAB2IP (also ...
 118-297 1.92e-90

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: 289.30  E-value: 1.92e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  118 GFLSRRLKSSIKRTKSQPKLDRTSSFRQILPRFRSADHDRARLMQSFKESHSHESLLSPSSAAEALELNLDEDSIIKAVH 197
Cdd:cd13376      3 GFLSRRLKGSIKRTKSQPKLDRNSSFRHILPGFRSVDNERSHLMPRLKESRSHESLLSPSSAVEALDLSMEEEVVIKPVH 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  198 SSILGQEFCFEVTTASGTKCFACRSAAERDKWIENLQRAVKPNKDNSRRVDNVLKLWVIEARDLPPKKRYYCELCLDDML 277
Cdd:cd13376     83 SSILGQDYCFEVTTSSGSKCFSCRSAAERDKWMENLRRAVHPNKDNSRRVENMLKLWIIEAKDLPAKKKYLCELCLDDVL 162

                          170       180
                   ....*....|....*....|
gi 1823433676  278 YARTTSKARTDNVFWGEHFE 297
Cdd:cd13376    163 YARTTCKLKTDNVFWGEHFE 182
RasGAP cd04519
Ras GTPase Activating Domain; RasGAP functions as an enhancer of the hydrolysis of GTP that is ...
 379-633 4.31e-78

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: 258.19  E-value: 4.31e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  379 ELYKEFAEYVTNNYRMLCAVLEPVLSVKSKEEVACALVHILQSTGKAKDFLSDMAMTEVDRFMDrEHLIFRENTLATKAI 458
Cdd:cd04519      1 EEYRLLSLLLTESPLALLRELSQVLPVKDKEEVATALLRIFESRGLALEFLRYLVRSEVKNTKN-PNTLFRGNSLATKLL 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  459 EEYLKLIGQKYLKDAIGEFIRALYESEENCEVDPMKCSASTLADHQANLRMCCELALCKVVNSHCVFPRELKEVFASWRL 538
Cdd:cd04519     80 DQYMKLVGQEYLKETLSPLIREILESKESCEIDTKLPVGEDLEENLENLLELVNKLVDRILSSLDRLPPELRYVFKILRE 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  539 RCAERGRED--IADRLISASLFLRFLCPAVMSPSLFGLMQEYPDEQTARTLTLIAKVIQNLANFTKFGSKEEYMAFMNEF 616
Cdd:cd04519    160 FLAERFPEEpdEAYQAVSGFLFLRFICPAIVSPELFGLVPDEPSEQARRNLTLISKVLQSLANGVEFGDKEPFMKPLNDF 239

                          250
                   ....*....|....*..
gi 1823433676  617 LELEWASMQQFLYEISN 633
Cdd:cd04519    240 IKSNKPKLKQFLDELSS 256
C2_SynGAP_like cd04013
C2 domain present in Ras GTPase activating protein (GAP) family; SynGAP, GAP1, RasGAP, and ...
 239-378 1.88e-74

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: 243.37  E-value: 1.88e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  239 PNKDNSRRVDNVLKLWVIEARDLPPKKRYYCELCLDDMLYARTTSKARTDNVFWGEHFEFNNLPAVRTIRLHLYKDTDKK 318
Cdd:cd04013      1 PNRDNSRRTENSLKLWIIEAKGLPPKKRYYCELCLDKTLYARTTSKLKTDTLFWGEHFEFSNLPPVSVITVNLYRESDKK 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1823433676  319 RKKDKSNYVGMVSIPIASVTGRHFAEQWYPLSQPSGSKS------KAGCPALRVKSRFQTMSILPM 378
Cdd:cd04013     81 KKKDKSQLIGTVNIPVTDVSSRQFVEKWYPVSTPKGNGKsggkegKGESPSIRIKARYQSTRVLPL 146
RasGAP_CLA2_BUD2 cd05137
Ras-GTPase Activating Domain of CLA2/BUD2; CLA2/BUD2 functions as a GTPase-activating protein ...
 375-618 3.77e-52

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: 187.39  E-value: 3.77e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  375 ILPMELYKEFAEYVTN-NYRML--CAVLEPVLSVkskEEVACALVHILQSTGKAKDFLSDMAMTEVD------------- 438
Cdd:cd05137      9 VLPSKNYKPLEELLHNfDLGLTlqIAELVPGDKL---ERLSEILLDIFQASGREDEWFMALVEDEIDgidkstsknkdmg 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  439 RFMDREH-LIFRENTLATKAIEEYLKLIGQKYLKDAIGEFIRALYESEENCEVDPMKCSAST-------LADHQANLR-M 509
Cdd:cd05137     86 KSSNNEAnLLFRGNSLLTKSLEKYMRRIGKEYLEKSIGDVIRKICEENKDCEVDPSRVKESDsiekeedLEENWENLIsL 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  510 CCELALCKVVNSHCvFPRELKEVFASWR----LRCAERGREDIadrL--ISASLFLRFLCPAVMSPSLFGLMQEYPDEQT 583
Cdd:cd05137    166 TEEIWNSIYITSND-CPPELRKILKHIRakveDRYGDFLRTVT---LnsVSGFLFLRFFCPAILNPKLFGLLKDHPRPRA 241

                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1823433676  584 ARTLTLIAKVIQNLANFTKFGSKEEYMAFMNEFLE 618
Cdd:cd05137    242 QRTLTLIAKVLQNLANLTTFGQKEPWMEPMNEFLT 276
PH_RasSynGAP-like cd13262
Synaptic Ras-GTPase activating protein family Pleckstrin homology (PH) domain; The RasSynGAP ...
 117-247 5.26e-52

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: 178.39  E-value: 5.26e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  117 QGFLSRRLKSSIKRTKSQPKLDRTSSFRqiLPRFRSADHDRarlMQSFKESHSHESLLSPSSAAEalELNLDEDSIIKAV 196
Cdd:cd13262      2 SGFFSRRLKGPLKRTKSVTKLERKSSKR--LPRTRLARAPA---GPRLRGSRSHESLLSSSSAAL--DLSADEDVVIRPL 74

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1823433676  197 HSSILGQEFCFEVTTASGTKCFACRSAAERDKWIENLQRAVKPNKDNSRRV 247
Cdd:cd13262     75 HSSILGRKHCFQVTTSEGTRCFSCRSAAERDRWIEDLRRAAQPNKDNCRRT 125
PH_nGAP cd13373
Neuronal growth-associated proteins Pleckstrin homology (PH) domain; nGAP (also called RASAL2 ...
 112-253 4.21e-51

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: 176.46  E-value: 4.21e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  112 PFRPSqGFLSRRLKSSIKRTKSQPKLDRTSSFRqiLPRFRSADhDRARLMQSFKESHSHESLLSPSSAAEALELNLDEDS 191
Cdd:cd13373      1 PFKVS-GFFSKRLKGSIKRTKSQSKLDRNTSFR--LPSLRSAD-DRSRGLPKLKESRSHESLLSPGSAVEALDLGREEKV 76

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1823433676  192 IIKAVHSSILGQEFCFEVTTASGTKCFACRSAAERDKWIENLQRAVKPNKDNSRRVDNVLKL 253
Cdd:cd13373     77 SVKPLHSSILGQDFCFEVTYSSGSKCFSCSSAAERDKWMENLRRTVQPNKDNCRRAENVLRL 138
RasGAP_GAP1_like cd05128
Ras-GTPase Activating Domain of GAP1 and similar proteins; The GAP1 family of Ras ...
 395-632 2.10e-50

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: 179.37  E-value: 2.10e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  395 LCAVLEPVLSVkSKEEVACALVHILQSTGKAKDFLSDMAMTEVDRFMDrEHLIFRENTLATKAIEEYLKLIGQKYLKDAI 474
Cdd:cd05128     23 AVYLLEELVKV-DKDDVARPLVRIFLHHGQIVPLLRALASREISKTQD-PNTLFRGNSLASKCMDEFMKLVGMQYLHETL 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  475 GEFIRALYESEENCEVDPMKCSASTLAD-HQANLRMCCELALCKVVNS--HCvfPRELKEVFASWRLRCAER--GREDIA 549
Cdd:cd05128    101 KPVIDEIFSEKKSCEIDPSKLKDGEVLEtNLANLRGYVERVFKAITSSarRC--PTLMCEIFSDLRESAAQRfpDNEDVP 178

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  550 DRLISASLFLRFLCPAVMSPSLFGLMQEYPDEQTARTLTLIAKVIQNLANFTKFGS----KEEYMA-FMNEFLELEW-AS 623
Cdd:cd05128    179 YTAVSGFIFLRFFAPAILNPKLFGLREEHPDPQTARTLTLISKTIQTLGNLGSSSSglgvKEAYMSpLYERFTDEQHvDA 258


                   ....*....
gi 1823433676  624 MQQFLYEIS 632
Cdd:cd05128    259 VKKFLDRIS 267
RasGAP_Neurofibromin_like cd05392
Ras-GTPase Activating Domain of proteins similar to neurofibromin; Neurofibromin-like proteins ...
 377-657 2.92e-44

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: 163.61  E-value: 2.92e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  377 PMELYKEFAEYVTNNYRMLCAVLEpVLSVKSKEEVACALVHILQSTGKAKDFLSDMAMTEVDRfMDREHLIFRENTLATK 456
Cdd:cd05392      2 KSEAYDELLELLIEDPQLLLAIAE-VCPSSEVDLLAQSLLNLFETRNRLLPLISWLIEDEISH-TSRAADLFRRNSVATR 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  457 AIEEYLKLIGQKYLKDAIGEFIRALYESEENCEVDPMKCSASTLADHQANLRMCCELALCKVVNSHCVFPRELKEVFASW 536
Cdd:cd05392     80 LLTLYAKSVGNKYLRKVLRPLLTEIVDNKDYFEVEKIKPDDENLEENADLLMKYAQMLLDSITDSVDQLPPSFRYICNTI 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  537 RlRCAERGREDIADRLISASLFLRFLCPAVMSPSLFGLMQEYPDEQTARTLTLIAKVIQNLANFTKFGSKEEYMAFMNEF 616
Cdd:cd05392    160 Y-ESVSKKFPDAALIAVGGFLFLRFICPAIVSPESENLLDPPPTPEARRSLILIAKVLQNIANGVLFSLKEPYLESLNEF 238

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1823433676  617 LELEWASMQQFLYEISNLDTLTNSTSFEGYIDLGRELSTLH 657
Cdd:cd05392    239 LKKNSDRIQQFLSEVSTIPPTDPIFDESDEEPITADLRYLH 279
RasGAP_RASA3 cd05134
Ras-GTPase Activating Domain of RASA3; RASA3 (or GAP1_IP4BP) is a member of the GAP1 family ...
 406-633 3.66e-38

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: 144.40  E-value: 3.66e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  406 KSKEEVACALVHILQSTGKAKDFLSDMAMTEVDRFMDrEHLIFRENTLATKAIEEYLKLIGQKYLKDAIGEFIRALYESE 485
Cdd:cd05134     33 REKQEAAIPLVRLFLHYGKIVPFISAIASAEVNRTQD-PNTIFRGNSLTSKCIDETMKLAGMHYLQVTLKPIIDEICQEH 111

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  486 ENCEVDPMKCSAS-TLADHQANLRMCCELALCKVVNSHCVFPRELKEVFASWRLRCAERGREDIADRL--ISASLFLRFL 562
Cdd:cd05134    112 KPCEIDPVKLKDGeNLENNRENLRQYVDRIFRVITKSGVSCPTVMCDIFFSLRESAAKRFQVDPDVRYtaVSSFIFLRFF 191

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1823433676  563 CPAVMSPSLFGLMQEYPDEQTARTLTLIAKVIQNLANFTKFGS---KEEYMA-FMNEFLELEWA-SMQQFLYEISN 633
Cdd:cd05134    192 APAILSPNLFQLTPHHPDPQTSRTLTLISKTIQTLGSLSKSKSanfKESYMAaFYDYFNEQKYAdAVKNFLDLISS 267
RasGAP_p120GAP cd05391
Ras-GTPase Activating Domain of p120; p120GAP is a negative regulator of Ras that stimulates ...
 375-699 1.02e-37

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: 144.94  E-value: 1.02e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  375 ILPMELYKEFAEYVTNNYRMLCAVLEPVLSvKSKEEVACALVHILQSTGKAKDFLSDMAMTEVDRfMDREHLIFRENTLA 454
Cdd:cd05391      4 IMPEEEYSELKELILQKELHVVYALAHVCG-QDRTLLASILLRIFRHEKLESLLLRTLNDREISM-EDEATTLFRATTLA 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  455 TKAIEEYLKLIGQKYLKDAIGEFIRALYESEENCEVDPMKCSAStlADHQANLRMCCELALC---KVVNSHCVFPRELKE 531
Cdd:cd05391     82 STLMEQYMKATATPFVHHALKDTILKILESKQSCELNPSKLEKN--EDVNTNLEHLLNILSElveKIFMAAEILPPTLRY 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  532 VFASWRLRCAERGRED--IADRLISASLFLRFLCPAVMSPSLFGLMQEYPDEQTARTLTLIAKVIQNLANFTKFGSKEEY 609
Cdd:cd05391    160 IYGCLQKSVQQKWPTNttVRTRVVSGFVFLRLICPAILNPRMFNIISETPSPTAARTLTLVAKSLQNLANLVEFGAKEPY 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  610 MAFMNEFLELEWASMQQFLYEISNLDTLtNSTSFEGYIDLGRELSTLHALLwEVMSQLSKEALLKLGPLPRLLTdISVAL 689
Cdd:cd05391    240 MEGVNPFIKKNKERMIMFLDELGNVPEL-PDTTEHSRTDLSRDLAALHEIC-VAHSDELRTLSNERGALKKLLA-VTELL 316

                          330
                   ....*....|
gi 1823433676  690 RNPHLQRQPS 699
Cdd:cd05391    317 QQKQNQYTQS 326
RasGAP_RASAL cd05135
Ras-GTPase Activating Domain of RASAL1 and similar proteins; Ras GTPase activating-like ...
 397-635 1.11e-32

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: 128.78  E-value: 1.11e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  397 AVLEPVLSVKSKEEVACALVHILQSTGKAKDFLSDMAMTEVDRFMDREHLiFRENTLATKAIEEYLKLIGQKYLKDAIGE 476
Cdd:cd05135     29 AMLEEVTTGESRQDVATKLVKIFLGQGLVVPFLDYLNTREVGRTTDPNTL-FRSNSLASKSMEQFMKVVGMPYLHEVLKP 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  477 FIRALYESEENCEVDPMKCSAS---------TLADHQ------ANLRMCCELALCKVVNSHCVFPRELKEVFASWRLRCA 541
Cdd:cd05135    108 VINRIFEEKKYVELDPCKIDLNrtrrisfkgSLSEAQvresslELLQGYLGSIIDAIVGSVDQCPPVMRVAFKQLHKRVE 187

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  542 ER----GREDIADRLISASLFLRFLCPAVMSPSLFGLMQEYPDEQTARTLTLIAKVIQNLANF-TKFGS-KEEYMAFMNE 615
Cdd:cd05135    188 ERfpeaEHQDVKYLAISGFLFLRFFAPAILTPKLFQLREQHADPRTSRTLLLLAKAVQSIGNLgLQLGQgKEQWMAPLHP 267

                          250       260
                   ....*....|....*....|
gi 1823433676  616 FLELEWASMQQFLYEISNLD 635
Cdd:cd05135    268 FILQSVARVKDFLDRLIDID 287
RasGAP pfam00616
GTPase-activator protein for Ras-like GTPase; All alpha-helical domain that accelerates the ...
 428-599 1.74e-31

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: 122.78  E-value: 1.74e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  428 FLSDMAMTEVDRFMDREHLiFRENTLATKAIEEYLKL-IGQKYLKDAIGEFIRALYESEE-NCEVDPMKCSAS------- 498
Cdd:pfam00616    1 LISELIEEEIESSDNPNDL-LRGNSLVSKLLETYNRRpRGQEYLKKVLGPLVRKIIEDEDlDLESDPRKIYESlinqeel 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  499 ------------------------TLADHQANLRMCCELALCKVVNSHCVFPREL----KEVFASWRLRCAERGREDIAd 550
Cdd:pfam00616   80 ktgrsdlprdvspeeaiedpevrqIFEDNLQKLRELADEFLDAIYSSLNQLPYGIryicKQLYELLEEKFPDASEEEIL- 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1823433676  551 RLISASLFLRFLCPAVMSPSLFGLMQEYPDEQTARTLTLIAKVIQNLAN 599
Cdd:pfam00616  159 NAIGGFLFLRFFCPAIVNPDLFGLVDHQISPKQRRNLTLIAKVLQNLAN 207
RasGAP_RASA2 cd05394
Ras-GTPase Activating Domain of RASA2; RASA2 (or GAP1(m)) is a member of the GAP1 family of ...
 406-633 2.65e-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: 112.68  E-value: 2.65e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  406 KSKEEVACALVHILQSTGKAKDFLSDMAMTEVDRFMDrEHLIFRENTLATKAIEEYLKLIGQKYLKDAIGEFIRALYESE 485
Cdd:cd05394     33 RDKYDAVLPLVRLLLHHNKLVPFVAAVAALDLKDTQE-ANTIFRGNSLATRCLDEMMKIVGKHYLKVTLKPVLDEICESP 111

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  486 ENCEVDPMKC-SASTLADHQANLRMCCELALCKVVNSHCVFPRELKEVFASWRLRCAERGRED--IADRLISASLFLRFL 562
Cdd:cd05394    112 KPCEIDPIKLkEGDNVENNKENLRYYVDKVFFSIVKSSMSCPTLMCDVFRSLRHLAVKRFPNDphVQYSAVSSFVFLRFF 191

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1823433676  563 CPAVMSPSLFGLMQEYPDEQTARTLTLIAKVIQNLANF-----TKFGS-KEEYMA-FMNEFLELEWA-SMQQFLYEISN 633
Cdd:cd05394    192 AVAVVSPHTFQLRPHHPDAQTSRTLTLISKTIQTLGSWgslskSKLSSfKETFMCdFFKMFQEEKYIeKVKKFLDEISS 270
RasGAP_Neurofibromin cd05130
Ras-GTPase Activating Domain of neurofibromin; Neurofibromin is the product of the ...
 410-662 1.79e-26

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: 112.03  E-value: 1.79e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  410 EVACALVHILQSTGKAKDFLSDMAMTEVDrFMDREHLIFRENTLATKAIEEYLKLIGQKYLKDAIGEFIRALYESEE--N 487
Cdd:cd05130     41 ELARVLVTLFDSKHLLYQLLWNMFSKEVE-LADSMQTLFRGNSLASKIMTFCFKVYGATYLQSLLEPLLRTMITSSEwvS 119

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  488 CEVDPMKC-SASTLADHQANLRMCCELALCKVVNSHCVFPRELKEVfaswrLRC-----AERGREDIADRLISAsLFLRF 561
Cdd:cd05130    120 YEVDPTRLeGNENLEENQRNLLQLTEKFFHAIISSSDEFPPQLRSV-----CHClyqvvSHRFPNSGLGAVGSA-IFLRF 193

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  562 LCPAVMSPSLFGLMQEYPDEQTARTLTLIAKVIQNLANFTKFgSKEEYMAFMNEFLELEWASMQQFLYEISNLDTLT--N 639
Cdd:cd05130    194 INPAIVSPYEYGILDREPPPRVKRGLKLMSKILQNIANHVLF-TKEAHMLPFNDFLRNHFEAGRRFFSSIASDCGAVdgP 272

                          250       260
                   ....*....|....*....|...
gi 1823433676  640 STSFEGYIDLGRELStLHALLWE 662
Cdd:cd05130    273 SSKYLSFINDANVLA-LHRLLWN 294
PH_RASAL3 cd13374
RAS protein activator like-3 Pleckstrin homology (PH) domain; RASAL3 is thought to be a Ras ...
 144-262 9.44e-25

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: 101.24  E-value: 9.44e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  144 RQILPRFRSADHDRARLMQSFKES--HSHESLLSPSSAAEaLELNLDEDSIIKAVHSSILGQEFCFEVTTASGTKCFACR 221
Cdd:cd13374     23 RGLLKRLKEKKKAKAESTGTGRDGppSALGSRESLATISE-LDLGAERDVRVWPLHPSLLGEPHCFQVTWPGGSRCFSCR 101

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1823433676  222 SAAERDKWIENLQRAVKPNKDNSRRVDNVLKLWVIEARDLP 262
Cdd:cd13374    102 SAAERDRWIEDLRRSFQPHQDNVEREETWLSVWVHEAKGLP 142
RasGAP_GAPA cd05132
Ras-GTPase Activating Domain of GAPA; GAPA is an IQGAP-related protein and is predicted to ...
 466-682 1.46e-24

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: 106.67  E-value: 1.46e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  466 GQKYLKDAIGEFIRALYESEE-NCEVDPMKCSASTLADHQAN-----------------------------LRMCCELA- 514
Cdd:cd05132     67 GQSYLKTVLADRINDLISLKDlNLEINPLKVYEQMINDIELDtglpsnlprgitpeeaaenpavqniieprLEMLEEITn 146

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  515 --LCKVVNSHCVFPRELKEVFASWRLRCAER----GREDIADrLISASLFLRFLCPAVMSPSLFGLMQEYPDEQTARTLT 588
Cdd:cd05132    147 sfLEAIINSLDEVPYGIRWICKQIRSLTRRKfpdaSDETICS-LIGGFFLLRFINPAIVSPQAYMLVDGKPSDNTRRTLT 225

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  589 LIAKVIQNLANFTKFgSKEEYMAFMNEFLELEWASMQQFLYEISNLDTLTNSTSFEGYIDLGR----------ELSTLHA 658
Cdd:cd05132    226 LIAKLLQNLANKPSY-SKEPYMAPLQPFVEENKERLNKFLNDLCEVDDFYESLELDQYIALSKkdlsinitlnEIYNTHS 304

                          250       260
                   ....*....|....*....|....
gi 1823433676  659 LLWEVMSQLSKEALLKLGPLPRLL 682
Cdd:cd05132    305 LLVKHLAELAPDHNDHLRLILQEL 328
RasGAP_RASA4 cd05395
Ras-GTPase Activating Domain of RASA4; Ras GTPase activating-like 4 protein (RASAL4), also ...
 395-635 7.34e-24

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: 103.03  E-value: 7.34e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  395 LCAVLEPVLSVKSKEEVACALVHILQSTGKAKDFLSDMAMTEVDRFMDREHLiFRENTLATKAIEEYLKLIGQKYLKDAI 474
Cdd:cd05395     27 LISLIDETTTAECRQEVATNLVKLFLGQGLAKEFLDLLFQLELDKTTEPNTL-FRSNSLASKSMESFLKVAGMQYLHSVL 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  475 GEFIRALYESEENCEVDPMKC----------------------SASTLADHQANLrmccelaLCKVVNSHCVFPRELKEV 532
Cdd:cd05395    106 GPTINRVFEEKKYVELDPSKVeikdvgcsglhriqtesevieqSAQLLQSYLGEL-------LSAISKSVKYCPAVIRAT 178

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  533 FASWRLRCAERGREDIADRL----ISASLFLRFLCPAVMSPSLFGLMQEYPDEQTARTLTLIAKVIQNLANFTKFGS--K 606
Cdd:cd05395    179 FRQLFKRVQERFPENQHQNVkfiaVTSFLCLRFFSPAIMSPKLFHLREKHADARTSRTLLLLAKAVQNVGNMDTLASraK 258

                          250       260
                   ....*....|....*....|....*....
gi 1823433676  607 EEYMAFMNEFLELEWASMQQFLYEISNLD 635
Cdd:cd05395    259 EAWMAPLQPAIQQGVAQLKDFITKLVDIE 287
C2 cd00030
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
 251-349 3.30e-11

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: 61.31  E-value: 3.30e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  251 LKLWVIEARDLPPKKR-----YYCELCLDDMLYARTTSKARTDNVFWGEHFEFNNL-PAVRTIRLHLYKDTDKKRKKdks 324
Cdd:cd00030      1 LRVTVIEARNLPAKDLngksdPYVKVSLGGKQKFKTKVVKNTLNPVWNETFEFPVLdPESDTLTVEVWDKDRFSKDD--- 77

                           90       100
                   ....*....|....*....|....*.
gi 1823433676  325 nYVGMVSIPIASVTGR-HFAEQWYPL 349
Cdd:cd00030     78 -FLGEVEIPLSELLDSgKEGELWLPL 102
C2 pfam00168
C2 domain;
249-349 1.82e-09

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 56.17  E-value: 1.82e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  249 NVLKLWVIEARDLPPKKRY-----YCELCL-DDMLYARTTSKARTDNVFWGEHFEFN-NLPAVRTIRLHLYKDTDKKRkk 321
Cdd:pfam00168    1 GRLTVTVIEAKNLPPKDGNgtsdpYVKVYLlDGKQKKKTKVVKNTLNPVWNETFTFSvPDPENAVLEIEVYDYDRFGR-- 78

                           90       100
                   ....*....|....*....|....*...
gi 1823433676  322 dkSNYVGMVSIPIASVTGRHFAEQWYPL 349
Cdd:pfam00168   79 --DDFIGEVRIPLSELDSGEGLDGWYPL 104
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 250-346 7.68e-09

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: 54.42  E-value: 7.68e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676   250 VLKLWVIEARDLPPKKRY-----YCELCLDDMLY--ARTTSKARTDNVFWGEHFEFN-NLPAVRTIRLHLYkdtdKKRKK 321
Cdd:smart00239    1 TLTVKIISARNLPPKDKGgksdpYVKVSLDGDPKekKKTKVVKNTLNPVWNETFEFEvPPPELAELEIEVY----DKDRF 76

                            90       100
                    ....*....|....*....|....*
gi 1823433676   322 DKSNYVGMVSIPIASVTGRHFAEQW 346
Cdd:smart00239   77 GRDDFIGQVTIPLSDLLLGGRHEKL 101
RasGAP_IQGAP_like cd05127
Ras-GTPase Activating Domain of IQ motif containing GTPase activating proteins; This family ...
 557-679 1.11e-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: 55.28  E-value: 1.11e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  557 LFLRFLCPAVMSPSLFGLMQEYPDEQTA----RTLTLIAKVIQNLANFTKFGSKEEYMAFMNEFLELEWASMQQFLYEIS 632
Cdd:cd05127    179 LYYRYMNPAIVAPEAFDIIDLSVGGQLSplqrRNLGSIAKVLQQAASGKLFGGENPYLSPLNPYISESHEKFKKFFLEAC 258

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1823433676  633 NLDT------------LTNSTSFEGYIDLgRELSTLHALLWEVMSQLS-------KEALLKLGPLP 679
Cdd:cd05127    259 TVPEaeehfnideysdLTMLTKPTIYISL-QEIFATHKLLLEHQDEIApdpddplRELLDDLGPAP 323
C2_Ras_p21A1 cd08400
C2 domain present in RAS p21 protein activator 1 (RasA1); RasA1 is a GAP1 (GTPase activating ...
 251-370 4.04e-07

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: 50.06  E-value: 4.04e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  251 LKLWVIEARDLPPKK--RYYCELCLDDMLYARTtsKARTD-NVFWGEHFEFNNLPA-VRTIRLHLYKDTDKKRKKDksny 326
Cdd:cd08400      6 LQLNVLEAHKLPVKHvpHPYCVISLNEVKVART--KVREGpNPVWSEEFVFDDLPPdVNSFTISLSNKAKRSKDSE---- 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1823433676  327 VGMVSIPIASVTGRHFAEQWYPLSQPSGSKsKAGCPALRVKSRF 370
Cdd:cd08400     80 IAEVTVQLSKLQNGQETDEWYPLSSASPLK-GGEWGSLRIRARY 122
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 184-238 1.38e-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: 47.93  E-value: 1.38e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 1823433676   184 ELNLDEDSIIKAVHSSILGQEFCFEVTTASG-TKCFACRSAAERDKWIENLQRAVK 238
Cdd:smart00233   47 SIDLSGCTVREAPDPDSSKKPHCFEIKTSDRkTLLLQAESEEEREKWVEALRKAIA 102
C2A_RasGAP cd08383
C2 domain (first repeat) of Ras GTPase activating proteins (GAPs); RasGAPs suppress Ras ...
 251-350 1.41e-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: 48.41  E-value: 1.41e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  251 LKLWVIEARDLPPKK--RYYCELCLDDMLYARTTSKARTdNVFWGEHFEFNNLPAV---RTIRLHLYKDTDKKRKkdksn 325
Cdd:cd08383      2 LRLRILEAKNLPSKGtrDPYCTVSLDQVEVARTKTVEKL-NPFWGEEFVFDDPPPDvtfFTLSFYNKDKRSKDRD----- 75

                           90       100
                   ....*....|....*....|....*
gi 1823433676  326 yVGMVSIPIASVTGRHFAEQWYPLS 350
Cdd:cd08383     76 -IVIGKVALSKLDLGQGKDEWFPLT 99
C2A_MCTP_PRT_plant cd04022
C2 domain first repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP); ...
 255-366 7.88e-06

C2 domain first repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP); plant subset; MCTPs are involved in Ca2+ signaling at the membrane. Plant-MCTPs are composed of a variable N-terminal sequence, four C2 domains, two transmembrane regions (TMRs), and a short C-terminal sequence. It is one of four protein classes that are anchored to membranes via a transmembrane region; the others being synaptotagmins, extended synaptotagmins, and ferlins. MCTPs are the only membrane-bound C2 domain proteins that contain two functional TMRs. MCTPs are unique in that they bind Ca2+ but not phospholipids. 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. This cd contains the first C2 repeat, C2A, and has a type-II topology.


Pssm-ID: 175989 [Multi-domain]  Cd Length: 127  Bit Score: 46.56  E-value: 7.88e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  255 VIEARDLPPKKRY-----YCELCLDDMLYaRTTSKARTDNVFWGEHFEFN--NLPAVRTIRLHLYkDTDKKRKKDKSNYV 327
Cdd:cd04022      6 VVDAQDLMPKDGQgsssaYVELDFDGQKK-RTRTKPKDLNPVWNEKLVFNvsDPSRLSNLVLEVY-VYNDRRSGRRRSFL 83

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1823433676  328 GMVSIPIASVTGR-HFAEQWYPLSQPSGSKSKAGCPALRV 366
Cdd:cd04022     84 GRVRISGTSFVPPsEAVVQRYPLEKRGLFSRVRGEIGLKV 123
PRK12704 PRK12704
phosphodiesterase; Provisional
 1079-1161 1.75e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 45.54  E-value: 1.75e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676 1079 LKEYSKSMDESRLDRVKEYEEEIHSLKERLHMS----NRKLEEYERRLVTQEEQTSR---ILLQYQQRLELSEKRLRQQQ 1151
Cdd:PRK12704    44 LEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKElrerRNELQKLEKRLLQKEENLDRkleLLEKREEELEKKEKELEQKQ 123

                           90
                   ....*....|
gi 1823433676 1152 QEKDSQIKSI 1161
Cdd:PRK12704   124 QELEKKEEEL 133
DivIVA COG3599
Cell division septum initiation protein DivIVA, interacts with FtsZ and MinD [Cell cycle ...
 1080-1159 2.97e-04

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


Pssm-ID: 442818 [Multi-domain]  Cd Length: 125  Bit Score: 41.76  E-value: 2.97e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676 1080 KEYSKSM-----DESR--LDRV-KEYE---EEIHSLKERLHMSNRKLEEYERRlvtqEEQTSRILLQYQqrlELSEKRLR 1148
Cdd:COG3599     11 KEFKKGFrgydeDEVDefLDEVaEDYErliRENKELKEKLEELEEELEEYREL----EETLQKTLVVAQ---ETAEEVKE 83

                           90
                   ....*....|.
gi 1823433676 1149 QQQQEKDSQIK 1159
Cdd:COG3599     84 NAEKEAELIIK 94
RasGAP_IQGAP2 cd05131
Ras-GTPase Activating Domain of IQ motif containing GTPase activating protein 2; IQGAP2 is a ...
 437-679 3.95e-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: 3.95e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  437 VDRFMDREHLIfrentLATKAIEEYLKLIGQkyLKDAIGEFIRALYE-SEENCEVDPMkcSASTLADHQANLRMCCELAL 515
Cdd:cd05131     74 VKEIIEDKSLI-----INTNPVEVYKAWVNQ--LETATGEASKLPYDvTTEQALTHPE--VVNKLESSIQSLRSVTDKVL 144

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  516 CKVVNSHCVFPRELKEVFASWRLRCAER---GREDIADRLISASLFLRFLCPAVMSPSLFGLMQ-----EYPDEQTaRTL 587
Cdd:cd05131    145 GSIFSSLDLIPYGMRYIAKVLKNSLHEKfpdATEDELLKIVGNLLYYRYMNPAIVAPDGFDIIDmtaggQIHSEQR-RNL 223

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  588 TLIAKVIQNLANFTKFGSKEEYMAFMNEFLELEWASMQQFLY---------EISNLDTLTNSTSFEG---YIDLgRELST 655
Cdd:cd05131    224 GSVAKVLQHAASNKLFEGENAHLSSMNSYLSQTYQKFRKFFQaacdvpepeEKFNIDEYSDMVTLSKpviYISI-EEIIN 302

                          250       260       270
                   ....*....|....*....|....*....|.
gi 1823433676  656 LHALLWEVM-------SQLSKEALLKLGPLP 679
Cdd:cd05131    303 THSLLLEHQdaiapdqNDLLHELLKDLGEVP 333
PHA03247 PHA03247
large tegument protein UL36; Provisional
 748-1053 6.29e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.54  E-value: 6.29e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  748 RLPSPPQEKGPPEVLVLSRPPLARSSP------------AYCTSSSDLTEPEGGRGGALGVGKSVSMLDL--QDGRVDSI 813
Cdd:PHA03247  2654 DDPAPGRVSRPRRARRLGRAAQASSPPqrprrraarptvGSLTSLADPPPPPPTPEPAPHALVSATPLPPgpAAARQASP 2733

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  814 PSLPAELLAGGPAPGGAGQGGLRPGR--LSQGSASSlAPPRlgVPePGGPQLRVPLSFQNPLFHL--AADGPLRGPDGGG 889
Cdd:PHA03247  2734 ALPAAPAPPAVPAGPATPGGPARPARppTTAGPPAP-APPA--AP-AAGPPRRLTRPAVASLSESreSLPSPWDPADPPA 2809

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  890 GGGGRGEGGGGDGGHFGGVAPPPLHGYSKSEELATPPQKHITHSHSYSdefgrPGGDFGRRqlslqdtlAPPQitigaPP 969
Cdd:PHA03247  2810 AVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVA-----PGGDVRRR--------PPSR-----SP 2871

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  970 PPTPRGSRagkgggGPSALGVPQKPRPASGNLLASPEPayGPPRSRQPSLAKEASVAGMKPPVTKQASQTPSTLNPVLPA 1049
Cdd:PHA03247  2872 AAKPAAPA------RPPVRRLARPAVSRSTESFALPPD--QPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPL 2943


                   ....
gi 1823433676 1050 SERT 1053
Cdd:PHA03247  2944 APTT 2947
C2A_C2C_Synaptotagmin_like cd08391
C2 domain first and third repeat in Synaptotagmin-like proteins; Synaptotagmin is a ...
 250-372 6.32e-04

C2 domain first and third repeat in Synaptotagmin-like proteins; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. Previously all synaptotagmins were thought to be calcium sensors in the regulation of neurotransmitter release and hormone secretion, but it has been shown that not all of them bind calcium. Of the 17 identified synaptotagmins only 8 bind calcium (1-3, 5-7, 9, 10). The function of the two C2 domains that bind calcium are: regulating the fusion step of synaptic vesicle exocytosis (C2A) and binding to phosphatidyl-inositol-3,4,5-triphosphate (PIP3) in the absence of calcium ions and to phosphatidylinositol bisphosphate (PIP2) in their presence (C2B). C2B also regulates also the recycling step of synaptic vesicles. 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. This cd contains either the first or third repeat in Synaptotagmin-like proteins with a type-I topology.


Pssm-ID: 176037 [Multi-domain]  Cd Length: 121  Bit Score: 40.74  E-value: 6.32e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  250 VLKLWVIEARDLPPKKRY-----------YCELCLDDMLYaRTTSKARTDNVFWGEHFEF--NNLPAVrTIRLHLYKDTD 316
Cdd:cd08391      2 VLRIHVIEAQDLVAKDKFvgglvkgksdpYVIVRVGAQTF-KSKVIKENLNPKWNEVYEAvvDEVPGQ-ELEIELFDEDP 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1823433676  317 KKrkkdkSNYVGMVSIPIASVTGRHFAEQWYPLSqpsgskskaGCPALRVKSRFQT 372
Cdd:cd08391     80 DK-----DDFLGRLSIDLGSVEKKGFIDEWLPLE---------DVKSGRLHLKLEW 121
PHA03247 PHA03247
large tegument protein UL36; Provisional
 692-1071 9.11e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.77  E-value: 9.11e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  692 PHLQRQPSQGERlpPKGLVLRGPSADLQPYLVRDLNSSVDLQSYMVRGLNSSMDVPRLPSPPQekGPpevlvlsRPPLAR 771
Cdd:PHA03247  2621 THAPDPPPPSPS--PAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQ--RP-------RRRAAR 2689

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  772 SSPAYCTSSSDLTEPEGGRGGALGVGKSVSMLDL--QDGRVDSIPSLPAELLAGGPAPGGAGQGGLRPGR--LSQGSASS 847
Cdd:PHA03247  2690 PTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPgpAAARQASPALPAAPAPPAVPAGPATPGGPARPARppTTAGPPAP 2769

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  848 lAPPRlgVPePGGPQLRVPLSFQNPLFHL--AADGPLRGPDGGGGGGGRGEGGGGDGGHFGGVAPPPLHGYSKSEELATP 925
Cdd:PHA03247  2770 -APPA--AP-AAGPPRRLTRPAVASLSESreSLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGP 2845

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  926 PQKHITHSHSYSdefgrPGGDFGRRQLSLQDTLAP---------------------------------PQITIGAPPPPT 972
Cdd:PHA03247  2846 PPPSLPLGGSVA-----PGGDVRRRPPSRSPAAKPaaparppvrrlarpavsrstesfalppdqperpPQPQAPPPPQPQ 2920

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  973 PRGSRAGKGGGGPSALGVPQKPRPASGNLLASPEPAYGPPRSRQPSLAK------EASVAGMKPPVTKQASQTPSTLNPV 1046
Cdd:PHA03247  2921 PQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPgrvavpRFRVPQPAPSREAPASSTPPLTGHS 3000

                          410       420
                   ....*....|....*....|....*
gi 1823433676 1047 LPaseRTVAWVSNmphLSADIESSH 1071
Cdd:PHA03247  3001 LS---RVSSWASS---LALHEETDP 3019
C2_C21orf25-like cd08678
C2 domain found in the Human chromosome 21 open reading frame 25 (C21orf25) protein; The ...
 268-360 1.06e-03

C2 domain found in the Human chromosome 21 open reading frame 25 (C21orf25) protein; The members in this cd are named after the Human C21orf25 which contains a single C2 domain. Several other members contain a C1 domain downstream of the C2 domain. No other information on this protein is currently known. 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: 176060 [Multi-domain]  Cd Length: 126  Bit Score: 40.43  E-value: 1.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  268 YCELCLDD-MLYARTTSKARTDNVFWGEHFEFNNLPAVRTIRLHLYkdtdKKRKKDKSNYVGMVSIPIASVTGRHFAEQW 346
Cdd:cd08678     21 YCVLEMDEpPQKYQSSTQKNTSNPFWDEHFLFELSPNSKELLFEVY----DNGKKSDSKFLGLAIVPFDELRKNPSGRQI 96

                           90
                   ....*....|....*
gi 1823433676  347 YPL-SQPSGSKSKAG 360
Cdd:cd08678     97 FPLqGRPYEGDSVSG 111
RasGAP_IQGAP1 cd05133
Ras-GTPase Activating Domain of IQ motif containing GTPase activating protein 1; IQGAP1 is a ...
 546-685 1.07e-03

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: 43.11  E-value: 1.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  546 EDIADRLISASLFLRFLCPAVMSPSLFGLM------QEYPDEQtaRTLTLIAKVIQNLANFTKFGSKEEYMAFMNEFLEL 619
Cdd:cd05133    178 EDELLKIVGNLLYYRYMNPAIVAPDAFDIIdlsaggQLTTDQR--RNLGSIAKMLQHAASNKMFLGDNAHLSPINEYLSQ 255

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  620 EWASMQQFLY---------------EISNLDTLTNSTSfegYIDLGRELSTlHALLWEVMSQLSKEallKLGPLPRLLTD 684
Cdd:cd05133    256 SYQKFRRFFQaacdvpeledkfnvdEYSDLVTLTKPVI---YISIGEIINT-HTLLLDHQDAIAPE---HNDPIHELLDD 328


                   .
gi 1823433676  685 I 685
Cdd:cd05133    329 L 329
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
1088-1161 1.71e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.45  E-value: 1.71e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1823433676 1088 ESRLDRVKEYEEEIHSLKERLHMSNRKLEEYERRLVTQEEQTSRILLQYQQRLELSEKRLRQQQQEKDSQIKSI 1161
Cdd:COG4717    145 PERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEA 218
PHA03247 PHA03247
large tegument protein UL36; Provisional
 943-1066 1.85e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.00  E-value: 1.85e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  943 PGGDFGRRQLSLQDTLAPPQITIGAPPPPTPRGSRAGKGGGGPSALGVPQKPRPASG----------NLLASPEPAYGPP 1012
Cdd:PHA03247  2601 PVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPApgrvsrprraRRLGRAAQASSPP 2680

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1823433676 1013 RSRQPSLAKE--ASVAGMK--PPVTKQASQTPSTLNPVLPASERTVAWVSNMPHLSAD 1066
Cdd:PHA03247  2681 QRPRRRAARPtvGSLTSLAdpPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAA 2738
C2A_RasA2_RasA3 cd08401
C2 domain first repeat present in RasA2 and RasA3; RasA2 and RasA3 are GAP1s (GTPase ...
 250-352 2.36e-03

C2 domain first repeat present in RasA2 and RasA3; RasA2 and RasA3 are GAP1s (GTPase activating protein 1s ), Ras-specific GAP members, 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. RasA2 and RasA3 are both inositol 1,3,4,5-tetrakisphosphate-binding proteins and contain an N-terminal C2 domain, a Ras-GAP domain, a pleckstrin-homology (PH) domain which localizes it to the plasma membrane, and Bruton's Tyrosine Kinase (BTK) a zinc binding 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. This cd contains the first C2 repeat, C2A, and has a type-I topology.


Pssm-ID: 176046 [Multi-domain]  Cd Length: 121  Bit Score: 39.34  E-value: 2.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  250 VLKLWVIEARDLPPKKR------YYCELCLDDMLYARTTSKARTDNVFWGEHFEFNNLPAVRTIRLHLYKDTDKKRKKDk 323
Cdd:cd08401      1 SLKIKIGEAKNLPPRSGpnkmrdCYCTVNLDQEEVFRTKTVEKSLCPFFGEDFYFEIPRTFRHLSFYIYDRDVLRRDSV- 79

                           90       100
                   ....*....|....*....|....*....
gi 1823433676  324 snyVGMVSIPIASVTGRHFAEQWYPLsQP 352
Cdd:cd08401     80 ---IGKVAIKKEDLHKYYGKDTWFPL-QP 104
RasGAP_RAP6 cd05129
Ras-GTPase Activating Domain of Rab5-activating protein 6; Rab5-activating protein 6 (RAP6) is ...
 545-618 2.39e-03

Ras-GTPase Activating Domain of Rab5-activating protein 6; Rab5-activating protein 6 (RAP6) is an endosomal protein with a role in the regulation of receptor-mediated endocytosis. RAP6 contains a Vps9 domain, which is involved in the activation of Rab5, and a Ras GAP domain (RGD). Rab5 is a small GTPase required for the control of the endocytic route, and its activity is regulated by guanine nucleotide exchange factor, such as Rabex5, and GAPs, such as RN-tre. Human Rap6 protein is localized on the plasma membrane and on the endosome. RAP6 binds to Rab5 and Ras through the Vps9 and RGD domains, respectively.


Pssm-ID: 213331  Cd Length: 365  Bit Score: 41.94  E-value: 2.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  545 REDIADRLisaslFLRFLCPAVMSPSLFGLMQEYPDEQTAR-TLTLIAKVIQNLAnFTKFGS-----KEEYMAF----MN 614
Cdd:cd05129    220 RALCTDLL-----FTNFICPAIVNPEQYGIISDAPISEVARhNLMQVAQILQVLA-LTEFESpdprlKELLSKFdkdcVS 293


                   ....
gi 1823433676  615 EFLE 618
Cdd:cd05129    294 AFLD 297
C2_PKC_epsilon cd04014
C2 domain in Protein Kinase C (PKC) epsilon; A single C2 domain is found in PKC epsilon. The ...
 251-297 3.28e-03

C2 domain in Protein Kinase C (PKC) epsilon; A single C2 domain is found in PKC epsilon. The PKC family of serine/threonine kinases regulates apoptosis, proliferation, migration, motility, chemo-resistance, and differentiation. There are 3 groups: group 1 (alpha, betaI, beta II, gamma) which require phospholipids and calcium, group 2 (delta, epsilon, theta, eta) which do not require calcium for activation, and group 3 (xi, iota/lambda) which are atypical and can be activated in the absence of diacylglycerol and calcium. 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-II topology.


Pssm-ID: 175981 [Multi-domain]  Cd Length: 132  Bit Score: 39.18  E-value: 3.28e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1823433676  251 LKLWVIEARDLPP---KKRY------------YCELCLDDMLYARTTSKARTDNVFWGEHFE 297
Cdd:cd04014      6 LKIKICEAVDLKPtdwSTRHavpkkgsqlldpYVSIDVDDTHIGKTSTKPKTNSPVWNEEFT 67
MAT1 pfam06391
CDK-activating kinase assembly factor MAT1; MAT1 is an assembly/targeting factor for ...
 1072-1160 3.89e-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: 39.92  E-value: 3.89e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676 1072 IEREEYKLKEY---SKSMDESRLDRVKEYEEEIHSLKERLHmsnrklEEYERRLVTQEEQTSRILLQYQQRLELSEKRLR 1148
Cdd:pfam06391   88 LSQEEEELEELlelEKREKEERRKEEKQEEEEEKEKKEKAK------QELIDELMTSNKDAEEIIAQHKKTAKKRKSERR 161

                           90
                   ....*....|..
gi 1823433676 1149 QQQQEKDSQIKS 1160
Cdd:pfam06391  162 RKLEELNRVLEQ 173
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 1056-1157 4.51e-03

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: 41.59  E-value: 4.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676 1056 WVSNMPHLSADIESSHIERE--EYKLKEYSKSMDESRlDRVKEYEEEIHSLKERLHMSNRKLEEYERRLVTQEEQTSRIl 1133
Cdd:TIGR02169  810 IEARLREIEQKLNRLTLEKEylEKEIQELQEQRIDLK-EQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDL- 887

                           90       100
                   ....*....|....*....|....
gi 1823433676 1134 lqYQQRLELsEKRLRQQQQEKDSQ 1157
Cdd:TIGR02169  888 --KKERDEL-EAQLRELERKIEEL 908
IQG1 COG5261
Protein involved in regulation of cellular morphogenesis/cytokinesis [Cell division and ...
 551-651 5.69e-03

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: 41.02  E-value: 5.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676  551 RLISASLFLRFLCPAVMSPSLFGLMQEYPDEQTaRTLTLIAKVIQNLANFTKFGSkeeYMAFMNEFLELEWASMQQFLYE 630
Cdd:COG5261    613 GLIGGFFFLRFVNEALVSPQTSMLKDSCPSDNV-RKLATLSKILQSVFEITSSDK---FDVPLQPFLKEYKEKVHNLLRK 688

                           90       100
                   ....*....|....*....|.
gi 1823433676  631 ISNLDTLTNSTSFEGYIDLGR 651
Cdd:COG5261    689 LGNVGDFEEYFEFDQYIDLVK 709
Nuf2_DHR10-like pfam18595
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This ...
 1068-1159 7.95e-03

Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This domain was identified as MazG related domain also designated as Designed helical repeat protein 10 (DHR10) that actually adopts a coiled-coil structure. Nuf2 is part of the Ndc80 complex, which binds to the spindle and is required for chromosome segregation and spindle checkpoint activity.


Pssm-ID: 465814 [Multi-domain]  Cd Length: 117  Bit Score: 37.56  E-value: 7.95e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676 1068 ESSHIEREEYKLKEYSKSMD---------ESRLDRVKEYEEEIHSLKERLHMSNRKLEEYERR------LVTQEEQTSRI 1132
Cdd:pfam18595    7 EKEELAELERKARELQAKIDalqvvekdlRSCIKLLEEIEAELAKLEEAKKKLKELRDALEEKeielreLERREERLQRQ 86

                           90       100
                   ....*....|....*....|....*..
gi 1823433676 1133 LLQYQQRLElsekRLRQQQQEKDSQIK 1159
Cdd:pfam18595   87 LENAQEKLE----RLREQAEEKREAAQ 109
COG5022 COG5022
Myosin heavy chain [General function prediction only];
1069-1161 9.07e-03

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 40.45  E-value: 9.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676 1069 SSHIEREEYK-----LKEYSKSMDESRLdrVKEYEEEIHSLKERLhMSNRKLEEYERRLVTQEEQTSRILLQYQQRLELS 1143
Cdd:COG5022    804 SLLGSRKEYRsylacIIKLQKTIKREKK--LRETEEVEFSLKAEV-LIQKFGRSLKAKKRFSLLKKETIYLQSAQRVELA 880

                           90
                   ....*....|....*...
gi 1823433676 1144 EKRLrqqqQEKDSQIKSI 1161
Cdd:COG5022    881 ERQL----QELKIDVKSI 894
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 1063-1164 9.32e-03

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 40.54  E-value: 9.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823433676 1063 LSADIESSHIEREEY---------KLKEYSKSMDESRLDRvkeyeEEIHSLKErlhmsnrkleEYERRLVTQEEQtsriL 1133
Cdd:pfam01576  782 LEAQIDAANKGREEAvkqlkklqaQMKDLQRELEEARASR-----DEILAQSK----------ESEKKLKNLEAE----L 842

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1823433676 1134 LQYQQRLELSEKRLRQQQQEKDSQIKSIIGS 1164
Cdd:pfam01576  843 LQLQEDLAASERARRQAQQERDELADEIASG 873
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH