NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|594591553|ref|NP_001277570|]
View 

disabled homolog 2-interacting protein isoform 6 [Mus musculus]

Protein Classification

RASAL2/DAB2IP family protein( domain architecture ID 11686133)

RASAL2/DAB2IP family protein similar to Homo sapien Ras GTPase-activating protein nGAP (RASAL2/NGAP) and disabled homolog 2-interacting protein (DAB2IP/AIP1)

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
DUF3498 pfam12004
Domain of unknown function (DUF3498); This presumed domain is functionally uncharacterized. ...
 522-1035 0e+00

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


:

Pssm-ID: 463427 [Multi-domain]  Cd Length: 511  Bit Score: 681.10  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553   522 LRDVHTALSTPGSGQLPG--TNDLASTPGSGSSSVSAGLQKMVIENDLsGLIDFTRLPSPTPENKDLFFVTRSSGVQPSP 599
Cdd:pfam12004    1 LRDITTALTNPTPIQQQLrrFSEHSSSPPVPGRSISSGLQKMFEDPDD-GLSDFTRLPSPTPENKDLFFVTRPPLLQPSP 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553   600 ARSSSYSEANEPDLQMANGSKSLSMVDLQDARTLDGEAgSPVGPDALPADGQVPATQLLAG---WPARAAPVSLAGLATV 676
Cdd:pfam12004   80 ARSSSYSDANEPDQQLPNGNKSLSMVDLQDSRSLQGSP-SPPLHDAPLNLSQAGSQASVGLrpaWAARTSQGNPQSAPQV 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553   677 RRAVPTPTTPGTSEgapgrPQLLAPLSFQNPVYQMAAGLPLSPRGLG--DSGSEGHSSLSSHSNSEELAAAAK----LGS 750
Cdd:pfam12004  159 RRPLQTPVTQGTRP-----QQLLAPLSFQNPVYHMAAGLPVSPRGLGspDSSSETHSSFSSHSNSEDLSSAAAnkksGPS 233

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553   751 FSTAAEELARRPGELARRQMSLTEKGGQPTVPRQNSAGPQRRIDQPPPPPPPPPPAPRGRtppTLLSTLQYPRPSSGTLA 830
Cdd:pfam12004  234 NSSYSEDFARRSTEFTRRQLSLTELQHQPAVPRQNSAGPQRRIDQQGLGGPPLTRGRTPP---SLLNSASYPRPSSGSLM 310

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553   831 SASPDWagPGTRLRQQSSSSKGDSPELKPRAMHKQGPSPVSPNALD---RTAAWLLTMNAQLLEDEGLGPDpphrdrlrS 907
Cdd:pfam12004  311 SSSPDW--PPARLRQQSSSSKGDSPETKQRTQHQQVPSPVNPSTLSpveRTAAWVLNMNGQYEEEESSGPE--------S 380

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553   908 KEELSQAEK---DLAVLQDKLRISTKKLEEYETLFKCQEETTQKLVLEYQARLEEGEERLRRQQEDKDIQMKGIISRLMS 984
Cdd:pfam12004  381 REELKQAEKyeqEISKLKERLRVSNRKLEEYERRLLAQEEQTQKLLLEYQARLEDSEERLRRQQEEKDSQMKSIISRLMA 460

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|.
gi 594591553   985 VEEELKKDHAEMQAAVDSKQKIIDAQEKRIASLDAANARLMSALTQLKERY 1035
Cdd:pfam12004  461 VEEELKKDHAEMQAVIDSKQKIIDAQEKRIASLDAANARLMSALTQLKERY 511
RasGAP_DAB2IP cd05136
Ras-GTPase Activating Domain of DAB2IP and similar proteins; The DAB2IP family of Ras ...
 209-532 0e+00

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


:

Pssm-ID: 213338  Cd Length: 324  Bit Score: 615.75  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553  209 RYQTVSILPMEMYKEFAEHITNHYLGLCAALEPILSAKTKEEMASALVHILQSTGKVKDFLTDLMMSEVDRCgDNEHLIF 288
Cdd:cd05136     1 RYQSVDILPLEVYKEFLEYLTNNYLDLCEVLEPVLSVKAKEELATALVHILQSTGKAKEFLTDLVMAEVDRL-DDEHLIF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553  289 RENTLATKAIEEYLKLVGQKYLQDALGEFIKALYESDENCEVDPSKCS-SADLPEHQGNLKMCCELAFCKIINSYCVFPR 367
Cdd:cd05136    80 RGNTLATKAMEAYLKLVGQKYLQETLGEFIRALYESEEDCEVDPSKCPpSASLSRNQANLRRSVELAWCKILSSHCVFPR 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553  368 ELKEVFASWRQECSSRGRPDISERLISASLFLRFLCPAIMSPSLFNLLQEYPDDRTARTLTLIAKVTQNLANFAKFGSKE 447
Cdd:cd05136   160 ELREVFSSWRERLEERGREDIADRLISASLFLRFLCPAILSPSLFNLTQEYPSERAARNLTLIAKVIQNLANFTRFGGKE 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553  448 EYMSFMNQFLEHEWTNMQRFLLEISNPETLSNTAGFEGYIDLGRELSSLHSLLWEAVSQLDQSVVSKLGPLPRILRDVHT 527
Cdd:cd05136   240 EYMEFMNDFVEQEWPNMKQFLQEISSPSPSSNSSDFDGYIDLGRELSLLHSLLVEIISKLNQTTLDKLGPLPRILNDITE 319


                  ....*
gi 594591553  528 ALSTP 532
Cdd:cd05136   320 ALRNP 324
PH-like super family cl17171
Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like ...
 1-137 8.09e-86

Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like and IRS-like PTB domains, the ran-binding domain, the EVH1 domain, a domain in neurobeachin and the third domain of FERM. All of these domains have a PH fold, but lack significant sequence similarity. They are generally involved in targeting to protein to the appropriate cellular location or interacting with a binding partner. This domain family possesses multiple functions including the ability to bind inositol phosphates and to other proteins.


The actual alignment was detected with superfamily member cd13376:

Pssm-ID: 473070  Cd Length: 182  Bit Score: 274.66  E-value: 8.09e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553    1 MPRLKESRSHESLLSPSSAVEALDLSMEEEVIIKPVHSSILGQDYCFEVTTSSGSKCFSCRSAAERDKWMENLRRAVHPN 80
Cdd:cd13376    46 MPRLKESRSHESLLSPSSAVEALDLSMEEEVVIKPVHSSILGQDYCFEVTTSSGSKCFSCRSAAERDKWMENLRRAVHPN 125

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 594591553   81 KDNSRRVEHILKLWVIEAKDLPAKKKYLCELCLDDVLYARTTSKLKTDNVFWGEHFE 137
Cdd:cd13376   126 KDNSRRVENMLKLWIIEAKDLPAKKKYLCELCLDDVLYARTTCKLKTDNVFWGEHFE 182
C2_SynGAP_like cd04013
C2 domain present in Ras GTPase activating protein (GAP) family; SynGAP, GAP1, RasGAP, and ...
 79-218 1.14e-80

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: 259.16  E-value: 1.14e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553   79 PNKDNSRRVEHILKLWVIEAKDLPAKKKYLCELCLDDVLYARTTSKLKTDNVFWGEHFEFHNLPPLRTVTVHLYRETDKK 158
Cdd:cd04013     1 PNRDNSRRTENSLKLWIIEAKGLPPKKRYYCELCLDKTLYARTTSKLKTDTLFWGEHFEFSNLPPVSVITVNLYRESDKK 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 594591553  159 KKKERNSYLGLVSLPAASVAGRQFVEKWYPVVTPNP------KGGKGPGPMIRIKARYQTVSILPM 218
Cdd:cd04013    81 KKKDKSQLIGTVNIPVTDVSSRQFVEKWYPVSTPKGngksggKEGKGESPSIRIKARYQSTRVLPL 146
 
Name Accession Description Interval E-value
DUF3498 pfam12004
Domain of unknown function (DUF3498); This presumed domain is functionally uncharacterized. ...
 522-1035 0e+00

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


Pssm-ID: 463427 [Multi-domain]  Cd Length: 511  Bit Score: 681.10  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553   522 LRDVHTALSTPGSGQLPG--TNDLASTPGSGSSSVSAGLQKMVIENDLsGLIDFTRLPSPTPENKDLFFVTRSSGVQPSP 599
Cdd:pfam12004    1 LRDITTALTNPTPIQQQLrrFSEHSSSPPVPGRSISSGLQKMFEDPDD-GLSDFTRLPSPTPENKDLFFVTRPPLLQPSP 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553   600 ARSSSYSEANEPDLQMANGSKSLSMVDLQDARTLDGEAgSPVGPDALPADGQVPATQLLAG---WPARAAPVSLAGLATV 676
Cdd:pfam12004   80 ARSSSYSDANEPDQQLPNGNKSLSMVDLQDSRSLQGSP-SPPLHDAPLNLSQAGSQASVGLrpaWAARTSQGNPQSAPQV 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553   677 RRAVPTPTTPGTSEgapgrPQLLAPLSFQNPVYQMAAGLPLSPRGLG--DSGSEGHSSLSSHSNSEELAAAAK----LGS 750
Cdd:pfam12004  159 RRPLQTPVTQGTRP-----QQLLAPLSFQNPVYHMAAGLPVSPRGLGspDSSSETHSSFSSHSNSEDLSSAAAnkksGPS 233

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553   751 FSTAAEELARRPGELARRQMSLTEKGGQPTVPRQNSAGPQRRIDQPPPPPPPPPPAPRGRtppTLLSTLQYPRPSSGTLA 830
Cdd:pfam12004  234 NSSYSEDFARRSTEFTRRQLSLTELQHQPAVPRQNSAGPQRRIDQQGLGGPPLTRGRTPP---SLLNSASYPRPSSGSLM 310

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553   831 SASPDWagPGTRLRQQSSSSKGDSPELKPRAMHKQGPSPVSPNALD---RTAAWLLTMNAQLLEDEGLGPDpphrdrlrS 907
Cdd:pfam12004  311 SSSPDW--PPARLRQQSSSSKGDSPETKQRTQHQQVPSPVNPSTLSpveRTAAWVLNMNGQYEEEESSGPE--------S 380

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553   908 KEELSQAEK---DLAVLQDKLRISTKKLEEYETLFKCQEETTQKLVLEYQARLEEGEERLRRQQEDKDIQMKGIISRLMS 984
Cdd:pfam12004  381 REELKQAEKyeqEISKLKERLRVSNRKLEEYERRLLAQEEQTQKLLLEYQARLEDSEERLRRQQEEKDSQMKSIISRLMA 460

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|.
gi 594591553   985 VEEELKKDHAEMQAAVDSKQKIIDAQEKRIASLDAANARLMSALTQLKERY 1035
Cdd:pfam12004  461 VEEELKKDHAEMQAVIDSKQKIIDAQEKRIASLDAANARLMSALTQLKERY 511
RasGAP_DAB2IP cd05136
Ras-GTPase Activating Domain of DAB2IP and similar proteins; The DAB2IP family of Ras ...
 209-532 0e+00

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


Pssm-ID: 213338  Cd Length: 324  Bit Score: 615.75  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553  209 RYQTVSILPMEMYKEFAEHITNHYLGLCAALEPILSAKTKEEMASALVHILQSTGKVKDFLTDLMMSEVDRCgDNEHLIF 288
Cdd:cd05136     1 RYQSVDILPLEVYKEFLEYLTNNYLDLCEVLEPVLSVKAKEELATALVHILQSTGKAKEFLTDLVMAEVDRL-DDEHLIF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553  289 RENTLATKAIEEYLKLVGQKYLQDALGEFIKALYESDENCEVDPSKCS-SADLPEHQGNLKMCCELAFCKIINSYCVFPR 367
Cdd:cd05136    80 RGNTLATKAMEAYLKLVGQKYLQETLGEFIRALYESEEDCEVDPSKCPpSASLSRNQANLRRSVELAWCKILSSHCVFPR 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553  368 ELKEVFASWRQECSSRGRPDISERLISASLFLRFLCPAIMSPSLFNLLQEYPDDRTARTLTLIAKVTQNLANFAKFGSKE 447
Cdd:cd05136   160 ELREVFSSWRERLEERGREDIADRLISASLFLRFLCPAILSPSLFNLTQEYPSERAARNLTLIAKVIQNLANFTRFGGKE 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553  448 EYMSFMNQFLEHEWTNMQRFLLEISNPETLSNTAGFEGYIDLGRELSSLHSLLWEAVSQLDQSVVSKLGPLPRILRDVHT 527
Cdd:cd05136   240 EYMEFMNDFVEQEWPNMKQFLQEISSPSPSSNSSDFDGYIDLGRELSLLHSLLVEIISKLNQTTLDKLGPLPRILNDITE 319


                  ....*
gi 594591553  528 ALSTP 532
Cdd:cd05136   320 ALRNP 324
RasGAP smart00323
GTPase-activator protein for Ras-like GTPases; All alpha-helical domain that accelerates the ...
 204-522 4.84e-113

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: 353.54  E-value: 4.84e-113
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553    204 IRIKARYQTVSILPMEMYKEFAEHITNHYLG-LCAALEPILSAKTKEEMASALVHILQSTGKVKDFLTDLMMSEVDRCgD 282
Cdd:smart00323    9 LRLKTVYTTDFILPSEYYEELLELLLFSLDLsLASALSEVCSGLDKDELATKLVRLFLRRGRGHPFLRALIDPEVERT-D 87

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553    283 NEHLIFRENTLATKAIEEYLKLVGQKYLQDALGEFIKALYESDENCEVDPSKCSSADLPEHQGNLKMCCELAFCKIINSY 362
Cdd:smart00323   88 DPNTIFRGNSLATKSMEVYMKLVGNQYLHTTLKPVLKKIVESKKSCEVDPAKLEGEDLETNLENLLQYVERLFDAIINSS 167

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553    363 CVFPRELKEVFASWRQECSSR-GRPDISERLISASLFLRFLCPAIMSPSLFNLLQEYPDDRTARTLTLIAKVTQNLANFA 441
Cdd:smart00323  168 DRLPYGLRDICKQLRQAAEKRfPDADVIYKAVSSFVFLRFFCPAIVSPKLFNLVDEHPDPTTRRTLTLIAKVLQNLANLS 247

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553    442 KFGSKEEYMSFMNQFLEHEWTNMQRFLLEISNPETLSNTAGFEGYIDLGRELSSLHSLLWEAVSQLDQsVVSKLGPLPRI 521
Cdd:smart00323  248 EFGSKEPWMEPLNDFLLSHKDRVKDFLDELSSVPEILVDKVSDSTTISGRELSLLHSLLLENGDALKR-ELNNEDPLGKL 326


                    .
gi 594591553    522 L 522
Cdd:smart00323  327 L 327
PH_DAB2IP cd13376
DOC-2/Disabled homolog 2-interacting protein Pleckstrin homology (PH) domain; DAB2IP (also ...
 1-137 8.09e-86

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: 274.66  E-value: 8.09e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553    1 MPRLKESRSHESLLSPSSAVEALDLSMEEEVIIKPVHSSILGQDYCFEVTTSSGSKCFSCRSAAERDKWMENLRRAVHPN 80
Cdd:cd13376    46 MPRLKESRSHESLLSPSSAVEALDLSMEEEVVIKPVHSSILGQDYCFEVTTSSGSKCFSCRSAAERDKWMENLRRAVHPN 125

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 594591553   81 KDNSRRVEHILKLWVIEAKDLPAKKKYLCELCLDDVLYARTTSKLKTDNVFWGEHFE 137
Cdd:cd13376   126 KDNSRRVENMLKLWIIEAKDLPAKKKYLCELCLDDVLYARTTCKLKTDNVFWGEHFE 182
C2_SynGAP_like cd04013
C2 domain present in Ras GTPase activating protein (GAP) family; SynGAP, GAP1, RasGAP, and ...
 79-218 1.14e-80

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: 259.16  E-value: 1.14e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553   79 PNKDNSRRVEHILKLWVIEAKDLPAKKKYLCELCLDDVLYARTTSKLKTDNVFWGEHFEFHNLPPLRTVTVHLYRETDKK 158
Cdd:cd04013     1 PNRDNSRRTENSLKLWIIEAKGLPPKKRYYCELCLDKTLYARTTSKLKTDTLFWGEHFEFSNLPPVSVITVNLYRESDKK 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 594591553  159 KKKERNSYLGLVSLPAASVAGRQFVEKWYPVVTPNP------KGGKGPGPMIRIKARYQTVSILPM 218
Cdd:cd04013    81 KKKDKSQLIGTVNIPVTDVSSRQFVEKWYPVSTPKGngksggKEGKGESPSIRIKARYQSTRVLPL 146
RasGAP pfam00616
GTPase-activator protein for Ras-like GTPase; All alpha-helical domain that accelerates the ...
 268-439 1.21e-28

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: 114.30  E-value: 1.21e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553   268 FLTDLMMSEVDRCgDNEHLIFRENTLATKAIEEYLKL-VGQKYLQDALGEFIKALYESDE-NCEVDPSK----------- 334
Cdd:pfam00616    1 LISELIEEEIESS-DNPNDLLRGNSLVSKLLETYNRRpRGQEYLKKVLGPLVRKIIEDEDlDLESDPRKiyeslinqeel 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553   335 -CSSADLP-------------------EHQGNLKMCCELAFCKIINSYCVFPREL----KEVFASWRQECssrgrPDISE 390
Cdd:pfam00616   80 kTGRSDLPrdvspeeaiedpevrqifeDNLQKLRELADEFLDAIYSSLNQLPYGIryicKQLYELLEEKF-----PDASE 154

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 594591553   391 R----LISASLFLRFLCPAIMSPSLFNLLQEYPDDRTARTLTLIAKVTQNLAN 439
Cdd:pfam00616  155 EeilnAIGGFLFLRFFCPAIVNPDLFGLVDHQISPKQRRNLTLIAKVLQNLAN 207
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 90-186 3.24e-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: 55.19  E-value: 3.24e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553     90 ILKLWVIEAKDLPAKKKYL-----CELCLDDVLY--ARTTSKLKTDNVFWGEHFEFH-NLPPLRTVTVHLYretDKKKKK 161
Cdd:smart00239    1 TLTVKIISARNLPPKDKGGksdpyVKVSLDGDPKekKKTKVVKNTLNPVWNETFEFEvPPPELAELEIEVY---DKDRFG 77

                            90       100
                    ....*....|....*....|....*
gi 594591553    162 eRNSYLGLVSLPAASVAGRQFVEKW 186
Cdd:smart00239   78 -RDDFIGQVTIPLSDLLLGGRHEKL 101
C2 pfam00168
C2 domain;
89-189 7.78e-09

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 54.25  E-value: 7.78e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553    89 HILKLWVIEAKDLPAKKK------YlCELCLDDVLY-ARTTSKLKTDNVFWGEHFEFH-NLPPLRTVTVHLYretDKKKK 160
Cdd:pfam00168    1 GRLTVTVIEAKNLPPKDGngtsdpY-VKVYLLDGKQkKKTKVVKNTLNPVWNETFTFSvPDPENAVLEIEVY---DYDRF 76

                           90       100
                   ....*....|....*....|....*....
gi 594591553   161 KeRNSYLGLVSLPAASVAGRQFVEKWYPV 189
Cdd:pfam00168   77 G-RDDFIGEVRIPLSELDSGEGLDGWYPL 104
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 25-78 2.39e-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: 47.16  E-value: 2.39e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 594591553     25 LSMEEEVIIKPVHSSILGQDYCFEVTTSSG-SKCFSCRSAAERDKWMENLRRAVH 78
Cdd:smart00233   48 IDLSGCTVREAPDPDSSKKPHCFEIKTSDRkTLLLQAESEEEREKWVEALRKAIA 102
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 896-1035 5.05e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 50.83  E-value: 5.05e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553   896 GPDPPHRDRLRSKEELSQAEKDLAVLQDKLRISTKKLEEYETLF-----------KCQEETTQKLVLEYQ--ARLEEGEE 962
Cdd:TIGR02168  664 GSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELeeleeeleqlrKELEELSRQISALRKdlARLEAEVE 743

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 594591553   963 RLRRQQEDKDIQMKGIISRLMSVEEELKKDHAEMQAAVDSKQKI---IDAQEKRIASLDAANARLMSALTQLKERY 1035
Cdd:TIGR02168  744 QLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELeaqIEQLKEELKALREALDELRAELTLLNEEA 819
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 886-1040 1.60e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.16  E-value: 1.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553  886 NAQLLEDEGLgpdppHRDRLRSKEELSQAEKDLAVLQDKLRISTKKLEEYETlfkcQEETTQKLVLEYQARLEEGEERLR 965
Cdd:COG1196   228 ELLLLKLREL-----EAELEELEAELEELEAELEELEAELAELEAELEELRL----ELEELELELEEAQAEEYELLAELA 298

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 594591553  966 RQQEDKDIQMKGIIsRLMSVEEELKKDHAEMQAAVDSKQKIIDAQEKRIASLDAANARLMSALTQLKERYSMQAR 1040
Cdd:COG1196   299 RLEQDIARLEERRR-ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
908-1033 4.83e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 47.37  E-value: 4.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553  908 KEELSQAEKDLAVLQDKLRISTKKLEEYETLFKCQEETTQKLVlEYQARLEEGEERLRRQQEDKDI--QMKGIISRLMSV 985
Cdd:PRK03918  306 LDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLK-ELEKRLEELEERHELYEEAKAKkeELERLKKRLTGL 384

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 594591553  986 E-EELKKdhaEMQAAVDSKQKIIDAQEK---RIASLDAANARLMSALTQLKE 1033
Cdd:PRK03918  385 TpEKLEK---ELEELEKAKEEIEEEISKitaRIGELKKEIKELKKAIEELKK 433
 
Name Accession Description Interval E-value
DUF3498 pfam12004
Domain of unknown function (DUF3498); This presumed domain is functionally uncharacterized. ...
 522-1035 0e+00

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


Pssm-ID: 463427 [Multi-domain]  Cd Length: 511  Bit Score: 681.10  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553   522 LRDVHTALSTPGSGQLPG--TNDLASTPGSGSSSVSAGLQKMVIENDLsGLIDFTRLPSPTPENKDLFFVTRSSGVQPSP 599
Cdd:pfam12004    1 LRDITTALTNPTPIQQQLrrFSEHSSSPPVPGRSISSGLQKMFEDPDD-GLSDFTRLPSPTPENKDLFFVTRPPLLQPSP 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553   600 ARSSSYSEANEPDLQMANGSKSLSMVDLQDARTLDGEAgSPVGPDALPADGQVPATQLLAG---WPARAAPVSLAGLATV 676
Cdd:pfam12004   80 ARSSSYSDANEPDQQLPNGNKSLSMVDLQDSRSLQGSP-SPPLHDAPLNLSQAGSQASVGLrpaWAARTSQGNPQSAPQV 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553   677 RRAVPTPTTPGTSEgapgrPQLLAPLSFQNPVYQMAAGLPLSPRGLG--DSGSEGHSSLSSHSNSEELAAAAK----LGS 750
Cdd:pfam12004  159 RRPLQTPVTQGTRP-----QQLLAPLSFQNPVYHMAAGLPVSPRGLGspDSSSETHSSFSSHSNSEDLSSAAAnkksGPS 233

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553   751 FSTAAEELARRPGELARRQMSLTEKGGQPTVPRQNSAGPQRRIDQPPPPPPPPPPAPRGRtppTLLSTLQYPRPSSGTLA 830
Cdd:pfam12004  234 NSSYSEDFARRSTEFTRRQLSLTELQHQPAVPRQNSAGPQRRIDQQGLGGPPLTRGRTPP---SLLNSASYPRPSSGSLM 310

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553   831 SASPDWagPGTRLRQQSSSSKGDSPELKPRAMHKQGPSPVSPNALD---RTAAWLLTMNAQLLEDEGLGPDpphrdrlrS 907
Cdd:pfam12004  311 SSSPDW--PPARLRQQSSSSKGDSPETKQRTQHQQVPSPVNPSTLSpveRTAAWVLNMNGQYEEEESSGPE--------S 380

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553   908 KEELSQAEK---DLAVLQDKLRISTKKLEEYETLFKCQEETTQKLVLEYQARLEEGEERLRRQQEDKDIQMKGIISRLMS 984
Cdd:pfam12004  381 REELKQAEKyeqEISKLKERLRVSNRKLEEYERRLLAQEEQTQKLLLEYQARLEDSEERLRRQQEEKDSQMKSIISRLMA 460

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|.
gi 594591553   985 VEEELKKDHAEMQAAVDSKQKIIDAQEKRIASLDAANARLMSALTQLKERY 1035
Cdd:pfam12004  461 VEEELKKDHAEMQAVIDSKQKIIDAQEKRIASLDAANARLMSALTQLKERY 511
RasGAP_DAB2IP cd05136
Ras-GTPase Activating Domain of DAB2IP and similar proteins; The DAB2IP family of Ras ...
 209-532 0e+00

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


Pssm-ID: 213338  Cd Length: 324  Bit Score: 615.75  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553  209 RYQTVSILPMEMYKEFAEHITNHYLGLCAALEPILSAKTKEEMASALVHILQSTGKVKDFLTDLMMSEVDRCgDNEHLIF 288
Cdd:cd05136     1 RYQSVDILPLEVYKEFLEYLTNNYLDLCEVLEPVLSVKAKEELATALVHILQSTGKAKEFLTDLVMAEVDRL-DDEHLIF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553  289 RENTLATKAIEEYLKLVGQKYLQDALGEFIKALYESDENCEVDPSKCS-SADLPEHQGNLKMCCELAFCKIINSYCVFPR 367
Cdd:cd05136    80 RGNTLATKAMEAYLKLVGQKYLQETLGEFIRALYESEEDCEVDPSKCPpSASLSRNQANLRRSVELAWCKILSSHCVFPR 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553  368 ELKEVFASWRQECSSRGRPDISERLISASLFLRFLCPAIMSPSLFNLLQEYPDDRTARTLTLIAKVTQNLANFAKFGSKE 447
Cdd:cd05136   160 ELREVFSSWRERLEERGREDIADRLISASLFLRFLCPAILSPSLFNLTQEYPSERAARNLTLIAKVIQNLANFTRFGGKE 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553  448 EYMSFMNQFLEHEWTNMQRFLLEISNPETLSNTAGFEGYIDLGRELSSLHSLLWEAVSQLDQSVVSKLGPLPRILRDVHT 527
Cdd:cd05136   240 EYMEFMNDFVEQEWPNMKQFLQEISSPSPSSNSSDFDGYIDLGRELSLLHSLLVEIISKLNQTTLDKLGPLPRILNDITE 319


                  ....*
gi 594591553  528 ALSTP 532
Cdd:cd05136   320 ALRNP 324
RasGAP smart00323
GTPase-activator protein for Ras-like GTPases; All alpha-helical domain that accelerates the ...
 204-522 4.84e-113

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: 353.54  E-value: 4.84e-113
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553    204 IRIKARYQTVSILPMEMYKEFAEHITNHYLG-LCAALEPILSAKTKEEMASALVHILQSTGKVKDFLTDLMMSEVDRCgD 282
Cdd:smart00323    9 LRLKTVYTTDFILPSEYYEELLELLLFSLDLsLASALSEVCSGLDKDELATKLVRLFLRRGRGHPFLRALIDPEVERT-D 87

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553    283 NEHLIFRENTLATKAIEEYLKLVGQKYLQDALGEFIKALYESDENCEVDPSKCSSADLPEHQGNLKMCCELAFCKIINSY 362
Cdd:smart00323   88 DPNTIFRGNSLATKSMEVYMKLVGNQYLHTTLKPVLKKIVESKKSCEVDPAKLEGEDLETNLENLLQYVERLFDAIINSS 167

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553    363 CVFPRELKEVFASWRQECSSR-GRPDISERLISASLFLRFLCPAIMSPSLFNLLQEYPDDRTARTLTLIAKVTQNLANFA 441
Cdd:smart00323  168 DRLPYGLRDICKQLRQAAEKRfPDADVIYKAVSSFVFLRFFCPAIVSPKLFNLVDEHPDPTTRRTLTLIAKVLQNLANLS 247

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553    442 KFGSKEEYMSFMNQFLEHEWTNMQRFLLEISNPETLSNTAGFEGYIDLGRELSSLHSLLWEAVSQLDQsVVSKLGPLPRI 521
Cdd:smart00323  248 EFGSKEPWMEPLNDFLLSHKDRVKDFLDELSSVPEILVDKVSDSTTISGRELSLLHSLLLENGDALKR-ELNNEDPLGKL 326


                    .
gi 594591553    522 L 522
Cdd:smart00323  327 L 327
PH_DAB2IP cd13376
DOC-2/Disabled homolog 2-interacting protein Pleckstrin homology (PH) domain; DAB2IP (also ...
 1-137 8.09e-86

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: 274.66  E-value: 8.09e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553    1 MPRLKESRSHESLLSPSSAVEALDLSMEEEVIIKPVHSSILGQDYCFEVTTSSGSKCFSCRSAAERDKWMENLRRAVHPN 80
Cdd:cd13376    46 MPRLKESRSHESLLSPSSAVEALDLSMEEEVVIKPVHSSILGQDYCFEVTTSSGSKCFSCRSAAERDKWMENLRRAVHPN 125

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 594591553   81 KDNSRRVEHILKLWVIEAKDLPAKKKYLCELCLDDVLYARTTSKLKTDNVFWGEHFE 137
Cdd:cd13376   126 KDNSRRVENMLKLWIIEAKDLPAKKKYLCELCLDDVLYARTTCKLKTDNVFWGEHFE 182
C2_SynGAP_like cd04013
C2 domain present in Ras GTPase activating protein (GAP) family; SynGAP, GAP1, RasGAP, and ...
 79-218 1.14e-80

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: 259.16  E-value: 1.14e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553   79 PNKDNSRRVEHILKLWVIEAKDLPAKKKYLCELCLDDVLYARTTSKLKTDNVFWGEHFEFHNLPPLRTVTVHLYRETDKK 158
Cdd:cd04013     1 PNRDNSRRTENSLKLWIIEAKGLPPKKRYYCELCLDKTLYARTTSKLKTDTLFWGEHFEFSNLPPVSVITVNLYRESDKK 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 594591553  159 KKKERNSYLGLVSLPAASVAGRQFVEKWYPVVTPNP------KGGKGPGPMIRIKARYQTVSILPM 218
Cdd:cd04013    81 KKKDKSQLIGTVNIPVTDVSSRQFVEKWYPVSTPKGngksggKEGKGESPSIRIKARYQSTRVLPL 146
PH_SynGAP cd13375
Synaptic Ras-GTPase activating protein Pleckstrin homology (PH) domain; SynGAP is a member of ...
 1-137 1.81e-79

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: 257.70  E-value: 1.81e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553    1 MPRLKESRSHESLLSPSSAVEALDLSMEEEVIIKPVHSSILGQDYCFEVTTSSGSKCFSCRSAAERDKWMENLRRAVHPN 80
Cdd:cd13375    53 MQSFKESHSHESLLSPSSAAEALDLNLDEDSIIKPVHSSILGQEFCFEVTTASGTKCFACRSAAERDKWIENLQRAVKPN 132

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 594591553   81 KDNSRRVEHILKLWVIEAKDLPAKKKYLCELCLDDVLYARTTSKLKTDNVFWGEHFE 137
Cdd:cd13375   133 KDNSRRVDNVLKLWIIEARELPPKKRYYCELCLDDMLYARTTSKPRTDTVFWGEHFE 189
RasGAP cd04519
Ras GTPase Activating Domain; RasGAP functions as an enhancer of the hydrolysis of GTP that is ...
 221-473 2.39e-74

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


Pssm-ID: 213328  Cd Length: 256  Bit Score: 246.25  E-value: 2.39e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553  221 YKEFAEHITNHYLGLCAALEPILSAKTKEEMASALVHILQSTGKVKDFLTDLMMSEVDRCgDNEHLIFRENTLATKAIEE 300
Cdd:cd04519     3 YRLLSLLLTESPLALLRELSQVLPVKDKEEVATALLRIFESRGLALEFLRYLVRSEVKNT-KNPNTLFRGNSLATKLLDQ 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553  301 YLKLVGQKYLQDALGEFIKALYESDENCEVDPSKCSSADLPEHQGNLKMCCELAFCKIINSYCVFPRELKEVFASWRQEC 380
Cdd:cd04519    82 YMKLVGQEYLKETLSPLIREILESKESCEIDTKLPVGEDLEENLENLLELVNKLVDRILSSLDRLPPELRYVFKILREFL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553  381 SSR--GRPDISERLISASLFLRFLCPAIMSPSLFNLLQEYPDDRTARTLTLIAKVTQNLANFAKFGSKEEYMSFMNQFLE 458
Cdd:cd04519   162 AERfpEEPDEAYQAVSGFLFLRFICPAIVSPELFGLVPDEPSEQARRNLTLISKVLQSLANGVEFGDKEPFMKPLNDFIK 241

                         250
                  ....*....|....*
gi 594591553  459 HEWTNMQRFLLEISN 473
Cdd:cd04519   242 SNKPKLKQFLDELSS 256
RasGAP_CLA2_BUD2 cd05137
Ras-GTPase Activating Domain of CLA2/BUD2; CLA2/BUD2 functions as a GTPase-activating protein ...
 207-458 1.36e-55

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: 197.02  E-value: 1.36e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553  207 KARYQTVSILPMEMYKEFAEHITNHYLGLCAALEPILSAKTKEEMASALVHILQSTGKVKDFLTDLMMSEVD-------- 278
Cdd:cd05137     1 KVRLDENVVLPSKNYKPLEELLHNFDLGLTLQIAELVPGDKLERLSEILLDIFQASGREDEWFMALVEDEIDgidkstsk 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553  279 -----RCGDNEH-LIFRENTLATKAIEEYLKLVGQKYLQDALGEFIKALYESDENCEVDPSKCSSA-------DLPEHQG 345
Cdd:cd05137    81 nkdmgKSSNNEAnLLFRGNSLLTKSLEKYMRRIGKEYLEKSIGDVIRKICEENKDCEVDPSRVKESdsiekeeDLEENWE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553  346 NLKMCCELAFCKIINSYCVFPRELKEVFASWRQECSSRGRPDISE-RL--ISASLFLRFLCPAIMSPSLFNLLQEYPDDR 422
Cdd:cd05137   161 NLISLTEEIWNSIYITSNDCPPELRKILKHIRAKVEDRYGDFLRTvTLnsVSGFLFLRFFCPAILNPKLFGLLKDHPRPR 240

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 594591553  423 TARTLTLIAKVTQNLANFAKFGSKEEYMSFMNQFLE 458
Cdd:cd05137   241 AQRTLTLIAKVLQNLANLTTFGQKEPWMEPMNEFLT 276
RasGAP_GAP1_like cd05128
Ras-GTPase Activating Domain of GAP1 and similar proteins; The GAP1 family of Ras ...
 234-474 1.10e-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: 180.14  E-value: 1.10e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553  234 GLCAALEPILSAKtKEEMASALVHILQSTGKVKDFLTDLMMSEVDRCGDnEHLIFRENTLATKAIEEYLKLVGQKYLQDA 313
Cdd:cd05128    22 SAVYLLEELVKVD-KDDVARPLVRIFLHHGQIVPLLRALASREISKTQD-PNTLFRGNSLASKCMDEFMKLVGMQYLHET 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553  314 LGEFIKALYESDENCEVDPSKCSSADLPE-HQGNLKMCCELAFCKIINSYCVFPRELKEVFASWRQECSSR--GRPDISE 390
Cdd:cd05128   100 LKPVIDEIFSEKKSCEIDPSKLKDGEVLEtNLANLRGYVERVFKAITSSARRCPTLMCEIFSDLRESAAQRfpDNEDVPY 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553  391 RLISASLFLRFLCPAIMSPSLFNLLQEYPDDRTARTLTLIAKVTQNLANFAKFGS----KEEYMS-FMNQFL-EHEWTNM 464
Cdd:cd05128   180 TAVSGFIFLRFFAPAILNPKLFGLREEHPDPQTARTLTLISKTIQTLGNLGSSSSglgvKEAYMSpLYERFTdEQHVDAV 259

                         250
                  ....*....|
gi 594591553  465 QRFLLEISNP 474
Cdd:cd05128   260 KKFLDRISSV 269
PH_RasSynGAP-like cd13262
Synaptic Ras-GTPase activating protein family Pleckstrin homology (PH) domain; The RasSynGAP ...
 1-87 1.65e-46

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: 162.60  E-value: 1.65e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553    1 MPRLKESRSHESLLSPSSAveALDLSMEEEVIIKPVHSSILGQDYCFEVTTSSGSKCFSCRSAAERDKWMENLRRAVHPN 80
Cdd:cd13262    41 GPRLRGSRSHESLLSSSSA--ALDLSADEDVVIRPLHSSILGRKHCFQVTTSEGTRCFSCRSAAERDRWIEDLRRAAQPN 118


                  ....*..
gi 594591553   81 KDNSRRV 87
Cdd:cd13262   119 KDNCRRT 125
RasGAP_Neurofibromin_like cd05392
Ras-GTPase Activating Domain of proteins similar to neurofibromin; Neurofibromin-like proteins ...
 217-513 4.29e-46

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: 168.62  E-value: 4.29e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553  217 PMEMYKEFAEHITNHYLGLCAALEpILSAKTKEEMASALVHILQSTGKVKDFLTDLMMSEVDRCgDNEHLIFRENTLATK 296
Cdd:cd05392     2 KSEAYDELLELLIEDPQLLLAIAE-VCPSSEVDLLAQSLLNLFETRNRLLPLISWLIEDEISHT-SRAADLFRRNSVATR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553  297 AIEEYLKLVGQKYLQDALGEFIKALYESDENCEVDPSKCSSADLPEHQGNLKMCCELAFCKIINSYCVFPRELKEVFASW 376
Cdd:cd05392    80 LLTLYAKSVGNKYLRKVLRPLLTEIVDNKDYFEVEKIKPDDENLEENADLLMKYAQMLLDSITDSVDQLPPSFRYICNTI 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553  377 RQECSSRgRPDISERLISASLFLRFLCPAIMSPSLFNLLQEYPDDRTARTLTLIAKVTQNLANFAKFGSKEEYMSFMNQF 456
Cdd:cd05392   160 YESVSKK-FPDAALIAVGGFLFLRFICPAIVSPESENLLDPPPTPEARRSLILIAKVLQNIANGVLFSLKEPYLESLNEF 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 594591553  457 LEHEWTNMQRFLLEISNPETLSNTAGFEGYIDLGRELSSLHSLLWEAVSQLDQSVVS 513
Cdd:cd05392   239 LKKNSDRIQQFLSEVSTIPPTDPIFDESDEEPITADLRYLHKFLYLHFLEIRKEVLK 295
PH_nGAP cd13373
Neuronal growth-associated proteins Pleckstrin homology (PH) domain; nGAP (also called RASAL2 ...
 1-93 4.31e-44

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: 156.04  E-value: 4.31e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553    1 MPRLKESRSHESLLSPSSAVEALDLSMEEEVIIKPVHSSILGQDYCFEVTTSSGSKCFSCRSAAERDKWMENLRRAVHPN 80
Cdd:cd13373    46 LPKLKESRSHESLLSPGSAVEALDLGREEKVSVKPLHSSILGQDFCFEVTYSSGSKCFSCSSAAERDKWMENLRRTVQPN 125

                          90
                  ....*....|...
gi 594591553   81 KDNSRRVEHILKL 93
Cdd:cd13373   126 KDNCRRAENVLRL 138
RasGAP_p120GAP cd05391
Ras-GTPase Activating Domain of p120; p120GAP is a negative regulator of Ras that stimulates ...
 215-499 5.56e-43

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: 159.96  E-value: 5.56e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553  215 ILPMEMYKEFAEHITNHYLGLCAALEPiLSAKTKEEMASALVHILQSTGKVKDFLTDLMMSEVDRcGDNEHLIFRENTLA 294
Cdd:cd05391     4 IMPEEEYSELKELILQKELHVVYALAH-VCGQDRTLLASILLRIFRHEKLESLLLRTLNDREISM-EDEATTLFRATTLA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553  295 TKAIEEYLKLVGQKYLQDALGEFIKALYESDENCEVDPSKCSSADlpEHQGNLKMCCELAFC---KIINSYCVFPRELKE 371
Cdd:cd05391    82 STLMEQYMKATATPFVHHALKDTILKILESKQSCELNPSKLEKNE--DVNTNLEHLLNILSElveKIFMAAEILPPTLRY 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553  372 VFaSWRQECSSRGRPD---ISERLISASLFLRFLCPAIMSPSLFNLLQEYPDDRTARTLTLIAKVTQNLANFAKFGSKEE 448
Cdd:cd05391   160 IY-GCLQKSVQQKWPTnttVRTRVVSGFVFLRLICPAILNPRMFNIISETPSPTAARTLTLVAKSLQNLANLVEFGAKEP 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 594591553  449 YMSFMNQFLEHEWTNMQRFLLEISN-PETLSNTAGFEGyiDLGRELSSLHSL 499
Cdd:cd05391   239 YMEGVNPFIKKNKERMIMFLDELGNvPELPDTTEHSRT--DLSRDLAALHEI 288
RasGAP_RASA3 cd05134
Ras-GTPase Activating Domain of RASA3; RASA3 (or GAP1_IP4BP) is a member of the GAP1 family ...
 246-473 6.79e-39

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: 145.94  E-value: 6.79e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553  246 KTKEEMASALVHILQSTGKVKDFLTDLMMSEVDRCGDnEHLIFRENTLATKAIEEYLKLVGQKYLQDALGEFIKALYESD 325
Cdd:cd05134    33 REKQEAAIPLVRLFLHYGKIVPFISAIASAEVNRTQD-PNTIFRGNSLTSKCIDETMKLAGMHYLQVTLKPIIDEICQEH 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553  326 ENCEVDPSKCS-SADLPEHQGNLKMCCELAFCKIINSYCVFPRELKEVFASWRQECSSR--GRPDISERLISASLFLRFL 402
Cdd:cd05134   112 KPCEIDPVKLKdGENLENNRENLRQYVDRIFRVITKSGVSCPTVMCDIFFSLRESAAKRfqVDPDVRYTAVSSFIFLRFF 191

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 594591553  403 CPAIMSPSLFNLLQEYPDDRTARTLTLIAKVTQNLANFAKFGS---KEEYM-SFMNQFLEHEWTN-MQRFLLEISN 473
Cdd:cd05134   192 APAILSPNLFQLTPHHPDPQTSRTLTLISKTIQTLGSLSKSKSanfKESYMaAFYDYFNEQKYADaVKNFLDLISS 267
RasGAP_Neurofibromin cd05130
Ras-GTPase Activating Domain of neurofibromin; Neurofibromin is the product of the ...
 250-502 1.04e-33

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: 132.83  E-value: 1.04e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553  250 EMASALVHILQSTGKVKDFLTDLMMSEVDRCGDNEHLiFRENTLATKAIEEYLKLVGQKYLQDALGEFIKALYESDE--N 327
Cdd:cd05130    41 ELARVLVTLFDSKHLLYQLLWNMFSKEVELADSMQTL-FRGNSLASKIMTFCFKVYGATYLQSLLEPLLRTMITSSEwvS 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553  328 CEVDPSKC-SSADLPEHQGNLKMCCELAFCKIINSYCVFPRELKEVFASWRQECSSRGrPDISERLISASLFLRFLCPAI 406
Cdd:cd05130   120 YEVDPTRLeGNENLEENQRNLLQLTEKFFHAIISSSDEFPPQLRSVCHCLYQVVSHRF-PNSGLGAVGSAIFLRFINPAI 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553  407 MSPSLFNLLQEYPDDRTARTLTLIAKVTQNLANFAKFgSKEEYMSFMNQFLEHEWTNMQRFLLEI-SNPETLSNTAG-FE 484
Cdd:cd05130   199 VSPYEYGILDREPPPRVKRGLKLMSKILQNIANHVLF-TKEAHMLPFNDFLRNHFEAGRRFFSSIaSDCGAVDGPSSkYL 277

                         250
                  ....*....|....*...
gi 594591553  485 GYIDLGrELSSLHSLLWE 502
Cdd:cd05130   278 SFINDA-NVLALHRLLWN 294
PH_RASAL3 cd13374
RAS protein activator like-3 Pleckstrin homology (PH) domain; RASAL3 is thought to be a Ras ...
 3-102 7.36e-31

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: 118.58  E-value: 7.36e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553    3 RLKESRSHESLL------SPSSAVEA---------LDLSMEEEVIIKPVHSSILGQDYCFEVTTSSGSKCFSCRSAAERD 67
Cdd:cd13374    28 RLKEKKKAKAEStgtgrdGPPSALGSreslatiseLDLGAERDVRVWPLHPSLLGEPHCFQVTWPGGSRCFSCRSAAERD 107

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 594591553   68 KWMENLRRAVHPNKDNSRRVEHILKLWVIEAKDLP 102
Cdd:cd13374   108 RWIEDLRRSFQPHQDNVEREETWLSVWVHEAKGLP 142
RasGAP_RASAL cd05135
Ras-GTPase Activating Domain of RASAL1 and similar proteins; Ras GTPase activating-like ...
 237-468 8.75e-30

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


Pssm-ID: 213337  Cd Length: 287  Bit Score: 120.30  E-value: 8.75e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553  237 AALEPILSAKTKEEMASALVHILQSTGKVKDFLTDLMMSEVDRCGDNEHLiFRENTLATKAIEEYLKLVGQKYLQDALGE 316
Cdd:cd05135    29 AMLEEVTTGESRQDVATKLVKIFLGQGLVVPFLDYLNTREVGRTTDPNTL-FRSNSLASKSMEQFMKVVGMPYLHEVLKP 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553  317 FIKALYESDENCEVDPSK--------------CSSADLPEH-----QGNLKMCCElafcKIINSYCVFPRELKEVFASWR 377
Cdd:cd05135   108 VINRIFEEKKYVELDPCKidlnrtrrisfkgsLSEAQVRESslellQGYLGSIID----AIVGSVDQCPPVMRVAFKQLH 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553  378 QECSSR----GRPDISERLISASLFLRFLCPAIMSPSLFNLLQEYPDDRTARTLTLIAKVTQNLANF-AKFGS-KEEYMS 451
Cdd:cd05135   184 KRVEERfpeaEHQDVKYLAISGFLFLRFFAPAILTPKLFQLREQHADPRTSRTLLLLAKAVQSIGNLgLQLGQgKEQWMA 263

                         250
                  ....*....|....*..
gi 594591553  452 FMNQFLEHEWTNMQRFL 468
Cdd:cd05135   264 PLHPFILQSVARVKDFL 280
RasGAP_RASA2 cd05394
Ras-GTPase Activating Domain of RASA2; RASA2 (or GAP1(m)) is a member of the GAP1 family of ...
 255-475 2.90e-29

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: 118.46  E-value: 2.90e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553  255 LVHILQSTGKVKDFLTDLMMSEVDRCGDnEHLIFRENTLATKAIEEYLKLVGQKYLQDALGEFIKALYESDENCEVDPSK 334
Cdd:cd05394    42 LVRLLLHHNKLVPFVAAVAALDLKDTQE-ANTIFRGNSLATRCLDEMMKIVGKHYLKVTLKPVLDEICESPKPCEIDPIK 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553  335 CSSADLPE-HQGNLKMCCELAFCKIINSYCVFPRELKEVFASWRQECSSR--GRPDISERLISASLFLRFLCPAIMSPSL 411
Cdd:cd05394   121 LKEGDNVEnNKENLRYYVDKVFFSIVKSSMSCPTLMCDVFRSLRHLAVKRfpNDPHVQYSAVSSFVFLRFFAVAVVSPHT 200

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 594591553  412 FNLLQEYPDDRTARTLTLIAKVTQNLANFAKFGS------KEEYM-SFMNQFLEHEWT-NMQRFLLEISNPE 475
Cdd:cd05394   201 FQLRPHHPDAQTSRTLTLISKTIQTLGSWGSLSKsklssfKETFMcDFFKMFQEEKYIeKVKKFLDEISSTE 272
RasGAP pfam00616
GTPase-activator protein for Ras-like GTPase; All alpha-helical domain that accelerates the ...
 268-439 1.21e-28

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: 114.30  E-value: 1.21e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553   268 FLTDLMMSEVDRCgDNEHLIFRENTLATKAIEEYLKL-VGQKYLQDALGEFIKALYESDE-NCEVDPSK----------- 334
Cdd:pfam00616    1 LISELIEEEIESS-DNPNDLLRGNSLVSKLLETYNRRpRGQEYLKKVLGPLVRKIIEDEDlDLESDPRKiyeslinqeel 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553   335 -CSSADLP-------------------EHQGNLKMCCELAFCKIINSYCVFPREL----KEVFASWRQECssrgrPDISE 390
Cdd:pfam00616   80 kTGRSDLPrdvspeeaiedpevrqifeDNLQKLRELADEFLDAIYSSLNQLPYGIryicKQLYELLEEKF-----PDASE 154

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 594591553   391 R----LISASLFLRFLCPAIMSPSLFNLLQEYPDDRTARTLTLIAKVTQNLAN 439
Cdd:pfam00616  155 EeilnAIGGFLFLRFFCPAIVNPDLFGLVDHQISPKQRRNLTLIAKVLQNLAN 207
RasGAP_RASA4 cd05395
Ras-GTPase Activating Domain of RASA4; Ras GTPase activating-like 4 protein (RASAL4), also ...
 235-475 2.76e-25

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: 107.26  E-value: 2.76e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553  235 LCAALEPILSAKTKEEMASALVHILQSTGKVKDFLTDLMMSEVDRCGDNEHLiFRENTLATKAIEEYLKLVGQKYLQDAL 314
Cdd:cd05395    27 LISLIDETTTAECRQEVATNLVKLFLGQGLAKEFLDLLFQLELDKTTEPNTL-FRSNSLASKSMESFLKVAGMQYLHSVL 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553  315 GEFIKALYESDENCEVDPSK-------CSSADLPEHQGN--------LKMCCELAFCKIINSYCVFPRELKEVFASWRQE 379
Cdd:cd05395   106 GPTINRVFEEKKYVELDPSKveikdvgCSGLHRIQTESEvieqsaqlLQSYLGELLSAISKSVKYCPAVIRATFRQLFKR 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553  380 CSSRgRPDISER-----LISASLFLRFLCPAIMSPSLFNLLQEYPDDRTARTLTLIAKVTQNLANFAKFGS--KEEYMSF 452
Cdd:cd05395   186 VQER-FPENQHQnvkfiAVTSFLCLRFFSPAIMSPKLFHLREKHADARTSRTLLLLAKAVQNVGNMDTLASraKEAWMAP 264

                         250       260
                  ....*....|....*....|...
gi 594591553  453 MNQFLEHEWTNMQRFLLEISNPE 475
Cdd:cd05395   265 LQPAIQQGVAQLKDFITKLVDIE 287
RasGAP_GAPA cd05132
Ras-GTPase Activating Domain of GAPA; GAPA is an IQGAP-related protein and is predicted to ...
 289-519 1.16e-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: 1.16e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553  289 RENTLATKAIEEYLKLV-GQKYLQDALGEFIKALYE-SDENCEVDPSKC-------------------------SSADLP 341
Cdd:cd05132    49 RANTAVSRMMTTYTRRGpGQSYLKTVLADRINDLISlKDLNLEINPLKVyeqmindieldtglpsnlprgitpeEAAENP 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553  342 EHQG----NLKMCCELA---FCKIINSYCVFPRELKEVFASWRQECSSRgRPDISER----LISASLFLRFLCPAIMSPS 410
Cdd:cd05132   129 AVQNiiepRLEMLEEITnsfLEAIINSLDEVPYGIRWICKQIRSLTRRK-FPDASDEticsLIGGFFLLRFINPAIVSPQ 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553  411 LFNLLQEYPDDRTARTLTLIAKVTQNLANFAKFgSKEEYMSFMNQFLEHEWTNMQRFLLEISNPETLSNTAGFEGYIDLG 490
Cdd:cd05132   208 AYMLVDGKPSDNTRRTLTLIAKLLQNLANKPSY-SKEPYMAPLQPFVEENKERLNKFLNDLCEVDDFYESLELDQYIALS 286

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 594591553  491 R----------ELSSLHSLLWEAVSQLDQS-------VVSKLGPLP 519
Cdd:cd05132   287 KkdlsinitlnEIYNTHSLLVKHLAELAPDhndhlrlILQELGPAP 332
C2A_RasGAP cd08383
C2 domain (first repeat) of Ras GTPase activating proteins (GAPs); RasGAPs suppress Ras ...
 91-210 1.19e-11

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: 62.67  E-value: 1.19e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553   91 LKLWVIEAKDLPAKKK---YlCELCLDDVLYARTTSKLKTdNVFWGEHFEFHNLPPL---RTVTVHLYretdKKKKKERN 164
Cdd:cd08383     2 LRLRILEAKNLPSKGTrdpY-CTVSLDQVEVARTKTVEKL-NPFWGEEFVFDDPPPDvtfFTLSFYNK----DKRSKDRD 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 594591553  165 SYLGLVSLpaASVAGRQFVEKWYPVVTPNPKGGKgPGpMIRIKARY 210
Cdd:cd08383    76 IVIGKVAL--SKLDLGQGKDEWFPLTPVDPDSEV-QG-SVRLRARY 117
C2 cd00030
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
 91-188 4.57e-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: 60.54  E-value: 4.57e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553   91 LKLWVIEAKDLPAKKK-----YLCELCLDDVLYARTTSKLKTDNVFWGEHFEFHNLPPL-RTVTVHLYretDKKKKKeRN 164
Cdd:cd00030     1 LRVTVIEARNLPAKDLngksdPYVKVSLGGKQKFKTKVVKNTLNPVWNETFEFPVLDPEsDTLTVEVW---DKDRFS-KD 76

                          90       100
                  ....*....|....*....|....*
gi 594591553  165 SYLGLVSLPAASVAGR-QFVEKWYP 188
Cdd:cd00030    77 DFLGEVEIPLSELLDSgKEGELWLP 101
C2_Ras_p21A1 cd08400
C2 domain present in RAS p21 protein activator 1 (RasA1); RasA1 is a GAP1 (GTPase activating ...
 91-210 8.33e-11

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: 60.46  E-value: 8.33e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553   91 LKLWVIEAKDLPAKK---KYlCELCLDDVLYARTTSKLKTDNVfWGEHFEFHNLPP-LRTVTVHLYretdKKKKKERNSY 166
Cdd:cd08400     6 LQLNVLEAHKLPVKHvphPY-CVISLNEVKVARTKVREGPNPV-WSEEFVFDDLPPdVNSFTISLS----NKAKRSKDSE 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 594591553  167 LGLVSLPAASVAGRQFVEKWYPVVTPNPKGGKGPGpMIRIKARY 210
Cdd:cd08400    80 IAEVTVQLSKLQNGQETDEWYPLSSASPLKGGEWG-SLRIRARY 122
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 90-186 3.24e-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: 55.19  E-value: 3.24e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553     90 ILKLWVIEAKDLPAKKKYL-----CELCLDDVLY--ARTTSKLKTDNVFWGEHFEFH-NLPPLRTVTVHLYretDKKKKK 161
Cdd:smart00239    1 TLTVKIISARNLPPKDKGGksdpyVKVSLDGDPKekKKTKVVKNTLNPVWNETFEFEvPPPELAELEIEVY---DKDRFG 77

                            90       100
                    ....*....|....*....|....*
gi 594591553    162 eRNSYLGLVSLPAASVAGRQFVEKW 186
Cdd:smart00239   78 -RDDFIGQVTIPLSDLLLGGRHEKL 101
C2 pfam00168
C2 domain;
89-189 7.78e-09

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 54.25  E-value: 7.78e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553    89 HILKLWVIEAKDLPAKKK------YlCELCLDDVLY-ARTTSKLKTDNVFWGEHFEFH-NLPPLRTVTVHLYretDKKKK 160
Cdd:pfam00168    1 GRLTVTVIEAKNLPPKDGngtsdpY-VKVYLLDGKQkKKTKVVKNTLNPVWNETFTFSvPDPENAVLEIEVY---DYDRF 76

                           90       100
                   ....*....|....*....|....*....
gi 594591553   161 KeRNSYLGLVSLPAASVAGRQFVEKWYPV 189
Cdd:pfam00168   77 G-RDDFIGEVRIPLSELDSGEGLDGWYPL 104
RasGAP_IQGAP2 cd05131
Ras-GTPase Activating Domain of IQ motif containing GTPase activating protein 2; IQGAP2 is a ...
 295-543 1.80e-07

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: 54.62  E-value: 1.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553  295 TKAIEEYLKLVGQkyLQDALGEFIKALYE-SDENCEVDPSkcSSADLPEHQGNLKMCCELAFCKIINSYCVFPRELKEVF 373
Cdd:cd05131    87 TNPVEVYKAWVNQ--LETATGEASKLPYDvTTEQALTHPE--VVNKLESSIQSLRSVTDKVLGSIFSSLDLIPYGMRYIA 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553  374 ASWRQECSSRgRPDISE----RLISASLFLRFLCPAIMSPSLFNLL------QEYPDDRtaRTLTLIAKVTQNLANFAKF 443
Cdd:cd05131   163 KVLKNSLHEK-FPDATEdellKIVGNLLYYRYMNPAIVAPDGFDIIdmtaggQIHSEQR--RNLGSVAKVLQHAASNKLF 239

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553  444 GSKEEYMSFMNQFLEHEWTNMQRFL---LEISNPETLSNTAGFEGYIDLGR--------ELSSLHSLLWE---AVSQlDQ 509
Cdd:cd05131   240 EGENAHLSSMNSYLSQTYQKFRKFFqaaCDVPEPEEKFNIDEYSDMVTLSKpviyisieEIINTHSLLLEhqdAIAP-DQ 318

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 594591553  510 S-----VVSKLGPLPrilrDVHTALstpGSGQLpGTNDL 543
Cdd:cd05131   319 NdllheLLKDLGEVP----DVESFL---GEGTV-DPNDP 349
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 25-78 2.39e-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: 47.16  E-value: 2.39e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 594591553     25 LSMEEEVIIKPVHSSILGQDYCFEVTTSSG-SKCFSCRSAAERDKWMENLRRAVH 78
Cdd:smart00233   48 IDLSGCTVREAPDPDSSKKPHCFEIKTSDRkTLLLQAESEEEREKWVEALRKAIA 102
RasGAP_IQGAP_like cd05127
Ras-GTPase Activating Domain of IQ motif containing GTPase activating proteins; This family ...
 397-524 4.17e-06

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: 49.89  E-value: 4.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553  397 LFLRFLCPAIMSPSLFNLLQEYPDDRTA----RTLTLIAKVTQNLANFAKFGSKEEYMSFMNQFLEHEWTNMQRFLLEIS 472
Cdd:cd05127   179 LYYRYMNPAIVAPEAFDIIDLSVGGQLSplqrRNLGSIAKVLQQAASGKLFGGENPYLSPLNPYISESHEKFKKFFLEAC 258

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 594591553  473 NPETLSNTAGFEGYIDLG-----------RELSSLHSLLWEavsQLDQSVVSKLGPLPRILRD 524
Cdd:cd05127   259 TVPEAEEHFNIDEYSDLTmltkptiyislQEIFATHKLLLE---HQDEIAPDPDDPLRELLDD 318
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 896-1035 5.05e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 50.83  E-value: 5.05e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553   896 GPDPPHRDRLRSKEELSQAEKDLAVLQDKLRISTKKLEEYETLF-----------KCQEETTQKLVLEYQ--ARLEEGEE 962
Cdd:TIGR02168  664 GSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELeeleeeleqlrKELEELSRQISALRKdlARLEAEVE 743

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 594591553   963 RLRRQQEDKDIQMKGIISRLMSVEEELKKDHAEMQAAVDSKQKI---IDAQEKRIASLDAANARLMSALTQLKERY 1035
Cdd:TIGR02168  744 QLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELeaqIEQLKEELKALREALDELRAELTLLNEEA 819
C2A_C2C_Synaptotagmin_like cd08391
C2 domain first and third repeat in Synaptotagmin-like proteins; Synaptotagmin is a ...
 89-188 1.09e-05

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: 45.75  E-value: 1.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553   89 HILKLWVIEAKDLPAKKKYLCEL--------CLDDVLYARTTSKLKTDNV--FWGEHFEF--HNLPPLrTVTVHLYretD 156
Cdd:cd08391     1 GVLRIHVIEAQDLVAKDKFVGGLvkgksdpyVIVRVGAQTFKSKVIKENLnpKWNEVYEAvvDEVPGQ-ELEIELF---D 76

                          90       100       110
                  ....*....|....*....|....*....|..
gi 594591553  157 KKKKKErnSYLGLVSLPAASVAGRQFVEKWYP 188
Cdd:cd08391    77 EDPDKD--DFLGRLSIDLGSVEKKGFIDEWLP 106
C2A_MCTP_PRT_plant cd04022
C2 domain first repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP); ...
 95-188 1.16e-05

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: 45.79  E-value: 1.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553   95 VIEAKDLPAKKKY-----LCELCLDDVLYaRTTSKLKTDNVFWGEHFEF--HNLPPLRTVTVHLYRETDKKKKKeRNSYL 167
Cdd:cd04022     6 VVDAQDLMPKDGQgsssaYVELDFDGQKK-RTRTKPKDLNPVWNEKLVFnvSDPSRLSNLVLEVYVYNDRRSGR-RRSFL 83

                          90       100
                  ....*....|....*....|..
gi 594591553  168 GLVSLPAASVAGRQ-FVEKWYP 188
Cdd:cd04022    84 GRVRISGTSFVPPSeAVVQRYP 105
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 886-1040 1.60e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.16  E-value: 1.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553  886 NAQLLEDEGLgpdppHRDRLRSKEELSQAEKDLAVLQDKLRISTKKLEEYETlfkcQEETTQKLVLEYQARLEEGEERLR 965
Cdd:COG1196   228 ELLLLKLREL-----EAELEELEAELEELEAELEELEAELAELEAELEELRL----ELEELELELEEAQAEEYELLAELA 298

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 594591553  966 RQQEDKDIQMKGIIsRLMSVEEELKKDHAEMQAAVDSKQKIIDAQEKRIASLDAANARLMSALTQLKERYSMQAR 1040
Cdd:COG1196   299 RLEQDIARLEERRR-ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
908-1036 3.14e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 47.59  E-value: 3.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553  908 KEELSQAEKDLAVLQDKLRISTKKLEEYETlfkcQEETTQKLVLEYQARLEEGEERLRRQQEDKDiQMKGIISRLMSVEE 987
Cdd:COG4372    51 REELEQAREELEQLEEELEQARSELEQLEE----ELEELNEQLQAAQAELAQAQEELESLQEEAE-ELQEELEELQKERQ 125

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 594591553  988 ELKKDHAEMQAAVDSKQKIIDAQEKRIASLDAANARLMSALTQLKERYS 1036
Cdd:COG4372   126 DLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQ 174
RasGAP_IQGAP1 cd05133
Ras-GTPase Activating Domain of IQ motif containing GTPase activating protein 1; IQGAP1 is a ...
 386-489 3.58e-05

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: 47.35  E-value: 3.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553  386 PDISE----RLISASLFLRFLCPAIMSPSLFNLL------QEYPDDRtaRTLTLIAKVTQNLANFAKFGSKEEYMSFMNQ 455
Cdd:cd05133   174 PDAGEdellKIVGNLLYYRYMNPAIVAPDAFDIIdlsaggQLTTDQR--RNLGSIAKMLQHAASNKMFLGDNAHLSPINE 251

                          90       100       110
                  ....*....|....*....|....*....|....
gi 594591553  456 FLEHEWTNMQRFLLEISNPETLSNTAGFEGYIDL 489
Cdd:cd05133   252 YLSQSYQKFRRFFQAACDVPELEDKFNVDEYSDL 285
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 908-1033 3.93e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.01  E-value: 3.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553  908 KEELSQAEKDLAVLQDKLRISTKKLEEYETLFKCQEETTQKLVLEyQARLEEGEERLRRQQEDKDIQMKGIISRLMSVEE 987
Cdd:COG1196   273 RLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER-LEELEEELAELEEELEELEEELEELEEELEEAEE 351

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 594591553  988 ELKKDHAEMQAAVDSKQKIIDAQEKRIASLDAANARLMSALTQLKE 1033
Cdd:COG1196   352 ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE 397
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
908-1033 4.83e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 47.37  E-value: 4.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553  908 KEELSQAEKDLAVLQDKLRISTKKLEEYETLFKCQEETTQKLVlEYQARLEEGEERLRRQQEDKDI--QMKGIISRLMSV 985
Cdd:PRK03918  306 LDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLK-ELEKRLEELEERHELYEEAKAKkeELERLKKRLTGL 384

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 594591553  986 E-EELKKdhaEMQAAVDSKQKIIDAQEK---RIASLDAANARLMSALTQLKE 1033
Cdd:PRK03918  385 TpEKLEK---ELEELEKAKEEIEEEISKitaRIGELKKEIKELKKAIEELKK 433
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 903-1041 6.04e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 47.36  E-value: 6.04e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553   903 DRLRS-KEELSQAEKDLAVLQDKLRISTKKLEEYETLF----------KCQEETTQKLVLEYQARLEEGEERLRRQQE-- 969
Cdd:TIGR02168  232 LRLEElREELEELQEELKEAEEELEELTAELQELEEKLeelrlevselEEEIEELQKELYALANEISRLEQQKQILRErl 311

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 594591553   970 ---DKDIQMK-GIISRLMSVEEELKKDHAEMQAAVDSKQKIIDAQEKRIASLDAANARLMSALTQLKERYSMQARN 1041
Cdd:TIGR02168  312 anlERQLEELeAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSK 387
RasGAP_IQGAP3 cd12207
Ras-GTPase Activating Domain of IQ motif containing GTPase activating protein 3; This family ...
 397-534 6.48e-05

Ras-GTPase Activating Domain of IQ motif containing GTPase activating protein 3; This family represents the IQ motif containing GTPase activating protein 3 (IQGAP3), which associates with Ras GTP-binding proteins. 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: 213346 [Multi-domain]  Cd Length: 350  Bit Score: 46.36  E-value: 6.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553  397 LFLRFLCPAIMSPSLFNLLQE------YPDDRtaRTLTLIAKVTQNLANFAKFGSKEEYMSFMNQFLEHEWTNMQRFLLE 470
Cdd:cd12207   189 LYYRFMNPAVVAPDGFDIVDCsaggalQPEQR--RMLGSVAKVLQHAAANKHFQGDSEHLQALNQYLEETHVKFRKFILQ 266

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553  471 ---ISNPETLSNTAGFEG---------YIDLGrELSSLHSLLWEAVSQL--DQS-----VVSKLGPLPRILRDVHTALST 531
Cdd:cd12207   267 accVPEPEERFNVDEYSEmvavakpviYITVG-ELINTHKLLLEHQDSIapDHSdplheLLEDLGEVPTVQSLIGESWAD 345


                  ...
gi 594591553  532 PGS 534
Cdd:cd12207   346 LGD 348
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 903-1034 6.97e-05

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 45.69  E-value: 6.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553  903 DRLRSK-----EELSQAEKDLAVLQDKLRISTKKLEEYETLFKCQE---ETTQKLVLEYQARLEEG------------EE 962
Cdd:COG1579    20 DRLEHRlkelpAELAELEDELAALEARLEAAKTELEDLEKEIKRLEleiEEVEARIKKYEEQLGNVrnnkeyealqkeIE 99

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 594591553  963 RLRRQQEDKDIQMKGIISRLmsveEELKKDHAEMQAAVDSKQKIIDAQEKRiasLDAANARLMSALTQLKER 1034
Cdd:COG1579   100 SLKRRISDLEDEILELMERI----EELEEELAELEAELAELEAELEEKKAE---LDEELAELEAELEELEAE 164
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
906-1039 9.08e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 46.05  E-value: 9.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553  906 RSKEELSQAEKDLAVLQDKLRISTKKLEEYETLfkcQEETTQKLvleyqARLEEGEERLRRQQEdkdiQMKGIISRLMSV 985
Cdd:COG4372    63 QLEEELEQARSELEQLEEELEELNEQLQAAQAE---LAQAQEEL-----ESLQEEAEELQEELE----ELQKERQDLEQQ 130

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 594591553  986 EEELKKDHAEMQAAVDSKQKIIDAQEKRIASLDAANARLMSALTQLKERYSMQA 1039
Cdd:COG4372   131 RKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQA 184
C2A_Rasal1_RasA4 cd04054
C2 domain first repeat present in RasA1 and RasA4; Rasal1 and RasA4 are both members of GAP1 ...
 95-186 3.01e-04

C2 domain first repeat present in RasA1 and RasA4; Rasal1 and RasA4 are both members of GAP1 (GTPase activating protein 1). Rasal1 responds to repetitive Ca2+ signals by associating with the plasma membrane and deactivating Ras. RasA4 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. Both of these proteins contains two C2 domains, a Ras-GAP domain, a plextrin homology (PH)-like domain, and a Bruton's Tyrosine Kinase (BTK) 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: 176018 [Multi-domain]  Cd Length: 121  Bit Score: 41.73  E-value: 3.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553   95 VIEAKDLPAK-----KKYLCELCLDDVLYARTTSKLKTDNVFWGEHFEFHNLPPLRTVTVHLYREtdkkKKKERNSYLGL 169
Cdd:cd04054     6 IVEGKNLPAKditgsSDPYCIVKVDNEVIIRTATVWKTLNPFWGEEYTVHLPPGFHTVSFYVLDE----DTLSRDDVIGK 81

                          90
                  ....*....|....*...
gi 594591553  170 VSLPAASVAGR-QFVEKW 186
Cdd:cd04054    82 VSLTREVISAHpRGIDGW 99
C2A_RasA2_RasA3 cd08401
C2 domain first repeat present in RasA2 and RasA3; RasA2 and RasA3 are GAP1s (GTPase ...
 93-189 1.05e-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: 40.11  E-value: 1.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553   93 LWVI-EAKDLPAKKK------YLCELCLDDVLYARTTSKLKTDNVFWGEHFEFHNLPPLRTVTVHLYretdKKKKKERNS 165
Cdd:cd08401     3 KIKIgEAKNLPPRSGpnkmrdCYCTVNLDQEEVFRTKTVEKSLCPFFGEDFYFEIPRTFRHLSFYIY----DRDVLRRDS 78

                          90       100
                  ....*....|....*....|....
gi 594591553  166 YLGLVSLPAASVAGRQFVEKWYPV 189
Cdd:cd08401    79 VIGKVAIKKEDLHKYYGKDTWFPL 102
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 908-1034 1.09e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.00  E-value: 1.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553  908 KEELSQAEKDLAVLQDKLRisTKKLEEYETlfkcQEETTQKLVLEYQARLEEGEERLRRQQEDkdiqmkgiISRLMSVEE 987
Cdd:COG1196   219 KEELKELEAELLLLKLREL--EAELEELEA----ELEELEAELEELEAELAELEAELEELRLE--------LEELELELE 284

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 594591553  988 ELKKDHAEMQAAVDSKQKIIDAQEKRIASLDAANARLMSALTQLKER 1034
Cdd:COG1196   285 EAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEE 331
Caldesmon pfam02029
Caldesmon;
842-1057 1.16e-03

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 42.93  E-value: 1.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553   842 RLRQ-QSSSSKGDSPELKPRAMHKQGPS-----PVSPNALDRTAAWLLTMnaQLLEDeglgpdpphRDRLRSKEELS-QA 914
Cdd:pfam02029   19 RRRQkEEEEPSGQVTESVEPNEHNSYEEdselkPSGQGGLDEEEAFLDRT--AKREE---------RRQKRLQEALErQK 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553   915 EKDLAVLQDKLRISTKK----LEEYET----------LFKCQEETTQKLVLEYQARL---------EEGEERLRRQQEDK 971
Cdd:pfam02029   88 EFDPTIADEKESVAERKenneEEENSSwekeekrdsrLGRYKEEETEIREKEYQENKwstevrqaeEEGEEEEDKSEEAE 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553   972 DIQmkgiisRLMSVEEELKKDHAEMQAAVDSKQKIIDAQEKRIASLDAANARLMSALTQLKERYSMQARNGVSPTNPTKL 1051
Cdd:pfam02029  168 EVP------TENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAE 241


                   ....*.
gi 594591553  1052 QITENG 1057
Cdd:pfam02029  242 VFLEAE 247
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
907-1033 1.47e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.20  E-value: 1.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553  907 SKEELSQAEKDLAVLQDKLRISTKKLEEYET--------LFKCQEE--TTQKLVLEYQARLEEGEERLRRQQEdkdiQMK 976
Cdd:COG4372    29 LSEQLRKALFELDKLQEELEQLREELEQAREeleqleeeLEQARSEleQLEEELEELNEQLQAAQAELAQAQE----ELE 104

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 594591553  977 GIISRLMSVEEELKKDHAEMQAAVDSKQKIIDAQEKRIASLDAANARLMSALTQLKE 1033
Cdd:COG4372   105 SLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLES 161
RasGAP_RAP6 cd05129
Ras-GTPase Activating Domain of Rab5-activating protein 6; Rab5-activating protein 6 (RAP6) is ...
 301-515 1.51e-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: 1.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553  301 YLKLVGQKYLQDALGEFIKALYESDE-NCEVDPSKC-------------SSADLPEHQGNLKMCCE------LAFCKII- 359
Cdd:cd05129   104 ELLFSAKLYLTAALHKPIMQVLVDDEiFLETDPQKAlcrfspaeqekrfGEEGTPEQQRKLQQYRAeflsrlVALVNKFi 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553  360 -----NSYCvFPRELKE-VFASWRQECSSRGRPDISERLISASL-FLRFLCPAIMSPSLFNLLQEYPDDRTAR-TLTLIA 431
Cdd:cd05129   184 sslrqSVYC-FPQSLRWiVRQLRKILTRSGDDEEAEARALCTDLlFTNFICPAIVNPEQYGIISDAPISEVARhNLMQVA 262

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553  432 KVTQNLAnFAKFGSKE-EYMSFMNQFLEHEWTNMQRFLLE----------ISNPETLSNTAGFEGYIDLGRELSSLHSLL 500
Cdd:cd05129   263 QILQVLA-LTEFESPDpRLKELLSKFDKDCVSAFLDVVIVgravetpppsSSALLEGSRTAVLITESDLATLVEFLRSVK 341

                         250
                  ....*....|....*
gi 594591553  501 WEAVSQLDQSVVSKL 515
Cdd:cd05129   342 TGDEEKEDQMALDNL 356
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
916-1044 1.57e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.45  E-value: 1.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553  916 KDLAVLQDKLRISTKKLEEYETLFKCQEETTQKLVlEYQARLEEGEERLRRQqeDKDIQMKGIISRLMSVEEELKKDHAE 995
Cdd:COG4717    71 KELKELEEELKEAEEKEEEYAELQEELEELEEELE-ELEAELEELREELEKL--EKLLQLLPLYQELEALEAELAELPER 147

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 594591553  996 MQAAVDSKQKIIDAQEkRIASLDAANARLMSALTQLKERYSMQARNGVS 1044
Cdd:COG4717   148 LEELEERLEELRELEE-ELEELEAELAELQEELEELLEQLSLATEEELQ 195
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 902-1034 1.64e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 41.45  E-value: 1.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553  902 RDRL-RSKEELSQAEKDLAVLQDKLRISTKKLEEYETlfKCQEETTQKlvlEYQARLEEgEERLRRQQEDKDIQMKGIIS 980
Cdd:COG1579    44 EARLeAAKTELEDLEKEIKRLELEIEEVEARIKKYEE--QLGNVRNNK---EYEALQKE-IESLKRRISDLEDEILELME 117

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 594591553  981 RLMSVEEELKKDHAEMQAAVDSKQKIIDAQEKRIASLDAANARLMSALTQLKER 1034
Cdd:COG1579   118 RIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
909-1024 1.92e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.06  E-value: 1.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553  909 EELSQAEKDLAVLQDKLRISTKKLEEYETLfkcqEETTQKLvleyQARLEEGEERLRRQQEDKDIQMKGIISRLMSVEEE 988
Cdd:COG4717   132 QELEALEAELAELPERLEELEERLEELREL----EEELEEL----EAELAELQEELEELLEQLSLATEEELQDLAEELEE 203

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 594591553  989 LKKDHAEMQAAVDSKQKIIDAQEKRIASLDAANARL 1024
Cdd:COG4717   204 LQQRLAELEEELEEAQEELEELEEELEQLENELEAA 239
C2_plant_PLD cd04015
C2 domain present in plant phospholipase D (PLD); PLD hydrolyzes terminal phosphodiester bonds ...
 167-210 2.25e-03

C2 domain present in plant phospholipase D (PLD); PLD hydrolyzes terminal phosphodiester bonds in diester glycerophospholipids resulting in the degradation of phospholipids. In vitro PLD transfers phosphatidic acid to primary alcohols. In plants PLD plays a role in germination, seedling growth, phosphatidylinositol metabolism, and changes in phospholipid composition. There is a single Ca(2+)/phospholipid-binding C2 domain in PLD. 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: 175982 [Multi-domain]  Cd Length: 158  Bit Score: 39.98  E-value: 2.25e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 594591553  167 LGLVSLPAASVAGRQFVEKWYPVVTPNPKGGKgPGPMIRIKARY 210
Cdd:cd04015   115 IGRAYIPVEDLLSGEPVEGWLPILDSNGKPPK-PGAKIRVSLQF 157
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
902-1026 2.28e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.43  E-value: 2.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553  902 RDRLRSKEELSQAEKDLAVLQDKLRISTKKLEEYETLFKCQEETTQKLVLEYQaRLEEGEERLRRQQEDKDIQMKGIISR 981
Cdd:COG4372    73 SELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQ-DLEQQRKQLEAQIAELQSEIAEREEE 151

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 594591553  982 LMSVEEELKKDHAEMQAAVDSKQKIIDAQ-EKRIASL-DAANARLMS 1026
Cdd:COG4372   152 LKELEEQLESLQEELAALEQELQALSEAEaEQALDELlKEANRNAEK 198
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 882-1038 2.91e-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: 41.98  E-value: 2.91e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553   882 LLTMNAQLLEDEGL---GPDPPHRDRLRSKEELSQAEKdlavLQDKLristKKLE-EYETLFKCQEETtQKLVLEYQARL 957
Cdd:TIGR02169  641 MVTLEGELFEKSGAmtgGSRAPRGGILFSRSEPAELQR----LRERL----EGLKrELSSLQSELRRI-ENRLDELSQEL 711

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553   958 EEGEERLRRQQedKDIQM-KGIISRLMSVEEELKKDHAEMQAAVDSKQKIIDAQEKRIASLDAANARLMSALTQLKERYS 1036
Cdd:TIGR02169  712 SDASRKIGEIE--KEIEQlEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLS 789


                   ..
gi 594591553  1037 MQ 1038
Cdd:TIGR02169  790 HS 791
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
882-1035 2.97e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.68  E-value: 2.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553  882 LLTMNAQLLEDEGLGPDPPHRDRLRSKEELSQAEKDLAVLQDKLRISTKKLEEYETLFkcQEETTQKLVLEYQARLEEGE 961
Cdd:COG4717   368 LEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEAL--DEEELEEELEELEEELEELE 445

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 594591553  962 ERLRRQQEDKdIQMKGIISRLMSvEEELkkdhAEMQAAVDSKQKIIDAQEKRIASLDAANARLMSALTQLKERY 1035
Cdd:COG4717   446 EELEELREEL-AELEAELEQLEE-DGEL----AELLQELEELKAELRELAEEWAALKLALELLEEAREEYREER 513
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 906-1055 3.14e-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: 3.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553   906 RSKEELSQAEKDLAVLQ----------DKLRISTKKLEEYETLFKCQEETTQKLVL-EYQARLEEGE------ERLRRQQ 968
Cdd:TIGR02169  174 KALEELEEVEENIERLDliidekrqqlERLRREREKAERYQALLKEKREYEGYELLkEKEALERQKEaierqlASLEEEL 253

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553   969 EDKDIQMKGIISRLMSVEEELKKDHAEMQAAVDSKQKIIdaqEKRIASLDAANARLMSALTQLK---ERYSMQARNGVSP 1045
Cdd:TIGR02169  254 EKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRV---KEKIGELEAEIASLERSIAEKErelEDAEERLAKLEAE 330

                          170
                   ....*....|
gi 594591553  1046 TNPTKLQITE 1055
Cdd:TIGR02169  331 IDKLLAEIEE 340
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 902-1034 3.40e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.46  E-value: 3.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553  902 RDRLRSKEELSQAEKDLAVLQDKLRISTKKLEEYETLFKCQEETTQKLVLEYQARLEEGEERLRRQQEDKDIQMkgiisR 981
Cdd:COG1196   316 ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL-----E 390

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 594591553  982 LMSVEEELKKDHAEMQAAVDSKQKIIDAQEKRIASLDAANARLMSALTQLKER 1034
Cdd:COG1196   391 ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEA 443
GOLGA2L5 pfam15070
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein ...
 875-997 4.49e-03

Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein family remains unknown. This family of proteins is thought to be found in the Golgi apparatus of eukaryotes.


Pssm-ID: 464485 [Multi-domain]  Cd Length: 521  Bit Score: 40.82  E-value: 4.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553   875 LDRTAAWLLTMNAQLLEDEGLGPDPPHRDRLRSKEELSQAEKDLAVLQDKLRISTKKLEEYETLfkCQEETTQKLVLEYQ 954
Cdd:pfam15070   55 LETSLAELKNQAAVPPAEEEQPPAGPSEEEQRLQEEAEQLQKELEALAGQLQAQVQDNEQLSRL--NQEQEQRLLELERA 132

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 594591553   955 ARLEeGEERLRRQQEDKDIQM-KGIISRLMSVEEELKKDHAEMQ 997
Cdd:pfam15070  133 AERW-GEQAEDRKQILEDMQSdRATISRALSQNRELKEQLAELQ 175
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 886-1035 4.49e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.20  E-value: 4.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553   886 NAQLLEDEglgpdpphRDRLRSKEELSQAEKDLAVLQDKLRISTKKLEEYETLFKCQEETTQKL--VLEYQAR----LEE 959
Cdd:TIGR02168  322 EAQLEELE--------SKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELeeQLETLRSkvaqLEL 393

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 594591553   960 GEERLRRQQEDKDIQMKGIISRLMSVEEELKKDHAEMQ-AAVDSKQKIIDAQEKRIASLDAANARLMSALTQLKERY 1035
Cdd:TIGR02168  394 QIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEeAELKELQAELEELEEELEELQEELERLEEALEELREEL 470
PH cd00821
Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are ...
 25-73 4.97e-03

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


Pssm-ID: 275388 [Multi-domain]  Cd Length: 92  Bit Score: 37.52  E-value: 4.97e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 594591553   25 LSMEEEVIIKPVHSSilGQDYCFEVTTSSGSK-CFSCRSAAERDKWMENL 73
Cdd:cd00821    45 IPLSGILEVEEVSPK--ERPHCFELVTPDGRTyYLQADSEEERQEWLKAL 92
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 908-1034 5.80e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.20  E-value: 5.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553  908 KEELSQAEKDLAVLQDKLRISTKKLEEYETlfkcQEETTQKLVLEYQARLEEGEE----RLRRQQED------------- 970
Cdd:COG3883    36 QAELDALQAELEELNEEYNELQAELEALQA----EIDKLQAEIAEAEAEIEERREelgeRARALYRSggsvsyldvllgs 111

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 594591553  971 KDI---------------QMKGIISRLMSVEEELKKDHAEMQAAVDSKQKIIDAQEKRIASLDAANARLMSALTQLKER 1034
Cdd:COG3883   112 ESFsdfldrlsalskiadADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAE 190
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
908-1034 7.10e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.67  E-value: 7.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553  908 KEELSQAEKDLAVLQDKLRISTKKLEEYETLFKCQEEttQKLVLEYQARLEEGEERLRRQQEDKDIqmkgiISRLMSVEE 987
Cdd:COG4913   623 EEELAEAEERLEALEAELDALQERREALQRLAEYSWD--EIDVASAEREIAELEAELERLDASSDD-----LAALEEQLE 695

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 594591553  988 ELKKDHAEMQAAvdskqkiIDAQEKRIASLDAANARLMSALTQLKER 1034
Cdd:COG4913   696 ELEAELEELEEE-------LDELKGEIGRLEKELEQAEEELDELQDR 735
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 906-1034 7.57e-03

Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 40.33  E-value: 7.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553  906 RSKEELSQAEKDLAVLQDKLRISTKKLEEYETLFKCQEETTQKLVleyqarlEEGEERLRRQQEDKDIQMKGIISRLMSV 985
Cdd:COG5185   374 KSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAA-------DRQIEELQRQIEQATSSNEEVSKLLNEL 446

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 594591553  986 EEELKKDHAEMQaaVDSKQKIIDAQEKRIASLDAANARLMSALTQLKER 1034
Cdd:COG5185   447 ISELNKVMREAD--EESQSRLEEAYDEINRSVRSKKEDLNEELTQIESR 493
PH_RASA1 cd13260
RAS p21 protein activator (GTPase activating protein) 1 Pleckstrin homology (PH) domain; RASA1 ...
 23-75 7.62e-03

RAS p21 protein activator (GTPase activating protein) 1 Pleckstrin homology (PH) domain; RASA1 (also called RasGap1 or p120) is a member of the RasGAP family of GTPase-activating proteins. RASA1 contains N-terminal SH2-SH3-SH2 domains, followed by two C2 domains, a PH domain, a RasGAP domain, and a BTK domain. Splice variants lack the N-terminal domains. It is a cytosolic vertebrate protein that acts as a suppressor of RAS via its C-terminal GAP domain function, enhancing the weak intrinsic GTPase activity of RAS proteins resulting in the inactive GDP-bound form of RAS, allowing control of cellular proliferation and differentiation. Additionally, it is involved in mitogenic signal transmission towards downstream interacting partners through its N-terminal SH2-SH3-SH2 domains. RASA1 interacts with a number of proteins including: G3BP1, SOCS3, ANXA6, Huntingtin, KHDRBS1, Src, EPHB3, EPH receptor B2, Insulin-like growth factor 1 receptor, PTK2B, DOK1, PDGFRB, HCK, Caveolin 2, DNAJA3, HRAS, GNB2L1 and NCK1. 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: 270080  Cd Length: 103  Bit Score: 36.94  E-value: 7.62e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 594591553   23 LDLSmeeEVIIKPVHSSILGQDYCFEVTTSSGSKC----FSCRSAAERDKWMENLRR 75
Cdd:cd13260    48 IDLS---YCSLYPVHDSLFGRPNCFQIVVRALNEStityLCADTAELAQEWMRALRA 101
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 906-1034 9.25e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.81  E-value: 9.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553  906 RSKEELSQAEKDLAVLQDKLRISTKKLEEY--------------ETLFKCQ--EETTQKL-----VLEYQARLEEGEERL 964
Cdd:COG3883    62 ALQAEIDKLQAEIAEAEAEIEERREELGERaralyrsggsvsylDVLLGSEsfSDFLDRLsalskIADADADLLEELKAD 141

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553  965 RRQQEDKDIQMKGIISRLMSVEEELKKDHAEMQAAVDSKQKIIDAQEKRIASLDAANARLMSALTQLKER 1034
Cdd:COG3883   142 KAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAA 211
RNase_Y_N pfam12072
RNase Y N-terminal region;
903-996 9.37e-03

RNase Y N-terminal region;


Pssm-ID: 463456 [Multi-domain]  Cd Length: 201  Bit Score: 38.71  E-value: 9.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591553   903 DRLRSKEE--------LSQAEKDLAVLQDKLRISTKKLEEyetlfkcQEETTQKLVLEYQARLEE--GeerlRRQQEDKD 972
Cdd:pfam12072   85 RRLLQKEEtldrkdesLEKKEESLEKKEKELEAQQQQLEE-------KEEELEELIEEQRQELERisG----LTSEEAKE 153

                           90       100
                   ....*....|....*....|....
gi 594591553   973 IQMKgiisrlmSVEEELKKDHAEM 996
Cdd:pfam12072  154 ILLD-------EVEEELRHEAAVM 170
 
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