NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|442622939|ref|NP_001260812|]
View 

uncharacterized protein Dmel_CG8272, isoform B [Drosophila melanogaster]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 515-642 3.50e-13

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: 69.28  E-value: 3.50e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622939 515 YEMNLIREDDFEGHNIQQLRGLRSLNLRGCnKISDVSLKYGLKHIELRRLMLSNCQQISLLGMEAMASSCPSIEELDLSD 594
Cdd:cd09293    9 HKLGQITQSNISQLLRILHSGLEWLELYMC-PISDPPLDQLSNCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRA 87

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 442622939 595 CYNITDKTIQVVTSKLPRLKALHIS---GCSQLTEHTLDAIITNCSCLQTL 642
Cdd:cd09293   88 CENITDSGIVALATNCPKLQTINLGrhrNGHLITDVSLSALGKNCTFLQTV 138
AMN1 super family cl39120
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 269-440 3.41e-09

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: 57.72  E-value: 3.41e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622939 269 QLQRLYLAGCRQLNctTILNFLATQPQLCALDLSATMCVNDENLAALVQTNPQLEHLKVNGCLSITNAGAIHLA-KLKCL 347
Cdd:cd09293   29 GLEWLELYMCPISD--PPLDQLSNCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALAtNCPKL 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622939 348 KSLDIS---NCDNLTSSGIIEgiASEENPVIQELNVSYLQICEECIKAIASNLRC-LRSLHLNHCVNgATDEAIQSVIGQ 423
Cdd:cd09293  107 QTINLGrhrNGHLITDVSLSA--LGKNCTFLQTVGFAGCDVTDKGVWELASGCSKsLERLSLNNCRN-LTDQSIPAILAS 183

                        170
                 ....*....|....*....
gi 442622939 424 LRW--LRELSLEHCSGLTD 440
Cdd:cd09293  184 NYFpnLSVLEFRGCPLITD 202
F-box_SF super family cl45894
F-box domain superfamily; This short domain is commonly found at the N-terminus of various ...
 11-58 3.62e-09

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.


The actual alignment was detected with superfamily member cd22104:

Pssm-ID: 459239  Cd Length: 48  Bit Score: 52.64  E-value: 3.62e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 442622939  11 YDDLPLEIVLKIFSYLGYSDLQAAGSTCQRWHAALDQAEFNQRTRVCF 58
Cdd:cd22104    1 WANLPSVVLVHIFSYLPPRDRLRASSTCRRWREALFHPSLWRSLRLHL 48
C2 super family cl14603
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
 231-274 2.22e-03

C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


The actual alignment was detected with superfamily member cd08390:

Pssm-ID: 472691 [Multi-domain]  Cd Length: 123  Bit Score: 38.78  E-value: 2.22e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 442622939 231 TFKFILTILNLQRRTLRVLNFS------HTLIGQALLALCDLNLQLQRLY 274
Cdd:cd08390   68 TFVFQVSFKELQRRTLRLSVYDvdrfsrHCIIGHVLFPLKDLDLVKGGVV 117
 
Name Accession Description Interval E-value
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 515-642 3.50e-13

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: 69.28  E-value: 3.50e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622939 515 YEMNLIREDDFEGHNIQQLRGLRSLNLRGCnKISDVSLKYGLKHIELRRLMLSNCQQISLLGMEAMASSCPSIEELDLSD 594
Cdd:cd09293    9 HKLGQITQSNISQLLRILHSGLEWLELYMC-PISDPPLDQLSNCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRA 87

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 442622939 595 CYNITDKTIQVVTSKLPRLKALHIS---GCSQLTEHTLDAIITNCSCLQTL 642
Cdd:cd09293   88 CENITDSGIVALATNCPKLQTINLGrhrNGHLITDVSLSALGKNCTFLQTV 138
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 269-440 3.41e-09

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: 57.72  E-value: 3.41e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622939 269 QLQRLYLAGCRQLNctTILNFLATQPQLCALDLSATMCVNDENLAALVQTNPQLEHLKVNGCLSITNAGAIHLA-KLKCL 347
Cdd:cd09293   29 GLEWLELYMCPISD--PPLDQLSNCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALAtNCPKL 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622939 348 KSLDIS---NCDNLTSSGIIEgiASEENPVIQELNVSYLQICEECIKAIASNLRC-LRSLHLNHCVNgATDEAIQSVIGQ 423
Cdd:cd09293  107 QTINLGrhrNGHLITDVSLSA--LGKNCTFLQTVGFAGCDVTDKGVWELASGCSKsLERLSLNNCRN-LTDQSIPAILAS 183

                        170
                 ....*....|....*....
gi 442622939 424 LRW--LRELSLEHCSGLTD 440
Cdd:cd09293  184 NYFpnLSVLEFRGCPLITD 202
F-box_FBXO33 cd22104
F-box domain found in F-box only protein 33 (FBXO33) and similar proteins; FBXO33, also called ...
 11-58 3.62e-09

F-box domain found in F-box only protein 33 (FBXO33) and similar proteins; FBXO33, also called FBX33, is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. It exerts similar functions as F-box involved in polyQ pathogenesis (FipoQ) in modulating the ubiquitination and solubility of expanded SCA3-polyQ proteins. 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: 438876  Cd Length: 48  Bit Score: 52.64  E-value: 3.62e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 442622939  11 YDDLPLEIVLKIFSYLGYSDLQAAGSTCQRWHAALDQAEFNQRTRVCF 58
Cdd:cd22104    1 WANLPSVVLVHIFSYLPPRDRLRASSTCRRWREALFHPSLWRSLRLHL 48
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 290-415 3.02e-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: 3.02e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622939 290 LATQPQLCALDLSATmCVNDENLAAL---VQTNPQLEHLKVNGClSITNAGAIHLAKL----KCLKSLDISNcDNLTSSG 362
Cdd:COG5238  232 LKGNKSLTTLDLSNN-QIGDEGVIALaeaLKNNTTVETLYLSGN-QIGAEGAIALAKAlqgnTTLTSLDLSV-NRIGDEG 308

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 442622939 363 ---IIEGIasEENPVIQELNVSYLQICEECIKAIASNLRCLRSLH-LNHCVNGATDE 415
Cdd:COG5238  309 aiaLAEGL--QGNKTLHTLNLAYNGIGAQGAIALAKALQENTTLHsLDLSDNQIGDE 363
F-box-like pfam12937
F-box-like; This is an F-box-like family.
 12-44 2.11e-06

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


Pssm-ID: 463757 [Multi-domain]  Cd Length: 45  Bit Score: 44.78  E-value: 2.11e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 442622939   12 DDLPLEIVLKIFSYLGYSDLQAAGSTCQRWHAA 44
Cdd:pfam12937   2 SSLPDEILLQIFSYLDPKDLLRLALVCRRWREL 34
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
518-675 3.37e-06

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 49.93  E-value: 3.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622939 518 NLIREDDFEGHNIQQLRGLRSLNLRGcNKISDVSLK-YGLKHieLRRLMLSNCQQISLlgmEAMASSCPSIEELDLSDCy 596
Cdd:COG4886   97 NLTELDLSGNEELSNLTNLESLDLSG-NQLTDLPEElANLTN--LKELDLSNNQLTDL---PEPLGNLTNLKSLDLSNN- 169

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622939 597 NITDktIQVVTSKLPRLKALHISGCsQLTEhtLDAIITNCSCLQTLSIYRCRsmYTDLEERLSGVKTLRNLNMDN--LTS 674
Cdd:COG4886  170 QLTD--LPEELGNLTNLKELDLSNN-QITD--LPEPLGNLTNLEELDLSGNQ--LTDLPEPLANLTNLETLDLSNnqLTD 242


                 .
gi 442622939 675 I 675
Cdd:COG4886  243 L 243
FBOX smart00256
A Receptor for Ubiquitination Targets;
14-54 1.70e-04

A Receptor for Ubiquitination Targets;


Pssm-ID: 197608  Cd Length: 41  Bit Score: 39.34  E-value: 1.70e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 442622939    14 LPLEIVLKIFSYLGYSDLQAAGSTCQRWHAALDQAEFNQRT 54
Cdd:smart00256   1 LPDEILEEILSKLDPKDLLRLRKVSRKWRSLIDSHDFWFKL 41
LRR_CC smart00367
Leucine-rich repeat - CC (cysteine-containing) subfamily;
584-604 2.06e-03

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


Pssm-ID: 197685 [Multi-domain]  Cd Length: 26  Bit Score: 35.84  E-value: 2.06e-03
                           10        20
                   ....*....|....*....|.
gi 442622939   584 CPSIEELDLSDCYNITDKTIQ 604
Cdd:smart00367   1 CPNLRELDLSGCTNITDEGLQ 21
C2A_Synaptotagmin-15-17 cd08390
C2A domain first repeat present in Synaptotagmins 15 and 17; Synaptotagmin is a ...
 231-274 2.22e-03

C2A domain first repeat present in Synaptotagmins 15 and 17; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. It is thought to be involved in the trafficking and exocytosis of secretory vesicles in non-neuronal tissues and is Ca2+ independent. Human synaptotagmin 15 has 2 alternatively spliced forms that encode proteins with different C-termini. The larger, SYT15a, contains a N-terminal TM region, a putative fatty-acylation site, and 2 tandem C terminal C2 domains. The smaller, SYT15b, lacks the C-terminal portion of the second C2 domain. Unlike most other synaptotagmins it is nearly absent in the brain and rather is found in the heart, lungs, skeletal muscle, and testis. Synaptotagmin 17 is located in the brain, kidney, and prostate and is thought to be a peripheral membrane protein. Previously all synaptotagmins were thought to be calcium sensors in the regulation of neurotransmitter release and hormone secretion, but it has been shown that not all of them bind calcium. Of the 17 identified synaptotagmins only 8 bind calcium (1-3, 5-7, 9, 10). The function of the two C2 domains that bind calcium are: regulating the fusion step of synaptic vesicle exocytosis (C2A) and binding to phosphatidyl-inositol-3,4,5-triphosphate (PIP3) in the absence of calcium ions and to phosphatidylinositol bisphosphate (PIP2) in their presence (C2B). C2B also regulates also the recycling step of synaptic vesicles. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-I topology.


Pssm-ID: 176036 [Multi-domain]  Cd Length: 123  Bit Score: 38.78  E-value: 2.22e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 442622939 231 TFKFILTILNLQRRTLRVLNFS------HTLIGQALLALCDLNLQLQRLY 274
Cdd:cd08390   68 TFVFQVSFKELQRRTLRLSVYDvdrfsrHCIIGHVLFPLKDLDLVKGGVV 117
PLN03210 PLN03210
Resistant to P. syringae 6; Provisional
 530-672 2.31e-03

Resistant to P. syringae 6; Provisional


Pssm-ID: 215633 [Multi-domain]  Cd Length: 1153  Bit Score: 41.40  E-value: 2.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622939  530 IQQLRGLRSLNLRGCN---KISDVSLKYGLKhielrRLMLSNCQqiSLLGMEAMASSCPSIEELDLSDCYNITDKTIQVv 606
Cdd:PLN03210  630 VHSLTGLRNIDLRGSKnlkEIPDLSMATNLE-----TLKLSDCS--SLVELPSSIQYLNKLEDLDMSRCENLEILPTGI- 701

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442622939  607 tsKLPRLKALHISGCSQLteHTLDAIITNCSclqTLSIYRcrsmyTDLEERLSgvktlrNLNMDNL 672
Cdd:PLN03210  702 --NLKSLYRLNLSGCSRL--KSFPDISTNIS---WLDLDE-----TAIEEFPS------NLRLENL 749
PRK15386 PRK15386
type III secretion effector GogB;
299-504 9.88e-03

type III secretion effector GogB;


Pssm-ID: 237954 [Multi-domain]  Cd Length: 426  Bit Score: 39.08  E-value: 9.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622939 299 LDLSATMCVNDENLAALVQT--NPQLEHLKVNGCLSITNAGAIHLAKL-KCLKSLDISNCDNLTSsgiIEGIASEEnpvI 375
Cdd:PRK15386  23 LEPDGTFCSNSTETSAEIRSeiTPQIEEARASGRLYIKDCDIESLPVLpNELTEITIENCNNLTT---LPGSIPEG---L 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622939 376 QELNVSYlqiCEEcikaIASNLRCLRSLHLnhcvNGATDEAIQSVIGQlrwLRELSLEHCSGLTDAALTGIniskleMSR 455
Cdd:PRK15386  97 EKLTVCH---CPE----ISGLPESVRSLEI----KGSATDSIKNVPNG---LTSLSINSYNPENQARIDNL------ISP 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 442622939 456 KQSGSQVSSMDNFYPPysntlaerDSLAGSLQSIKISLRSKAEDEIVRD 504
Cdd:PRK15386 157 SLKTLSLTGCSNIILP--------EKLPESLQSITLHIEQKTTWNISFE 197
 
Name Accession Description Interval E-value
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 515-642 3.50e-13

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: 69.28  E-value: 3.50e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622939 515 YEMNLIREDDFEGHNIQQLRGLRSLNLRGCnKISDVSLKYGLKHIELRRLMLSNCQQISLLGMEAMASSCPSIEELDLSD 594
Cdd:cd09293    9 HKLGQITQSNISQLLRILHSGLEWLELYMC-PISDPPLDQLSNCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRA 87

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 442622939 595 CYNITDKTIQVVTSKLPRLKALHIS---GCSQLTEHTLDAIITNCSCLQTL 642
Cdd:cd09293   88 CENITDSGIVALATNCPKLQTINLGrhrNGHLITDVSLSALGKNCTFLQTV 138
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 530-647 2.00e-09

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: 58.49  E-value: 2.00e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622939 530 IQQLRGLRSLNLRGCNKISDVSLKY------GLKHIELRRLmlSNCQQISLLGMEAMASSCPSIEELDLSDCyNITDKT- 602
Cdd:cd09293   74 AQSCPNLQVLDLRACENITDSGIVAlatncpKLQTINLGRH--RNGHLITDVSLSALGKNCTFLQTVGFAGC-DVTDKGv 150

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 442622939 603 IQVVTSKLPRLKALHISGCSQLTEHTLDAII--TNCSCLQTLSIYRC 647
Cdd:cd09293  151 WELASGCSKSLERLSLNNCRNLTDQSIPAILasNYFPNLSVLEFRGC 197
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 269-440 3.41e-09

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: 57.72  E-value: 3.41e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622939 269 QLQRLYLAGCRQLNctTILNFLATQPQLCALDLSATMCVNDENLAALVQTNPQLEHLKVNGCLSITNAGAIHLA-KLKCL 347
Cdd:cd09293   29 GLEWLELYMCPISD--PPLDQLSNCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALAtNCPKL 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622939 348 KSLDIS---NCDNLTSSGIIEgiASEENPVIQELNVSYLQICEECIKAIASNLRC-LRSLHLNHCVNgATDEAIQSVIGQ 423
Cdd:cd09293  107 QTINLGrhrNGHLITDVSLSA--LGKNCTFLQTVGFAGCDVTDKGVWELASGCSKsLERLSLNNCRN-LTDQSIPAILAS 183

                        170
                 ....*....|....*....
gi 442622939 424 LRW--LRELSLEHCSGLTD 440
Cdd:cd09293  184 NYFpnLSVLEFRGCPLITD 202
F-box_FBXO33 cd22104
F-box domain found in F-box only protein 33 (FBXO33) and similar proteins; FBXO33, also called ...
 11-58 3.62e-09

F-box domain found in F-box only protein 33 (FBXO33) and similar proteins; FBXO33, also called FBX33, is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. It exerts similar functions as F-box involved in polyQ pathogenesis (FipoQ) in modulating the ubiquitination and solubility of expanded SCA3-polyQ proteins. 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: 438876  Cd Length: 48  Bit Score: 52.64  E-value: 3.62e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 442622939  11 YDDLPLEIVLKIFSYLGYSDLQAAGSTCQRWHAALDQAEFNQRTRVCF 58
Cdd:cd22104    1 WANLPSVVLVHIFSYLPPRDRLRASSTCRRWREALFHPSLWRSLRLHL 48
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 290-415 3.02e-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: 3.02e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622939 290 LATQPQLCALDLSATmCVNDENLAAL---VQTNPQLEHLKVNGClSITNAGAIHLAKL----KCLKSLDISNcDNLTSSG 362
Cdd:COG5238  232 LKGNKSLTTLDLSNN-QIGDEGVIALaeaLKNNTTVETLYLSGN-QIGAEGAIALAKAlqgnTTLTSLDLSV-NRIGDEG 308

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 442622939 363 ---IIEGIasEENPVIQELNVSYLQICEECIKAIASNLRCLRSLH-LNHCVNGATDE 415
Cdd:COG5238  309 aiaLAEGL--QGNKTLHTLNLAYNGIGAQGAIALAKALQENTTLHsLDLSDNQIGDE 363
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 321-452 3.88e-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: 51.56  E-value: 3.88e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622939 321 QLEHLKVNGCLSITNAGAIHLAKlKC--LKSLDISNCDNLTSSGIIEgIASEeNPVIQELNVSYLQ----ICEECIKAIA 394
Cdd:cd09293   53 KLKKLILPGSKLIDDEGLIALAQ-SCpnLQVLDLRACENITDSGIVA-LATN-CPKLQTINLGRHRnghlITDVSLSALG 129

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442622939 395 SNLRCLRSLHLNHCvnGATDEA-IQSVIGQLRWLRELSLEHCSGLTDAALTGI-------NISKLE 452
Cdd:cd09293  130 KNCTFLQTVGFAGC--DVTDKGvWELASGCSKSLERLSLNNCRNLTDQSIPAIlasnyfpNLSVLE 193
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 245-424 5.51e-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: 52.48  E-value: 5.51e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622939 245 TLRVLNFSHTLIG-QALLALCDL---NLQLQRLYLaGCRQLNCTT---ILNFLATQPQLCALDLSatmcVND------EN 311
Cdd:COG5238  237 SLTTLDLSNNQIGdEGVIALAEAlknNTTVETLYL-SGNQIGAEGaiaLAKALQGNTTLTSLDLS----VNRigdegaIA 311

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622939 312 LAALVQTNPQLEHLKVNGClSITNAGAI----HLAKLKCLKSLDIsnCDNLTSSGIIEGIAS--EENPVIQELNVSYLQI 385
Cdd:COG5238  312 LAEGLQGNKTLHTLNLAYN-GIGAQGAIalakALQENTTLHSLDL--SDNQIGDEGAIALAKylEGNTTLRELNLGKNNI 388

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 442622939 386 CEECIKAIASNLRCLRSLHLNHCVNGATDEAIQSVIGQL 424
Cdd:COG5238  389 GKQGAEALIDALQTNRLHTLILDGNLIGAEAQQRLEQLL 427
F-box_SF cd09917
F-box domain superfamily; This short domain is commonly found at the N-terminus of various ...
 12-46 1.78e-06

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: 44.74  E-value: 1.78e-06
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 442622939  12 DDLPLEIVLKIFSYLGYSDLQAAGSTCQRWHAALD 46
Cdd:cd09917    1 SDLPDEILLKILSYLDPRDLLRLSLVCKRWRELAS 35
F-box-like pfam12937
F-box-like; This is an F-box-like family.
 12-44 2.11e-06

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


Pssm-ID: 463757 [Multi-domain]  Cd Length: 45  Bit Score: 44.78  E-value: 2.11e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 442622939   12 DDLPLEIVLKIFSYLGYSDLQAAGSTCQRWHAA 44
Cdd:pfam12937   2 SSLPDEILLQIFSYLDPKDLLRLALVCRRWREL 34
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 536-628 3.02e-06

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: 48.86  E-value: 3.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622939 536 LRSLNL---RGCNKISDVSL-KYGLKHIELRRLMLSNCQqISLLGMEAMASSC-PSIEELDLSDCYNITDKTIQVVTSKL 610
Cdd:cd09293  106 LQTINLgrhRNGHLITDVSLsALGKNCTFLQTVGFAGCD-VTDKGVWELASGCsKSLERLSLNNCRNLTDQSIPAILASN 184

                         90       100
                 ....*....|....*....|
gi 442622939 611 --PRLKALHISGCSQLTEHT 628
Cdd:cd09293  185 yfPNLSVLEFRGCPLITDFS 204
F-box_FBXW5 cd22132
F-box domain found in F-box/WD repeat-containing protein 5 (FBXW5) and similar proteins; FBXW5, ...
 12-44 3.23e-06

F-box domain found in F-box/WD repeat-containing protein 5 (FBXW5) and similar proteins; FBXW5, also called F-box and WD-40 domain-containing protein 5, is the substrate-recognition component of both SCF (SKP1-CUL1-F-box protein) and DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes. 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: 438904 [Multi-domain]  Cd Length: 46  Bit Score: 44.52  E-value: 3.23e-06
                         10        20        30
                 ....*....|....*....|....*....|...
gi 442622939  12 DDLPLEIVLKIFSYLGYSDLQAAGSTCQRWHAA 44
Cdd:cd22132    2 PLLPDSLLLHIFSYLSPKDLLAAGQVCKQWYRV 34
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
518-675 3.37e-06

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 49.93  E-value: 3.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622939 518 NLIREDDFEGHNIQQLRGLRSLNLRGcNKISDVSLK-YGLKHieLRRLMLSNCQQISLlgmEAMASSCPSIEELDLSDCy 596
Cdd:COG4886   97 NLTELDLSGNEELSNLTNLESLDLSG-NQLTDLPEElANLTN--LKELDLSNNQLTDL---PEPLGNLTNLKSLDLSNN- 169

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622939 597 NITDktIQVVTSKLPRLKALHISGCsQLTEhtLDAIITNCSCLQTLSIYRCRsmYTDLEERLSGVKTLRNLNMDN--LTS 674
Cdd:COG4886  170 QLTD--LPEELGNLTNLKELDLSNN-QITD--LPEPLGNLTNLEELDLSGNQ--LTDLPEPLANLTNLETLDLSNnqLTD 242


                 .
gi 442622939 675 I 675
Cdd:COG4886  243 L 243
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 241-401 1.46e-05

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: 47.74  E-value: 1.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622939 241 LQRRTLRVLNFSHTLIGQALL-----ALCDLNLQLQRLYLAGCR-------------QLNCT-TILNF------------ 289
Cdd:cd00116  105 LRSSSLQELKLNNNGLGDRGLrllakGLKDLPPALEKLVLGRNRlegascealakalRANRDlKELNLanngigdagira 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622939 290 ----LATQPQLCALDLSATmCVNDEN---LAALVQTNPQLEHLKVNGCLsITNAGAIHLAK-----LKCLKSLDISNCDn 357
Cdd:cd00116  185 laegLKANCNLEVLDLNNN-GLTDEGasaLAETLASLKSLEVLNLGDNN-LTDAGAAALASallspNISLLTLSLSCND- 261

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 442622939 358 LTSSG---IIEGIAseENPVIQELNVSYLQICEECIKAIASNLRCLR 401
Cdd:cd00116  262 ITDDGakdLAEVLA--EKESLLELDLRGNKFGEEGAQLLAESLLEPG 306
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
529-688 1.91e-05

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 47.62  E-value: 1.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622939 529 NIQQLRGLRSLNLRGcNKISDVSLK-YGLKHieLRRLMLSNCqQISLLGMEamASSCPSIEELDLSDCyNITDktIQVVT 607
Cdd:COG4886  131 ELANLTNLKELDLSN-NQLTDLPEPlGNLTN--LKSLDLSNN-QLTDLPEE--LGNLTNLKELDLSNN-QITD--LPEPL 201

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622939 608 SKLPRLKALHISGCsQLTEhtLDAIITNCSCLQTLSIYRCRsmYTDLEErLSGVKTLRNLNMDN--LTSIDNAEFFRLKK 685
Cdd:COG4886  202 GNLTNLEELDLSGN-QLTD--LPEPLANLTNLETLDLSNNQ--LTDLPE-LGNLTNLEELDLSNnqLTDLPPLANLTNLK 275


                 ...
gi 442622939 686 RLD 688
Cdd:COG4886  276 TLD 278
F-box_FBXO42 cd22110
F-box domain found in F-box only protein 42 (FBXO42) and similar proteins; FBXO42, also called ...
 12-43 2.39e-05

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: 41.94  E-value: 2.39e-05
                         10        20        30
                 ....*....|....*....|....*....|...
gi 442622939  12 DDLPLEIVLKIFSYLG-YSDLQAAGSTCQRWHA 43
Cdd:cd22110    2 NDLPEEILEYILSYLSpYGDLKSAALVCKRWHR 34
F-box_FBXL1 cd22114
F-box domain found in F-box/LRR-repeat protein 1 (FBXL1) and similar proteins; FBXL1, also ...
 11-42 8.53e-05

F-box domain found in F-box/LRR-repeat protein 1 (FBXL1) and similar proteins; FBXL1, also called S-phase kinase-associated protein 2, cyclin-A/CDK2-associated protein p45, F-box protein Skp2, or p45skp2, is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins involved in cell cycle progression, signal transduction and transcription. It specifically recognizes phosphorylated CDKN1B/p27kip and is involved in regulation of G1/S transition. 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: 438886  Cd Length: 41  Bit Score: 40.47  E-value: 8.53e-05
                         10        20        30
                 ....*....|....*....|....*....|..
gi 442622939  11 YDDLPLEIVLKIFSYLGYSDLQAAGSTCQRWH 42
Cdd:cd22114    1 WDSLPDELLLGIFSCLCLPDLLKVSQVCKRWY 32
FBOX smart00256
A Receptor for Ubiquitination Targets;
14-54 1.70e-04

A Receptor for Ubiquitination Targets;


Pssm-ID: 197608  Cd Length: 41  Bit Score: 39.34  E-value: 1.70e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 442622939    14 LPLEIVLKIFSYLGYSDLQAAGSTCQRWHAALDQAEFNQRT 54
Cdd:smart00256   1 LPDEILEEILSKLDPKDLLRLRKVSRKWRSLIDSHDFWFKL 41
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 310-441 4.72e-04

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: 43.24  E-value: 4.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622939 310 ENLAALVQTNPQLEHLKVNGcLSITNAGAI----HLAKLKCLKSLDISNcDNLTSSGIIE-GIASEENPVIQELNVSYLQ 384
Cdd:COG5238  198 EELAEALTQNTTVTTLWLKR-NPIGDEGAEilaeALKGNKSLTTLDLSN-NQIGDEGVIAlAEALKNNTTVETLYLSGNQ 275

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442622939 385 ICEECIKAIASNLR---CLRSLHLNhcVNGATDE---AIQSVIGQLRWLRELSLEHCsGLTDA 441
Cdd:COG5238  276 IGAEGAIALAKALQgntTLTSLDLS--VNRIGDEgaiALAEGLQGNKTLHTLNLAYN-GIGAQ 335
F-box_FBXO11 cd22091
F-box domain found in F-box only protein 11 (FBXO11) and similar proteins; FBXO11, also called ...
 12-42 4.75e-04

F-box domain found in F-box only protein 11 (FBXO11) and similar proteins; FBXO11, also called FBX11, protein arginine N-methyltransferase 9 (PRMT9), or vitiligo-associated protein 1 (VIT-1), is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins, such as DTL/CDT2, BCL6 and PRDM1/BLIMP1. 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: 438863  Cd Length: 45  Bit Score: 38.17  E-value: 4.75e-04
                         10        20        30
                 ....*....|....*....|....*....|.
gi 442622939  12 DDLPLEIVLKIFSYLGYSDLQAAGSTCQRWH 42
Cdd:cd22091    2 EELPDEVLLKIFSYLLEQDLCRAAQVCKRFN 32
F-box pfam00646
F-box domain; This domain is approximately 50 amino acids long, and is usually found in the ...
 12-53 7.55e-04

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: 37.52  E-value: 7.55e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 442622939   12 DDLPLEIVLKIFSYLGYSDLQAAGSTCQRWHAALDQAEFNQR 53
Cdd:pfam00646   2 LDLPDDLLLEILSRLDPKDLLRLSLVSKRWRSLVDSLKLWKK 43
F-box_FBXL5 cd22118
F-box domain found in F-box/LRR-repeat protein 5 (FBXL5) and similar proteins; FBXL5, also ...
 12-42 1.19e-03

F-box domain found in F-box/LRR-repeat protein 5 (FBXL5) and similar proteins; FBXL5, also called F-box and leucine-rich repeat protein 5, F-box protein FBL4/FBL5, or p45SKP2-like protein, is the substrate-recognition component of an SCF (SKP1-cullin-F-box) protein ligase complex that plays a central role in iron homeostasis by promoting the ubiquitination and subsequent degradation of IREB2/IRP2. 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: 438890  Cd Length: 41  Bit Score: 36.93  E-value: 1.19e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 442622939  12 DDLPLEIVLKIFSYLGYSDLQAAGSTCQRWH 42
Cdd:cd22118    2 SSLPPEIMLKIFSYLNPQDLCRCAQVCTKWS 32
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
230-452 1.39e-03

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 41.84  E-value: 1.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622939 230 LTFKFILTILNLQRRTLRVLNFSHTLIGQALLALCDLNLQLQRLYLAGCRQLNCTTILNFLATQPQLCALDLSatmcvND 309
Cdd:COG4886   32 LLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLS-----GN 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622939 310 ENLAALvqtnPQLEHLKVNGClSITNAGAiHLAKLKCLKSLDISNCdNLTSsgIIEGIASEENpvIQELNVSYLQIceEC 389
Cdd:COG4886  107 EELSNL----TNLESLDLSGN-QLTDLPE-ELANLTNLKELDLSNN-QLTD--LPEPLGNLTN--LKSLDLSNNQL--TD 173

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442622939 390 IKAIASNLRCLRSLHLNHcvNGATDeaIQSVIGQLRWLRELSLEHCsGLTDAALTGINISKLE 452
Cdd:COG4886  174 LPEELGNLTNLKELDLSN--NQITD--LPEPLGNLTNLEELDLSGN-QLTDLPEPLANLTNLE 231
LRR_CC smart00367
Leucine-rich repeat - CC (cysteine-containing) subfamily;
584-604 2.06e-03

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


Pssm-ID: 197685 [Multi-domain]  Cd Length: 26  Bit Score: 35.84  E-value: 2.06e-03
                           10        20
                   ....*....|....*....|.
gi 442622939   584 CPSIEELDLSDCYNITDKTIQ 604
Cdd:smart00367   1 CPNLRELDLSGCTNITDEGLQ 21
C2A_Synaptotagmin-15-17 cd08390
C2A domain first repeat present in Synaptotagmins 15 and 17; Synaptotagmin is a ...
 231-274 2.22e-03

C2A domain first repeat present in Synaptotagmins 15 and 17; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. It is thought to be involved in the trafficking and exocytosis of secretory vesicles in non-neuronal tissues and is Ca2+ independent. Human synaptotagmin 15 has 2 alternatively spliced forms that encode proteins with different C-termini. The larger, SYT15a, contains a N-terminal TM region, a putative fatty-acylation site, and 2 tandem C terminal C2 domains. The smaller, SYT15b, lacks the C-terminal portion of the second C2 domain. Unlike most other synaptotagmins it is nearly absent in the brain and rather is found in the heart, lungs, skeletal muscle, and testis. Synaptotagmin 17 is located in the brain, kidney, and prostate and is thought to be a peripheral membrane protein. Previously all synaptotagmins were thought to be calcium sensors in the regulation of neurotransmitter release and hormone secretion, but it has been shown that not all of them bind calcium. Of the 17 identified synaptotagmins only 8 bind calcium (1-3, 5-7, 9, 10). The function of the two C2 domains that bind calcium are: regulating the fusion step of synaptic vesicle exocytosis (C2A) and binding to phosphatidyl-inositol-3,4,5-triphosphate (PIP3) in the absence of calcium ions and to phosphatidylinositol bisphosphate (PIP2) in their presence (C2B). C2B also regulates also the recycling step of synaptic vesicles. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-I topology.


Pssm-ID: 176036 [Multi-domain]  Cd Length: 123  Bit Score: 38.78  E-value: 2.22e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 442622939 231 TFKFILTILNLQRRTLRVLNFS------HTLIGQALLALCDLNLQLQRLY 274
Cdd:cd08390   68 TFVFQVSFKELQRRTLRLSVYDvdrfsrHCIIGHVLFPLKDLDLVKGGVV 117
PLN03210 PLN03210
Resistant to P. syringae 6; Provisional
 530-672 2.31e-03

Resistant to P. syringae 6; Provisional


Pssm-ID: 215633 [Multi-domain]  Cd Length: 1153  Bit Score: 41.40  E-value: 2.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622939  530 IQQLRGLRSLNLRGCN---KISDVSLKYGLKhielrRLMLSNCQqiSLLGMEAMASSCPSIEELDLSDCYNITDKTIQVv 606
Cdd:PLN03210  630 VHSLTGLRNIDLRGSKnlkEIPDLSMATNLE-----TLKLSDCS--SLVELPSSIQYLNKLEDLDMSRCENLEILPTGI- 701

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442622939  607 tsKLPRLKALHISGCSQLteHTLDAIITNCSclqTLSIYRcrsmyTDLEERLSgvktlrNLNMDNL 672
Cdd:PLN03210  702 --NLKSLYRLNLSGCSRL--KSFPDISTNIS---WLDLDE-----TAIEEFPS------NLRLENL 749
F-box_FBXO3 cd22084
F-box domain found in F-box only protein 3 (FBXO3) and similar proteins; FBXO3, also called ...
 12-43 6.23e-03

F-box domain found in F-box only protein 3 (FBXO3) and similar proteins; FBXO3, also called FBX3, is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. It mediates the ubiquitination of HIPK2 and probably that of EP300, leading to rapid degradation by the proteasome. It also promotes ubiquitylation and transcriptional activity of AIRE (autoimmune regulator). 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: 438856  Cd Length: 49  Bit Score: 35.31  E-value: 6.23e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 442622939  12 DDLPLEIVLKIFSYLGYSDLQAAGSTCQRWHA 43
Cdd:cd22084    2 DDLPSDPLLNILSFLDYRDLISCSQVCRRLNQ 33
F-box_FBXL8 cd22121
F-box domain found in F-box/LRR-repeat protein 8 (FBXL8) and similar proteins; FBXL8, also ...
 14-44 6.38e-03

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: 35.03  E-value: 6.38e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 442622939  14 LPLEIVLKIFSYLGYSDLQAAGSTCQRWHAA 44
Cdd:cd22121    3 LPEEILVHIFRHLSLRDRYAAAQVCKHWREA 33
F-box_FBXL21 cd22179
F-box domain found in F-box/LRR-repeat protein 21 (FBXL21) and similar proteins; FBXL21, also ...
 11-42 6.98e-03

F-box domain found in F-box/LRR-repeat protein 21 (FBXL21) and similar proteins; FBXL21, also called F-box and leucine-rich repeat protein 21, F-box and leucine-rich repeat protein 3B (FBXL3B), or F-box/LRR-repeat protein 3B, is the substrate-recognition component of the SCF(FBXL21) E3 ubiquitin ligase complex that mainly acts in the cytosol and mediates ubiquitination of CRY proteins (CRY1 and CRY2), leading to CRY protein stabilization, and thus, is involved in circadian rhythm function. It regulates the oscillation of the circadian clock through ubiquitination and stabilization of cryptochromes. 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: 438950  Cd Length: 43  Bit Score: 34.88  E-value: 6.98e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 442622939  11 YDDLPLEIVLKIFSYLGYSDLQAAGSTCQRWH 42
Cdd:cd22179    3 WGNLPHHVVLHIFQYLPLVDRARASSVCRRWN 34
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
106-407 7.58e-03

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 39.53  E-value: 7.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622939 106 SLALDNVDLNDKQFYGMLGVLPHLHSLSLKRCLPL--FMSGSFLDSYNNSCPDLNDLASNLAGIKELTLCENQyLTDaIL 183
Cdd:COG4886   75 LLLSLLLLSLLLLGLTDLGDLTNLTELDLSGNEELsnLTNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQ-LTD-LP 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622939 184 MRLTSfMPSLEAINMSGCHIAfhnaihrrfypatsssdhVLPSEsvltfkfiltILNLQRrtLRVLNFSHTLIGQALLAL 263
Cdd:COG4886  153 EPLGN-LTNLKSLDLSNNQLT------------------DLPEE----------LGNLTN--LKELDLSNNQITDLPEPL 201

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622939 264 CDLNlQLQRLYLAGCRqlnCTTILNFLATQPQLCALDLSATMCVNDENLAALvqtnPQLEHLKVNGClSITNAGaiHLAK 343
Cdd:COG4886  202 GNLT-NLEELDLSGNQ---LTDLPEPLANLTNLETLDLSNNQLTDLPELGNL----TNLEELDLSNN-QLTDLP--PLAN 270

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442622939 344 LKCLKSLDISNcdNLTSSGIIEGIASEENPVIQELNVSYLQICEECIKAIASNLRCLRSLHLNH 407
Cdd:COG4886  271 LTNLKTLDLSN--NQLTDLKLKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKG 332
PRK15386 PRK15386
type III secretion effector GogB;
299-504 9.88e-03

type III secretion effector GogB;


Pssm-ID: 237954 [Multi-domain]  Cd Length: 426  Bit Score: 39.08  E-value: 9.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622939 299 LDLSATMCVNDENLAALVQT--NPQLEHLKVNGCLSITNAGAIHLAKL-KCLKSLDISNCDNLTSsgiIEGIASEEnpvI 375
Cdd:PRK15386  23 LEPDGTFCSNSTETSAEIRSeiTPQIEEARASGRLYIKDCDIESLPVLpNELTEITIENCNNLTT---LPGSIPEG---L 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622939 376 QELNVSYlqiCEEcikaIASNLRCLRSLHLnhcvNGATDEAIQSVIGQlrwLRELSLEHCSGLTDAALTGIniskleMSR 455
Cdd:PRK15386  97 EKLTVCH---CPE----ISGLPESVRSLEI----KGSATDSIKNVPNG---LTSLSINSYNPENQARIDNL------ISP 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 442622939 456 KQSGSQVSSMDNFYPPysntlaerDSLAGSLQSIKISLRSKAEDEIVRD 504
Cdd:PRK15386 157 SLKTLSLTGCSNIILP--------EKLPESLQSITLHIEQKTTWNISFE 197
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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