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Conserved domains on  [gi|1034641847|ref|XP_011512212|]
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slit homolog 2 protein isoform X5 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LamG smart00282
Laminin G domain;
813-946 5.96e-37

Laminin G domain;


:

Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 135.54  E-value: 5.96e-37
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641847   813 NITLQIATDEDSGILLY---KGDKDHIAVELYRGRVRASYDTGSHPASAIYSVETINDGNFHIVELLALDQSLSLSVDGG 889
Cdd:smart00282    1 SISFSFRTTSPNGLLLYagsKGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTPLNDGQWHRVAVERNGRSVTLSVDGG 80

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034641847   890 NPKIITNLSKQSTLNFDSPLYVGGMPgksnvASLRQAPGQNGTSFHGCIRNLYINSE 946
Cdd:smart00282   81 NRVSGESPGGLTILNLDGPLYLGGLP-----EDLKLPPLPVTPGFRGCIRNLKVNGK 132
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
145-491 2.96e-25

Leucine-rich repeat (LRR) protein [Transcription];


:

Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 110.02  E-value: 2.96e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641847  145 TTVDCSNQKLNKIPEHIPQYTAELRLNNNEFTVLEATGIFKKLPQLRKINFSNNKITDIEEGAFEGASGVNEILLTSNRL 224
Cdd:COG4886      3 LLLLSLTLKLLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLL 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641847  225 ENVQ--HKMFKGLESLKTLMLRsnritcvGNDSFIGLSSVRLLSLYDNQITTVaPGAFDTLHSLSTLNLLANPfncncyl 302
Cdd:COG4886     83 SLLLlgLTDLGDLTNLTELDLS-------GNEELSNLTNLESLDLSGNQLTDL-PEELANLTNLKELDLSNNQ------- 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641847  303 awlgewlrkkrivtgnprcqkpyfLKEIPiqdvaiqdftcddgnddnscSPLSRCPTectcLdTVVRCSNKGLKVLPKGI 382
Cdd:COG4886    148 ------------------------LTDLP--------------------EPLGNLTN----L-KSLDLSNNQLTDLPEEL 178

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641847  383 PR--DVTELYLDGNQFTLVPKELSNYKHLTLIDLSNNRISTLSNqSFSNMTQLLTLILSYNRLRCIPprTFDGLKSLRLL 460
Cdd:COG4886    179 GNltNLKELDLSNNQITDLPEPLGNLTNLEELDLSGNQLTDLPE-PLANLTNLETLDLSNNQLTDLP--ELGNLTNLEEL 255

                          330       340       350
                   ....*....|....*....|....*....|.
gi 1034641847  461 SLHGNDISVVPEGAfnDLSALSHLAIGANPL 491
Cdd:COG4886    256 DLSNNQLTDLPPLA--NLTNLKTLDLSNNQL 284
PCC super family cl28216
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
 462-643 1.67e-11

polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) Polycystin is a huge protein of 4303aas. Its repeated leucine-rich (LRR) segment is found in many proteins. It contains 16 polycystic kidney disease (PKD) domains, one LDL-receptor class A domain, one C-type lectin family domain, and 16-18 putative TMSs in positions between residues 2200 and 4100. Polycystin-L has been shown to be a cation (Na+, K+ and Ca2+) channel that is activated by Ca2+. Two members of the PCC family (polycystin 1 and 2) are mutated in autosomal dominant polycystic kidney disease, and polycystin-L is deleted in mice with renal and retinal defects. Note: this model is restricted to the amino half.


The actual alignment was detected with superfamily member TIGR00864:

Pssm-ID: 188093 [Multi-domain]  Cd Length: 2740  Bit Score: 69.34  E-value: 1.67e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641847  462 LHGNDISVVPEGAFNDLSALSHLAIGANPLYCDCNMQWLSDWVKSE---YKEPGIARCAGPGEMADKLLLTTPSKKFTCq 538
Cdd:TIGR00864    2 ISNNKISTIEEGICANLCNLSEIDLSGNPFECDCGLARLPRWAEEKgvkVRQPEAALCAGPGALAGQPLLGIPLLDSGC- 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641847  539 gpvDVNILAkcnpCLSNPCKNDGTCNSDPVDFYRCTcPYGFKGQDCDVpihACISNPCKHGGTchlkeGEEDgfWCICAD 618
Cdd:TIGR00864   81 ---DEEYVA----CLKDNSSGGGAARSELVIFSAAH-EGLFQPEACNA---FCFSAGHGLAAL-----GEQG--ECLCGA 142

                          170       180
                   ....*....|....*....|....*
gi 1034641847  619 GFEGENCEVNVDDCEDNDCENNSTC 643
Cdd:TIGR00864  143 AQPSEANFACESLCSGPPPPPAAAC 167
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 706-742 5.85e-07

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


:

Pssm-ID: 238011  Cd Length: 38  Bit Score: 46.86  E-value: 5.85e-07
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1034641847  706 DFDDCQD-NKCKNGAHCTDAVNGYTCICPEGYSGLFCE 742
Cdd:cd00054      1 DIDECASgNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 628-664 1.03e-06

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


:

Pssm-ID: 238011  Cd Length: 38  Bit Score: 46.09  E-value: 1.03e-06
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1034641847  628 NVDDCED-NDCENNSTCVDGINNYTCLCPPEYTGELCE 664
Cdd:cd00054      1 DIDECASgNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 668-703 2.50e-05

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


:

Pssm-ID: 238011  Cd Length: 38  Bit Score: 42.24  E-value: 2.50e-05
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1034641847  668 DFCAQDlNPCQHDSKCILTPKGFKCDCTPGYVGEHC 703
Cdd:cd00054      3 DECASG-NPCQNGGTCVNTVGSYRCSCPPGYTGRNC 37
PCC super family cl28216
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
 33-96 1.44e-04

polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) Polycystin is a huge protein of 4303aas. Its repeated leucine-rich (LRR) segment is found in many proteins. It contains 16 polycystic kidney disease (PKD) domains, one LDL-receptor class A domain, one C-type lectin family domain, and 16-18 putative TMSs in positions between residues 2200 and 4100. Polycystin-L has been shown to be a cation (Na+, K+ and Ca2+) channel that is activated by Ca2+. Two members of the PCC family (polycystin 1 and 2) are mutated in autosomal dominant polycystic kidney disease, and polycystin-L is deleted in mice with renal and retinal defects. Note: this model is restricted to the amino half.


The actual alignment was detected with superfamily member TIGR00864:

Pssm-ID: 188093 [Multi-domain]  Cd Length: 2740  Bit Score: 46.23  E-value: 1.44e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034641847   33 LYNNTLQTITKGTFSPLRAIQTMHLAQNPFICDCHLKWLADYLHTNPIET---SGARCTSPRRLANK 96
Cdd:TIGR00864    2 ISNNKISTIEEGICANLCNLSEIDLSGNPFECDCGLARLPRWAEEKGVKVrqpEAALCAGPGALAGQ 68
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 760-787 8.89e-03

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


:

Pssm-ID: 238011  Cd Length: 38  Bit Score: 34.92  E-value: 8.89e-03
                           10        20
                   ....*....|....*....|....*...
gi 1034641847  760 CQNGAQCIVRINEPICQCLPGYQGEKCE 787
Cdd:cd00054     11 CQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
 
Name Accession Description Interval E-value
LamG smart00282
Laminin G domain;
813-946 5.96e-37

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 135.54  E-value: 5.96e-37
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641847   813 NITLQIATDEDSGILLY---KGDKDHIAVELYRGRVRASYDTGSHPASAIYSVETINDGNFHIVELLALDQSLSLSVDGG 889
Cdd:smart00282    1 SISFSFRTTSPNGLLLYagsKGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTPLNDGQWHRVAVERNGRSVTLSVDGG 80

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034641847   890 NPKIITNLSKQSTLNFDSPLYVGGMPgksnvASLRQAPGQNGTSFHGCIRNLYINSE 946
Cdd:smart00282   81 NRVSGESPGGLTILNLDGPLYLGGLP-----EDLKLPPLPVTPGFRGCIRNLKVNGK 132
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
 791-944 6.44e-33

Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.


Pssm-ID: 238058 [Multi-domain]  Cd Length: 151  Bit Score: 124.84  E-value: 6.44e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641847  791 SVNFiNKESYLQIP-SAKVRPQTNITLQIATDEDSGILLYKGDK---DHIAVELYRGRVRASYDTGSHPASaIYSVETIN 866
Cdd:cd00110      1 GVSF-SGSSYVRLPtLPAPRTRLSISFSFRTTSPNGLLLYAGSQnggDFLALELEDGRLVLRYDLGSGSLV-LSSKTPLN 78

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034641847  867 DGNFHIVELLALDQSLSLSVDGGNPKIITNLSKQSTLNFDSPLYVGGMPgksnvASLRQAPGQNGTSFHGCIRNLYIN 944
Cdd:cd00110     79 DGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLNLDGPLYLGGLP-----EDLKSPGLPVSPGFVGCIRDLKVN 151
Laminin_G_2 pfam02210
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ...
 820-946 6.43e-32

Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.


Pssm-ID: 460494 [Multi-domain]  Cd Length: 126  Bit Score: 120.99  E-value: 6.43e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641847  820 TDEDSGILLYKGD--KDHIAVELYRGRVRASYDTGSHPASAIYSVETINDGNFHIVELLALDQSLSLSVDGGNPKIITNL 897
Cdd:pfam02210    3 TRQPNGLLLYAGGggSDFLALELVNGRLVLRYDLGSGPESLLSSGKNLNDGQWHSVRVERNGNTLTLSVDGQTVVSSLPP 82

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1034641847  898 SKQSTLNFDSPLYVGGMPGKSNVASLRQAPGqngtsFHGCIRNLYINSE 946
Cdd:pfam02210   83 GESLLLNLNGPLYLGGLPPLLLLPALPVRAG-----FVGCIRDVRVNGE 126
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
145-491 2.96e-25

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 110.02  E-value: 2.96e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641847  145 TTVDCSNQKLNKIPEHIPQYTAELRLNNNEFTVLEATGIFKKLPQLRKINFSNNKITDIEEGAFEGASGVNEILLTSNRL 224
Cdd:COG4886      3 LLLLSLTLKLLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLL 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641847  225 ENVQ--HKMFKGLESLKTLMLRsnritcvGNDSFIGLSSVRLLSLYDNQITTVaPGAFDTLHSLSTLNLLANPfncncyl 302
Cdd:COG4886     83 SLLLlgLTDLGDLTNLTELDLS-------GNEELSNLTNLESLDLSGNQLTDL-PEELANLTNLKELDLSNNQ------- 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641847  303 awlgewlrkkrivtgnprcqkpyfLKEIPiqdvaiqdftcddgnddnscSPLSRCPTectcLdTVVRCSNKGLKVLPKGI 382
Cdd:COG4886    148 ------------------------LTDLP--------------------EPLGNLTN----L-KSLDLSNNQLTDLPEEL 178

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641847  383 PR--DVTELYLDGNQFTLVPKELSNYKHLTLIDLSNNRISTLSNqSFSNMTQLLTLILSYNRLRCIPprTFDGLKSLRLL 460
Cdd:COG4886    179 GNltNLKELDLSNNQITDLPEPLGNLTNLEELDLSGNQLTDLPE-PLANLTNLETLDLSNNQLTDLP--ELGNLTNLEEL 255

                          330       340       350
                   ....*....|....*....|....*....|.
gi 1034641847  461 SLHGNDISVVPEGAfnDLSALSHLAIGANPL 491
Cdd:COG4886    256 DLSNNQLTDLPPLA--NLTNLKTLDLSNNQL 284
LRR_8 pfam13855
Leucine rich repeat;
408-467 1.88e-17

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 77.18  E-value: 1.88e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641847  408 HLTLIDLSNNRISTLSNQSFSNMTQLLTLILSYNRLRCIPPRTFDGLKSLRLLSLHGNDI 467
Cdd:pfam13855    2 NLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
PCC TIGR00864
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
 462-643 1.67e-11

polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) Polycystin is a huge protein of 4303aas. Its repeated leucine-rich (LRR) segment is found in many proteins. It contains 16 polycystic kidney disease (PKD) domains, one LDL-receptor class A domain, one C-type lectin family domain, and 16-18 putative TMSs in positions between residues 2200 and 4100. Polycystin-L has been shown to be a cation (Na+, K+ and Ca2+) channel that is activated by Ca2+. Two members of the PCC family (polycystin 1 and 2) are mutated in autosomal dominant polycystic kidney disease, and polycystin-L is deleted in mice with renal and retinal defects. Note: this model is restricted to the amino half.


Pssm-ID: 188093 [Multi-domain]  Cd Length: 2740  Bit Score: 69.34  E-value: 1.67e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641847  462 LHGNDISVVPEGAFNDLSALSHLAIGANPLYCDCNMQWLSDWVKSE---YKEPGIARCAGPGEMADKLLLTTPSKKFTCq 538
Cdd:TIGR00864    2 ISNNKISTIEEGICANLCNLSEIDLSGNPFECDCGLARLPRWAEEKgvkVRQPEAALCAGPGALAGQPLLGIPLLDSGC- 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641847  539 gpvDVNILAkcnpCLSNPCKNDGTCNSDPVDFYRCTcPYGFKGQDCDVpihACISNPCKHGGTchlkeGEEDgfWCICAD 618
Cdd:TIGR00864   81 ---DEEYVA----CLKDNSSGGGAARSELVIFSAAH-EGLFQPEACNA---FCFSAGHGLAAL-----GEQG--ECLCGA 142

                          170       180
                   ....*....|....*....|....*
gi 1034641847  619 GFEGENCEVNVDDCEDNDCENNSTC 643
Cdd:TIGR00864  143 AQPSEANFACESLCSGPPPPPAAAC 167
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 384-484 6.04e-11

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 63.65  E-value: 6.04e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641847  384 RDVTELYLDGNQFTLVPkELSNYKHLTLIDLSNNRISTLSNqsFSNMTQLLTLILSYNRLRCIPPrtFDGLKSLRLLSLH 463
Cdd:cd21340      2 KRITHLYLNDKNITKID-NLSLCKNLKVLYLYDNKITKIEN--LEFLTNLTHLYLQNNQIEKIEN--LENLVNLKKLYLG 76

                           90       100
                   ....*....|....*....|.
gi 1034641847  464 GNDISVVpEGaFNDLSALSHL 484
Cdd:cd21340     77 GNRISVV-EG-LENLTNLEEL 95
PCC TIGR00864
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
 267-343 7.63e-11

polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) Polycystin is a huge protein of 4303aas. Its repeated leucine-rich (LRR) segment is found in many proteins. It contains 16 polycystic kidney disease (PKD) domains, one LDL-receptor class A domain, one C-type lectin family domain, and 16-18 putative TMSs in positions between residues 2200 and 4100. Polycystin-L has been shown to be a cation (Na+, K+ and Ca2+) channel that is activated by Ca2+. Two members of the PCC family (polycystin 1 and 2) are mutated in autosomal dominant polycystic kidney disease, and polycystin-L is deleted in mice with renal and retinal defects. Note: this model is restricted to the amino half.


Pssm-ID: 188093 [Multi-domain]  Cd Length: 2740  Bit Score: 67.03  E-value: 7.63e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641847  267 LYDNQITTVAPGAFDTLHSLSTLNLLANPFNCNCYLAWLGEWLRKKRIVTGNPR---CQKPYFLKEIPIQDVAIQDFTCD 343
Cdd:TIGR00864    2 ISNNKISTIEEGICANLCNLSEIDLSGNPFECDCGLARLPRWAEEKGVKVRQPEaalCAGPGALAGQPLLGIPLLDSGCD 81
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
153-461 1.19e-09

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 62.79  E-value: 1.19e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641847  153 KLNKIPEHIPQYTAELRLNNNEftvleatgiFKKLPQ-----LRKINFSNNKITDIEEGAfegASGVNEILLTSNRLENV 227
Cdd:PRK15370   189 GLTTIPACIPEQITTLILDNNE---------LKSLPEnlqgnIKTLYANSNQLTSIPATL---PDTIQEMELSINRITEL 256

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641847  228 QHKMfkgLESLKTLMLRSNRITCVGNDSFIGLssvRLLSLYDNQITTVaPGAFDTlhSLSTLNLLANPfncncyLAWLGE 307
Cdd:PRK15370   257 PERL---PSALQSLDLFHNKISCLPENLPEEL---RYLSVYDNSIRTL-PAHLPS--GITHLNVQSNS------LTALPE 321

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641847  308 WLrkkrivtgnprcqkPYFLKEIPIQDVAIqdftcddgnddnSCSPLSrCPTECTCLDTvvrcSNKGLKVLPKGIPRDVT 387
Cdd:PRK15370   322 TL--------------PPGLKTLEAGENAL------------TSLPAS-LPPELQVLDV----SKNQITVLPETLPPTIT 370

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034641847  388 ELYLDGNQFTLVPKELSnyKHLTLIDLSNNRISTL--SNQSF-SNMTQLLTLILSYNRlrcIPPRTFDGLKslRLLS 461
Cdd:PRK15370   371 TLDVSRNALTNLPENLP--AALQIMQASRNNLVRLpeSLPHFrGEGPQPTRIIVEYNP---FSERTIQNMQ--RLMS 440
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 706-742 5.85e-07

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 46.86  E-value: 5.85e-07
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1034641847  706 DFDDCQD-NKCKNGAHCTDAVNGYTCICPEGYSGLFCE 742
Cdd:cd00054      1 DIDECASgNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 628-664 1.03e-06

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 46.09  E-value: 1.03e-06
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1034641847  628 NVDDCED-NDCENNSTCVDGINNYTCLCPPEYTGELCE 664
Cdd:cd00054      1 DIDECASgNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
LRRCT smart00082
Leucine rich repeat C-terminal domain;
489-538 4.61e-06

Leucine rich repeat C-terminal domain;


Pssm-ID: 214507 [Multi-domain]  Cd Length: 51  Bit Score: 44.73  E-value: 4.61e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 1034641847   489 NPLYCDCNMQWLSDWVKSE--YKEPGIARCAGPGEMADKLLLTTPSkKFTCQ 538
Cdd:smart00082    1 NPFICDCELRWLLRWLQANehLQDPVDLRCASPSSLRGPLLELLHS-EFKCP 51
EGF_CA smart00179
Calcium-binding EGF-like domain;
706-742 1.63e-05

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 43.00  E-value: 1.63e-05
                            10        20        30
                    ....*....|....*....|....*....|....*....
gi 1034641847   706 DFDDCQ-DNKCKNGAHCTDAVNGYTCICPEGYS-GLFCE 742
Cdd:smart00179    1 DIDECAsGNPCQNGGTCVNTVGSYRCECPPGYTdGRNCE 39
LRRNT smart00013
Leucine rich repeat N-terminal domain;
357-388 1.74e-05

Leucine rich repeat N-terminal domain;


Pssm-ID: 214470 [Multi-domain]  Cd Length: 33  Bit Score: 42.69  E-value: 1.74e-05
                            10        20        30
                    ....*....|....*....|....*....|..
gi 1034641847   357 CPTECTCLDTVVRCSNKGLKVLPKGIPRDVTE 388
Cdd:smart00013    2 CPAPCNCSGTAVDCSGRGLTEVPLDLPPDTTL 33
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 710-738 1.99e-05

EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.


Pssm-ID: 394967  Cd Length: 31  Bit Score: 42.37  E-value: 1.99e-05
                           10        20
                   ....*....|....*....|....*....
gi 1034641847  710 CQDNKCKNGAHCTDAVNGYTCICPEGYSG 738
Cdd:pfam00008    1 CAPNPCSNGGTCVDTPGGYTCICPEGYTG 29
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 668-703 2.50e-05

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 42.24  E-value: 2.50e-05
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1034641847  668 DFCAQDlNPCQHDSKCILTPKGFKCDCTPGYVGEHC 703
Cdd:cd00054      3 DECASG-NPCQNGGTCVNTVGSYRCSCPPGYTGRNC 37
EGF_CA smart00179
Calcium-binding EGF-like domain;
628-664 3.55e-05

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 41.85  E-value: 3.55e-05
                            10        20        30
                    ....*....|....*....|....*....|....*....
gi 1034641847   628 NVDDCE-DNDCENNSTCVDGINNYTCLCPPEYT-GELCE 664
Cdd:smart00179    1 DIDECAsGNPCQNGGTCVNTVGSYRCECPPGYTdGRNCE 39
PCC TIGR00864
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
 33-96 1.44e-04

polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) Polycystin is a huge protein of 4303aas. Its repeated leucine-rich (LRR) segment is found in many proteins. It contains 16 polycystic kidney disease (PKD) domains, one LDL-receptor class A domain, one C-type lectin family domain, and 16-18 putative TMSs in positions between residues 2200 and 4100. Polycystin-L has been shown to be a cation (Na+, K+ and Ca2+) channel that is activated by Ca2+. Two members of the PCC family (polycystin 1 and 2) are mutated in autosomal dominant polycystic kidney disease, and polycystin-L is deleted in mice with renal and retinal defects. Note: this model is restricted to the amino half.


Pssm-ID: 188093 [Multi-domain]  Cd Length: 2740  Bit Score: 46.23  E-value: 1.44e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034641847   33 LYNNTLQTITKGTFSPLRAIQTMHLAQNPFICDCHLKWLADYLHTNPIET---SGARCTSPRRLANK 96
Cdd:TIGR00864    2 ISNNKISTIEEGICANLCNLSEIDLSGNPFECDCGLARLPRWAEEKGVKVrqpEAALCAGPGALAGQ 68
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 632-661 2.08e-04

EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.


Pssm-ID: 394967  Cd Length: 31  Bit Score: 39.67  E-value: 2.08e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 1034641847  632 CEDNDCENNSTCVDGINNYTCLCPPEYTGE 661
Cdd:pfam00008    1 CAPNPCSNGGTCVDTPGGYTCICPEGYTGK 30
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 673-702 4.80e-04

EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.


Pssm-ID: 394967  Cd Length: 31  Bit Score: 38.52  E-value: 4.80e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 1034641847  673 DLNPCQHDSKCILTPKGFKCDCTPGYVGEH 702
Cdd:pfam00008    2 APNPCSNGGTCVDTPGGYTCICPEGYTGKR 31
LRRCT smart00082
Leucine rich repeat C-terminal domain;
60-90 9.98e-04

Leucine rich repeat C-terminal domain;


Pssm-ID: 214507 [Multi-domain]  Cd Length: 51  Bit Score: 38.18  E-value: 9.98e-04
                            10        20        30
                    ....*....|....*....|....*....|...
gi 1034641847    60 NPFICDCHLKWLADYLHTNPI--ETSGARCTSP 90
Cdd:smart00082    1 NPFICDCELRWLLRWLQANEHlqDPVDLRCASP 33
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 594-626 2.75e-03

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 36.46  E-value: 2.75e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1034641847  594 NPCKHGGTCHLKEGeedGFWCICADGFEGENCE 626
Cdd:cd00054      9 NPCQNGGTCVNTVG---SYRCSCPPGYTGRNCE 38
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 591-624 5.23e-03

EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.


Pssm-ID: 394967  Cd Length: 31  Bit Score: 35.44  E-value: 5.23e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1034641847  591 CISNPCKHGGTCHLKEGeedGFWCICADGFEGEN 624
Cdd:pfam00008    1 CAPNPCSNGGTCVDTPG---GYTCICPEGYTGKR 31
EGF_CA smart00179
Calcium-binding EGF-like domain;
668-704 6.59e-03

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 35.69  E-value: 6.59e-03
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 1034641847   668 DFCAQDlNPCQHDSKCILTPKGFKCDCTPGYV-GEHCD 704
Cdd:smart00179    3 DECASG-NPCQNGGTCVNTVGSYRCECPPGYTdGRNCE 39
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 760-787 8.89e-03

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 34.92  E-value: 8.89e-03
                           10        20
                   ....*....|....*....|....*...
gi 1034641847  760 CQNGAQCIVRINEPICQCLPGYQGEKCE 787
Cdd:cd00054     11 CQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
 
Name Accession Description Interval E-value
LamG smart00282
Laminin G domain;
813-946 5.96e-37

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 135.54  E-value: 5.96e-37
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641847   813 NITLQIATDEDSGILLY---KGDKDHIAVELYRGRVRASYDTGSHPASAIYSVETINDGNFHIVELLALDQSLSLSVDGG 889
Cdd:smart00282    1 SISFSFRTTSPNGLLLYagsKGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTPLNDGQWHRVAVERNGRSVTLSVDGG 80

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034641847   890 NPKIITNLSKQSTLNFDSPLYVGGMPgksnvASLRQAPGQNGTSFHGCIRNLYINSE 946
Cdd:smart00282   81 NRVSGESPGGLTILNLDGPLYLGGLP-----EDLKLPPLPVTPGFRGCIRNLKVNGK 132
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
 791-944 6.44e-33

Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.


Pssm-ID: 238058 [Multi-domain]  Cd Length: 151  Bit Score: 124.84  E-value: 6.44e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641847  791 SVNFiNKESYLQIP-SAKVRPQTNITLQIATDEDSGILLYKGDK---DHIAVELYRGRVRASYDTGSHPASaIYSVETIN 866
Cdd:cd00110      1 GVSF-SGSSYVRLPtLPAPRTRLSISFSFRTTSPNGLLLYAGSQnggDFLALELEDGRLVLRYDLGSGSLV-LSSKTPLN 78

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034641847  867 DGNFHIVELLALDQSLSLSVDGGNPKIITNLSKQSTLNFDSPLYVGGMPgksnvASLRQAPGQNGTSFHGCIRNLYIN 944
Cdd:cd00110     79 DGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLNLDGPLYLGGLP-----EDLKSPGLPVSPGFVGCIRDLKVN 151
Laminin_G_2 pfam02210
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ...
 820-946 6.43e-32

Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.


Pssm-ID: 460494 [Multi-domain]  Cd Length: 126  Bit Score: 120.99  E-value: 6.43e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641847  820 TDEDSGILLYKGD--KDHIAVELYRGRVRASYDTGSHPASAIYSVETINDGNFHIVELLALDQSLSLSVDGGNPKIITNL 897
Cdd:pfam02210    3 TRQPNGLLLYAGGggSDFLALELVNGRLVLRYDLGSGPESLLSSGKNLNDGQWHSVRVERNGNTLTLSVDGQTVVSSLPP 82

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1034641847  898 SKQSTLNFDSPLYVGGMPGKSNVASLRQAPGqngtsFHGCIRNLYINSE 946
Cdd:pfam02210   83 GESLLLNLNGPLYLGGLPPLLLLPALPVRAG-----FVGCIRDVRVNGE 126
Laminin_G_1 pfam00054
Laminin G domain;
818-949 1.42e-28

Laminin G domain;


Pssm-ID: 395008 [Multi-domain]  Cd Length: 131  Bit Score: 111.64  E-value: 1.42e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641847  818 IATDEDSGILLYKGDKDH---IAVELYRGRVRASYDTGSHPASaIYSVETINDGNFHIVELLALDQSLSLSVDGG-NPKI 893
Cdd:pfam00054    1 FRTTEPSGLLLYNGTQTErdfLALELRDGRLEVSYDLGSGAAV-VRSGDKLNDGKWHSVELERNGRSGTLSVDGEaRPTG 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034641847  894 ITNLSKQSTLNFDSPLYVGGMPgkSNVASLRQAPgqNGTSFHGCIRNLYINSELQD 949
Cdd:pfam00054   80 ESPLGATTDLDVDGPLYVGGLP--SLGVKKRRLA--ISPSFDGCIRDVIVNGKPLD 131
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
145-491 2.96e-25

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 110.02  E-value: 2.96e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641847  145 TTVDCSNQKLNKIPEHIPQYTAELRLNNNEFTVLEATGIFKKLPQLRKINFSNNKITDIEEGAFEGASGVNEILLTSNRL 224
Cdd:COG4886      3 LLLLSLTLKLLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLL 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641847  225 ENVQ--HKMFKGLESLKTLMLRsnritcvGNDSFIGLSSVRLLSLYDNQITTVaPGAFDTLHSLSTLNLLANPfncncyl 302
Cdd:COG4886     83 SLLLlgLTDLGDLTNLTELDLS-------GNEELSNLTNLESLDLSGNQLTDL-PEELANLTNLKELDLSNNQ------- 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641847  303 awlgewlrkkrivtgnprcqkpyfLKEIPiqdvaiqdftcddgnddnscSPLSRCPTectcLdTVVRCSNKGLKVLPKGI 382
Cdd:COG4886    148 ------------------------LTDLP--------------------EPLGNLTN----L-KSLDLSNNQLTDLPEEL 178

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641847  383 PR--DVTELYLDGNQFTLVPKELSNYKHLTLIDLSNNRISTLSNqSFSNMTQLLTLILSYNRLRCIPprTFDGLKSLRLL 460
Cdd:COG4886    179 GNltNLKELDLSNNQITDLPEPLGNLTNLEELDLSGNQLTDLPE-PLANLTNLETLDLSNNQLTDLP--ELGNLTNLEEL 255

                          330       340       350
                   ....*....|....*....|....*....|.
gi 1034641847  461 SLHGNDISVVPEGAfnDLSALSHLAIGANPL 491
Cdd:COG4886    256 DLSNNQLTDLPPLA--NLTNLKTLDLSNNQL 284
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
150-468 1.04e-24

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 108.48  E-value: 1.04e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641847  150 SNQKLNKIPEHIPQYTAELRLNNNEFTVLEATGIFKKLPQLRKINFSNNKITDIEEGafegasgvneilltsnrlenvqh 229
Cdd:COG4886     75 LLLSLLLLSLLLLGLTDLGDLTNLTELDLSGNEELSNLTNLESLDLSGNQLTDLPEE----------------------- 131

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641847  230 kmFKGLESLKTLMLRSNRITCVGnDSFIGLSSVRLLSLYDNQITTVaPGAFDTLHSLSTLNLlanpfncncylawlgewl 309
Cdd:COG4886    132 --LANLTNLKELDLSNNQLTDLP-EPLGNLTNLKSLDLSNNQLTDL-PEELGNLTNLKELDL------------------ 189

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641847  310 rkkrivTGNPrcqkpyfLKEIPiqdvaiqdftcddgnddnscSPLSRCPTectcldtvvrcsnkglkvlpkgiprdVTEL 389
Cdd:COG4886    190 ------SNNQ-------ITDLP--------------------EPLGNLTN--------------------------LEEL 210

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034641847  390 YLDGNQFTLVPKELSNYKHLTLIDLSNNRISTLSnqSFSNMTQLLTLILSYNRLRCIPPrtFDGLKSLRLLSLHGNDIS 468
Cdd:COG4886    211 DLSGNQLTDLPEPLANLTNLETLDLSNNQLTDLP--ELGNLTNLEELDLSNNQLTDLPP--LANLTNLKTLDLSNNQLT 285
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
264-491 3.53e-20

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 94.62  E-value: 3.53e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641847  264 LLSLYDNQITTVAPGAFDTLHSLSTLNLLANPFNCNCYLAWLGEWLRKKRIVTGNPRCQKPYFLKEIPIQDVAIQDFTCD 343
Cdd:COG4886      2 LLLLLSLTLKLLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLL 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641847  344 DGNDDNSCSPLSRCpTECTCLDTvvrCSNKGLKVLPkgiprDVTELYLDGNQFTLVPKELSNYKHLTLIDLSNNRISTLS 423
Cdd:COG4886     82 LSLLLLGLTDLGDL-TNLTELDL---SGNEELSNLT-----NLESLDLSGNQLTDLPEELANLTNLKELDLSNNQLTDLP 152

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034641847  424 NqSFSNMTQLLTLILSYNRLRCIPPrTFDGLKSLRLLSLHGNDISVVPEgAFNDLSALSHLAIGANPL 491
Cdd:COG4886    153 E-PLGNLTNLKSLDLSNNQLTDLPE-ELGNLTNLKELDLSNNQITDLPE-PLGNLTNLEELDLSGNQL 217
LRR_8 pfam13855
Leucine rich repeat;
408-467 1.88e-17

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 77.18  E-value: 1.88e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641847  408 HLTLIDLSNNRISTLSNQSFSNMTQLLTLILSYNRLRCIPPRTFDGLKSLRLLSLHGNDI 467
Cdd:pfam13855    2 NLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
LRR_8 pfam13855
Leucine rich repeat;
212-272 3.54e-13

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 65.24  E-value: 3.54e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034641847  212 SGVNEILLTSNRLENVQHKMFKGLESLKTLMLRSNRITCVGNDSFIGLSSVRLLSLYDNQI 272
Cdd:pfam13855    1 PNLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
LRR_8 pfam13855
Leucine rich repeat;
237-296 4.26e-13

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 64.85  E-value: 4.26e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641847  237 SLKTLMLRSNRITCVGNDSFIGLSSVRLLSLYDNQITTVAPGAFDTLHSLSTLNLLANPF 296
Cdd:pfam13855    2 NLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
PCC TIGR00864
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
 462-643 1.67e-11

polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) Polycystin is a huge protein of 4303aas. Its repeated leucine-rich (LRR) segment is found in many proteins. It contains 16 polycystic kidney disease (PKD) domains, one LDL-receptor class A domain, one C-type lectin family domain, and 16-18 putative TMSs in positions between residues 2200 and 4100. Polycystin-L has been shown to be a cation (Na+, K+ and Ca2+) channel that is activated by Ca2+. Two members of the PCC family (polycystin 1 and 2) are mutated in autosomal dominant polycystic kidney disease, and polycystin-L is deleted in mice with renal and retinal defects. Note: this model is restricted to the amino half.


Pssm-ID: 188093 [Multi-domain]  Cd Length: 2740  Bit Score: 69.34  E-value: 1.67e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641847  462 LHGNDISVVPEGAFNDLSALSHLAIGANPLYCDCNMQWLSDWVKSE---YKEPGIARCAGPGEMADKLLLTTPSKKFTCq 538
Cdd:TIGR00864    2 ISNNKISTIEEGICANLCNLSEIDLSGNPFECDCGLARLPRWAEEKgvkVRQPEAALCAGPGALAGQPLLGIPLLDSGC- 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641847  539 gpvDVNILAkcnpCLSNPCKNDGTCNSDPVDFYRCTcPYGFKGQDCDVpihACISNPCKHGGTchlkeGEEDgfWCICAD 618
Cdd:TIGR00864   81 ---DEEYVA----CLKDNSSGGGAARSELVIFSAAH-EGLFQPEACNA---FCFSAGHGLAAL-----GEQG--ECLCGA 142

                          170       180
                   ....*....|....*....|....*
gi 1034641847  619 GFEGENCEVNVDDCEDNDCENNSTC 643
Cdd:TIGR00864  143 AQPSEANFACESLCSGPPPPPAAAC 167
LRR_8 pfam13855
Leucine rich repeat;
386-443 5.57e-11

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 59.08  E-value: 5.57e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034641847  386 VTELYLDGNQFTLVPKE-LSNYKHLTLIDLSNNRISTLSNQSFSNMTQLLTLILSYNRL 443
Cdd:pfam13855    3 LRSLDLSNNRLTSLDDGaFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 384-484 6.04e-11

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 63.65  E-value: 6.04e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641847  384 RDVTELYLDGNQFTLVPkELSNYKHLTLIDLSNNRISTLSNqsFSNMTQLLTLILSYNRLRCIPPrtFDGLKSLRLLSLH 463
Cdd:cd21340      2 KRITHLYLNDKNITKID-NLSLCKNLKVLYLYDNKITKIEN--LEFLTNLTHLYLQNNQIEKIEN--LENLVNLKKLYLG 76

                           90       100
                   ....*....|....*....|.
gi 1034641847  464 GNDISVVpEGaFNDLSALSHL 484
Cdd:cd21340     77 GNRISVV-EG-LENLTNLEEL 95
PCC TIGR00864
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
 267-343 7.63e-11

polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) Polycystin is a huge protein of 4303aas. Its repeated leucine-rich (LRR) segment is found in many proteins. It contains 16 polycystic kidney disease (PKD) domains, one LDL-receptor class A domain, one C-type lectin family domain, and 16-18 putative TMSs in positions between residues 2200 and 4100. Polycystin-L has been shown to be a cation (Na+, K+ and Ca2+) channel that is activated by Ca2+. Two members of the PCC family (polycystin 1 and 2) are mutated in autosomal dominant polycystic kidney disease, and polycystin-L is deleted in mice with renal and retinal defects. Note: this model is restricted to the amino half.


Pssm-ID: 188093 [Multi-domain]  Cd Length: 2740  Bit Score: 67.03  E-value: 7.63e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641847  267 LYDNQITTVAPGAFDTLHSLSTLNLLANPFNCNCYLAWLGEWLRKKRIVTGNPR---CQKPYFLKEIPIQDVAIQDFTCD 343
Cdd:TIGR00864    2 ISNNKISTIEEGICANLCNLSEIDLSGNPFECDCGLARLPRWAEEKGVKVRQPEaalCAGPGALAGQPLLGIPLLDSGCD 81
LRR_8 pfam13855
Leucine rich repeat;
431-491 1.47e-10

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 57.92  E-value: 1.47e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034641847  431 TQLLTLILSYNRLRCIPPRTFDGLKSLRLLSLHGNDISVVPEGAFNDLSALSHLAIGANPL 491
Cdd:pfam13855    1 PNLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
LRR_8 pfam13855
Leucine rich repeat;
167-224 9.14e-10

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 55.61  E-value: 9.14e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034641847  167 ELRLNNNEFTVLEAtGIFKKLPQLRKINFSNNKITDIEEGAFEGASGVNEILLTSNRL 224
Cdd:pfam13855    5 SLDLSNNRLTSLDD-GAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
153-461 1.19e-09

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 62.79  E-value: 1.19e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641847  153 KLNKIPEHIPQYTAELRLNNNEftvleatgiFKKLPQ-----LRKINFSNNKITDIEEGAfegASGVNEILLTSNRLENV 227
Cdd:PRK15370   189 GLTTIPACIPEQITTLILDNNE---------LKSLPEnlqgnIKTLYANSNQLTSIPATL---PDTIQEMELSINRITEL 256

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641847  228 QHKMfkgLESLKTLMLRSNRITCVGNDSFIGLssvRLLSLYDNQITTVaPGAFDTlhSLSTLNLLANPfncncyLAWLGE 307
Cdd:PRK15370   257 PERL---PSALQSLDLFHNKISCLPENLPEEL---RYLSVYDNSIRTL-PAHLPS--GITHLNVQSNS------LTALPE 321

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641847  308 WLrkkrivtgnprcqkPYFLKEIPIQDVAIqdftcddgnddnSCSPLSrCPTECTCLDTvvrcSNKGLKVLPKGIPRDVT 387
Cdd:PRK15370   322 TL--------------PPGLKTLEAGENAL------------TSLPAS-LPPELQVLDV----SKNQITVLPETLPPTIT 370

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034641847  388 ELYLDGNQFTLVPKELSnyKHLTLIDLSNNRISTL--SNQSF-SNMTQLLTLILSYNRlrcIPPRTFDGLKslRLLS 461
Cdd:PRK15370   371 TLDVSRNALTNLPENLP--AALQIMQASRNNLVRLpeSLPHFrGEGPQPTRIIVEYNP---FSERTIQNMQ--RLMS 440
PLN03150 PLN03150
hypothetical protein; Provisional
 399-468 1.39e-08

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 59.06  E-value: 1.39e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641847  399 VPKELSNYKHLTLIDLSNNRISTLSNQSFSNMTQLLTLILSYNRLRCIPPRTFDGLKSLRLLSLHGNDIS 468
Cdd:PLN03150   434 IPNDISKLRHLQSINLSGNSIRGNIPPSLGSITSLEVLDLSYNSFNGSIPESLGQLTSLRILNLNGNSLS 503
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
363-491 2.33e-08

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 58.55  E-value: 2.33e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641847  363 CL---DTVVRCSNKGLKVLPKGIPRDVTELYLDGNQFTLVPKEL-SNYKHLT------------------LIDLSNNRIS 420
Cdd:PRK15370   175 CLknnKTELRLKILGLTTIPACIPEQITTLILDNNELKSLPENLqGNIKTLYansnqltsipatlpdtiqEMELSINRIT 254

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034641847  421 TLSNQSFSnmtQLLTLILSYNRLRCIPPRTFDGlksLRLLSLHGNDISVVPEgafNDLSALSHLAIGANPL 491
Cdd:PRK15370   255 ELPERLPS---ALQSLDLFHNKISCLPENLPEE---LRYLSVYDNSIRTLPA---HLPSGITHLNVQSNSL 316
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 706-742 5.85e-07

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 46.86  E-value: 5.85e-07
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1034641847  706 DFDDCQD-NKCKNGAHCTDAVNGYTCICPEGYSGLFCE 742
Cdd:cd00054      1 DIDECASgNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 628-664 1.03e-06

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 46.09  E-value: 1.03e-06
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1034641847  628 NVDDCED-NDCENNSTCVDGINNYTCLCPPEYTGELCE 664
Cdd:cd00054      1 DIDECASgNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
LRRCT smart00082
Leucine rich repeat C-terminal domain;
489-538 4.61e-06

Leucine rich repeat C-terminal domain;


Pssm-ID: 214507 [Multi-domain]  Cd Length: 51  Bit Score: 44.73  E-value: 4.61e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 1034641847   489 NPLYCDCNMQWLSDWVKSE--YKEPGIARCAGPGEMADKLLLTTPSkKFTCQ 538
Cdd:smart00082    1 NPFICDCELRWLLRWLQANehLQDPVDLRCASPSSLRGPLLELLHS-EFKCP 51
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 146-491 5.80e-06

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 50.62  E-value: 5.80e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641847  146 TVDCSNQKLN-KIPEHIPQYTAELR---LNNNEFTVLEATGifkKLPQLRKINFSNNKITD---IEEGAFegaSGVNEIL 218
Cdd:PLN00113    97 TINLSNNQLSgPIPDDIFTTSSSLRylnLSNNNFTGSIPRG---SIPNLETLDLSNNMLSGeipNDIGSF---SSLKVLD 170

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641847  219 LTSNRLENVQHKMFKGLESLKTLMLRSNRITCVGNDSFIGLSSVRLLSLYDNQITTVAPGAFDTLHSLSTLNLLANPFNC 298
Cdd:PLN00113   171 LGGNVLVGKIPNSLTNLTSLEFLTLASNQLVGQIPRELGQMKSLKWIYLGYNNLSGEIPYEIGGLTSLNHLDLVYNNLTG 250

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641847  299 NCYLAWlgewlrkkrivtGNPRCQKPYFLKE------IPIQDVAIQDFTCDDGNDDNSCSPLSRCPTECTCLDTVVRCSN 372
Cdd:PLN00113   251 PIPSSL------------GNLKNLQYLFLYQnklsgpIPPSIFSLQKLISLDLSDNSLSGEIPELVIQLQNLEILHLFSN 318

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641847  373 KGLKVLPKGI---PRdVTELYLDGNQFT-LVPKELSNYKHLTLIDLSNNRISTLSNQSFSNMTQLLTLILSYNRLRCIPP 448
Cdd:PLN00113   319 NFTGKIPVALtslPR-LQVLQLWSNKFSgEIPKNLGKHNNLTVLDLSTNNLTGEIPEGLCSSGNLFKLILFSNSLEGEIP 397

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|...
gi 1034641847  449 RTFDGLKSLRLLSLHGNDISVVPEGAFNDLSALSHLAIGANPL 491
Cdd:PLN00113   398 KSLGACRSLRRVRLQDNSFSGELPSEFTKLPLVYFLDISNNNL 440
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 385-493 8.35e-06

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 50.23  E-value: 8.35e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641847  385 DVTELYLDGNQFT-LVPKELSNYKHLTLIDLSNNRISTLSNQSFSNMTQLLTLILSYNRLRCIPPRTFDGLKSLRLLSLH 463
Cdd:PLN00113   500 ELMQLKLSENKLSgEIPDELSSCKKLVSLDLSHNQLSGQIPASFSEMPVLSQLDLSQNQLSGEIPKNLGNVESLVQVNIS 579

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1034641847  464 GNDI--SVVPEGAFndlSALSHLAIGANPLYC 493
Cdd:PLN00113   580 HNHLhgSLPSTGAF---LAINASAVAGNIDLC 608
EGF_CA smart00179
Calcium-binding EGF-like domain;
706-742 1.63e-05

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 43.00  E-value: 1.63e-05
                            10        20        30
                    ....*....|....*....|....*....|....*....
gi 1034641847   706 DFDDCQ-DNKCKNGAHCTDAVNGYTCICPEGYS-GLFCE 742
Cdd:smart00179    1 DIDECAsGNPCQNGGTCVNTVGSYRCECPPGYTdGRNCE 39
LRRNT smart00013
Leucine rich repeat N-terminal domain;
357-388 1.74e-05

Leucine rich repeat N-terminal domain;


Pssm-ID: 214470 [Multi-domain]  Cd Length: 33  Bit Score: 42.69  E-value: 1.74e-05
                            10        20        30
                    ....*....|....*....|....*....|..
gi 1034641847   357 CPTECTCLDTVVRCSNKGLKVLPKGIPRDVTE 388
Cdd:smart00013    2 CPAPCNCSGTAVDCSGRGLTEVPLDLPPDTTL 33
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 710-738 1.99e-05

EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.


Pssm-ID: 394967  Cd Length: 31  Bit Score: 42.37  E-value: 1.99e-05
                           10        20
                   ....*....|....*....|....*....
gi 1034641847  710 CQDNKCKNGAHCTDAVNGYTCICPEGYSG 738
Cdd:pfam00008    1 CAPNPCSNGGTCVDTPGGYTCICPEGYTG 29
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 668-703 2.50e-05

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 42.24  E-value: 2.50e-05
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1034641847  668 DFCAQDlNPCQHDSKCILTPKGFKCDCTPGYVGEHC 703
Cdd:cd00054      3 DECASG-NPCQNGGTCVNTVGSYRCSCPPGYTGRNC 37
EGF_CA smart00179
Calcium-binding EGF-like domain;
628-664 3.55e-05

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 41.85  E-value: 3.55e-05
                            10        20        30
                    ....*....|....*....|....*....|....*....
gi 1034641847   628 NVDDCE-DNDCENNSTCVDGINNYTCLCPPEYT-GELCE 664
Cdd:smart00179    1 DIDECAsGNPCQNGGTCVNTVGSYRCECPPGYTdGRNCE 39
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 150-295 5.84e-05

Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 47.09  E-value: 5.84e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641847  150 SNQKLNKIPEHIPQYTA--ELRLNNNEFTVLEATGIFKKL---PQLRKINFSNNKITDieegafEGASGVNEILLTSNRL 224
Cdd:COG5238    193 GDEGIEELAEALTQNTTvtTLWLKRNPIGDEGAEILAEALkgnKSLTTLDLSNNQIGD------EGVIALAEALKNNTTV 266

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641847  225 E-------NVQH-------KMFKGLESLKTLMLRSNRItcvGNDSFIGL-------SSVRLLSLYDNQITTV-APGAFDT 282
Cdd:COG5238    267 EtlylsgnQIGAegaialaKALQGNTTLTSLDLSVNRI---GDEGAIALaeglqgnKTLHTLNLAYNGIGAQgAIALAKA 343

                          170
                   ....*....|....*.
gi 1034641847  283 LH---SLSTLNLLANP 295
Cdd:COG5238    344 LQentTLHSLDLSDNQ 359
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 387-468 8.43e-05

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 45.16  E-value: 8.43e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641847  387 TELYLD------GNQFTLVP---KELSNykHLTLIDLSNNRISTLSnqSFSNMTQLLTLILSYNRLRCIPP--RTFDGLK 455
Cdd:cd21340     93 EELHIEnqrlppGEKLTFDPrslAALSN--SLRVLNISGNNIDSLE--PLAPLRNLEQLDASNNQISDLEEllDLLSSWP 168

                           90
                   ....*....|...
gi 1034641847  456 SLRLLSLHGNDIS 468
Cdd:cd21340    169 SLRELDLTGNPVC 181
PCC TIGR00864
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
 33-96 1.44e-04

polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) Polycystin is a huge protein of 4303aas. Its repeated leucine-rich (LRR) segment is found in many proteins. It contains 16 polycystic kidney disease (PKD) domains, one LDL-receptor class A domain, one C-type lectin family domain, and 16-18 putative TMSs in positions between residues 2200 and 4100. Polycystin-L has been shown to be a cation (Na+, K+ and Ca2+) channel that is activated by Ca2+. Two members of the PCC family (polycystin 1 and 2) are mutated in autosomal dominant polycystic kidney disease, and polycystin-L is deleted in mice with renal and retinal defects. Note: this model is restricted to the amino half.


Pssm-ID: 188093 [Multi-domain]  Cd Length: 2740  Bit Score: 46.23  E-value: 1.44e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034641847   33 LYNNTLQTITKGTFSPLRAIQTMHLAQNPFICDCHLKWLADYLHTNPIET---SGARCTSPRRLANK 96
Cdd:TIGR00864    2 ISNNKISTIEEGICANLCNLSEIDLSGNPFECDCGLARLPRWAEEKGVKVrqpEAALCAGPGALAGQ 68
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 632-661 2.08e-04

EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.


Pssm-ID: 394967  Cd Length: 31  Bit Score: 39.67  E-value: 2.08e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 1034641847  632 CEDNDCENNSTCVDGINNYTCLCPPEYTGE 661
Cdd:pfam00008    1 CAPNPCSNGGTCVDTPGGYTCICPEGYTGK 30
LRRNT pfam01462
Leucine rich repeat N-terminal domain; Leucine Rich Repeats pfam00560 are short sequence ...
 357-383 2.38e-04

Leucine rich repeat N-terminal domain; Leucine Rich Repeats pfam00560 are short sequence motifs present in a number of proteins with diverse functions and cellular locations. Leucine Rich Repeats are often flanked by cysteine rich domains. This domain is often found at the N-terminus of tandem leucine rich repeats.


Pssm-ID: 396168 [Multi-domain]  Cd Length: 28  Bit Score: 39.15  E-value: 2.38e-04
                           10        20
                   ....*....|....*....|....*..
gi 1034641847  357 CPTECTCLDTVVRCSNKGLKVLPKGIP 383
Cdd:pfam01462    2 CPVPCHCSATVVNCSDRGLTAVPRDLP 28
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
145-310 3.45e-04

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 44.54  E-value: 3.45e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641847  145 TTVDCSNQKLNKIPE--HIPQYTaELRLNNNEFTVLEATGifkKLPQLRKINFSNNKITDIEEGAFEGASGVNeiLLTSN 222
Cdd:COG4886    231 ETLDLSNNQLTDLPElgNLTNLE-ELDLSNNQLTDLPPLA---NLTNLKTLDLSNNQLTDLKLKELELLLGLN--SLLLL 304

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641847  223 RLENVQHKMFKGLESLKTLMLRSNRITCVGNDSFIGLSSVRLLSLYDNQITTVAPGAFDTLHSLSTLNLLANPFNCNCYL 302
Cdd:COG4886    305 LLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLSLLLTLLLTLGLLGLLEATLLTLAL 384


                   ....*...
gi 1034641847  303 AWLGEWLR 310
Cdd:COG4886    385 LLLTLLLL 392
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 160-491 4.41e-04

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 44.45  E-value: 4.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641847  160 HIPQYTAE------LRLNNNEFTvleaTGIFKKLPQLRKINF----SNNKITDI--EEGafeGASGVNEILLTSNRLENV 227
Cdd:PLN00113   179 KIPNSLTNltslefLTLASNQLV----GQIPRELGQMKSLKWiylgYNNLSGEIpyEIG---GLTSLNHLDLVYNNLTGP 251

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641847  228 QHKMFKGLESLKTLMLRSNRITCVGNDSFIGLSSVRLLSLYDNQITTVAPGAFDTLHSLSTLNLLANPFNCNCYLAwlge 307
Cdd:PLN00113   252 IPSSLGNLKNLQYLFLYQNKLSGPIPPSIFSLQKLISLDLSDNSLSGEIPELVIQLQNLEILHLFSNNFTGKIPVA---- 327

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641847  308 wlrkkriVTGNPRCQ-----KPYFLKEIP----------IQDVAIQDFT-------CDDGN-----------------DD 348
Cdd:PLN00113   328 -------LTSLPRLQvlqlwSNKFSGEIPknlgkhnnltVLDLSTNNLTgeipeglCSSGNlfklilfsnslegeipkSL 400

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641847  349 NSCSPLSRC-----------PTECTCLDTV--VRCSNKGLKVLPKGIPRDVTELY---LDGNQFTLVPKELSNYKHLTLI 412
Cdd:PLN00113   401 GACRSLRRVrlqdnsfsgelPSEFTKLPLVyfLDISNNNLQGRINSRKWDMPSLQmlsLARNKFFGGLPDSFGSKRLENL 480

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034641847  413 DLSNNRISTLSNQSFSNMTQLLTLILSYNRLRCIPPRTFDGLKSLRLLSLHGNDISVVPEGAFNDLSALSHLAIGANPL 491
Cdd:PLN00113   481 DLSRNQFSGAVPRKLGSLSELMQLKLSENKLSGEIPDELSSCKKLVSLDLSHNQLSGQIPASFSEMPVLSQLDLSQNQL 559
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 673-702 4.80e-04

EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.


Pssm-ID: 394967  Cd Length: 31  Bit Score: 38.52  E-value: 4.80e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 1034641847  673 DLNPCQHDSKCILTPKGFKCDCTPGYVGEH 702
Cdd:pfam00008    2 APNPCSNGGTCVDTPGGYTCICPEGYTGKR 31
hEGF pfam12661
Human growth factor-like EGF; hEGF, or human growth factor-like EGF, domains have six ...
 715-736 5.30e-04

Human growth factor-like EGF; hEGF, or human growth factor-like EGF, domains have six conserved residues disulfide-bonded into the characteriztic 'ababcc' pattern. They are involved in growth and proliferation of cells, in proteins of the Notch/Delta pathway, neurogulin and selectins. hEGFs are also found in mosaic proteins with four-disulfide laminin EGFs such as aggrecan and perlecan. The core fold of the EGF domain consists of two small beta-hairpins packed against each other. Two major structural variants have been identified based on the structural context of the C-terminal Cys residue of disulfide 'c' in the C-terminal hairpin: hEGFs and cEGFs. In hEGFs the C-terminal thiol resides in the beta-turn, resulting in shorter loop-lengths between the Cys residues of disulfide 'c', typically C[8-9]XC. These shorter loop-lengths are also typical of the four-disulfide EGF domains, laminin ad integrin. Tandem hEGF domains have six linking residues between terminal cysteines of adjacent domains. hEGF domains may or may not bind calcium in the linker region. hEGF domains with the consensus motif CXD4X[F,Y]XCXC are hydroxylated exclusively in the Asp residue.


Pssm-ID: 463660  Cd Length: 22  Bit Score: 38.08  E-value: 5.30e-04
                           10        20
                   ....*....|....*....|..
gi 1034641847  715 CKNGAHCTDAVNGYTCICPEGY 736
Cdd:pfam12661    1 CQNGGTCVDGVNGYKCQCPPGY 22
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 153-296 5.77e-04

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 42.47  E-value: 5.77e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641847  153 KLNKIP--EHIPQYTaELRLNNNEFTVLEAtgiFKKLPQLRKINFSNNKITDIEegAFEGASGVNEILLTSNRLENvQHK 230
Cdd:cd21340     35 KITKIEnlEFLTNLT-HLYLQNNQIEKIEN---LENLVNLKKLYLGGNRISVVE--GLENLTNLEELHIENQRLPP-GEK 107

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034641847  231 MF------KGL-ESLKTLMLRSNRITCVgnDSFIGLSSVRLLSLYDNQITTVAP--GAFDTLHSLSTLNLLANPF 296
Cdd:cd21340    108 LTfdprslAALsNSLRVLNISGNNIDSL--EPLAPLRNLEQLDASNNQISDLEEllDLLSSWPSLRELDLTGNPV 180
LRRCT smart00082
Leucine rich repeat C-terminal domain;
294-343 6.04e-04

Leucine rich repeat C-terminal domain;


Pssm-ID: 214507 [Multi-domain]  Cd Length: 51  Bit Score: 38.95  E-value: 6.04e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 1034641847   294 NPFNCNCYLAWLGEWLRKKRIV--TGNPRCQKPYFLKEiPIQDVAIQDFTCD 343
Cdd:smart00082    1 NPFICDCELRWLLRWLQANEHLqdPVDLRCASPSSLRG-PLLELLHSEFKCP 51
LRRNT smart00013
Leucine rich repeat N-terminal domain;
135-165 8.03e-04

Leucine rich repeat N-terminal domain;


Pssm-ID: 214470 [Multi-domain]  Cd Length: 33  Bit Score: 38.07  E-value: 8.03e-04
                            10        20        30
                    ....*....|....*....|....*....|.
gi 1034641847   135 ACPEKCRCEGTTVDCSNQKLNKIPEHIPQYT 165
Cdd:smart00013    1 ACPAPCNCSGTAVDCSGRGLTEVPLDLPPDT 31
LRRCT smart00082
Leucine rich repeat C-terminal domain;
60-90 9.98e-04

Leucine rich repeat C-terminal domain;


Pssm-ID: 214507 [Multi-domain]  Cd Length: 51  Bit Score: 38.18  E-value: 9.98e-04
                            10        20        30
                    ....*....|....*....|....*....|...
gi 1034641847    60 NPFICDCHLKWLADYLHTNPI--ETSGARCTSP 90
Cdd:smart00082    1 NPFICDCELRWLLRWLQANEHlqDPVDLRCASP 33
EGF cd00053
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ...
 711-738 1.82e-03

Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large number of proteins, mostly animal; the list of proteins currently known to contain one or more copies of an EGF-like pattern is large and varied; the functional significance of EGF-like domains in what appear to be unrelated proteins is not yet clear; a common feature is that these repeats are found in the extracellular domain of membrane-bound proteins or in proteins known to be secreted (exception: prostaglandin G/H synthase); the domain includes six cysteine residues which have been shown to be involved in disulfide bonds; the main structure is a two-stranded beta-sheet followed by a loop to a C-terminal short two-stranded sheet; Subdomains between the conserved cysteines vary in length; the region between the 5th and 6th cysteine contains two conserved glycines of which at least one is present in most EGF-like domains; a subset of these bind calcium.


Pssm-ID: 238010  Cd Length: 36  Bit Score: 37.07  E-value: 1.82e-03
                           10        20
                   ....*....|....*....|....*...
gi 1034641847  711 QDNKCKNGAHCTDAVNGYTCICPEGYSG 738
Cdd:cd00053      4 ASNPCSNGGTCVNTPGSYRCVCPPGYTG 31
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 594-626 2.75e-03

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 36.46  E-value: 2.75e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1034641847  594 NPCKHGGTCHLKEGeedGFWCICADGFEGENCE 626
Cdd:cd00054      9 NPCQNGGTCVNTVG---SYRCSCPPGYTGRNCE 38
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
 167-205 2.80e-03

Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a number of proteins with diverse functions and cellular locations. These repeats are usually involved in protein-protein interactions. Each Leucine Rich Repeat is composed of a beta-alpha unit. These units form elongated non-globular structures. Leucine Rich Repeats are often flanked by cysteine rich domains.


Pssm-ID: 463713 [Multi-domain]  Cd Length: 44  Bit Score: 36.84  E-value: 2.80e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1034641847  167 ELRLNNNEFTVLEAtgiFKKLPQLRKINFS-NNKITDIEE 205
Cdd:pfam12799    5 VLDLSNNQITDIPP---LAKLPNLETLDLSgNNKITDLSD 41
LRR_9 pfam14580
Leucine-rich repeat;
170-249 3.65e-03

Leucine-rich repeat;


Pssm-ID: 405295 [Multi-domain]  Cd Length: 175  Bit Score: 39.75  E-value: 3.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641847  170 LNNNEFTVLEAtgiFKKLPQLRKINFSNNKITDIEEGAFEGASGVNEILLTSNRL-ENVQHKMFKGLESLKTLMLRSNRI 248
Cdd:pfam14580   49 FSDNEIRKLDG---FPLLRRLKTLLLNNNRICRIGEGLGEALPNLTELILTNNNLqELGDLDPLASLKKLTFLSLLRNPV 125


                   .
gi 1034641847  249 T 249
Cdd:pfam14580  126 T 126
LRR_TYP smart00369
Leucine-rich repeats, typical (most populated) subfamily;
430-453 3.76e-03

Leucine-rich repeats, typical (most populated) subfamily;


Pssm-ID: 197687 [Multi-domain]  Cd Length: 24  Bit Score: 35.79  E-value: 3.76e-03
                            10        20
                    ....*....|....*....|....
gi 1034641847   430 MTQLLTLILSYNRLRCIPPRTFDG 453
Cdd:smart00369    1 LPNLRELDLSNNQLSSLPPGAFQG 24
LRR smart00370
Leucine-rich repeats, outliers;
430-453 3.76e-03

Leucine-rich repeats, outliers;


Pssm-ID: 197688 [Multi-domain]  Cd Length: 24  Bit Score: 35.79  E-value: 3.76e-03
                            10        20
                    ....*....|....*....|....
gi 1034641847   430 MTQLLTLILSYNRLRCIPPRTFDG 453
Cdd:smart00370    1 LPNLRELDLSNNQLSSLPPGAFQG 24
EGF cd00053
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ...
 633-661 4.28e-03

Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large number of proteins, mostly animal; the list of proteins currently known to contain one or more copies of an EGF-like pattern is large and varied; the functional significance of EGF-like domains in what appear to be unrelated proteins is not yet clear; a common feature is that these repeats are found in the extracellular domain of membrane-bound proteins or in proteins known to be secreted (exception: prostaglandin G/H synthase); the domain includes six cysteine residues which have been shown to be involved in disulfide bonds; the main structure is a two-stranded beta-sheet followed by a loop to a C-terminal short two-stranded sheet; Subdomains between the conserved cysteines vary in length; the region between the 5th and 6th cysteine contains two conserved glycines of which at least one is present in most EGF-like domains; a subset of these bind calcium.


Pssm-ID: 238010  Cd Length: 36  Bit Score: 35.92  E-value: 4.28e-03
                           10        20
                   ....*....|....*....|....*....
gi 1034641847  633 EDNDCENNSTCVDGINNYTCLCPPEYTGE 661
Cdd:cd00053      4 ASNPCSNGGTCVNTPGSYRCVCPPGYTGD 32
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 591-624 5.23e-03

EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.


Pssm-ID: 394967  Cd Length: 31  Bit Score: 35.44  E-value: 5.23e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1034641847  591 CISNPCKHGGTCHLKEGeedGFWCICADGFEGEN 624
Cdd:pfam00008    1 CAPNPCSNGGTCVDTPG---GYTCICPEGYTGKR 31
hEGF pfam12661
Human growth factor-like EGF; hEGF, or human growth factor-like EGF, domains have six ...
 637-658 6.15e-03

Human growth factor-like EGF; hEGF, or human growth factor-like EGF, domains have six conserved residues disulfide-bonded into the characteriztic 'ababcc' pattern. They are involved in growth and proliferation of cells, in proteins of the Notch/Delta pathway, neurogulin and selectins. hEGFs are also found in mosaic proteins with four-disulfide laminin EGFs such as aggrecan and perlecan. The core fold of the EGF domain consists of two small beta-hairpins packed against each other. Two major structural variants have been identified based on the structural context of the C-terminal Cys residue of disulfide 'c' in the C-terminal hairpin: hEGFs and cEGFs. In hEGFs the C-terminal thiol resides in the beta-turn, resulting in shorter loop-lengths between the Cys residues of disulfide 'c', typically C[8-9]XC. These shorter loop-lengths are also typical of the four-disulfide EGF domains, laminin ad integrin. Tandem hEGF domains have six linking residues between terminal cysteines of adjacent domains. hEGF domains may or may not bind calcium in the linker region. hEGF domains with the consensus motif CXD4X[F,Y]XCXC are hydroxylated exclusively in the Asp residue.


Pssm-ID: 463660  Cd Length: 22  Bit Score: 35.39  E-value: 6.15e-03
                           10        20
                   ....*....|....*....|..
gi 1034641847  637 CENNSTCVDGINNYTCLCPPEY 658
Cdd:pfam12661    1 CQNGGTCVDGVNGYKCQCPPGY 22
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 167-276 6.51e-03

Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 40.03  E-value: 6.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034641847  167 ELRLNNNEFTV--LEATG-IFKKLPQLRKINFSNNKITDIEEGAFEGAsgvneilltsnrlenvqhkmFKGLESLKTLML 243
Cdd:cd00116    169 ELNLANNGIGDagIRALAeGLKANCNLEVLDLNNNGLTDEGASALAET--------------------LASLKSLEVLNL 228

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1034641847  244 RSNRITCVG-----NDSFIGLSSVRLLSLYDNQITTVA 276
Cdd:cd00116    229 GDNNLTDAGaaalaSALLSPNISLLTLSLSCNDITDDG 266
EGF cd00053
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ...
 675-702 6.53e-03

Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large number of proteins, mostly animal; the list of proteins currently known to contain one or more copies of an EGF-like pattern is large and varied; the functional significance of EGF-like domains in what appear to be unrelated proteins is not yet clear; a common feature is that these repeats are found in the extracellular domain of membrane-bound proteins or in proteins known to be secreted (exception: prostaglandin G/H synthase); the domain includes six cysteine residues which have been shown to be involved in disulfide bonds; the main structure is a two-stranded beta-sheet followed by a loop to a C-terminal short two-stranded sheet; Subdomains between the conserved cysteines vary in length; the region between the 5th and 6th cysteine contains two conserved glycines of which at least one is present in most EGF-like domains; a subset of these bind calcium.


Pssm-ID: 238010  Cd Length: 36  Bit Score: 35.53  E-value: 6.53e-03
                           10        20
                   ....*....|....*....|....*...
gi 1034641847  675 NPCQHDSKCILTPKGFKCDCTPGYVGEH 702
Cdd:cd00053      6 NPCSNGGTCVNTPGSYRCVCPPGYTGDR 33
EGF_CA smart00179
Calcium-binding EGF-like domain;
668-704 6.59e-03

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 35.69  E-value: 6.59e-03
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 1034641847   668 DFCAQDlNPCQHDSKCILTPKGFKCDCTPGYV-GEHCD 704
Cdd:smart00179    3 DECASG-NPCQNGGTCVNTVGSYRCECPPGYTdGRNCE 39
LRR smart00370
Leucine-rich repeats, outliers;
454-477 7.34e-03

Leucine-rich repeats, outliers;


Pssm-ID: 197688 [Multi-domain]  Cd Length: 24  Bit Score: 35.02  E-value: 7.34e-03
                            10        20
                    ....*....|....*....|....
gi 1034641847   454 LKSLRLLSLHGNDISVVPEGAFND 477
Cdd:smart00370    1 LPNLRELDLSNNQLSSLPPGAFQG 24
LRR_TYP smart00369
Leucine-rich repeats, typical (most populated) subfamily;
454-477 7.34e-03

Leucine-rich repeats, typical (most populated) subfamily;


Pssm-ID: 197687 [Multi-domain]  Cd Length: 24  Bit Score: 35.02  E-value: 7.34e-03
                            10        20
                    ....*....|....*....|....
gi 1034641847   454 LKSLRLLSLHGNDISVVPEGAFND 477
Cdd:smart00369    1 LPNLRELDLSNNQLSSLPPGAFQG 24
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 760-787 8.89e-03

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 34.92  E-value: 8.89e-03
                           10        20
                   ....*....|....*....|....*...
gi 1034641847  760 CQNGAQCIVRINEPICQCLPGYQGEKCE 787
Cdd:cd00054     11 CQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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