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Conserved domains on  [gi|153791466|ref|NP_065754|]
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amphoterin-induced protein 1 precursor [Homo sapiens]

Protein Classification

LRR and IG_like domain-containing protein( domain architecture ID 11471650)

LRR and IG_like domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
66-223 4.95e-26

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


:

Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 110.02  E-value: 4.95e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791466  66 LDLSHNNLSRLRAEwtPTRLTQLHSLLLSHNHLNFISSEaFSPVPNLRYLDLSSNQLRTLDEFLfSDLQVLEVLLLYNNH 145
Cdd:COG4886  118 LDLSGNQLTDLPEE--LANLTNLKELDLSNNQLTDLPEP-LGNLTNLKSLDLSNNQLTDLPEEL-GNLTNLKELDLSNNQ 193

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 153791466 146 IMAVDrCAFDDMAQLQKLYLSQNQISRFPLELvkegAKLPKLTLLDLSSNKLKNlpLPDLQKLPAWIKngLYLHNNPL 223
Cdd:COG4886  194 ITDLP-EPLGNLTNLEELDLSGNQLTDLPEPL----ANLTNLETLDLSNNQLTD--LPELGNLTNLEE--LDLSNNQL 262
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 279-358 5.62e-07

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


:

Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 47.50  E-value: 5.62e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791466   279 EAHLGDTLIIKCDTKQQGMTKV-WVTPSNERVLdevTNGTVSVSKDG---SLLFQQVQVEDGGVYTCYAMGETFNETLSV 354
Cdd:smart00410   5 TVKEGESVTLSCEASGSPPPEVtWYKQGGKLLA---ESGRFSVSRSGstsTLTISNVTPEDSGTYTCAATNSSGSASSGT 81


                   ....
gi 153791466   355 ELKV 358
Cdd:smart00410  82 TLTV 85
 
Name Accession Description Interval E-value
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
66-223 4.95e-26

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 110.02  E-value: 4.95e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791466  66 LDLSHNNLSRLRAEwtPTRLTQLHSLLLSHNHLNFISSEaFSPVPNLRYLDLSSNQLRTLDEFLfSDLQVLEVLLLYNNH 145
Cdd:COG4886  118 LDLSGNQLTDLPEE--LANLTNLKELDLSNNQLTDLPEP-LGNLTNLKSLDLSNNQLTDLPEEL-GNLTNLKELDLSNNQ 193

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 153791466 146 IMAVDrCAFDDMAQLQKLYLSQNQISRFPLELvkegAKLPKLTLLDLSSNKLKNlpLPDLQKLPAWIKngLYLHNNPL 223
Cdd:COG4886  194 ITDLP-EPLGNLTNLEELDLSGNQLTDLPEPL----ANLTNLETLDLSNNQLTD--LPELGNLTNLEE--LDLSNNQL 262
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
45-213 1.32e-13

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 73.19  E-value: 1.32e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791466  45 LSCSKQQLPNVPHSLPSYTALLDLSHNNLSRLraewtPTRL-TQLHSLLLSHNHLNFISSEafspVPN-LRYLDLSSNQL 122
Cdd:PRK15370 225 LYANSNQLTSIPATLPDTIQEMELSINRITEL-----PERLpSALQSLDLFHNKISCLPEN----LPEeLRYLSVYDNSI 295

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791466 123 RTLDE---------FLFSD-LQVLEVLLLYNNHIMAVDRCAFDDM-----AQLQKLYLSQNQISRFPLELVkegaklPKL 187
Cdd:PRK15370 296 RTLPAhlpsgithlNVQSNsLTALPETLPPGLKTLEAGENALTSLpaslpPELQVLDVSKNQITVLPETLP------PTI 369

                        170       180
                 ....*....|....*....|....*.
gi 153791466 188 TLLDLSSNKLKNLPlpdlQKLPAWIK 213
Cdd:PRK15370 370 TTLDVSRNALTNLP----ENLPAALQ 391
LRR_8 pfam13855
Leucine rich repeat;
86-146 8.45e-12

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 60.23  E-value: 8.45e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153791466   86 TQLHSLLLSHNHLNFISSEAFSPVPNLRYLDLSSNQLRTLDEFLFSDLQVLEVLLLYNNHI 146
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 83-238 7.80e-10

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: 59.03  E-value: 7.80e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791466  83 TRLTQLHsllLSHNHLNFIssEAFSPVPNLRYLDLSSNQLRTLDEFLFsdLQVLEVLLLYNNHIMAVDRcaFDDMAQLQK 162
Cdd:cd21340    2 KRITHLY---LNDKNITKI--DNLSLCKNLKVLYLYDNKITKIENLEF--LTNLTHLYLQNNQIEKIEN--LENLVNLKK 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791466 163 LYLSQNQISR--------FPLELVKEGAKLPK-----------------LTLLDLSSNKLKNL-PLPDLQKLpawikNGL 216
Cdd:cd21340   73 LYLGGNRISVveglenltNLEELHIENQRLPPgekltfdprslaalsnsLRVLNISGNNIDSLePLAPLRNL-----EQL 147

                        170       180
                 ....*....|....*....|..
gi 153791466 217 YLHNNPLNCDCELYQLFSHWQY 238
Cdd:cd21340  148 DASNNQISDLEELLDLLSSWPS 169
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 279-358 5.62e-07

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 47.50  E-value: 5.62e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791466   279 EAHLGDTLIIKCDTKQQGMTKV-WVTPSNERVLdevTNGTVSVSKDG---SLLFQQVQVEDGGVYTCYAMGETFNETLSV 354
Cdd:smart00410   5 TVKEGESVTLSCEASGSPPPEVtWYKQGGKLLA---ESGRFSVSRSGstsTLTISNVTPEDSGTYTCAATNSSGSASSGT 81


                   ....
gi 153791466   355 ELKV 358
Cdd:smart00410  82 TLTV 85
Ig_Sema3 cd05871
Immunoglobulin (Ig)-like domain of class III semaphorin Sema3; The members here are composed ...
 283-358 2.78e-05

Immunoglobulin (Ig)-like domain of class III semaphorin Sema3; The members here are composed of the immunoglobulin (Ig)-like domain of Sema3 and similar proteins. Semaphorins are classified based on structural features additional to the Sema domain. Sema3 is a Class III semaphorin that is secreted. It is a vertebrate class having a Sema domain, an Ig domain, a short basic domain. They have been shown to be axonal guidance cues and have a part in the regulation of the cardiovascular, immune, and respiratory systems. Sema3A, the prototype member of this class III subfamily, induces growth cone collapse and is an inhibitor of axonal sprouting. In perinatal rat cortex, it acts as a chemoattractant and functions to direct the orientated extension of apical dendrites. It may play a role, prior to the development of apical dendrites, in signaling the radial migration of newborn cortical neurons towards the upper layers. Sema3A selectively inhibits vascular endothelial growth factor receptor (VEGF)-induced angiogenesis and induces microvascular permeability. This group also includes Sema3B, -C, -D, -E, -G.


Pssm-ID: 409455  Cd Length: 92  Bit Score: 42.72  E-value: 2.78e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 153791466 283 GDTLIIKCDTKQQGMTKVW-VTPSNERVLDEVTNGTVSVSKDGSLLFQQVQVEDGGVYTCYAMGETFNETLS-VELKV 358
Cdd:cd05871   12 GNSTFLECLPKSPQATVKWlFQRGGDQRKEEVKSEERLIVTDRGLLLRSLQRSDAGVYTCQAVEHGFSQTLVkIRLHV 89
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 279-343 2.08e-04

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 39.86  E-value: 2.08e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153791466  279 EAHLGDTLIIKCDTKQQGMTKVWVTPSNERVLDEVTNGTVSVSKDGSLLFQQVQVEDGGVYTCYA 343
Cdd:pfam13927  12 TVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVA 76
 
Name Accession Description Interval E-value
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
66-223 4.95e-26

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 110.02  E-value: 4.95e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791466  66 LDLSHNNLSRLRAEwtPTRLTQLHSLLLSHNHLNFISSEaFSPVPNLRYLDLSSNQLRTLDEFLfSDLQVLEVLLLYNNH 145
Cdd:COG4886  118 LDLSGNQLTDLPEE--LANLTNLKELDLSNNQLTDLPEP-LGNLTNLKSLDLSNNQLTDLPEEL-GNLTNLKELDLSNNQ 193

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 153791466 146 IMAVDrCAFDDMAQLQKLYLSQNQISRFPLELvkegAKLPKLTLLDLSSNKLKNlpLPDLQKLPAWIKngLYLHNNPL 223
Cdd:COG4886  194 ITDLP-EPLGNLTNLEELDLSGNQLTDLPEPL----ANLTNLETLDLSNNQLTD--LPELGNLTNLEE--LDLSNNQL 262
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
44-235 9.04e-25

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 106.17  E-value: 9.04e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791466  44 ILSCSKQQLPNVPHSLPSYTAL--LDLSHNNLSRLRAEWTPtrLTQLHSLLLSHNHLNFISsEAFSPVPNLRYLDLSSNQ 121
Cdd:COG4886  140 ELDLSNNQLTDLPEPLGNLTNLksLDLSNNQLTDLPEELGN--LTNLKELDLSNNQITDLP-EPLGNLTNLEELDLSGNQ 216

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791466 122 LRTLDEFLfSDLQVLEVLLLYNNHIMAVDrcAFDDMAQLQKLYLSQNQISRFPlelvkEGAKLPKLTLLDLSSNKLKNLP 201
Cdd:COG4886  217 LTDLPEPL-ANLTNLETLDLSNNQLTDLP--ELGNLTNLEELDLSNNQLTDLP-----PLANLTNLKTLDLSNNQLTDLK 288

                        170       180       190
                 ....*....|....*....|....*....|....
gi 153791466 202 LPDLQKLPAWIKNGLYLHNNPLNCDCELYQLFSH 235
Cdd:COG4886  289 LKELELLLGLNSLLLLLLLLNLLELLILLLLLTT 322
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
66-223 5.29e-22

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 98.08  E-value: 5.29e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791466  66 LDLSHNNLSrlraewtpTRLTQLHSLLLSHNHLNFIsSEAFSPVPNLRYLDLSSNQLRTLDEFLfSDLQVLEVLLLYNNH 145
Cdd:COG4886  101 LDLSGNEEL--------SNLTNLESLDLSGNQLTDL-PEELANLTNLKELDLSNNQLTDLPEPL-GNLTNLKSLDLSNNQ 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791466 146 IMAVDRcAFDDMAQLQKLYLSQNQISRFPLELvkegAKLPKLTLLDLSSNKLKNLP--LPDLQKLpawikNGLYLHNNPL 223
Cdd:COG4886  171 LTDLPE-ELGNLTNLKELDLSNNQITDLPEPL----GNLTNLEELDLSGNQLTDLPepLANLTNL-----ETLDLSNNQL 240
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
45-247 1.27e-18

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 88.07  E-value: 1.27e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791466  45 LSCSKQQLPNVPHSLPSYTAL--LDLSHNNLSRLRAEWTptRLTQLHSLLLSHNHLNFISSEaFSPVPNLRYLDLSSNQL 122
Cdd:COG4886  164 LDLSNNQLTDLPEELGNLTNLkeLDLSNNQITDLPEPLG--NLTNLEELDLSGNQLTDLPEP-LANLTNLETLDLSNNQL 240

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791466 123 RTLDEFlfSDLQVLEVLLLYNNHIMAVDRCAfdDMAQLQKLYLSQNQISRFPLELVKEGAKLPKLTLLDLSSNKLKNLPL 202
Cdd:COG4886  241 TDLPEL--GNLTNLEELDLSNNQLTDLPPLA--NLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLELLIL 316

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 153791466 203 PDLQKLPAWIKNGLYLHNNPLNCDCELYQLFSHWQYRQLSSVMDF 247
Cdd:COG4886  317 LLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLSL 361
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
45-213 1.32e-13

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 73.19  E-value: 1.32e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791466  45 LSCSKQQLPNVPHSLPSYTALLDLSHNNLSRLraewtPTRL-TQLHSLLLSHNHLNFISSEafspVPN-LRYLDLSSNQL 122
Cdd:PRK15370 225 LYANSNQLTSIPATLPDTIQEMELSINRITEL-----PERLpSALQSLDLFHNKISCLPEN----LPEeLRYLSVYDNSI 295

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791466 123 RTLDE---------FLFSD-LQVLEVLLLYNNHIMAVDRCAFDDM-----AQLQKLYLSQNQISRFPLELVkegaklPKL 187
Cdd:PRK15370 296 RTLPAhlpsgithlNVQSNsLTALPETLPPGLKTLEAGENALTSLpaslpPELQVLDVSKNQITVLPETLP------PTI 369

                        170       180
                 ....*....|....*....|....*.
gi 153791466 188 TLLDLSSNKLKNLPlpdlQKLPAWIK 213
Cdd:PRK15370 370 TTLDVSRNALTNLP----ENLPAALQ 391
LRR_8 pfam13855
Leucine rich repeat;
86-146 8.45e-12

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 60.23  E-value: 8.45e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153791466   86 TQLHSLLLSHNHLNFISSEAFSPVPNLRYLDLSSNQLRTLDEFLFSDLQVLEVLLLYNNHI 146
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
LRR_8 pfam13855
Leucine rich repeat;
110-170 1.76e-11

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 59.46  E-value: 1.76e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153791466  110 PNLRYLDLSSNQLRTLDEFLFSDLQVLEVLLLYNNHIMAVDRCAFDDMAQLQKLYLSQNQI 170
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
LRR_8 pfam13855
Leucine rich repeat;
66-122 1.02e-10

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 57.15  E-value: 1.02e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 153791466   66 LDLSHNNLSRLRAEWtPTRLTQLHSLLLSHNHLNFISSEAFSPVPNLRYLDLSSNQL 122
Cdd:pfam13855   6 LDLSNNRLTSLDDGA-FKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 83-238 7.80e-10

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: 59.03  E-value: 7.80e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791466  83 TRLTQLHsllLSHNHLNFIssEAFSPVPNLRYLDLSSNQLRTLDEFLFsdLQVLEVLLLYNNHIMAVDRcaFDDMAQLQK 162
Cdd:cd21340    2 KRITHLY---LNDKNITKI--DNLSLCKNLKVLYLYDNKITKIENLEF--LTNLTHLYLQNNQIEKIEN--LENLVNLKK 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791466 163 LYLSQNQISR--------FPLELVKEGAKLPK-----------------LTLLDLSSNKLKNL-PLPDLQKLpawikNGL 216
Cdd:cd21340   73 LYLGGNRISVveglenltNLEELHIENQRLPPgekltfdprslaalsnsLRVLNISGNNIDSLePLAPLRNL-----EQL 147

                        170       180
                 ....*....|....*....|..
gi 153791466 217 YLHNNPLNCDCELYQLFSHWQY 238
Cdd:cd21340  148 DASNNQISDLEELLDLLSSWPS 169
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
44-332 2.18e-07

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 53.55  E-value: 2.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791466  44 ILSCSKqqLPNVPHSLPSYTALLDLSHNNLSRLRAEwTPTRLTQLHsllLSHNHLNFISSeafSPVPNLRYLDLSSNQLR 123
Cdd:PRK15370 268 DLFHNK--ISCLPENLPEELRYLSVYDNSIRTLPAH-LPSGITHLN---VQSNSLTALPE---TLPPGLKTLEAGENALT 338

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791466 124 TLDEFLFSDLQVLEVlllYNNHIMAVDRCAfddMAQLQKLYLSQNQISRFPlelvkegAKLP-KLTLLDLSSNKLKNLPl 202
Cdd:PRK15370 339 SLPASLPPELQVLDV---SKNQITVLPETL---PPTITTLDVSRNALTNLP-------ENLPaALQIMQASRNNLVRLP- 404

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791466 203 pdlQKLPAWIKNG-----LYLHNNPLNCDC--ELYQLFSHWQYRQLSSVMDFQEDLYCMNSKKLHNVFNlSFLNCGEYKE 275
Cdd:PRK15370 405 ---ESLPHFRGEGpqptrIIVEYNPFSERTiqNMQRLMSSVGYQGPRVLFAMGDFSIVRVTRPLHQAVQ-GWLTNLEEED 480

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791466 276 ----RAWEA------------HLGDTLIIK-CDTKQQgmTKVWV------TPSNERVLDEVTNGTVSVSKDGSLLFQQVQ 332
Cdd:PRK15370 481 vnqwRAFETevnaaafsmfldRLSDTQNTRhPDFKEQ--VSAWLmrlaedSALRETAFIIAMDATISCEDRVTLAYHQMQ 558
LRR_8 pfam13855
Leucine rich repeat;
136-197 2.86e-07

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 47.52  E-value: 2.86e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153791466  136 LEVLLLYNNHIMAVDRCAFDDMAQLQKLYLSQNQISRFPLElvkEGAKLPKLTLLDLSSNKL 197
Cdd:pfam13855   3 LRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPG---AFSGLPSLRYLDLSGNRL 61
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 279-358 5.62e-07

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 47.50  E-value: 5.62e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791466   279 EAHLGDTLIIKCDTKQQGMTKV-WVTPSNERVLdevTNGTVSVSKDG---SLLFQQVQVEDGGVYTCYAMGETFNETLSV 354
Cdd:smart00410   5 TVKEGESVTLSCEASGSPPPEVtWYKQGGKLLA---ESGRFSVSRSGstsTLTISNVTPEDSGTYTCAATNSSGSASSGT 81


                   ....
gi 153791466   355 ELKV 358
Cdd:smart00410  82 TLTV 85
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 48-197 1.84e-06

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 50.62  E-value: 1.84e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791466  48 SKQQLPNVPHSLPSYTAL--LDLSHNNLSrlrAEwTPTRLTQLHSLllshNHLNFISSEAFSPVP-------NLRYLDLS 118
Cdd:PLN00113 197 SNQLVGQIPRELGQMKSLkwIYLGYNNLS---GE-IPYEIGGLTSL----NHLDLVYNNLTGPIPsslgnlkNLQYLFLY 268

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791466 119 SNQ-----------LRTLDEFLFSD-------------LQVLEVLLLYNNHIMAVDRCAFDDMAQLQKLYLSQNqisRFP 174
Cdd:PLN00113 269 QNKlsgpippsifsLQKLISLDLSDnslsgeipelviqLQNLEILHLFSNNFTGKIPVALTSLPRLQVLQLWSN---KFS 345

                        170       180
                 ....*....|....*....|...
gi 153791466 175 LELVKEGAKLPKLTLLDLSSNKL 197
Cdd:PLN00113 346 GEIPKNLGKHNNLTVLDLSTNNL 368
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 23-198 9.82e-06

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: 47.35  E-value: 9.82e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791466  23 EVARAGRAVVSCPAA--CLCASNILSCSKQQL-PNVPHSLPSYT-----ALLDLSHNNLS----RLRAEWTPTRLTQLHS 90
Cdd:cd00116   62 ETGRIPRGLQSLLQGltKGCGLQELDLSDNALgPDGCGVLESLLrssslQELKLNNNGLGdrglRLLAKGLKDLPPALEK 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791466  91 LLLSHNHLNFISSE----AFSPVPNLRYLDLSSNQL-----RTLDEFLfSDLQVLEVLLLYNNHIM---AVDRC-AFDDM 157
Cdd:cd00116  142 LVLGRNRLEGASCEalakALRANRDLKELNLANNGIgdagiRALAEGL-KANCNLEVLDLNNNGLTdegASALAeTLASL 220

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 153791466 158 AQLQKLYLSQNQISRFPLELVKEGAKLPKLTL--LDLSSNKLK 198
Cdd:cd00116  221 KSLEVLNLGDNNLTDAGAAALASALLSPNISLltLSLSCNDIT 263
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 66-195 1.27e-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: 46.32  E-value: 1.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791466  66 LDLSHNNLSRLRAEWTPTRLTQLHsllLSHNHLNFIssEAFSPVPNLRYLDLSSNQLRTLDEFLFSD---------LQVL 136
Cdd:cd21340   51 LYLQNNQIEKIENLENLVNLKKLY---LGGNRISVV--EGLENLTNLEELHIENQRLPPGEKLTFDPrslaalsnsLRVL 125

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153791466 137 EVlllYNNHIMAVDRCAFddMAQLQKLYLSQNQISRFP--LELVKegaKLPKLTLLDLSSN 195
Cdd:cd21340  126 NI---SGNNIDSLEPLAP--LRNLEQLDASNNQISDLEelLDLLS---SWPSLRELDLTGN 178
Ig_Sema3 cd05871
Immunoglobulin (Ig)-like domain of class III semaphorin Sema3; The members here are composed ...
 283-358 2.78e-05

Immunoglobulin (Ig)-like domain of class III semaphorin Sema3; The members here are composed of the immunoglobulin (Ig)-like domain of Sema3 and similar proteins. Semaphorins are classified based on structural features additional to the Sema domain. Sema3 is a Class III semaphorin that is secreted. It is a vertebrate class having a Sema domain, an Ig domain, a short basic domain. They have been shown to be axonal guidance cues and have a part in the regulation of the cardiovascular, immune, and respiratory systems. Sema3A, the prototype member of this class III subfamily, induces growth cone collapse and is an inhibitor of axonal sprouting. In perinatal rat cortex, it acts as a chemoattractant and functions to direct the orientated extension of apical dendrites. It may play a role, prior to the development of apical dendrites, in signaling the radial migration of newborn cortical neurons towards the upper layers. Sema3A selectively inhibits vascular endothelial growth factor receptor (VEGF)-induced angiogenesis and induces microvascular permeability. This group also includes Sema3B, -C, -D, -E, -G.


Pssm-ID: 409455  Cd Length: 92  Bit Score: 42.72  E-value: 2.78e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 153791466 283 GDTLIIKCDTKQQGMTKVW-VTPSNERVLDEVTNGTVSVSKDGSLLFQQVQVEDGGVYTCYAMGETFNETLS-VELKV 358
Cdd:cd05871   12 GNSTFLECLPKSPQATVKWlFQRGGDQRKEEVKSEERLIVTDRGLLLRSLQRSDAGVYTCQAVEHGFSQTLVkIRLHV 89
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 66-199 4.53e-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: 45.94  E-value: 4.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791466  66 LDLSHNNLSRLRAEWTPTRL---TQLHSLLLSHNHLNFISSEAFSP----VPNLRYLDLSSNQLRTLD-EFLFSDLQV-- 135
Cdd:COG5238  269 LYLSGNQIGAEGAIALAKALqgnTTLTSLDLSVNRIGDEGAIALAEglqgNKTLHTLNLAYNGIGAQGaIALAKALQEnt 348

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 153791466 136 -LEVLLLYNNHI----MAVDRCAFDDMAQLQKLYLSQNQISRFPLELVKEGAKLPKLTLLDLSSNKLKN 199
Cdd:COG5238  349 tLHSLDLSDNQIgdegAIALAKYLEGNTTLRELNLGKNNIGKQGAEALIDALQTNRLHTLILDGNLIGA 417
Ig_Semaphorin_C cd04979
Immunoglobulin (Ig)-like domain at the C-terminus of semaphorins; The members here are ...
 283-359 5.65e-05

Immunoglobulin (Ig)-like domain at the C-terminus of semaphorins; The members here are composed of the immunoglobulin (Ig)-like domain in semaphorins. Semaphorins are transmembrane protein that have important roles in a variety of tissues. Functionally, semaphorins were initially characterized for their importance in the development of the nervous system and in axonal guidance. Later they have been found to be important for the formation and functioning of the cardiovascular, endocrine, gastrointestinal, hepatic, immune, musculoskeletal, renal, reproductive, and respiratory systems. Semaphorins function through binding to their receptors and transmembrane semaphorins also serves as receptors themselves. Although molecular mechanism of semaphorins is poorly understood, the Ig-like domains may be involved in ligand binding or dimerization.


Pssm-ID: 409368  Cd Length: 88  Bit Score: 41.68  E-value: 5.65e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 153791466 283 GDTLIIKCDTKQQGMTKVWVTpsNERVLDEVTNGTVSVSKDGSLLFQQVQVEDGGVYTCYAmGETFNETLSVELKVH 359
Cdd:cd04979   11 GDTVILSCSVKSNNAPVTWIH--NGKKVPRYRSPRLVLKTERGLLIRSAQEADAGVYECHS-GERVLGSTLRSVTLH 84
IgV_HHLA2 cd16091
Immunoglobulin Variable (IgV) domain in HERV-H LTR-associating 2 (HHLA2); The members here are ...
 311-358 1.16e-04

Immunoglobulin Variable (IgV) domain in HERV-H LTR-associating 2 (HHLA2); The members here are composed of the immunoglobulin variable (IgV) region in HERV-H LTR-associating 2 (HHLA2; also known as B7-H7/B7 homolog 7). HHLA2 is a member of the B7 family of immune regulatory proteins. Mature human HHLA2 consists of an extracellular domain (ECD) with three immunoglobulin-like domains, a transmembrane segment, and a cytoplasmic domain. HHLA2 is widely expressed in human cancers including non-small cell lung carcinoma (NSCLS), triple negative breast cancer (TNBC), and melanoma, but has limited expression on normal tissues. Interestingly, unlike other members of B7 family, HHLA2 is not expressed in mice or rats. HHLA2 functions as a T cell coinhibitory molecules as it inhibits the proliferation of activated CD4(+) and CD8(+) T cells and their cytokine production. Furthermore, HHLA2 is constitutively expressed on the surface of human monocytes and is induced on B cells after stimulation, however it is not inducible on T cells.


Pssm-ID: 409512  Cd Length: 107  Bit Score: 41.22  E-value: 1.16e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 153791466 311 DEVTNGtvsvskDGSLLFQQVQVEDGGVYTCYAMGETFNETLSVELKV 358
Cdd:cd16091   66 DQISNG------NASLLLRRVQLQDEGRYKCYTSTIIGNQESFVNLKV 107
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 66-174 1.30e-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: 43.24  E-value: 1.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791466  66 LDLSHNNLSRLRAEWTPTRLTQLHsllLSHNHLNFISSEAFSP------VPNLRYLDLSSNQLRTLDEflFSDLQVLEVL 139
Cdd:cd21340   73 LYLGGNRISVVEGLENLTNLEELH---IENQRLPPGEKLTFDPrslaalSNSLRVLNISGNNIDSLEP--LAPLRNLEQL 147

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 153791466 140 LLYNNHIMAVDR--CAFDDMAQLQKLYLSQNQISRFP 174
Cdd:cd21340  148 DASNNQISDLEEllDLLSSWPSLRELDLTGNPVCKKP 184
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 279-343 2.08e-04

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 39.86  E-value: 2.08e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153791466  279 EAHLGDTLIIKCDTKQQGMTKVWVTPSNERVLDEVTNGTVSVSKDGSLLFQQVQVEDGGVYTCYA 343
Cdd:pfam13927  12 TVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVA 76
PRK15387 PRK15387
type III secretion system effector E3 ubiquitin transferase SspH2;
23-211 2.12e-04

type III secretion system effector E3 ubiquitin transferase SspH2;


Pssm-ID: 185285 [Multi-domain]  Cd Length: 788  Bit Score: 44.00  E-value: 2.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791466  23 EVARAGRAVVSCPAACLCASN-ILSCSKQQLPNVPHSLPSYTALLDLSHNNLSRLraewtPTRLTQLHSLLLSHNHLNFI 101
Cdd:PRK15387 183 EESRGRAAVVQKMRACLNNGNaVLNVGESGLTTLPDCLPAHITTLVIPDNNLTSL-----PALPPELRTLEVSGNQLTSL 257

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791466 102 sseafsPV--PNLRYLDLSSNQLRTLDEFLFSdlqvLEVLLLYNNHIMAVDRCAfddmAQLQKLYLSQNQISRFPL---E 176
Cdd:PRK15387 258 ------PVlpPGLLELSIFSNPLTHLPALPSG----LCKLWIFGNQLTSLPVLP----PGLQELSVSDNQLASLPAlpsE 323

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 153791466 177 LVKEGA------KLPK----LTLLDLSSNKLKNLP-LP-DLQKLPAW 211
Cdd:PRK15387 324 LCKLWAynnqltSLPTlpsgLQELSVSDNQLASLPtLPsELYKLWAY 370
IgV_CEACAM_D1 cd05774
First immunoglobulin (Ig)-like domain of carcinoembryonic antigen (CEA) related cell adhesion ...
 302-358 4.07e-04

First immunoglobulin (Ig)-like domain of carcinoembryonic antigen (CEA) related cell adhesion molecule (CEACAM); The members here are composed of the immunoglobulin (Ig)-like domain 1 in carcinoembryonic antigen (CEA) related cell adhesion molecule (CEACAM) proteins. The CEA family is a group of anchored or secreted glycoproteins, expressed by epithelial cells, leukocytes, endothelial cells, and placenta. The CEA family is divided into the CEACAM and pregnancy-specific glycoprotein (PSG) subfamilies. This group represents the CEACAM subfamily. CEACAM1 has many important cellular functions: it is a cell adhesion molecule and a signaling molecule that regulates the growth of tumor cells, an angiogenic factor, and a receptor for bacterial and viral pathogens, including mouse hepatitis virus (MHV). In mice, four isoforms of CEACAM1 generated by alternative splicing have either two (D1, D4) or four (D1-D4) Ig-like domains on the cell surface.


Pssm-ID: 409430  Cd Length: 105  Bit Score: 39.95  E-value: 4.07e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 153791466 302 VTPSNERVLDEVTNGTVSVSKDGSLLFQQVQVEDGGVYTCYAMGETFN-ETLSVELKV 358
Cdd:cd05774   48 IISTNSSTPGPAYSGRETIYPNGSLLIQNVTQKDTGFYTLQTITADLQtEQASVHLQV 105
Ig2_IL1R-like cd05757
Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 320-358 4.40e-04

Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; The members here are composed of the second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R; also known as cluster of differentiation (CD) 121). IL-1 alpha and IL-1 beta are cytokines which participate in the regulation of inflammation, immune responses, and hematopoiesis. These cytokines bind to the IL-1 receptor type 1 (IL1R1), which is activated on additional association with interleukin-1 receptor accessory protein (IL1RAP). IL-1 also binds a second receptor designated type II (IL1R2). Mature IL1R1 consists of three IG-like domains, a transmembrane domain, and a large cytoplasmic domain. Mature IL1R2 is organized similarly except that it has a short cytoplasmic domain. The latter does not initiate signal transduction. A naturally occurring cytokine IL-1RA (IL-1 receptor antagonist) is widely expressed and binds to IL-1 receptors, inhibiting the binding of IL-1 alpha and IL-1 beta. This group also contains ILIR-like 1 (IL1R1L) which maps to the same chromosomal location as IL1R1 and IL1R2.


Pssm-ID: 409415  Cd Length: 92  Bit Score: 39.23  E-value: 4.40e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 153791466 320 VSKDGSLLFQQVQVEDGGVYTCYA----MGETFNETLSVELKV 358
Cdd:cd05757   48 IPKGSKLLIQNVTEEDAGNYTCKFtythNGKQYNVTRTISLTV 90
IgI_Lingo-1 cd20969
Immunoglobulin I-set domain of the Leucine-rich repeat and immunoglobin-like domain-containing ...
 283-358 9.07e-04

Immunoglobulin I-set domain of the Leucine-rich repeat and immunoglobin-like domain-containing protein 1 (Lingo-1); The members here are composed of the immunoglobulin I-set (IgI) domain of the Leucine-rich repeat and immunoglobin-like domain-containing protein 1 (Lingo-1). Human Lingo-1 is a central nervous system-specific transmembrane glycoprotein also known as LERN-1, which functions as a negative regulator of neuronal survival, axonal regeneration, and oligodendrocyte differentiation and myelination. Lingo-1 is a key component of the Nogo receptor signaling complex (RTN4R/NGFR) in RhoA activation responsible for some inhibition of axonal regeneration by myelin-associated factors. The ligand-binding ectodomain of human Lingo-1 contains a bimodular, kinked structure composed of leucine-rich repeat (LRR) and immunoglobulin (Ig)-like modules. Diseases associated with Lingo-1 include mental retardation, autosomal recessive 64 and essential tremor. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the Lingo-1 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409561  Cd Length: 92  Bit Score: 38.52  E-value: 9.07e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 153791466 283 GDTLIIKCdtKQQGM---TKVWVTPsNERVLDEVTNGTVSVSKDGSLLFQQVQVEDGGVYTCYAMGETFNETLSVELKV 358
Cdd:cd20969   17 GHTVQFVC--RADGDpppAILWLSP-RKHLVSAKSNGRLTVFPDGTLEVRYAQVQDNGTYLCIAANAGGNDSMPAHLHV 92
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 59-223 1.29e-03

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 41.37  E-value: 1.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791466  59 LPsYTALLDLSHNNLSRLRAEWTPTRLTQLHSLLLSHNhlNFISSEAFSPVPNLRYLDLSSNQLR---TLDEFLFSDLQV 135
Cdd:PLN00113  92 LP-YIQTINLSNNQLSGPIPDDIFTTSSSLRYLNLSNN--NFTGSIPRGSIPNLETLDLSNNMLSgeiPNDIGSFSSLKV 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791466 136 ---------------------LEVLLLYNNHIMAVDRCAFDDMAQLQKLYLSQNQISRfplELVKEGAKLPKLTLLDLSS 194
Cdd:PLN00113 169 ldlggnvlvgkipnsltnltsLEFLTLASNQLVGQIPRELGQMKSLKWIYLGYNNLSG---EIPYEIGGLTSLNHLDLVY 245

                        170       180       190
                 ....*....|....*....|....*....|...
gi 153791466 195 NKLKNlPLP----DLQKLpawikNGLYLHNNPL 223
Cdd:PLN00113 246 NNLTG-PIPsslgNLKNL-----QYLFLYQNKL 272
LRR_9 pfam14580
Leucine-rich repeat;
115-201 1.30e-03

Leucine-rich repeat;


Pssm-ID: 405295 [Multi-domain]  Cd Length: 175  Bit Score: 39.75  E-value: 1.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791466  115 LDLSSNQLRTLDEFLFsdLQVLEVLLLYNNHIMAVDRCAFDDMAQLQKLYLSQNQISRF----PLelvkegAKLPKLTLL 190
Cdd:pfam14580  47 IDFSDNEIRKLDGFPL--LRRLKTLLLNNNRICRIGEGLGEALPNLTELILTNNNLQELgdldPL------ASLKKLTFL 118

                          90
                  ....*....|.
gi 153791466  191 DLSSNKLKNLP 201
Cdd:pfam14580 119 SLLRNPVTNKP 129
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 306-343 1.45e-03

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 37.31  E-value: 1.45e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 153791466 306 NERVLDEVTNGTVSVSKDGSLLFQQVQVEDGGVYTCYA 343
Cdd:cd00096   21 GKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVA 58
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 85-195 1.69e-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: 40.42  E-value: 1.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791466  85 LTQLHSLLLSHNHLNFIS----SEAFSPVPNLRYLDLSSNQLR-----TLDEFLFSDLQVLEVLLLYNNHIM---AVDRC 152
Cdd:cd00116  192 NCNLEVLDLNNNGLTDEGasalAETLASLKSLEVLNLGDNNLTdagaaALASALLSPNISLLTLSLSCNDITddgAKDLA 271

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 153791466 153 AF-DDMAQLQKLYLSQNQISRFPLELVKEG--AKLPKLTLLDLSSN 195
Cdd:cd00116  272 EVlAEKESLLELDLRGNKFGEEGAQLLAESllEPGNELESLWVKDD 317
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
 159-197 2.29e-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: 36.07  E-value: 2.29e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 153791466  159 QLQKLYLSQNQISRFPLElvkegAKLPKLTLLDLSSNKL 197
Cdd:pfam12799   2 NLEVLDLSNNQITDIPPL-----AKLPNLETLDLSGNNK 35
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
 86-128 2.48e-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: 35.68  E-value: 2.48e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 153791466   86 TQLHSLLLSHNHLNFIssEAFSPVPNLRYLDLSSN-QLRTLDEF 128
Cdd:pfam12799   1 PNLEVLDLSNNQITDI--PPLAKLPNLETLDLSGNnKITDLSDL 42
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 66-224 2.82e-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: 39.65  E-value: 2.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791466  66 LDLSHNNLSRLRAEWTPTRLTQLHSLLLSHNHLNFISS---------EAFSPVPNLRYLDLSSNqlrtldEFLFSDLQVL 136
Cdd:cd00116   28 LRLEGNTLGEEAAKALASALRPQPSLKELCLSLNETGRiprglqsllQGLTKGCGLQELDLSDN------ALGPDGCGVL 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791466 137 EVLLLynnhimavdrcafddMAQLQKLYLSQNQISRFPLELVKEGAK--LPKLTLLDLSSNKLKNLPLPDLQKlpAWIKN 214
Cdd:cd00116  102 ESLLR---------------SSSLQELKLNNNGLGDRGLRLLAKGLKdlPPALEKLVLGRNRLEGASCEALAK--ALRAN 164

                        170
                 ....*....|....
gi 153791466 215 G----LYLHNNPLN 224
Cdd:cd00116  165 RdlkeLNLANNGIG 178
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 321-359 2.94e-03

Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 and CTL4 amongst others.


Pssm-ID: 462230  Cd Length: 109  Bit Score: 37.44  E-value: 2.94e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 153791466  321 SKDGSLLFQQVQVEDGGVYTCYAMG-ETFNETLSVELKVH 359
Cdd:pfam07686  70 NGDGSLTIQNLTLSDSGTYTCAVIPsGEGVFGKGTRLTVL 109
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 83-199 3.05e-03

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: 39.77  E-value: 3.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791466  83 TRLTQLHSLLLSHNHLNFISSEAFSPV----PNLRYLDLSSNQL-----RTLDEFLfSDLQVLEVLLLYNNHIMAVDRCA 153
Cdd:COG5238  233 KGNKSLTTLDLSNNQIGDEGVIALAEAlknnTTVETLYLSGNQIgaegaIALAKAL-QGNTTLTSLDLSVNRIGDEGAIA 311

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 153791466 154 FDDMAQ----LQKLYLSQNQISRFPLE-LVKEGAKLPKLTLLDLSSNKLKN 199
Cdd:COG5238  312 LAEGLQgnktLHTLNLAYNGIGAQGAIaLAKALQENTTLHSLDLSDNQIGD 362
LRR_8 pfam13855
Leucine rich repeat;
159-223 4.31e-03

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 35.58  E-value: 4.31e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 153791466  159 QLQKLYLSQNQISRFPLELVKegaKLPKLTLLDLSSNKLKNLPLPDLQKLPA--WikngLYLHNNPL 223
Cdd:pfam13855   2 NLRSLDLSNNRLTSLDDGAFK---GLSNLKVLDLSNNLLTTLSPGAFSGLPSlrY----LDLSGNRL 61
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
44-225 5.38e-03

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 39.15  E-value: 5.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791466  44 ILSCSKQQLPNVPhSLPSYTAL--LDLSHNNLSRLRAEwtpTRLTQLHSLLLSHNH---LNFISSEAFSPVPNLRYLDLS 118
Cdd:COG4886  232 TLDLSNNQLTDLP-ELGNLTNLeeLDLSNNQLTDLPPL---ANLTNLKTLDLSNNQltdLKLKELELLLGLNSLLLLLLL 307

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791466 119 SNQLRTLDEFLFSDLQVLEVLLLYNNHIMAVDRCAFDDMAQLQKLYLSQNQISRFPLELVKEGAKLPKLTLLDLSSNKLK 198
Cdd:COG4886  308 LNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLSLLLTLLLTLGLLGLLEATLLTLALLLL 387

                        170       180
                 ....*....|....*....|....*..
gi 153791466 199 NLPLPDLQKLPAWIKNGLYLHNNPLNC 225
Cdd:COG4886  388 TLLLLLLTTTAGVLLLTLALLDAVNTE 414
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 55-122 6.11e-03

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 39.45  E-value: 6.11e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 153791466  55 VPHSLPSYTAL--LDLSHNNLSRLraewTPTRLT---QLHSLLLSHNHLNFISSEAFSPVPNLRYLDLSSNQL 122
Cdd:PLN00113 491 VPRKLGSLSELmqLKLSENKLSGE----IPDELSsckKLVSLDLSHNQLSGQIPASFSEMPVLSQLDLSQNQL 559
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 55-208 6.60e-03

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 39.06  E-value: 6.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791466  55 VPHSLPSYTAL--LDLSHNNLSrlrAEwTPTRLTQLHSLLLSH---NHLNFISSEAFSPVP------------------- 110
Cdd:PLN00113 276 IPPSIFSLQKLisLDLSDNSLS---GE-IPELVIQLQNLEILHlfsNNFTGKIPVALTSLPrlqvlqlwsnkfsgeipkn 351

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791466 111 -----NLRYLDLSSNQLR-TLDEFLFSDLQVLEvLLLYNNHIMAVDRCAFDDMAQLQKLYLSQNQISRfplELVKEGAKL 184
Cdd:PLN00113 352 lgkhnNLTVLDLSTNNLTgEIPEGLCSSGNLFK-LILFSNSLEGEIPKSLGACRSLRRVRLQDNSFSG---ELPSEFTKL 427

                        170       180       190
                 ....*....|....*....|....*....|
gi 153791466 185 PKLTLLDLSSNKL------KNLPLPDLQKL 208
Cdd:PLN00113 428 PLVYFLDISNNNLqgrinsRKWDMPSLQML 457
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 55-205 8.95e-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: 38.11  E-value: 8.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791466  55 VPHSLPSYTAL--LDLSHNNLSRLRAEWTP--TRLTQLHSLLLSHN-----HLNFISSEAFSPVPNLRYLDLSSNQLRTL 125
Cdd:cd00116   73 LLQGLTKGCGLqeLDLSDNALGPDGCGVLEslLRSSSLQELKLNNNglgdrGLRLLAKGLKDLPPALEKLVLGRNRLEGA 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791466 126 DEF----LFSDLQVLEVLLLYNNHI----MAVDRCAFDDMAQLQKLYLSQNQISRfplelvkEGAK--------LPKLTL 189
Cdd:cd00116  153 SCEalakALRANRDLKELNLANNGIgdagIRALAEGLKANCNLEVLDLNNNGLTD-------EGASalaetlasLKSLEV 225

                        170
                 ....*....|....*.
gi 153791466 190 LDLSSNKLKNLPLPDL 205
Cdd:cd00116  226 LNLGDNNLTDAGAAAL 241
 
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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