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Conserved domains on  [gi|18414458|ref|NP_567467|]
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F-box/RNI-like superfamily protein [Arabidopsis thaliana]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AMN1 super family cl39120
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 448-586 8.17e-21

Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in Saccharomyces cerevisiae as a component of the Antagonist of MEN pathway (AMEN). The AMEN network is activated by MEN (mitotic exit network) via an active Cdc14, and in turn switches off MEN. Amn1 constitutes one of the alternative mechanisms by which MEN may be disrupted. Specifically, Amn1 binds Tem1 (Termination of M-phase, a GTPase that belongs to the RAS superfamily), and disrupts its association with Cdc15, the primary downstream target. Amn1 is a leucine-rich repeat (LRR) protein, with 12 repeats in the S. cerevisiae ortholog. As a negative regulator of the signal transduction pathway MEN, overexpression of AMN1 slows the growth of wild type cells. The function of the vertebrate members of this family has not been determined experimentally, they have fewer LRRs that determine the extent of this model.


The actual alignment was detected with superfamily member cd09293:

Pssm-ID: 187754 [Multi-domain]  Cd Length: 226  Bit Score: 91.62  E-value: 8.17e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414458 448 HCKSLTELSLRFCDKVGNKALIAIGKGC-SLQQLNVSGCNQISDAGITAIARGCPQLTHLDISVLQN---IGDMPLAELG 523
Cdd:cd09293  50 NCNKLKKLILPGSKLIDDEGLIALAQSCpNLQVLDLRACENITDSGIVALATNCPKLQTINLGRHRNghlITDVSLSALG 129

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18414458 524 EGCPMLKDLVLSHChHITDNGLNHLVQKC-KLLETCHMVYCPGITSAGVATVVSS--CPHIKKVLI 586
Cdd:cd09293 130 KNCTFLQTVGFAGC-DVTDKGVWELASGCsKSLERLSLNNCRNLTDQSIPAILASnyFPNLSVLEF 194
AMN1 super family cl39120
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 345-514 2.63e-18

Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in Saccharomyces cerevisiae as a component of the Antagonist of MEN pathway (AMEN). The AMEN network is activated by MEN (mitotic exit network) via an active Cdc14, and in turn switches off MEN. Amn1 constitutes one of the alternative mechanisms by which MEN may be disrupted. Specifically, Amn1 binds Tem1 (Termination of M-phase, a GTPase that belongs to the RAS superfamily), and disrupts its association with Cdc15, the primary downstream target. Amn1 is a leucine-rich repeat (LRR) protein, with 12 repeats in the S. cerevisiae ortholog. As a negative regulator of the signal transduction pathway MEN, overexpression of AMN1 slows the growth of wild type cells. The function of the vertebrate members of this family has not been determined experimentally, they have fewer LRRs that determine the extent of this model.


The actual alignment was detected with superfamily member cd09293:

Pssm-ID: 187754 [Multi-domain]  Cd Length: 226  Bit Score: 84.30  E-value: 2.63e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414458 345 CKELERVEINGCHNIGTRGIEAIGKSCPRLKELALLYCQRIGNSALQEIGKGCKSLEILHL---VDCSGIGDIAMCSIAK 421
Cdd:cd09293  51 CNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALATNCPKLQTINLgrhRNGHLITDVSLSALGK 130

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414458 422 GCRNLKKLHIRRCyEIGNKGIISigkhcksltelslrfcdkvgnkalIAIGKGCSLQQLNVSGCNQISDAGITAIA---- 497
Cdd:cd09293 131 NCTFLQTVGFAGC-DVTDKGVWE------------------------LASGCSKSLERLSLNNCRNLTDQSIPAILasny 185

                       170       180
                ....*....|....*....|....*.
gi 18414458 498 ---------RGCPQLTHLDISVLQNI 514
Cdd:cd09293 186 fpnlsvlefRGCPLITDFSRIILFKL 211
AMN1 super family cl39120
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 190-359 6.50e-17

Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in Saccharomyces cerevisiae as a component of the Antagonist of MEN pathway (AMEN). The AMEN network is activated by MEN (mitotic exit network) via an active Cdc14, and in turn switches off MEN. Amn1 constitutes one of the alternative mechanisms by which MEN may be disrupted. Specifically, Amn1 binds Tem1 (Termination of M-phase, a GTPase that belongs to the RAS superfamily), and disrupts its association with Cdc15, the primary downstream target. Amn1 is a leucine-rich repeat (LRR) protein, with 12 repeats in the S. cerevisiae ortholog. As a negative regulator of the signal transduction pathway MEN, overexpression of AMN1 slows the growth of wild type cells. The function of the vertebrate members of this family has not been determined experimentally, they have fewer LRRs that determine the extent of this model.


The actual alignment was detected with superfamily member cd09293:

Pssm-ID: 187754 [Multi-domain]  Cd Length: 226  Bit Score: 80.06  E-value: 6.50e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414458 190 CKQLEELNLRFCEgltdvgVIDLVVG---CSKSLKSIGVAASAKITDLSLEAVGSHCKLLEVLYLD-SEYIHDKGLIAVA 265
Cdd:cd09293  27 HSGLEWLELYMCP------ISDPPLDqlsNCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRaCENITDSGIVALA 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414458 266 QGCHRLKNLKL----QCVSVTDVAFAAVGELCTSLERLALySFQHFTDKGMRAIGKG-SKKLKDLTLSDCYFVSCKGLEA 340
Cdd:cd09293 101 TNCPKLQTINLgrhrNGHLITDVSLSALGKNCTFLQTVGF-AGCDVTDKGVWELASGcSKSLERLSLNNCRNLTDQSIPA 179

                       170       180
                ....*....|....*....|.
gi 18414458 341 I--AHGCKELERVEINGCHNI 359
Cdd:cd09293 180 IlaSNYFPNLSVLEFRGCPLI 200
F-box_AtTIR1-like cd22159
F-box domain found in Arabidopsis thaliana transport inhibitor response 1 protein (TIR1), ...
 8-47 7.32e-12

F-box domain found in Arabidopsis thaliana transport inhibitor response 1 protein (TIR1), coronatine-insensitive protein 1 (COI1) and similar proteins; TIR1, also called F-box/LRR-repeat protein 1 (FBL1), is part of an SCF (SKP1-cullin-F-box) protein ligase complex that promotes the ubiquitin-dependent proteolysis of a family of transcriptional regulators known as Aux/IAAs in an auxin-dependent manner. TIR1 is an auxin receptor that plays a potential role in plant hormone signaling. COI1, also called F-box/LRR-repeat protein 2 (FBL2), is the substrate-recruiting module of an SCF ubiquitin E3 ligase complex. It mediates jasmonate signalling by promoting hormone-dependent ubiquitylation and degradation of transcriptional repressor JASMONATE ZIM-domain (JAZ) family proteins. This subfamily also includes Arabidopsis thaliana EIN3-binding F-box protein 1 (EBF1). EBF1, also called F-box/LRR-repeat protein 6 (FBL6), is a component of the SCF(EBF1) E3 ubiquitin ligase complex, which may mediate the ubiquitination and subsequent proteasomal degradation of target proteins (probably including EIN3 and EIL1). The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


:

Pssm-ID: 438930  Cd Length: 40  Bit Score: 60.17  E-value: 7.32e-12
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 18414458   8 NNCLPEELILEIFRRLESKPNRDACSLVCKRWLSLERFSR 47
Cdd:cd22159   1 IDLLPDEILELIFSYLSDPWDRNSCSLVCKRWYRLERATR 40
 
Name Accession Description Interval E-value
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 448-586 8.17e-21

Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in Saccharomyces cerevisiae as a component of the Antagonist of MEN pathway (AMEN). The AMEN network is activated by MEN (mitotic exit network) via an active Cdc14, and in turn switches off MEN. Amn1 constitutes one of the alternative mechanisms by which MEN may be disrupted. Specifically, Amn1 binds Tem1 (Termination of M-phase, a GTPase that belongs to the RAS superfamily), and disrupts its association with Cdc15, the primary downstream target. Amn1 is a leucine-rich repeat (LRR) protein, with 12 repeats in the S. cerevisiae ortholog. As a negative regulator of the signal transduction pathway MEN, overexpression of AMN1 slows the growth of wild type cells. The function of the vertebrate members of this family has not been determined experimentally, they have fewer LRRs that determine the extent of this model.


Pssm-ID: 187754 [Multi-domain]  Cd Length: 226  Bit Score: 91.62  E-value: 8.17e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414458 448 HCKSLTELSLRFCDKVGNKALIAIGKGC-SLQQLNVSGCNQISDAGITAIARGCPQLTHLDISVLQN---IGDMPLAELG 523
Cdd:cd09293  50 NCNKLKKLILPGSKLIDDEGLIALAQSCpNLQVLDLRACENITDSGIVALATNCPKLQTINLGRHRNghlITDVSLSALG 129

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18414458 524 EGCPMLKDLVLSHChHITDNGLNHLVQKC-KLLETCHMVYCPGITSAGVATVVSS--CPHIKKVLI 586
Cdd:cd09293 130 KNCTFLQTVGFAGC-DVTDKGVWELASGCsKSLERLSLNNCRNLTDQSIPAILASnyFPNLSVLEF 194
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 345-514 2.63e-18

Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in Saccharomyces cerevisiae as a component of the Antagonist of MEN pathway (AMEN). The AMEN network is activated by MEN (mitotic exit network) via an active Cdc14, and in turn switches off MEN. Amn1 constitutes one of the alternative mechanisms by which MEN may be disrupted. Specifically, Amn1 binds Tem1 (Termination of M-phase, a GTPase that belongs to the RAS superfamily), and disrupts its association with Cdc15, the primary downstream target. Amn1 is a leucine-rich repeat (LRR) protein, with 12 repeats in the S. cerevisiae ortholog. As a negative regulator of the signal transduction pathway MEN, overexpression of AMN1 slows the growth of wild type cells. The function of the vertebrate members of this family has not been determined experimentally, they have fewer LRRs that determine the extent of this model.


Pssm-ID: 187754 [Multi-domain]  Cd Length: 226  Bit Score: 84.30  E-value: 2.63e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414458 345 CKELERVEINGCHNIGTRGIEAIGKSCPRLKELALLYCQRIGNSALQEIGKGCKSLEILHL---VDCSGIGDIAMCSIAK 421
Cdd:cd09293  51 CNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALATNCPKLQTINLgrhRNGHLITDVSLSALGK 130

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414458 422 GCRNLKKLHIRRCyEIGNKGIISigkhcksltelslrfcdkvgnkalIAIGKGCSLQQLNVSGCNQISDAGITAIA---- 497
Cdd:cd09293 131 NCTFLQTVGFAGC-DVTDKGVWE------------------------LASGCSKSLERLSLNNCRNLTDQSIPAILasny 185

                       170       180
                ....*....|....*....|....*.
gi 18414458 498 ---------RGCPQLTHLDISVLQNI 514
Cdd:cd09293 186 fpnlsvlefRGCPLITDFSRIILFKL 211
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 190-359 6.50e-17

Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in Saccharomyces cerevisiae as a component of the Antagonist of MEN pathway (AMEN). The AMEN network is activated by MEN (mitotic exit network) via an active Cdc14, and in turn switches off MEN. Amn1 constitutes one of the alternative mechanisms by which MEN may be disrupted. Specifically, Amn1 binds Tem1 (Termination of M-phase, a GTPase that belongs to the RAS superfamily), and disrupts its association with Cdc15, the primary downstream target. Amn1 is a leucine-rich repeat (LRR) protein, with 12 repeats in the S. cerevisiae ortholog. As a negative regulator of the signal transduction pathway MEN, overexpression of AMN1 slows the growth of wild type cells. The function of the vertebrate members of this family has not been determined experimentally, they have fewer LRRs that determine the extent of this model.


Pssm-ID: 187754 [Multi-domain]  Cd Length: 226  Bit Score: 80.06  E-value: 6.50e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414458 190 CKQLEELNLRFCEgltdvgVIDLVVG---CSKSLKSIGVAASAKITDLSLEAVGSHCKLLEVLYLD-SEYIHDKGLIAVA 265
Cdd:cd09293  27 HSGLEWLELYMCP------ISDPPLDqlsNCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRaCENITDSGIVALA 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414458 266 QGCHRLKNLKL----QCVSVTDVAFAAVGELCTSLERLALySFQHFTDKGMRAIGKG-SKKLKDLTLSDCYFVSCKGLEA 340
Cdd:cd09293 101 TNCPKLQTINLgrhrNGHLITDVSLSALGKNCTFLQTVGF-AGCDVTDKGVWELASGcSKSLERLSLNNCRNLTDQSIPA 179

                       170       180
                ....*....|....*....|.
gi 18414458 341 I--AHGCKELERVEINGCHNI 359
Cdd:cd09293 180 IlaSNYFPNLSVLEFRGCPLI 200
F-box_AtTIR1-like cd22159
F-box domain found in Arabidopsis thaliana transport inhibitor response 1 protein (TIR1), ...
 8-47 7.32e-12

F-box domain found in Arabidopsis thaliana transport inhibitor response 1 protein (TIR1), coronatine-insensitive protein 1 (COI1) and similar proteins; TIR1, also called F-box/LRR-repeat protein 1 (FBL1), is part of an SCF (SKP1-cullin-F-box) protein ligase complex that promotes the ubiquitin-dependent proteolysis of a family of transcriptional regulators known as Aux/IAAs in an auxin-dependent manner. TIR1 is an auxin receptor that plays a potential role in plant hormone signaling. COI1, also called F-box/LRR-repeat protein 2 (FBL2), is the substrate-recruiting module of an SCF ubiquitin E3 ligase complex. It mediates jasmonate signalling by promoting hormone-dependent ubiquitylation and degradation of transcriptional repressor JASMONATE ZIM-domain (JAZ) family proteins. This subfamily also includes Arabidopsis thaliana EIN3-binding F-box protein 1 (EBF1). EBF1, also called F-box/LRR-repeat protein 6 (FBL6), is a component of the SCF(EBF1) E3 ubiquitin ligase complex, which may mediate the ubiquitination and subsequent proteasomal degradation of target proteins (probably including EIN3 and EIL1). The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438930  Cd Length: 40  Bit Score: 60.17  E-value: 7.32e-12
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 18414458   8 NNCLPEELILEIFRRLESKPNRDACSLVCKRWLSLERFSR 47
Cdd:cd22159   1 IDLLPDEILELIFSYLSDPWDRNSCSLVCKRWYRLERATR 40
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 398-559 3.46e-09

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: 59.42  E-value: 3.46e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414458 398 KSLEILHLvDCSGIGDIAMCSIAKGCR---NLKKLHIRRCYeIGNKG---IISIGKHCKSLTELSLRFcDKVGNKALIAI 471
Cdd:COG5238 180 NSVETVYL-GCNQIGDEGIEELAEALTqntTVTTLWLKRNP-IGDEGaeiLAEALKGNKSLTTLDLSN-NQIGDEGVIAL 256

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414458 472 GK----GCSLQQLNVSGcNQISDAGITAIA---RGCPQLTHLDISVlQNIGD---MPLAELGEGCPMLKDLVLSHChHIT 541
Cdd:COG5238 257 AEalknNTTVETLYLSG-NQIGAEGAIALAkalQGNTTLTSLDLSV-NRIGDegaIALAEGLQGNKTLHTLNLAYN-GIG 333

                       170
                ....*....|....*...
gi 18414458 542 DNGLNHLVQKCKLLETCH 559
Cdd:COG5238 334 AQGAIALAKALQENTTLH 351
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 140-458 2.03e-08

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: 56.72  E-value: 2.03e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414458 140 PRIENLSLIWCPNVSSVGLCSLAQ---------------KCTSLKSLDLQGCYVGDQGLAAvgkFCKQLEElnlrfcegl 204
Cdd:COG5238 139 RRINLIQVLKDPLGGNAVHLLGLAarlgllaaismakalQNNSVETVYLGCNQIGDEGIEE---LAEALTQ--------- 206

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414458 205 tdvgvidlvvgcSKSLKSIGVAASAkITDLSLEAVGSH---CKLLEVLYLDSEYIHDKGLIAVAqgchrlKNLKLQcvsv 281
Cdd:COG5238 207 ------------NTTVTTLWLKRNP-IGDEGAEILAEAlkgNKSLTTLDLSNNQIGDEGVIALA------EALKNN---- 263

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414458 282 tdvafaavgelcTSLERLALySFQHFTDKGMRAIGK---GSKKLKDLTLSDcyfvsckgleaiahgckelerveingcHN 358
Cdd:COG5238 264 ------------TTVETLYL-SGNQIGAEGAIALAKalqGNTTLTSLDLSV---------------------------NR 303

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414458 359 IGTRGIEAIGKSCPR---LKELALLYCQrIGNSALQEIGKGCKSLEILHLVDCSG--IGDIAMCSIAK---GCRNLKKLH 430
Cdd:COG5238 304 IGDEGAIALAEGLQGnktLHTLNLAYNG-IGAQGAIALAKALQENTTLHSLDLSDnqIGDEGAIALAKyleGNTTLRELN 382

                       330       340       350
                ....*....|....*....|....*....|
gi 18414458 431 IRRcYEIGNKGIISIGKHCK--SLTELSLR 458
Cdd:COG5238 383 LGK-NNIGKQGAEALIDALQtnRLHTLILD 411
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 355-525 6.45e-08

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: 55.18  E-value: 6.45e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414458 355 GCHNIGTRGIEAIGKSCPRLKELALLYCQR--IGNSALQEIGKGCKSLEILHLVDCSG--IGD----------------- 413
Cdd:COG5238 188 GCNQIGDEGIEELAEALTQNTTVTTLWLKRnpIGDEGAEILAEALKGNKSLTTLDLSNnqIGDegvialaealknnttve 267

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414458 414 --------------IAMCSIAKGCRNLKKLHIRRcYEIGNKGIISIGKH---CKSLTELSLRFCdKVGNKALIAIGK--- 473
Cdd:COG5238 268 tlylsgnqigaegaIALAKALQGNTTLTSLDLSV-NRIGDEGAIALAEGlqgNKTLHTLNLAYN-GIGAQGAIALAKalq 345

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 18414458 474 -GCSLQQLNVSGcNQISDAGITAIAR---GCPQLTHLDISVlQNIGDMPLAELGEG 525
Cdd:COG5238 346 eNTTLHSLDLSD-NQIGDEGAIALAKyleGNTTLRELNLGK-NNIGKQGAEALIDA 399
LRR_CC smart00367
Leucine-rich repeat - CC (cysteine-containing) subfamily;
526-551 1.02e-04

Leucine-rich repeat - CC (cysteine-containing) subfamily;


Pssm-ID: 197685 [Multi-domain]  Cd Length: 26  Bit Score: 39.31  E-value: 1.02e-04
                           10        20
                   ....*....|....*....|....*.
gi 18414458    526 CPMLKDLVLSHCHHITDNGLNHLVQK 551
Cdd:smart00367   1 CPNLRELDLSGCTNITDEGLQALAKG 26
FBOX smart00256
A Receptor for Ubiquitination Targets;
11-42 1.63e-04

A Receptor for Ubiquitination Targets;


Pssm-ID: 197608  Cd Length: 41  Bit Score: 39.34  E-value: 1.63e-04
                           10        20        30
                   ....*....|....*....|....*....|..
gi 18414458     11 LPEELILEIFRRLESKpNRDACSLVCKRWLSL 42
Cdd:smart00256   1 LPDEILEEILSKLDPK-DLLRLRKVSRKWRSL 31
F-box-like pfam12937
F-box-like; This is an F-box-like family.
 9-42 2.44e-04

F-box-like; This is an F-box-like family.


Pssm-ID: 463757 [Multi-domain]  Cd Length: 45  Bit Score: 39.00  E-value: 2.44e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 18414458     9 NCLPEELILEIFRRLeSKPNRDACSLVCKRWLSL 42
Cdd:pfam12937   2 SSLPDEILLQIFSYL-DPKDLLRLALVCRRWREL 34
LRR_CC smart00367
Leucine-rich repeat - CC (cysteine-containing) subfamily;
190-213 6.23e-03

Leucine-rich repeat - CC (cysteine-containing) subfamily;


Pssm-ID: 197685 [Multi-domain]  Cd Length: 26  Bit Score: 34.30  E-value: 6.23e-03
                           10        20
                   ....*....|....*....|....
gi 18414458    190 CKQLEELNLRFCEGLTDVGVIDLV 213
Cdd:smart00367   1 CPNLRELDLSGCTNITDEGLQALA 24
LRR_CC smart00367
Leucine-rich repeat - CC (cysteine-containing) subfamily;
371-396 7.65e-03

Leucine-rich repeat - CC (cysteine-containing) subfamily;


Pssm-ID: 197685 [Multi-domain]  Cd Length: 26  Bit Score: 34.30  E-value: 7.65e-03
                           10        20
                   ....*....|....*....|....*.
gi 18414458    371 CPRLKELALLYCQRIGNSALQEIGKG 396
Cdd:smart00367   1 CPNLRELDLSGCTNITDEGLQALAKG 26
 
Name Accession Description Interval E-value
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 448-586 8.17e-21

Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in Saccharomyces cerevisiae as a component of the Antagonist of MEN pathway (AMEN). The AMEN network is activated by MEN (mitotic exit network) via an active Cdc14, and in turn switches off MEN. Amn1 constitutes one of the alternative mechanisms by which MEN may be disrupted. Specifically, Amn1 binds Tem1 (Termination of M-phase, a GTPase that belongs to the RAS superfamily), and disrupts its association with Cdc15, the primary downstream target. Amn1 is a leucine-rich repeat (LRR) protein, with 12 repeats in the S. cerevisiae ortholog. As a negative regulator of the signal transduction pathway MEN, overexpression of AMN1 slows the growth of wild type cells. The function of the vertebrate members of this family has not been determined experimentally, they have fewer LRRs that determine the extent of this model.


Pssm-ID: 187754 [Multi-domain]  Cd Length: 226  Bit Score: 91.62  E-value: 8.17e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414458 448 HCKSLTELSLRFCDKVGNKALIAIGKGC-SLQQLNVSGCNQISDAGITAIARGCPQLTHLDISVLQN---IGDMPLAELG 523
Cdd:cd09293  50 NCNKLKKLILPGSKLIDDEGLIALAQSCpNLQVLDLRACENITDSGIVALATNCPKLQTINLGRHRNghlITDVSLSALG 129

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18414458 524 EGCPMLKDLVLSHChHITDNGLNHLVQKC-KLLETCHMVYCPGITSAGVATVVSS--CPHIKKVLI 586
Cdd:cd09293 130 KNCTFLQTVGFAGC-DVTDKGVWELASGCsKSLERLSLNNCRNLTDQSIPAILASnyFPNLSVLEF 194
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 345-514 2.63e-18

Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in Saccharomyces cerevisiae as a component of the Antagonist of MEN pathway (AMEN). The AMEN network is activated by MEN (mitotic exit network) via an active Cdc14, and in turn switches off MEN. Amn1 constitutes one of the alternative mechanisms by which MEN may be disrupted. Specifically, Amn1 binds Tem1 (Termination of M-phase, a GTPase that belongs to the RAS superfamily), and disrupts its association with Cdc15, the primary downstream target. Amn1 is a leucine-rich repeat (LRR) protein, with 12 repeats in the S. cerevisiae ortholog. As a negative regulator of the signal transduction pathway MEN, overexpression of AMN1 slows the growth of wild type cells. The function of the vertebrate members of this family has not been determined experimentally, they have fewer LRRs that determine the extent of this model.


Pssm-ID: 187754 [Multi-domain]  Cd Length: 226  Bit Score: 84.30  E-value: 2.63e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414458 345 CKELERVEINGCHNIGTRGIEAIGKSCPRLKELALLYCQRIGNSALQEIGKGCKSLEILHL---VDCSGIGDIAMCSIAK 421
Cdd:cd09293  51 CNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALATNCPKLQTINLgrhRNGHLITDVSLSALGK 130

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414458 422 GCRNLKKLHIRRCyEIGNKGIISigkhcksltelslrfcdkvgnkalIAIGKGCSLQQLNVSGCNQISDAGITAIA---- 497
Cdd:cd09293 131 NCTFLQTVGFAGC-DVTDKGVWE------------------------LASGCSKSLERLSLNNCRNLTDQSIPAILasny 185

                       170       180
                ....*....|....*....|....*.
gi 18414458 498 ---------RGCPQLTHLDISVLQNI 514
Cdd:cd09293 186 fpnlsvlefRGCPLITDFSRIILFKL 211
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 190-359 6.50e-17

Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in Saccharomyces cerevisiae as a component of the Antagonist of MEN pathway (AMEN). The AMEN network is activated by MEN (mitotic exit network) via an active Cdc14, and in turn switches off MEN. Amn1 constitutes one of the alternative mechanisms by which MEN may be disrupted. Specifically, Amn1 binds Tem1 (Termination of M-phase, a GTPase that belongs to the RAS superfamily), and disrupts its association with Cdc15, the primary downstream target. Amn1 is a leucine-rich repeat (LRR) protein, with 12 repeats in the S. cerevisiae ortholog. As a negative regulator of the signal transduction pathway MEN, overexpression of AMN1 slows the growth of wild type cells. The function of the vertebrate members of this family has not been determined experimentally, they have fewer LRRs that determine the extent of this model.


Pssm-ID: 187754 [Multi-domain]  Cd Length: 226  Bit Score: 80.06  E-value: 6.50e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414458 190 CKQLEELNLRFCEgltdvgVIDLVVG---CSKSLKSIGVAASAKITDLSLEAVGSHCKLLEVLYLD-SEYIHDKGLIAVA 265
Cdd:cd09293  27 HSGLEWLELYMCP------ISDPPLDqlsNCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRaCENITDSGIVALA 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414458 266 QGCHRLKNLKL----QCVSVTDVAFAAVGELCTSLERLALySFQHFTDKGMRAIGKG-SKKLKDLTLSDCYFVSCKGLEA 340
Cdd:cd09293 101 TNCPKLQTINLgrhrNGHLITDVSLSALGKNCTFLQTVGF-AGCDVTDKGVWELASGcSKSLERLSLNNCRNLTDQSIPA 179

                       170       180
                ....*....|....*....|.
gi 18414458 341 I--AHGCKELERVEINGCHNI 359
Cdd:cd09293 180 IlaSNYFPNLSVLEFRGCPLI 200
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 124-275 1.36e-15

Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in Saccharomyces cerevisiae as a component of the Antagonist of MEN pathway (AMEN). The AMEN network is activated by MEN (mitotic exit network) via an active Cdc14, and in turn switches off MEN. Amn1 constitutes one of the alternative mechanisms by which MEN may be disrupted. Specifically, Amn1 binds Tem1 (Termination of M-phase, a GTPase that belongs to the RAS superfamily), and disrupts its association with Cdc15, the primary downstream target. Amn1 is a leucine-rich repeat (LRR) protein, with 12 repeats in the S. cerevisiae ortholog. As a negative regulator of the signal transduction pathway MEN, overexpression of AMN1 slows the growth of wild type cells. The function of the vertebrate members of this family has not been determined experimentally, they have fewer LRRs that determine the extent of this model.


Pssm-ID: 187754 [Multi-domain]  Cd Length: 226  Bit Score: 76.21  E-value: 1.36e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414458 124 SSSLTDTGLTALANGFPRIENLSLIWCPNVSSVGLCSLAQKCTSLKSLDL---QGC-YVGDQGLAAVGKFCKQLEELNLR 199
Cdd:cd09293  62 SKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALATNCPKLQTINLgrhRNGhLITDVSLSALGKNCTFLQTVGFA 141

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18414458 200 FCEgLTDVGVIDLVVGCSKSLKSIGVAASAKITDLSLEAV--GSHCKLLEVLYLdseyihdkgliavaQGCHRLKNLK 275
Cdd:cd09293 142 GCD-VTDKGVWELASGCSKSLERLSLNNCRNLTDQSIPAIlaSNYFPNLSVLEF--------------RGCPLITDFS 204
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 142-289 1.29e-14

Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in Saccharomyces cerevisiae as a component of the Antagonist of MEN pathway (AMEN). The AMEN network is activated by MEN (mitotic exit network) via an active Cdc14, and in turn switches off MEN. Amn1 constitutes one of the alternative mechanisms by which MEN may be disrupted. Specifically, Amn1 binds Tem1 (Termination of M-phase, a GTPase that belongs to the RAS superfamily), and disrupts its association with Cdc15, the primary downstream target. Amn1 is a leucine-rich repeat (LRR) protein, with 12 repeats in the S. cerevisiae ortholog. As a negative regulator of the signal transduction pathway MEN, overexpression of AMN1 slows the growth of wild type cells. The function of the vertebrate members of this family has not been determined experimentally, they have fewer LRRs that determine the extent of this model.


Pssm-ID: 187754 [Multi-domain]  Cd Length: 226  Bit Score: 73.52  E-value: 1.29e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414458 142 IENLSLIWCPNVSSVGLCSLAQKCTSLKSLDLQGC-YVGDQGLAAVGKFCKQLEELNLRFCEgltdvgvidlvvGCSksl 220
Cdd:cd09293  54 LKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACeNITDSGIVALATNCPKLQTINLGRHR------------NGH--- 118

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18414458 221 ksigvaasaKITDLSLEAVGSHCKLLEVLYLDSEYIHDKGLIAVAQGC-HRLKNLKL-QCVSVTDVAFAAV 289
Cdd:cd09293 119 ---------LITDVSLSALGKNCTFLQTVGFAGCDVTDKGVWELASGCsKSLERLSLnNCRNLTDQSIPAI 180
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 319-485 2.58e-14

Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in Saccharomyces cerevisiae as a component of the Antagonist of MEN pathway (AMEN). The AMEN network is activated by MEN (mitotic exit network) via an active Cdc14, and in turn switches off MEN. Amn1 constitutes one of the alternative mechanisms by which MEN may be disrupted. Specifically, Amn1 binds Tem1 (Termination of M-phase, a GTPase that belongs to the RAS superfamily), and disrupts its association with Cdc15, the primary downstream target. Amn1 is a leucine-rich repeat (LRR) protein, with 12 repeats in the S. cerevisiae ortholog. As a negative regulator of the signal transduction pathway MEN, overexpression of AMN1 slows the growth of wild type cells. The function of the vertebrate members of this family has not been determined experimentally, they have fewer LRRs that determine the extent of this model.


Pssm-ID: 187754 [Multi-domain]  Cd Length: 226  Bit Score: 72.36  E-value: 2.58e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414458 319 SKKLKDLTLSDCYFVSCKGLEAIAHGCKELERVEINGCHNIGTRGIEAIGKSCPRLKELAL---LYCQRIGNSALQEIGK 395
Cdd:cd09293  51 CNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALATNCPKLQTINLgrhRNGHLITDVSLSALGK 130

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414458 396 GCKSLEILHLVDCsGIGDIAMCSIAKGC-RNLKKLHIRRCYEIGNKGIISI--GKHCKSLTELSLRFCDKVGNKALIA-- 470
Cdd:cd09293 131 NCTFLQTVGFAGC-DVTDKGVWELASGCsKSLERLSLNNCRNLTDQSIPAIlaSNYFPNLSVLEFRGCPLITDFSRIIlf 209

                       170
                ....*....|....*..
gi 18414458 471 --IGKGCSLQQLnVSGC 485
Cdd:cd09293 210 klWQPRLNKPIL-VEWC 225
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 293-440 3.37e-12

Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in Saccharomyces cerevisiae as a component of the Antagonist of MEN pathway (AMEN). The AMEN network is activated by MEN (mitotic exit network) via an active Cdc14, and in turn switches off MEN. Amn1 constitutes one of the alternative mechanisms by which MEN may be disrupted. Specifically, Amn1 binds Tem1 (Termination of M-phase, a GTPase that belongs to the RAS superfamily), and disrupts its association with Cdc15, the primary downstream target. Amn1 is a leucine-rich repeat (LRR) protein, with 12 repeats in the S. cerevisiae ortholog. As a negative regulator of the signal transduction pathway MEN, overexpression of AMN1 slows the growth of wild type cells. The function of the vertebrate members of this family has not been determined experimentally, they have fewer LRRs that determine the extent of this model.


Pssm-ID: 187754 [Multi-domain]  Cd Length: 226  Bit Score: 66.20  E-value: 3.37e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414458 293 CTSLERLALYSFQHFTDKGMRAIGKGSKKLKDLTLSDCYFVSCKGLEAIAHGCKELERVEI---NGCHNIGTRGIEAIGK 369
Cdd:cd09293  51 CNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALATNCPKLQTINLgrhRNGHLITDVSLSALGK 130

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18414458 370 SCPRLKELALLYCQrIGNSALQEIGKGC-KSLEILHLVDCSGIGDIAMCSI--AKGCRNLKKLHIRRCYEIGNK 440
Cdd:cd09293 131 NCTFLQTVGFAGCD-VTDKGVWELASGCsKSLERLSLNNCRNLTDQSIPAIlaSNYFPNLSVLEFRGCPLITDF 203
F-box_AtTIR1-like cd22159
F-box domain found in Arabidopsis thaliana transport inhibitor response 1 protein (TIR1), ...
 8-47 7.32e-12

F-box domain found in Arabidopsis thaliana transport inhibitor response 1 protein (TIR1), coronatine-insensitive protein 1 (COI1) and similar proteins; TIR1, also called F-box/LRR-repeat protein 1 (FBL1), is part of an SCF (SKP1-cullin-F-box) protein ligase complex that promotes the ubiquitin-dependent proteolysis of a family of transcriptional regulators known as Aux/IAAs in an auxin-dependent manner. TIR1 is an auxin receptor that plays a potential role in plant hormone signaling. COI1, also called F-box/LRR-repeat protein 2 (FBL2), is the substrate-recruiting module of an SCF ubiquitin E3 ligase complex. It mediates jasmonate signalling by promoting hormone-dependent ubiquitylation and degradation of transcriptional repressor JASMONATE ZIM-domain (JAZ) family proteins. This subfamily also includes Arabidopsis thaliana EIN3-binding F-box protein 1 (EBF1). EBF1, also called F-box/LRR-repeat protein 6 (FBL6), is a component of the SCF(EBF1) E3 ubiquitin ligase complex, which may mediate the ubiquitination and subsequent proteasomal degradation of target proteins (probably including EIN3 and EIL1). The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438930  Cd Length: 40  Bit Score: 60.17  E-value: 7.32e-12
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 18414458   8 NNCLPEELILEIFRRLESKPNRDACSLVCKRWLSLERFSR 47
Cdd:cd22159   1 IDLLPDEILELIFSYLSDPWDRNSCSLVCKRWYRLERATR 40
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 398-559 3.46e-09

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: 59.42  E-value: 3.46e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414458 398 KSLEILHLvDCSGIGDIAMCSIAKGCR---NLKKLHIRRCYeIGNKG---IISIGKHCKSLTELSLRFcDKVGNKALIAI 471
Cdd:COG5238 180 NSVETVYL-GCNQIGDEGIEELAEALTqntTVTTLWLKRNP-IGDEGaeiLAEALKGNKSLTTLDLSN-NQIGDEGVIAL 256

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414458 472 GK----GCSLQQLNVSGcNQISDAGITAIA---RGCPQLTHLDISVlQNIGD---MPLAELGEGCPMLKDLVLSHChHIT 541
Cdd:COG5238 257 AEalknNTTVETLYLSG-NQIGAEGAIALAkalQGNTTLTSLDLSV-NRIGDegaIALAEGLQGNKTLHTLNLAYN-GIG 333

                       170
                ....*....|....*...
gi 18414458 542 DNGLNHLVQKCKLLETCH 559
Cdd:COG5238 334 AQGAIALAKALQENTTLH 351
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 140-458 2.03e-08

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: 56.72  E-value: 2.03e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414458 140 PRIENLSLIWCPNVSSVGLCSLAQ---------------KCTSLKSLDLQGCYVGDQGLAAvgkFCKQLEElnlrfcegl 204
Cdd:COG5238 139 RRINLIQVLKDPLGGNAVHLLGLAarlgllaaismakalQNNSVETVYLGCNQIGDEGIEE---LAEALTQ--------- 206

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414458 205 tdvgvidlvvgcSKSLKSIGVAASAkITDLSLEAVGSH---CKLLEVLYLDSEYIHDKGLIAVAqgchrlKNLKLQcvsv 281
Cdd:COG5238 207 ------------NTTVTTLWLKRNP-IGDEGAEILAEAlkgNKSLTTLDLSNNQIGDEGVIALA------EALKNN---- 263

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414458 282 tdvafaavgelcTSLERLALySFQHFTDKGMRAIGK---GSKKLKDLTLSDcyfvsckgleaiahgckelerveingcHN 358
Cdd:COG5238 264 ------------TTVETLYL-SGNQIGAEGAIALAKalqGNTTLTSLDLSV---------------------------NR 303

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414458 359 IGTRGIEAIGKSCPR---LKELALLYCQrIGNSALQEIGKGCKSLEILHLVDCSG--IGDIAMCSIAK---GCRNLKKLH 430
Cdd:COG5238 304 IGDEGAIALAEGLQGnktLHTLNLAYNG-IGAQGAIALAKALQENTTLHSLDLSDnqIGDEGAIALAKyleGNTTLRELN 382

                       330       340       350
                ....*....|....*....|....*....|
gi 18414458 431 IRRcYEIGNKGIISIGKHCK--SLTELSLR 458
Cdd:COG5238 383 LGK-NNIGKQGAEALIDALQtnRLHTLILD 411
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 355-525 6.45e-08

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: 55.18  E-value: 6.45e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414458 355 GCHNIGTRGIEAIGKSCPRLKELALLYCQR--IGNSALQEIGKGCKSLEILHLVDCSG--IGD----------------- 413
Cdd:COG5238 188 GCNQIGDEGIEELAEALTQNTTVTTLWLKRnpIGDEGAEILAEALKGNKSLTTLDLSNnqIGDegvialaealknnttve 267

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414458 414 --------------IAMCSIAKGCRNLKKLHIRRcYEIGNKGIISIGKH---CKSLTELSLRFCdKVGNKALIAIGK--- 473
Cdd:COG5238 268 tlylsgnqigaegaIALAKALQGNTTLTSLDLSV-NRIGDEGAIALAEGlqgNKTLHTLNLAYN-GIGAQGAIALAKalq 345

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 18414458 474 -GCSLQQLNVSGcNQISDAGITAIAR---GCPQLTHLDISVlQNIGDMPLAELGEG 525
Cdd:COG5238 346 eNTTLHSLDLSD-NQIGDEGAIALAKyleGNTTLRELNLGK-NNIGKQGAEALIDA 399
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 449-584 1.05e-07

Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in Saccharomyces cerevisiae as a component of the Antagonist of MEN pathway (AMEN). The AMEN network is activated by MEN (mitotic exit network) via an active Cdc14, and in turn switches off MEN. Amn1 constitutes one of the alternative mechanisms by which MEN may be disrupted. Specifically, Amn1 binds Tem1 (Termination of M-phase, a GTPase that belongs to the RAS superfamily), and disrupts its association with Cdc15, the primary downstream target. Amn1 is a leucine-rich repeat (LRR) protein, with 12 repeats in the S. cerevisiae ortholog. As a negative regulator of the signal transduction pathway MEN, overexpression of AMN1 slows the growth of wild type cells. The function of the vertebrate members of this family has not been determined experimentally, they have fewer LRRs that determine the extent of this model.


Pssm-ID: 187754 [Multi-domain]  Cd Length: 226  Bit Score: 53.10  E-value: 1.05e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414458 449 CKSLTELSLRFCDKVgNKALIAIGKGCSLQQLNVSGCNQISDAGITAIARGCPQLTHLDisvlqnigdmplaelgegcpm 528
Cdd:cd09293  27 HSGLEWLELYMCPIS-DPPLDQLSNCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLD--------------------- 84

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 18414458 529 lkdlvLSHCHHITDNGLNHLVQKCKLLETCHM---VYCPGITSAGVATVVSSCPHIKKV 584
Cdd:cd09293  85 -----LRACENITDSGIVALATNCPKLQTINLgrhRNGHLITDVSLSALGKNCTFLQTV 138
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 121-329 9.17e-07

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: 51.71  E-value: 9.17e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414458 121 NVESSSLTDTGLTALANGFPRIENLSLIWCPNV-----SSVGLCSLAQKCTSLKSLDLQGCYVGDQGLAAVGKFCK---Q 192
Cdd:COG5238 186 YLGCNQIGDEGIEELAEALTQNTTVTTLWLKRNpigdeGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKnntT 265

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414458 193 LEELNLRfCEGLTDVGVIDLVVGCS--KSLKSI----------GVAASAKitdlSLEavgsHCKLLEVLYLDSEYIHDKG 260
Cdd:COG5238 266 VETLYLS-GNQIGAEGAIALAKALQgnTTLTSLdlsvnrigdeGAIALAE----GLQ----GNKTLHTLNLAYNGIGAQG 336

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18414458 261 LIAVA---QGCHRLKNLKLQCVSVTD---VAFAAVGELCTSLERLALYSFQhFTDKGMRAIGKGSK--KLKDLTLSD 329
Cdd:COG5238 337 AIALAkalQENTTLHSLDLSDNQIGDegaIALAKYLEGNTTLRELNLGKNN-IGKQGAEALIDALQtnRLHTLILDG 412
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 356-579 8.51e-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: 48.12  E-value: 8.51e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414458 356 CHNIGTRGIEAIGKSCPRLKELA-LLYC----QRIG---NSALQEIGKGCKsLEILHLVDCSgIGDIAMCSIAKGCRN-- 425
Cdd:cd00116  32 GNTLGEEAAKALASALRPQPSLKeLCLSlnetGRIPrglQSLLQGLTKGCG-LQELDLSDNA-LGPDGCGVLESLLRSss 109

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414458 426 LKKLHIRRCyEIGnkgiISIGKH-CKSLTELSLRFC------DKVGNKALIAIGK----GCSLQQLNVSGcNQISDAGIT 494
Cdd:cd00116 110 LQELKLNNN-GLG----DRGLRLlAKGLKDLPPALEklvlgrNRLEGASCEALAKalraNRDLKELNLAN-NGIGDAGIR 183

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414458 495 AIARGCPQLTHLDISVLQN-----IGDMPLAELGEGCPMLKDLVLSHChHITDNGLNHLVQKCKLLETCHMV---YCPGI 566
Cdd:cd00116 184 ALAEGLKANCNLEVLDLNNngltdEGASALAETLASLKSLEVLNLGDN-NLTDAGAAALASALLSPNISLLTlslSCNDI 262

                       250
                ....*....|...
gi 18414458 567 TSAGVATVVSSCP 579
Cdd:cd00116 263 TDDGAKDLAEVLA 275
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 376-499 1.58e-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: 47.48  E-value: 1.58e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414458 376 ELALLYCQRIGNSALQEIGKGCKSLEILHLVDCSG--IGDIAMCSIAKGCRNLKKLHIRRCYE--IGNKGIISIGKHCK- 450
Cdd:COG5238 183 ETVYLGCNQIGDEGIEELAEALTQNTTVTTLWLKRnpIGDEGAEILAEALKGNKSLTTLDLSNnqIGDEGVIALAEALKn 262

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 18414458 451 --SLTELSLRfCDKVGNKALIAIGKGCS----LQQLNVSGcNQISDAGITAIARG 499
Cdd:COG5238 263 ntTVETLYLS-GNQIGAEGAIALAKALQgnttLTSLDLSV-NRIGDEGAIALAEG 315
F-box_FBXL8 cd22121
F-box domain found in F-box/LRR-repeat protein 8 (FBXL8) and similar proteins; FBXL8, also ...
 9-39 1.83e-05

F-box domain found in F-box/LRR-repeat protein 8 (FBXL8) and similar proteins; FBXL8, also called F-box and leucine-rich repeat protein 8, or F-box protein FBL8, is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438893  Cd Length: 35  Bit Score: 41.96  E-value: 1.83e-05
                        10        20        30
                ....*....|....*....|....*....|.
gi 18414458   9 NCLPEELILEIFRRLeSKPNRDACSLVCKRW 39
Cdd:cd22121   1 NALPEEILVHIFRHL-SLRDRYAAAQVCKHW 30
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
117-275 9.03e-05

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 45.31  E-value: 9.03e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414458 117 SGAENVESSSLTDTGLTALANGFPRIENLSLIWCPN--VSSVGLcSLAQkCTSLKSLDLQGCYVGDqgLAAVGKFCKQLE 194
Cdd:COG4886 110 SNLTNLESLDLSGNQLTDLPEELANLTNLKELDLSNnqLTDLPE-PLGN-LTNLKSLDLSNNQLTD--LPEELGNLTNLK 185

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414458 195 ELNLRFCEgLTDvgvIDLVVGCSKSLKSIGVaASAKITDLSLEavGSHCKLLEVLYLDSEYIHDKGLIAvaqgchRLKNL 274
Cdd:COG4886 186 ELDLSNNQ-ITD---LPEPLGNLTNLEELDL-SGNQLTDLPEP--LANLTNLETLDLSNNQLTDLPELG------NLTNL 252


                .
gi 18414458 275 K 275
Cdd:COG4886 253 E 253
LRR_CC smart00367
Leucine-rich repeat - CC (cysteine-containing) subfamily;
526-551 1.02e-04

Leucine-rich repeat - CC (cysteine-containing) subfamily;


Pssm-ID: 197685 [Multi-domain]  Cd Length: 26  Bit Score: 39.31  E-value: 1.02e-04
                           10        20
                   ....*....|....*....|....*.
gi 18414458    526 CPMLKDLVLSHCHHITDNGLNHLVQK 551
Cdd:smart00367   1 CPNLRELDLSGCTNITDEGLQALAKG 26
FBOX smart00256
A Receptor for Ubiquitination Targets;
11-42 1.63e-04

A Receptor for Ubiquitination Targets;


Pssm-ID: 197608  Cd Length: 41  Bit Score: 39.34  E-value: 1.63e-04
                           10        20        30
                   ....*....|....*....|....*....|..
gi 18414458     11 LPEELILEIFRRLESKpNRDACSLVCKRWLSL 42
Cdd:smart00256   1 LPDEILEEILSKLDPK-DLLRLRKVSRKWRSL 31
FBXL3_LRR-like cd23951
Leucine-rich repeat domain of FBXL3 and related proteins; F-box/LRR-repeat proteins are part ...
 217-432 1.93e-04

Leucine-rich repeat domain of FBXL3 and related proteins; F-box/LRR-repeat proteins are part of Skp1-Cul1-F-box-protein (SCF) ubiquitin ligase complexes. They contain an F-Box, which binds to the core complex component SKP and a leucine-rich repeat (LRR) domain which gives substrate binding specificity. FBXL3 (F-box and leucine rich repeat protein 3) and FBXL21 have been shown to bind CRY1 repressors and are involved in regulation of circadian clock.


Pssm-ID: 467830 [Multi-domain]  Cd Length: 349  Bit Score: 43.91  E-value: 1.93e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414458 217 SKSLKSIGVAASAkITDLSLEAVGSHCK-LLEVLYLDS-EYIHDKGLIAVAQGCHRLKNLKLQCVSVTD---VAFAAVGE 291
Cdd:cd23951  93 SSSLSSLAIDDTP-VDDPSLQTLASSSSdTLELLKMKScPRVSPRGILAVADHCQHLRELSLNYHLLSDdllLALSSEEH 171

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414458 292 LCTSLERLALYS-------FQHFTDKGMRAIGKGSKklkDLTLSDCYFVSCKglEAIAHgckeLERVEIN------GCHn 358
Cdd:cd23951 172 VRLEHLRIDVVSendgpmpLHQISKESWDALIKHSP---DVNLVMYFFVLED--EDFDP----FFRSYTPvthlyfGRS- 241

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414458 359 IGTRGIEAIGKSCPRLKELALlycQRIGNS----ALQEIGKGCKSLEILHL----VDCSGIGDIA-MCSiakgcRNLKKL 429
Cdd:cd23951 242 VPKAVLGRVGQHCPRLVELVV---CANGNSpideELIRIAKNCKQLSSLGLgeceVSCSALVEFAkLCG-----PRLTEL 313


                ...
gi 18414458 430 HIR 432
Cdd:cd23951 314 YVM 316
F-box-like pfam12937
F-box-like; This is an F-box-like family.
 9-42 2.44e-04

F-box-like; This is an F-box-like family.


Pssm-ID: 463757 [Multi-domain]  Cd Length: 45  Bit Score: 39.00  E-value: 2.44e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 18414458     9 NCLPEELILEIFRRLeSKPNRDACSLVCKRWLSL 42
Cdd:pfam12937   2 SSLPDEILLQIFSYL-DPKDLLRLALVCRRWREL 34
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 157-299 3.38e-04

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: 43.11  E-value: 3.38e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414458 157 GLCSLAQKctsLKSLDLQGCYVGDQG---LAAVGKFCKQLEELNLRFcEGLTDVGVIDLVVG--CSKSLKSIGVAASAkI 231
Cdd:cd00116 131 GLKDLPPA---LEKLVLGRNRLEGASceaLAKALRANRDLKELNLAN-NGIGDAGIRALAEGlkANCNLEVLDLNNNG-L 205

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18414458 232 TDL---SLEAVGSHCKLLEVLYLDSEYIHDKGLIAVAQG----CHRLKNLKLQCVSVTDVAFAAVGELCTSLERL 299
Cdd:cd00116 206 TDEgasALAETLASLKSLEVLNLGDNNLTDAGAAALASAllspNISLLTLSLSCNDITDDGAKDLAEVLAEKESL 280
F-box_FBXO42 cd22110
F-box domain found in F-box only protein 42 (FBXO42) and similar proteins; FBXO42, also called ...
 7-42 4.28e-04

F-box domain found in F-box only protein 42 (FBXO42) and similar proteins; FBXO42, also called FBX42, or just one F-box and Kelch domain-containing protein (JFK), is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. It specifically recognizes p53/TP53, promoting its ubiquitination and degradation. FBXO42 is also involved in the ubiquitin-proteasome system that may play a role in the pathogenesis of Parkinson's disease (PD). The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438882  Cd Length: 38  Bit Score: 38.09  E-value: 4.28e-04
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 18414458   7 INNcLPEELILEIFRRLESKPNRDACSLVCKRWLSL 42
Cdd:cd22110   1 IND-LPEEILEYILSYLSPYGDLKSAALVCKRWHRI 35
F-box_5 pfam18511
F-box; Jasmonates are a family of plant hormones that regulate plant growth, development and ...
 23-47 7.94e-04

F-box; Jasmonates are a family of plant hormones that regulate plant growth, development and responses to stress. COI1 is an F-box protein that functions as the substrate-recruiting module of the Skp1-Cul1-F-box protein (SCF) ubiquitin E3 ligase complex. The role of COI1-mediated JAZ degradation in jasmonate (JA) signaling is analogous to auxin signaling through the receptor F-box protein transport inhibitor response 1 (TIR1), which promotes hormone-dependent turnover of the AUX/IAA transcriptional repressors. The crystal structure of COI1 reveals a TIR1-like overall architecture, with an N-terminal tri-helical F-box motif bound to ASK1 and a C-terminal horseshoe-shaped solenoid domain formed by 18 tandem leucine-rich repeats. This entry represents the N-terminal F-box domain which is also found in other auxin signaling f-box proteins such as AFB1, AFB2 and AFB3.


Pssm-ID: 436553  Cd Length: 42  Bit Score: 37.55  E-value: 7.94e-04
                          10        20
                  ....*....|....*....|....*
gi 18414458    23 LESKPNRDACSLVCKRWLSLERFSR 47
Cdd:pfam18511  16 ITSPRDRNAVSLVCKRWYRIEALTR 40
F-box pfam00646
F-box domain; This domain is approximately 50 amino acids long, and is usually found in the ...
 10-42 1.40e-03

F-box domain; This domain is approximately 50 amino acids long, and is usually found in the N-terminal half of a variety of proteins. Two motifs that are commonly found associated with the F-box domain are the leucine rich repeats (LRRs; pfam00560 and pfam07723) and the WD repeat (pfam00400). The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 425796  Cd Length: 43  Bit Score: 36.75  E-value: 1.40e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 18414458    10 CLPEELILEIFRRLESKpNRDACSLVCKRWLSL 42
Cdd:pfam00646   3 DLPDDLLLEILSRLDPK-DLLRLSLVSKRWRSL 34
F-box_SF cd09917
F-box domain superfamily; This short domain is commonly found at the N-terminus of various ...
 9-42 3.82e-03

F-box domain superfamily; This short domain is commonly found at the N-terminus of various proteins, and typically co-occurs with one or more other conserved domains or motifs, such as leucine rich repeats, WD40 repeats, kelch, tub, spry, and others. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression. One of the best researched roles of F-box proteins is their participation in SCF (Skp1-Cul1-F-box protein), a multi-protein complex that functions as a ubiquitin E3 ligase, where the role of the F-box protein is to recruit target substrates. Gene families containing the F-box are found greatly expanded in narrow taxonomic lineages, such as flowering plants and nematodes. In this hierarchical classification, many of the subfamilies are named according to their domain architectures.


Pssm-ID: 438852  Cd Length: 35  Bit Score: 35.11  E-value: 3.82e-03
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 18414458   9 NCLPEELILEIFRRLeskPNRD--ACSLVCKRWLSL 42
Cdd:cd09917   1 SDLPDEILLKILSYL---DPRDllRLSLVCKRWREL 33
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 362-535 5.10e-03

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: 38.61  E-value: 5.10e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414458 362 RGIEAIG--KSCPRLKELaLLYCQRIgnSALQEIGkGCKSLEILHLVD--CSGIGDIAmcsiakGCRNLKKLHIRrcyei 437
Cdd:cd21340  12 KNITKIDnlSLCKNLKVL-YLYDNKI--TKIENLE-FLTNLTHLYLQNnqIEKIENLE------NLVNLKKLYLG----- 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414458 438 GNKgiISI--G-KHCKSLTEL-----------SLRFcdkvGNKALIAIGKgcSLQQLNVSGCNqISDagITAIArGCPQL 503
Cdd:cd21340  77 GNR--ISVveGlENLTNLEELhienqrlppgeKLTF----DPRSLAALSN--SLRVLNISGNN-IDS--LEPLA-PLRNL 144

                       170       180       190
                ....*....|....*....|....*....|....
gi 18414458 504 THLDISV--LQNIGDmpLAELGEGCPMLKDLVLS 535
Cdd:cd21340 145 EQLDASNnqISDLEE--LLDLLSSWPSLRELDLT 176
LRR_CC smart00367
Leucine-rich repeat - CC (cysteine-containing) subfamily;
190-213 6.23e-03

Leucine-rich repeat - CC (cysteine-containing) subfamily;


Pssm-ID: 197685 [Multi-domain]  Cd Length: 26  Bit Score: 34.30  E-value: 6.23e-03
                           10        20
                   ....*....|....*....|....
gi 18414458    190 CKQLEELNLRFCEGLTDVGVIDLV 213
Cdd:smart00367   1 CPNLRELDLSGCTNITDEGLQALA 24
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 129-355 6.73e-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: 38.88  E-value: 6.73e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414458 129 DTGLTALANGFPRIENLSLIWCPNVS----SVGLCSLAQKCTSLKSLDLQGCYVGDQGLAAVgkfckqleelnlrfCEGL 204
Cdd:cd00116  67 PRGLQSLLQGLTKGCGLQELDLSDNAlgpdGCGVLESLLRSSSLQELKLNNNGLGDRGLRLL--------------AKGL 132

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414458 205 TDvgvidlvvgCSKSLKSIgVAASAKITDLSLEAVG---SHCKLLEVLYLDSEYIHDKGLIAVAQG----CHrLKNLKLQ 277
Cdd:cd00116 133 KD---------LPPALEKL-VLGRNRLEGASCEALAkalRANRDLKELNLANNGIGDAGIRALAEGlkanCN-LEVLDLN 201

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414458 278 CVSVTD---VAFAAVGELCTSLERLALySFQHFTDKGMRAIGKG----SKKLKDLTLSDCYfVSCKGLEAIAHGCKE--- 347
Cdd:cd00116 202 NNGLTDegaSALAETLASLKSLEVLNL-GDNNLTDAGAAALASAllspNISLLTLSLSCND-ITDDGAKDLAEVLAEkes 279


                ....*...
gi 18414458 348 LERVEING 355
Cdd:cd00116 280 LLELDLRG 287
LRR_CC smart00367
Leucine-rich repeat - CC (cysteine-containing) subfamily;
371-396 7.65e-03

Leucine-rich repeat - CC (cysteine-containing) subfamily;


Pssm-ID: 197685 [Multi-domain]  Cd Length: 26  Bit Score: 34.30  E-value: 7.65e-03
                           10        20
                   ....*....|....*....|....*.
gi 18414458    371 CPRLKELALLYCQRIGNSALQEIGKG 396
Cdd:smart00367   1 CPNLRELDLSGCTNITDEGLQALAKG 26
 
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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