NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2037976981|ref|XP_041456863|]
View 

EF-hand calcium-binding domain-containing protein 5-like isoform X7 [Lytechinus variegatus]

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
DD_EFCAB5 cd22968
dimerization/docking (D/D) domain found in EF-hand calcium-binding domain-containing protein 5 ...
 151-207 1.07e-27

dimerization/docking (D/D) domain found in EF-hand calcium-binding domain-containing protein 5 (EFCAB5) and similar proteins; EF-hand calcium-binding domain-containing protein 5 (EFCAB5) is an uncharacterized protein that contains an N-terminal domain that shows high sequence similarity to the dimerization/docking (D/D) domain of protein DPY-30/SDC1.


:

Pssm-ID: 438537  Cd Length: 60  Bit Score: 106.51  E-value: 1.07e-27
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976981  151 DARAYLLDKLLPTLILGIEKLLMEAERRDL---TEKNEANPNFNPLNYLAQYLMRNNPRY 207
Cdd:cd22968      1 ETRAYLVEKVLPTLVPGLEKLLKEVERRGLleeEGRPEPAPRFNPINWLAQYLMRNNPRY 60
LGT super family cl00478
Prolipoprotein diacylglyceryl transferase;
452-599 1.61e-08

Prolipoprotein diacylglyceryl transferase;


The actual alignment was detected with superfamily member PRK13108:

Pssm-ID: 469786 [Multi-domain]  Cd Length: 460  Bit Score: 58.84  E-value: 1.61e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976981  452 ESEPTAPSEGTVQEETT-GEVGAAPVVDGGEAPEegiKDEESEQAEKTAEPVKSEDPAAPVAETAEGTAETAEPQSKEQE 530
Cdd:PRK13108   292 VDEALEREPAELAAAAVaSAASAVGPVGPGEPNQ---PDDVAEAVKAEVAEVTDEVAAESVVQVADRDGESTPAVEETSE 368

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2037976981  531 PTSTDE--GATAAEVT-APEVTPGETMSGDAVPAEIAGGEKEKTEEGTRDQAAPgaeetQAGEDKLDELTSA 599
Cdd:PRK13108   369 ADIEREqpGDLAGQAPaAHQVDAEAASAAPEEPAALASEAHDETEPEVPEKAAP-----IPDPAKPDELAVA 435
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 724-751 9.88e-04

EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in pairs. Links between disease states and genes encoding EF-hands, particularly the S100 subclass, are emerging. Each motif consists of a 12 residue loop flanked on either side by a 12 residue alpha-helix. EF-hands undergo a conformational change unpon binding calcium ions.


:

Pssm-ID: 197492 [Multi-domain]  Cd Length: 29  Bit Score: 37.74  E-value: 9.88e-04
                            10        20
                    ....*....|....*....|....*...
gi 2037976981   724 VDQLFDKWDNDGSGYLDLEEFHSIMAKF 751
Cdd:smart00054    2 LKEAFRLFDKDGDGKIDFEEFKDLLKAL 29
FRQ1 super family cl34916
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
718-787 1.39e-03

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


The actual alignment was detected with superfamily member COG5126:

Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 40.55  E-value: 1.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976981  718 AKRRQMVDQLFDKWDNDGSGYLDLEEFHSIMAKFKDNMESRIMAKAKQKLEKEEL------------------------- 772
Cdd:COG5126      1 DLQRRKLDRRFDLLDADGDGVLERDDFEALFRRLWATLFSEADTDGDGRISREEFvagmeslfeatvepfaraafdlldt 80

                           90
                   ....*....|....*..
gi 2037976981  773 --DNRLSKPEFKAYIEA 787
Cdd:COG5126     81 dgDGKISADEFRRLLTA 97
 
Name Accession Description Interval E-value
DD_EFCAB5 cd22968
dimerization/docking (D/D) domain found in EF-hand calcium-binding domain-containing protein 5 ...
 151-207 1.07e-27

dimerization/docking (D/D) domain found in EF-hand calcium-binding domain-containing protein 5 (EFCAB5) and similar proteins; EF-hand calcium-binding domain-containing protein 5 (EFCAB5) is an uncharacterized protein that contains an N-terminal domain that shows high sequence similarity to the dimerization/docking (D/D) domain of protein DPY-30/SDC1.


Pssm-ID: 438537  Cd Length: 60  Bit Score: 106.51  E-value: 1.07e-27
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976981  151 DARAYLLDKLLPTLILGIEKLLMEAERRDL---TEKNEANPNFNPLNYLAQYLMRNNPRY 207
Cdd:cd22968      1 ETRAYLVEKVLPTLVPGLEKLLKEVERRGLleeEGRPEPAPRFNPINWLAQYLMRNNPRY 60
PRK13108 PRK13108
prolipoprotein diacylglyceryl transferase; Reviewed
 452-599 1.61e-08

prolipoprotein diacylglyceryl transferase; Reviewed


Pssm-ID: 237284 [Multi-domain]  Cd Length: 460  Bit Score: 58.84  E-value: 1.61e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976981  452 ESEPTAPSEGTVQEETT-GEVGAAPVVDGGEAPEegiKDEESEQAEKTAEPVKSEDPAAPVAETAEGTAETAEPQSKEQE 530
Cdd:PRK13108   292 VDEALEREPAELAAAAVaSAASAVGPVGPGEPNQ---PDDVAEAVKAEVAEVTDEVAAESVVQVADRDGESTPAVEETSE 368

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2037976981  531 PTSTDE--GATAAEVT-APEVTPGETMSGDAVPAEIAGGEKEKTEEGTRDQAAPgaeetQAGEDKLDELTSA 599
Cdd:PRK13108   369 ADIEREqpGDLAGQAPaAHQVDAEAASAAPEEPAALASEAHDETEPEVPEKAAP-----IPDPAKPDELAVA 435
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
 452-611 2.75e-05

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 48.84  E-value: 2.75e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976981  452 ESEPTAPSEGTVQEETTGEVGAAPVVDGGEAPEEGIKDEESEQAEKTAE--PVKSEDPAAPVAETAEGTAETAEPQSKEQ 529
Cdd:TIGR00927  680 ESEGEIPAERKGEQEGEGEIEAKEADHKGETEAEEVEHEGETEAEGTEDegEIETGEEGEEVEDEGEGEAEGKHEVETEG 759

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976981  530 EPTSTD-EGATAAEVTAPEvTPGETMSGDAVP------AEIAGGEKEKTEEGTRDQAAPGAEETQAGEDKLDELTSAKDR 602
Cdd:TIGR00927  760 DRKETEhEGETEAEGKEDE-DEGEIQAGEDGEmkgdegAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQELN 838


                   ....*....
gi 2037976981  603 ATLQPTTAN 611
Cdd:TIGR00927  839 AENQGEAKQ 847
Agg_substance NF033875
LPXTG-anchored aggregation substance; Aggregation substances, as described in Enterococcus, ...
 456-595 5.22e-05

LPXTG-anchored aggregation substance; Aggregation substances, as described in Enterococcus, are LPXTG-anchored large surface proteins that contribute to virulence. Several closely related paralogs may be found in a single strain.


Pssm-ID: 411439 [Multi-domain]  Cd Length: 1306  Bit Score: 47.78  E-value: 5.22e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976981  456 TAPSEGTVQEETTGevgaaPVVdGGEAPEEGIKDEESEQAEKTAEPVKSEDpAAPVAETAEGTAETAEPQSKEQEPTStd 535
Cdd:NF033875    48 TQPGTTTVQPDNPD-----PQS-GSETPKTAVSEEATVQKDTTSQPTKVEE-VASEKNGAEQSSATPNDTTNAQQPTV-- 118

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976981  536 eGATAAEVTAPEVTPGETMSGDAVPAEIAGGEKekteEGTRDQAAPGAEETQAGEDKLDE 595
Cdd:NF033875   119 -GAEKSAQEQPVVSPETTNEPLGQPTEVAPAEN----EANKSTSIPKEFETPDVDKAVDE 173
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 724-751 9.88e-04

EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in pairs. Links between disease states and genes encoding EF-hands, particularly the S100 subclass, are emerging. Each motif consists of a 12 residue loop flanked on either side by a 12 residue alpha-helix. EF-hands undergo a conformational change unpon binding calcium ions.


Pssm-ID: 197492 [Multi-domain]  Cd Length: 29  Bit Score: 37.74  E-value: 9.88e-04
                            10        20
                    ....*....|....*....|....*...
gi 2037976981   724 VDQLFDKWDNDGSGYLDLEEFHSIMAKF 751
Cdd:smart00054    2 LKEAFRLFDKDGDGKIDFEEFKDLLKAL 29
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
 724-751 1.21e-03

EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering/transport proteins. The first group is the largest and includes the most well-known members of the family such as calmodulin, troponin C and S100B. These proteins typically undergo a calcium-dependent conformational change which opens a target binding site. The latter group is represented by calbindin D9k and do not undergo calcium dependent conformational changes.


Pssm-ID: 425435 [Multi-domain]  Cd Length: 29  Bit Score: 37.38  E-value: 1.21e-03
                           10        20
                   ....*....|....*....|....*...
gi 2037976981  724 VDQLFDKWDNDGSGYLDLEEFHSIMAKF 751
Cdd:pfam00036    2 LKEIFRLFDKDGDGKIDFEEFKELLKKL 29
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
718-787 1.39e-03

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 40.55  E-value: 1.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976981  718 AKRRQMVDQLFDKWDNDGSGYLDLEEFHSIMAKFKDNMESRIMAKAKQKLEKEEL------------------------- 772
Cdd:COG5126      1 DLQRRKLDRRFDLLDADGDGVLERDDFEALFRRLWATLFSEADTDGDGRISREEFvagmeslfeatvepfaraafdlldt 80

                           90
                   ....*....|....*..
gi 2037976981  773 --DNRLSKPEFKAYIEA 787
Cdd:COG5126     81 dgDGKISADEFRRLLTA 97
EFh_PRIP cd16206
EF-hand motif found in phospholipase C-related but catalytically inactive proteins (PRIP); ...
 726-791 2.17e-03

EF-hand motif found in phospholipase C-related but catalytically inactive proteins (PRIP); This family represents a class of metazoan phospholipase C related, but catalytically inactive proteins (PRIP), which belong to a group of novel inositol 1,4,5-trisphosphate (InsP3) binding protein. PRIP has a primary structure and domain architecture, incorporating a pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core domain with highly conserved X- and Y-regions split by a linker sequence, and a C-terminal C2 domain, similar to phosphoinositide-specific phospholipases C (PI-PLC, EC 3.1.4.11)-delta isoforms. Due to replacement of critical catalytic residues, PRIP do not have PLC enzymatic activity. PRIP consists of two subfamilies, PRIP-1(also known as p130 or PLC-L1), which is predominantly expressed in the brain, and PRIP-2 (also known as PLC-L2), which exhibits a relatively ubiquitous expression. Experiments show both, PRIP-1 and PRIP-2, are involved in InsP3-mediated calcium signaling pathway and GABA(A)receptor-mediated signaling pathway. In addition, PRIP-2 acts as a negative regulator of B-cell receptor signaling and immune responses.


Pssm-ID: 320036 [Multi-domain]  Cd Length: 143  Bit Score: 39.89  E-value: 2.17e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2037976981  726 QLFDKWDNDGSGYLDLEEFHSIMAKFKDNM-ESRIMAKAKQKLEKEE-LDNRLSKPEFkayIEAVCSL 791
Cdd:cd16206      4 SVFEEADTNKSGFLDEEEAVQLIKQLNPGLsTSRIKQKLKELQKKKDgARGRVSSDEF---VELFKEL 68
Dpy-30 pfam05186
Dpy-30 motif; This motif is found in a wide variety of domain contexts. It is found in the ...
 152-205 3.35e-03

Dpy-30 motif; This motif is found in a wide variety of domain contexts. It is found in the Dpy-30 proteins hence the motifs name. It is about 40 residues long and is probably formed of two alpha-helices. It may be a dimerization motif analogous to pfam02197 (Bateman A pers obs).


Pssm-ID: 428357  Cd Length: 42  Bit Score: 36.43  E-value: 3.35e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2037976981  152 ARAYLLDKLLPTLILGiekllmeaerrdLTEKNEANPNfNPLNYLAQYLMRNNP 205
Cdd:pfam05186    2 ARQYLNKTVAPILLQG------------LTELAKERPE-DPIEYLADYLLKNNP 42
 
Name Accession Description Interval E-value
DD_EFCAB5 cd22968
dimerization/docking (D/D) domain found in EF-hand calcium-binding domain-containing protein 5 ...
 151-207 1.07e-27

dimerization/docking (D/D) domain found in EF-hand calcium-binding domain-containing protein 5 (EFCAB5) and similar proteins; EF-hand calcium-binding domain-containing protein 5 (EFCAB5) is an uncharacterized protein that contains an N-terminal domain that shows high sequence similarity to the dimerization/docking (D/D) domain of protein DPY-30/SDC1.


Pssm-ID: 438537  Cd Length: 60  Bit Score: 106.51  E-value: 1.07e-27
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976981  151 DARAYLLDKLLPTLILGIEKLLMEAERRDL---TEKNEANPNFNPLNYLAQYLMRNNPRY 207
Cdd:cd22968      1 ETRAYLVEKVLPTLVPGLEKLLKEVERRGLleeEGRPEPAPRFNPINWLAQYLMRNNPRY 60
PRK13108 PRK13108
prolipoprotein diacylglyceryl transferase; Reviewed
 452-599 1.61e-08

prolipoprotein diacylglyceryl transferase; Reviewed


Pssm-ID: 237284 [Multi-domain]  Cd Length: 460  Bit Score: 58.84  E-value: 1.61e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976981  452 ESEPTAPSEGTVQEETT-GEVGAAPVVDGGEAPEegiKDEESEQAEKTAEPVKSEDPAAPVAETAEGTAETAEPQSKEQE 530
Cdd:PRK13108   292 VDEALEREPAELAAAAVaSAASAVGPVGPGEPNQ---PDDVAEAVKAEVAEVTDEVAAESVVQVADRDGESTPAVEETSE 368

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2037976981  531 PTSTDE--GATAAEVT-APEVTPGETMSGDAVPAEIAGGEKEKTEEGTRDQAAPgaeetQAGEDKLDELTSA 599
Cdd:PRK13108   369 ADIEREqpGDLAGQAPaAHQVDAEAASAAPEEPAALASEAHDETEPEVPEKAAP-----IPDPAKPDELAVA 435
PHA03169 PHA03169
hypothetical protein; Provisional
 427-609 5.61e-07

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 53.44  E-value: 5.61e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976981  427 LTETDDTESLISEGSSISSVKSSMKESE--PTAPSEGTVQEETTGEVGAAPV-VDGGEAPEEGIKDEESEQAEKTA-EPV 502
Cdd:PHA03169    62 AEQGHRQTESDTETAEESRHGEKEERGQggPSGSGSESVGSPTPSPSGSAEElASGLSPENTSGSSPESPASHSPPpSPP 141

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976981  503 KSEDPAAPVAETAEGTAETAEPQSK-----EQEPTSTDEGATAAEVTAPEvtPGETMSGDAVPAEIAGGEKEKTEEGTRD 577
Cdd:PHA03169   142 SHPGPHEPAPPESHNPSPNQQPSSFlqpshEDSPEEPEPPTSEPEPDSPG--PPQSETPTSSPPPQSPPDEPGEPQSPTP 219

                          170       180       190
                   ....*....|....*....|....*....|..
gi 2037976981  578 QAAPGAEETQAGEDKlDELTSAKDRATLQPTT 609
Cdd:PHA03169   220 QQAPSPNTQQAVEHE-DEPTEPEREGPPFPGH 250
DD_DPY30_SDC1-like cd22958
dimerization/docking (D/D) domain found in the DPY30/SDC1-like family; The DPY30/SDC1-like ...
 152-204 1.52e-06

dimerization/docking (D/D) domain found in the DPY30/SDC1-like family; The DPY30/SDC1-like family includes DPY30 from animals and its homolog SDC1 from yeast, DPY30 domain-containing protein (DYDC), adenylate kinase 7 (AK7), IQ domain-containing protein K (IQCK), nucleoside diphosphate kinase homolog 5 (NDKH5), EF-hand calcium-binding domain-containing protein 5 (EFCAB5), and Chlamydomonas reinhardtii flagellar radial spoke proteins, RSP2 and RSP23. DPY30, also called dumpy-30, was initially discovered in Caenorhabditis elegans as a key player in X chromosome dosage compensation. Human DPY30 plays a dual function in moderately allosterically regulating the methyltransferase activity of SET1/COMPASS (COMplex of Proteins ASsociated with Set1) enzymes and contributing to the recruitment of the complex to chromatin. Yeast SDC1, also called complex proteins associated with SET1 protein SDC1, Set1C component SDC1, or suppressor of CDC25 protein 1, is the smallest subunit of COMPASS (COMplex of Proteins ASsociated with Set1) and interacts exclusively with Bre2 at the distal end of the catalytic module. It positively regulates the COMPASS catalytic module by stabilizing the non-canonical Bre2 SPRY domain. DYDC1 plays a crucial role during acrosome biogenesis. AK7 (EC2.7.4.3/EC 2.7.4.6), also called ATP-AMP transphosphorylase 7, is a nucleoside monophosphate (NMP) kinase that catalyzes the reversible transfer of the terminal phosphate group between nucleoside triphosphates and monophosphates. It is involved in maintaining ciliary structure and function. IQ motif-containing proteins may play an active role in cell polarization and migration, and even in ciliary function. The function of IQCK remains unclear. NDKH5, also called NME5, NDP kinase homolog 5, inhibitor of p53-induced apoptosis-beta (IPIA-beta), testis-specific nm23 homolog, or nm23-H5, is specifically expressed in testis germinal cells. It may not have NDK kinase activity. It confers protection from cell death by Bax and alters the cellular levels of several antioxidant enzymes including Gpx5. It may play a role in spermiogenesis by increasing the ability of late-stage spermatids to eliminate reactive oxygen species. RSP2 is a calmodulin binding spoke stalk protein required for motility in Chlamydomonas reinhardtii. It binds calmodulin in a calcium-dependent manner. RSP23, also called p61, is a functional Ca2+/calmodulin-regulated nucleoside diphosphate kinase (NDK) from the flagella of Chlamydomonas that is present in the radial spoke stalk. It binds calmodulin in a calcium-dependent manner. Members of this family contain a DPY30/SDC1 helical bundle domain that is formed by two alpha-helices. The DPY30/SDC1 helical bundle domain is also called D/D domain and might be analogous to the D/D domain found in the regulatory subunit of cAMP-dependent protein kinase (PKA).


Pssm-ID: 438527  Cd Length: 40  Bit Score: 45.90  E-value: 1.52e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2037976981  152 ARAYLLDKLLPTLILGIEKLLMeaerrdltekneANPNfNPLNYLAQYLMRNN 204
Cdd:cd22958      1 AREYLSETVLPTLIPALAELLK------------ARPE-DPLEWLAEYLLRNN 40
rne PRK10811
ribonuclease E; Reviewed
 462-610 1.16e-05

ribonuclease E; Reviewed


Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 50.04  E-value: 1.16e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976981  462 TVQEETTGEVGAAPVVdggeapeegikdeESEQAEKTAEPVKSEDPAAPVAETAEGTAETAEPQSKEQEPTSTDEGATAA 541
Cdd:PRK10811   855 VEEQREAEEVQVQPVV-------------AEVPVAAAVEPVVSAPVVEAVAEVVEEPVVVAEPQPEEVVVVETTHPEVIA 921

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2037976981  542 E--VTAPEVTPGETMSGDAVPAEIAGGEKEKTEEGTRDQAAPGAEETQAGEDKLDELTSAKDRATLQPTTA 610
Cdd:PRK10811   922 ApvTEQPQVITESDVAVAQEVAEHAEPVVEPQDETADIEEAAETAEVVVAEPEVVAQPAAPVVAEVAAEVE 992
DD_IQCK cd22969
dimerization/docking (D/D) domain found in IQ domain-containing protein K (IQCK) and similar ...
 152-205 1.32e-05

dimerization/docking (D/D) domain found in IQ domain-containing protein K (IQCK) and similar proteins; IQ motif-containing proteins may play an active role in cell polarization and migration, and even in ciliary function. Although its function remains unclear, IQCK contains a conserved region that shows high sequence similarity to the dimerization/docking (D/D) domains of regulatory subunit of cAMP-dependent protein kinase (PKA) and protein DPY-30/SDC1.


Pssm-ID: 438538  Cd Length: 58  Bit Score: 44.03  E-value: 1.32e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2037976981  152 ARAYLLDKLLPTLILGIEKLLMEAERRD-LTEKNEAnpnFNPLNYLAQYLMRNNP 205
Cdd:cd22969      7 PVEYLEEYIFPVLLPALEEMLEEAKKEDcFERKRTK---FNGLDFLTEYLYNNNP 58
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
 452-611 2.75e-05

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 48.84  E-value: 2.75e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976981  452 ESEPTAPSEGTVQEETTGEVGAAPVVDGGEAPEEGIKDEESEQAEKTAE--PVKSEDPAAPVAETAEGTAETAEPQSKEQ 529
Cdd:TIGR00927  680 ESEGEIPAERKGEQEGEGEIEAKEADHKGETEAEEVEHEGETEAEGTEDegEIETGEEGEEVEDEGEGEAEGKHEVETEG 759

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976981  530 EPTSTD-EGATAAEVTAPEvTPGETMSGDAVP------AEIAGGEKEKTEEGTRDQAAPGAEETQAGEDKLDELTSAKDR 602
Cdd:TIGR00927  760 DRKETEhEGETEAEGKEDE-DEGEIQAGEDGEmkgdegAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQELN 838


                   ....*....
gi 2037976981  603 ATLQPTTAN 611
Cdd:TIGR00927  839 AENQGEAKQ 847
rne PRK10811
ribonuclease E; Reviewed
 454-550 3.56e-05

ribonuclease E; Reviewed


Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 48.50  E-value: 3.56e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976981  454 EPTAPSEGTVQEETTGEVGAAPVVdggeAPEEGIKDEESEQAEKTAEPVKSEDPAAPVAETAEGTAETAEPQSKEQEPTS 533
Cdd:PRK10811   902 AEPQPEEVVVVETTHPEVIAAPVT----EQPQVITESDVAVAQEVAEHAEPVVEPQDETADIEEAAETAEVVVAEPEVVA 977

                           90
                   ....*....|....*..
gi 2037976981  534 TDEGATAAEVTAPEVTP 550
Cdd:PRK10811   978 QPAAPVVAEVAAEVETV 994
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 463-663 4.50e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 48.06  E-value: 4.50e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976981  463 VQEETTGEVGAAPVVDGGEAPEEGIKDEESEQ---AEKTAEPVKSEDPAAPVAETAEGTAETAEPQSKEQEPTSTDEGAT 539
Cdd:PRK07764   574 LAEELGGDWQVEAVVGPAPGAAGGEGPPAPASsgpPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHH 653

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976981  540 AAEVTAPEVTPGetmsGDAVPAEIAGGEKEKTEEGTRDQA-APGAEETQAGEDKLDELTSAKDRATLQPTT-ANTLTGRS 617
Cdd:PRK07764   654 PKHVAVPDASDG----GDGWPAKAGGAAPAAPPPAPAPAApAAPAGAAPAQPAPAPAATPPAGQADDPAAQpPQAAQGAS 729

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 2037976981  618 TSVSFHEDAIKLKEEKADSEDRPKTPVKTPTVRSGSRSGSAFDESA 663
Cdd:PRK07764   730 APSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPP 775
Agg_substance NF033875
LPXTG-anchored aggregation substance; Aggregation substances, as described in Enterococcus, ...
 456-595 5.22e-05

LPXTG-anchored aggregation substance; Aggregation substances, as described in Enterococcus, are LPXTG-anchored large surface proteins that contribute to virulence. Several closely related paralogs may be found in a single strain.


Pssm-ID: 411439 [Multi-domain]  Cd Length: 1306  Bit Score: 47.78  E-value: 5.22e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976981  456 TAPSEGTVQEETTGevgaaPVVdGGEAPEEGIKDEESEQAEKTAEPVKSEDpAAPVAETAEGTAETAEPQSKEQEPTStd 535
Cdd:NF033875    48 TQPGTTTVQPDNPD-----PQS-GSETPKTAVSEEATVQKDTTSQPTKVEE-VASEKNGAEQSSATPNDTTNAQQPTV-- 118

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976981  536 eGATAAEVTAPEVTPGETMSGDAVPAEIAGGEKekteEGTRDQAAPGAEETQAGEDKLDE 595
Cdd:NF033875   119 -GAEKSAQEQPVVSPETTNEPLGQPTEVAPAEN----EANKSTSIPKEFETPDVDKAVDE 173
PRK13108 PRK13108
prolipoprotein diacylglyceryl transferase; Reviewed
 482-660 1.70e-04

prolipoprotein diacylglyceryl transferase; Reviewed


Pssm-ID: 237284 [Multi-domain]  Cd Length: 460  Bit Score: 45.74  E-value: 1.70e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976981  482 APEeGIKDEESEQAEKTAEPVKSEDPAAPVAETAEGTAETAEPQSKEQEPTSTDEGATAAEVTAPEVTPGETMSGDAVPA 561
Cdd:PRK13108   275 APK-GREAPGALRGSEYVVDEALEREPAELAAAAVASAASAVGPVGPGEPNQPDDVAEAVKAEVAEVTDEVAAESVVQVA 353

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976981  562 EIAG---GEKEKTEEGTRDQAAPGAEETQA-GEDKLDELTSAKdratlQPTTANTLTGRSTSVSFHEDAIKlKEEKADSe 637
Cdd:PRK13108   354 DRDGestPAVEETSEADIEREQPGDLAGQApAAHQVDAEAASA-----APEEPAALASEAHDETEPEVPEK-AAPIPDP- 426

                          170       180
                   ....*....|....*....|....*...
gi 2037976981  638 DRPKTPV-----KTPTVRSGSRSGSAFD 660
Cdd:PRK13108   427 AKPDELAvagpgDDPAEPDGIRRQDDFS 454
PHA03169 PHA03169
hypothetical protein; Provisional
 452-574 2.34e-04

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 45.35  E-value: 2.34e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976981  452 ESEPTAPSEGTVQEETTGEVGAAPVVDGGEAPEEGIKDEESEQAEKTAEPVKSEDPAAPVAETAEGTAETAEPQSKEQEP 531
Cdd:PHA03169   138 PSPPSHPGPHEPAPPESHNPSPNQQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDEPGEPQSP 217

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2037976981  532 T--------STDEGATAAEVTAPEvTPGETMSGDAVPAEIAGGEKEKTEEG 574
Cdd:PHA03169   218 TpqqapspnTQQAVEHEDEPTEPE-REGPPFPGHRSHSYTVVGWKPSTRPG 267
motB PRK05996
MotB family protein;
474-597 4.47e-04

MotB family protein;


Pssm-ID: 235665 [Multi-domain]  Cd Length: 423  Bit Score: 44.30  E-value: 4.47e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976981  474 APVVDGGEAPEEGIKDEESEQAEK-TAEPVKSEDPAAPVAETAEGTAETAEPQSKEQEPTSTDEGATAAEVTAPEVTPge 552
Cdd:PRK05996   190 VEVTTAGDLLPPGQAREQAQGAKSaTAAPATVPQAAPLPQAQPKKAATEEELIADAKKAATGEPAANAAKAAKPEPMP-- 267

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 2037976981  553 tmSGDAVPAEIAGGEKEKTEEGTRDQAAPGAEETQAGEDKLDELT 597
Cdd:PRK05996   268 --DDQQKEAEQLQAAIAQAIGGVAGKLAEGVTVTPVEGGLLISLT 310
rne PRK10811
ribonuclease E; Reviewed
 452-593 8.28e-04

ribonuclease E; Reviewed


Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 43.87  E-value: 8.28e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976981  452 ESEPTAPSEGTVQEETTGEVGAAPVVDGGEAP--EEGIKDEESEQAEKTAEPVkSEDPAAPVAETAEGTAETAEPQSKEQ 529
Cdd:PRK10811   872 EVPVAAAVEPVVSAPVVEAVAEVVEEPVVVAEpqPEEVVVVETTHPEVIAAPV-TEQPQVITESDVAVAQEVAEHAEPVV 950

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2037976981  530 EPTSTDEGATAAEVTAPEVTPGETMSGDAVPAEIAGGEKEKTEEGTRDQAAPGAEETQAGEDKL 593
Cdd:PRK10811   951 EPQDETADIEEAAETAEVVVAEPEVVAQPAAPVVAEVAAEVETVTAVEPEVAPAQVPEATVEHN 1014
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
 452-594 8.61e-04

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 43.83  E-value: 8.61e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976981  452 ESEPTAPSEGTVQEETT---GEVGAAPVVDGGEAPEEGIKDEESEQAEKTAEPVKSEDP--------------------A 508
Cdd:TIGR00927  688 ERKGEQEGEGEIEAKEAdhkGETEAEEVEHEGETEAEGTEDEGEIETGEEGEEVEDEGEgeaegkhevetegdrketehE 767

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976981  509 APVAETAEGTAETAEPQSKEQEPTSTDEGATAAEVTAPEVTPGETMSGDAVPAEIAGGEKEKTEEGTRDQAAPGAEETQA 588
Cdd:TIGR00927  768 GETEAEGKEDEDEGEIQAGEDGEMKGDEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQELNAENQGEAKQ 847


                   ....*.
gi 2037976981  589 GEDKLD 594
Cdd:TIGR00927  848 DEKGVD 853
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 724-751 9.88e-04

EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in pairs. Links between disease states and genes encoding EF-hands, particularly the S100 subclass, are emerging. Each motif consists of a 12 residue loop flanked on either side by a 12 residue alpha-helix. EF-hands undergo a conformational change unpon binding calcium ions.


Pssm-ID: 197492 [Multi-domain]  Cd Length: 29  Bit Score: 37.74  E-value: 9.88e-04
                            10        20
                    ....*....|....*....|....*...
gi 2037976981   724 VDQLFDKWDNDGSGYLDLEEFHSIMAKF 751
Cdd:smart00054    2 LKEAFRLFDKDGDGKIDFEEFKDLLKAL 29
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
 724-751 1.21e-03

EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering/transport proteins. The first group is the largest and includes the most well-known members of the family such as calmodulin, troponin C and S100B. These proteins typically undergo a calcium-dependent conformational change which opens a target binding site. The latter group is represented by calbindin D9k and do not undergo calcium dependent conformational changes.


Pssm-ID: 425435 [Multi-domain]  Cd Length: 29  Bit Score: 37.38  E-value: 1.21e-03
                           10        20
                   ....*....|....*....|....*...
gi 2037976981  724 VDQLFDKWDNDGSGYLDLEEFHSIMAKF 751
Cdd:pfam00036    2 LKEIFRLFDKDGDGKIDFEEFKELLKKL 29
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
718-787 1.39e-03

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 40.55  E-value: 1.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976981  718 AKRRQMVDQLFDKWDNDGSGYLDLEEFHSIMAKFKDNMESRIMAKAKQKLEKEEL------------------------- 772
Cdd:COG5126      1 DLQRRKLDRRFDLLDADGDGVLERDDFEALFRRLWATLFSEADTDGDGRISREEFvagmeslfeatvepfaraafdlldt 80

                           90
                   ....*....|....*..
gi 2037976981  773 --DNRLSKPEFKAYIEA 787
Cdd:COG5126     81 dgDGKISADEFRRLLTA 97
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
689-786 2.00e-03

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 39.78  E-value: 2.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976981  689 LVKFITDGYVETEQEKFLRLQQARREAqsaKRRQMVDQLFDKWDNDGSGYLDLEEFHSIMAKFKDNMESriMAKAKQKLE 768
Cdd:COG5126     39 FSEADTDGDGRISREEFVAGMESLFEA---TVEPFARAAFDLLDTDGDGKISADEFRRLLTALGVSEEE--ADELFARLD 113

                           90
                   ....*....|....*...
gi 2037976981  769 KEElDNRLSKPEFKAYIE 786
Cdd:COG5126    114 TDG-DGKISFEEFVAAVR 130
EFh_PRIP cd16206
EF-hand motif found in phospholipase C-related but catalytically inactive proteins (PRIP); ...
 726-791 2.17e-03

EF-hand motif found in phospholipase C-related but catalytically inactive proteins (PRIP); This family represents a class of metazoan phospholipase C related, but catalytically inactive proteins (PRIP), which belong to a group of novel inositol 1,4,5-trisphosphate (InsP3) binding protein. PRIP has a primary structure and domain architecture, incorporating a pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core domain with highly conserved X- and Y-regions split by a linker sequence, and a C-terminal C2 domain, similar to phosphoinositide-specific phospholipases C (PI-PLC, EC 3.1.4.11)-delta isoforms. Due to replacement of critical catalytic residues, PRIP do not have PLC enzymatic activity. PRIP consists of two subfamilies, PRIP-1(also known as p130 or PLC-L1), which is predominantly expressed in the brain, and PRIP-2 (also known as PLC-L2), which exhibits a relatively ubiquitous expression. Experiments show both, PRIP-1 and PRIP-2, are involved in InsP3-mediated calcium signaling pathway and GABA(A)receptor-mediated signaling pathway. In addition, PRIP-2 acts as a negative regulator of B-cell receptor signaling and immune responses.


Pssm-ID: 320036 [Multi-domain]  Cd Length: 143  Bit Score: 39.89  E-value: 2.17e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2037976981  726 QLFDKWDNDGSGYLDLEEFHSIMAKFKDNM-ESRIMAKAKQKLEKEE-LDNRLSKPEFkayIEAVCSL 791
Cdd:cd16206      4 SVFEEADTNKSGFLDEEEAVQLIKQLNPGLsTSRIKQKLKELQKKKDgARGRVSSDEF---VELFKEL 68
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 695-749 2.61e-03

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 37.53  E-value: 2.61e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2037976981  695 DGYVeTEQEkflrLQQARREAQSAKRRQMVDQLFDKWDNDGSGYLDLEEFHSIMA 749
Cdd:cd00051     14 DGTI-SADE----LKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
 425-595 3.27e-03

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 41.90  E-value: 3.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976981  425 IELTETDDTESLISEGSSISSVKSSMKESEPTAPSEGTVQEETTGEVGAAPVVDGGEAPEEGIKDEESEQAEKTAEpVKS 504
Cdd:TIGR00927  715 VEHEGETEAEGTEDEGEIETGEEGEEVEDEGEGEAEGKHEVETEGDRKETEHEGETEAEGKEDEDEGEIQAGEDGE-MKG 793

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976981  505 EDPAAPVAETAEGTAETAEPQSKEQEPTSTDEgataaevtapEVTPGETMSGDAVpAEIAGGEKEKtEEGTRDQAAPGAE 584
Cdd:TIGR00927  794 DEGAEGKVEHEGETEAGEKDEHEGQSETQADD----------TEVKDETGEQELN-AENQGEAKQD-EKGVDGGGGSDGG 861

                          170
                   ....*....|.
gi 2037976981  585 ETQAGEDKLDE 595
Cdd:TIGR00927  862 DSEEEEEEEEE 872
Dpy-30 pfam05186
Dpy-30 motif; This motif is found in a wide variety of domain contexts. It is found in the ...
 152-205 3.35e-03

Dpy-30 motif; This motif is found in a wide variety of domain contexts. It is found in the Dpy-30 proteins hence the motifs name. It is about 40 residues long and is probably formed of two alpha-helices. It may be a dimerization motif analogous to pfam02197 (Bateman A pers obs).


Pssm-ID: 428357  Cd Length: 42  Bit Score: 36.43  E-value: 3.35e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2037976981  152 ARAYLLDKLLPTLILGiekllmeaerrdLTEKNEANPNfNPLNYLAQYLMRNNP 205
Cdd:pfam05186    2 ARQYLNKTVAPILLQG------------LTELAKERPE-DPIEYLADYLLKNNP 42
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 723-785 4.23e-03

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 36.76  E-value: 4.23e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2037976981  723 MVDQLFDKWDNDGSGYLDLEEFHSIMAKFKDNMESRIMAKAKQKLEKEElDNRLSKPEFKAYI 785
Cdd:cd00051      1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDG-DGKIDFEEFLELM 62
DD_AK7 cd22967
dimerization/docking (D/D) domain found in adenylate kinase 7 and similar proteins; Adenylate ...
 153-204 5.89e-03

dimerization/docking (D/D) domain found in adenylate kinase 7 and similar proteins; Adenylate kinase (AK7, EC2.7.4.3/EC 2.7.4.6), also called ATP-AMP transphosphorylase 7, is a nucleoside monophosphate (NMP) kinase that catalyzes the reversible transfer of the terminal phosphate group between nucleoside triphosphates and monophosphates. It has highest activity toward AMP, and weaker activity toward dAMP, CMP and dCMP. It also displays broad nucleoside diphosphate kinase activity. AK7 is involved in maintaining ciliary structure and function. This model corresponds to the C-terminal domain of AK7, which shows high sequence similarity to the dimerization/docking (D/D) domain of protein DPY-30/SDC1.


Pssm-ID: 438536 [Multi-domain]  Cd Length: 41  Bit Score: 35.93  E-value: 5.89e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2037976981  153 RAYLLDKLLPTLILGiekllmeaerrdLTEKNEANPNfNPLNYLAQYLMRNN 204
Cdd:cd22967      3 RNYLMKYVMPTLTEG------------LVEVCKVRPE-DPVDFLAEYLFKHN 41
DD_DPY30_SDC1 cd22965
dimerization/docking (D/D) domain found in the DPY30/SDC1 family; This family includes DPY30 ...
 152-205 6.15e-03

dimerization/docking (D/D) domain found in the DPY30/SDC1 family; This family includes DPY30 from animals and its homologs, including SDC1 from yeast. DPY30, also called dumpy-30, was initially discovered in Caenorhabditis elegans as a key player in X chromosome dosage compensation. Human DPY30 plays a dual function in moderately allosterically regulating the methyltransferase activity of SET1/COMPASS (COMplex of Proteins ASsociated with Set1) enzymes and contributing to the recruitment of the complex to chromatin. DPY30 is the core component of several methyltransferase-containing complexes including MLL1/MLL, MLL2/3 (also named ASCOM complex) and MLL4/WBP7. As part of the MLL1/MLL complex, DPY30 is involved in the methylation of histone H3 at 'Lys-4', particularly trimethylation. Histone H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. In a teratocarcinoma cell, DPY30 plays a crucial role in retinoic acid-induced differentiation along the neural lineage, regulating gene induction and H3 'Lys-4' methylation at key developmental loci. It may also play an indirect or direct role in endosomal transport. Yeast SDC1, also called complex proteins associated with SET1 (COMPASS) protein SDC1, Set1C component SDC1, or suppressor of CDC25 protein 1, is the smallest subunit of COMPASS and interacts exclusively with Bre2 at the distal end of the catalytic module. It positively regulates the COMPASS catalytic module by stabilizing the non-canonical Bre2 SPRY domain. The COMPASS (Set1C) complex specifically mono-, di- and trimethylates histone H3 to form H3K4me1/2/3, which subsequently activates gene expression by regulating transcription elongation and plays a role in telomere length maintenance. This model corresponds to the C-terminal helical bundle domain of DPY30/SDC1, which is called dimerization/docking (D/D) domain. It forms a homodimer, which directly interacts with the Ash2L (Bre2 in yeast) subunit of COMPASS through its DPY30-binding motif (DBM).


Pssm-ID: 438534  Cd Length: 41  Bit Score: 35.86  E-value: 6.15e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2037976981  152 ARAYLLDKLLPTLILGIEKLLMEaerRdltekneanPNfNPLNYLAQYLMRNNP 205
Cdd:cd22965      1 TRQYLDKTVVPVLLEGLKELAKE---R---------PE-DPLEFLAEYLLKNSP 41
EF-hand_6 pfam13405
EF-hand domain;
726-751 7.78e-03

EF-hand domain;


Pssm-ID: 463869 [Multi-domain]  Cd Length: 30  Bit Score: 35.23  E-value: 7.78e-03
                           10        20
                   ....*....|....*....|....*.
gi 2037976981  726 QLFDKWDNDGSGYLDLEEFHSIMAKF 751
Cdd:pfam13405    4 EAFKLFDKDGDGKISLEELRKALRSL 29
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
695-751 9.29e-03

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 37.85  E-value: 9.29e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2037976981  695 DGYVeTEQEkFLRLQQARREAQSAkrrqmVDQLFDKWDNDGSGYLDLEEFHSIMAKF 751
Cdd:COG5126     83 DGKI-SADE-FRRLLTALGVSEEE-----ADELFARLDTDGDGKISFEEFVAAVRDY 132
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
 453-595 9.83e-03

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 40.36  E-value: 9.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976981  453 SEPTAPSEGTVQEETTGEVGAAPVVD--GGEAPEEGikdeesEQAEKTAEPVKSEDPAAPVAETA---EGTAETAEPQSK 527
Cdd:TIGR00927  636 AEAEHTGERTGEEGERPTEAEGENGEesGGEAEQEG------ETETKGENESEGEIPAERKGEQEgegEIEAKEADHKGE 709

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2037976981  528 EQEPTSTDEGATAAEVTAPEvtpGET-------MSGDAVPAEIAGGEKEKTeEGTRDQAAPGAEETQAGEDKLDE 595
Cdd:TIGR00927  710 TEAEEVEHEGETEAEGTEDE---GEIetgeegeEVEDEGEGEAEGKHEVET-EGDRKETEHEGETEAEGKEDEDE 780
 
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