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Conserved domains on  [gi|2037976975|ref|XP_041456860|]
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EF-hand calcium-binding domain-containing protein 5-like isoform X4 [Lytechinus variegatus]

Protein Classification

Graphical summary

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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 5.14e-28

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: 107.67  E-value: 5.14e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  151 DARAYLLDKLLPTLILGIEKLLMEAERRDL---TEKNEANPNFNPLNYLAQYLMRNNPRY 207
Cdd:cd22968      1 ETRAYLVEKVLPTLVPGLEKLLKEVERRGLleeEGRPEPAPRFNPINWLAQYLMRNNPRY 60
2A1904 super family cl36772
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
 453-725 6.44e-09

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


The actual alignment was detected with superfamily member TIGR00927:

Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 60.78  E-value: 6.44e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  453 SEPTAPSEGTVQEETTGEVGAAPVVD--GGEAPEEGIKDEV--KQDDGPTVGEGEG-SKSEGVAPGGEGVTTGGEGVAPG 527
Cdd:TIGR00927  636 AEAEHTGERTGEEGERPTEAEGENGEesGGEAEQEGETETKgeNESEGEIPAERKGeQEGEGEIEAKEADHKGETEAEEV 715

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  528 GEGVAPSGEGvAPSEMDATVNGEGVATGDEGSKESVEKEGGEdtKEGEAtlvDENNAKEATDNSNKETADDTNTRVEENK 607
Cdd:TIGR00927  716 EHEGETEAEG-TEDEGEIETGEEGEEVEDEGEGEAEGKHEVE--TEGDR---KETEHEGETEAEGKEDEDEGEIQAGEDG 789

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  608 DSETQDSAEQQVESEPAKEESASGAGTGSDDKPVETTEGKETTKPEEAT---EVTAKEDtpraeeassaeEEKMKDGGGD 684
Cdd:TIGR00927  790 EMKGDEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQELNaenQGEAKQD-----------EKGVDGGGGS 858

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 2037976975  685 EVLMATETVIQENLVPDDAQKPVEESEQAEKTAEPVKSEDP 725
Cdd:TIGR00927  859 DGGDSEEEEEEEEEEEEEEEEEEEEEEEEEENEEPLSLEWP 899
rne super family cl35953
ribonuclease E; Reviewed
 686-828 5.50e-06

ribonuclease E; Reviewed


The actual alignment was detected with superfamily member PRK10811:

Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 51.19  E-value: 5.50e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  686 VLMATETVIQENLVPDDAQ-KPVEESEQAEKTAEPVKSEDPAAPVAETAEGTAETAEPQSKEQEPTSTDEGATAAE--VT 762
Cdd:PRK10811   847 VVRPQDVQVEEQREAEEVQvQPVVAEVPVAAAVEPVVSAPVVEAVAEVVEEPVVVAEPQPEEVVVVETTHPEVIAApvTE 926

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2037976975  763 APEVTPGETMSGDAVPAEIAGGEKEKTEEGTRDQAAPGAEETQAGEDKLDELTSAKDRATLQPTTA 828
Cdd:PRK10811   927 QPQVITESDVAVAQEVAEHAEPVVEPQDETADIEEAAETAEVVVAEPEVVAQPAAPVVAEVAAEVE 992
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 942-969 1.16e-03

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: 1.16e-03
                            10        20
                    ....*....|....*....|....*...
gi 2037976975   942 VDQLFDKWDNDGSGYLDLEEFHSIMAKF 969
Cdd:smart00054    2 LKEAFRLFDKDGDGKIDFEEFKDLLKAL 29
FRQ1 super family cl34916
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
936-1005 2.27e-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: 39.78  E-value: 2.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  936 AKRRQMVDQLFDKWDNDGSGYLDLEEFHSIMAKFKDNMESRIMAKAKQKLEKEEL------------------------- 990
Cdd:COG5126      1 DLQRRKLDRRFDLLDADGDGVLERDDFEALFRRLWATLFSEADTDGDGRISREEFvagmeslfeatvepfaraafdlldt 80

                           90
                   ....*....|....*..
gi 2037976975  991 --DNRLSKPEFKAYIEA 1005
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 5.14e-28

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: 107.67  E-value: 5.14e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  151 DARAYLLDKLLPTLILGIEKLLMEAERRDL---TEKNEANPNFNPLNYLAQYLMRNNPRY 207
Cdd:cd22968      1 ETRAYLVEKVLPTLVPGLEKLLKEVERRGLleeEGRPEPAPRFNPINWLAQYLMRNNPRY 60
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
 453-725 6.44e-09

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


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 60.78  E-value: 6.44e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  453 SEPTAPSEGTVQEETTGEVGAAPVVD--GGEAPEEGIKDEV--KQDDGPTVGEGEG-SKSEGVAPGGEGVTTGGEGVAPG 527
Cdd:TIGR00927  636 AEAEHTGERTGEEGERPTEAEGENGEesGGEAEQEGETETKgeNESEGEIPAERKGeQEGEGEIEAKEADHKGETEAEEV 715

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  528 GEGVAPSGEGvAPSEMDATVNGEGVATGDEGSKESVEKEGGEdtKEGEAtlvDENNAKEATDNSNKETADDTNTRVEENK 607
Cdd:TIGR00927  716 EHEGETEAEG-TEDEGEIETGEEGEEVEDEGEGEAEGKHEVE--TEGDR---KETEHEGETEAEGKEDEDEGEIQAGEDG 789

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  608 DSETQDSAEQQVESEPAKEESASGAGTGSDDKPVETTEGKETTKPEEAT---EVTAKEDtpraeeassaeEEKMKDGGGD 684
Cdd:TIGR00927  790 EMKGDEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQELNaenQGEAKQD-----------EKGVDGGGGS 858

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 2037976975  685 EVLMATETVIQENLVPDDAQKPVEESEQAEKTAEPVKSEDP 725
Cdd:TIGR00927  859 DGGDSEEEEEEEEEEEEEEEEEEEEEEEEEENEEPLSLEWP 899
PTZ00459 PTZ00459
mucin-associated surface protein (MASP); Provisional
 527-779 3.94e-07

mucin-associated surface protein (MASP); Provisional


Pssm-ID: 185638 [Multi-domain]  Cd Length: 291  Bit Score: 53.64  E-value: 3.94e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  527 GGEGVAPSGEGVAPSEMDATVNGEGVATGDEGSKESveKEGGEDTKEGEATLVDENNAKEATDNSNKETADDTNTRVEEN 606
Cdd:PTZ00459    23 GGRCEAGVGVGAQQDGGKSPPESKGLETSSQGTQDL--KGGAAGAKENSPPLPTEEDDEDVDDDSEEGDDDDGGAEDEEE 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  607 KDSETQDSAEQQVESEPAKEESASgagTGSDDKPVETTEGKETTKPEEA---------TEVTAKEDTPRAEEASSAEeek 677
Cdd:PTZ00459   101 EKVRGQSGQEGTVALGSGSTEKKL---IGSEKQTELSISSAESISPSGSrelnvnltqTEVEGKKETDKNTPAVENP--- 174

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  678 MKDGGGDEVLMAteTVIQENLVPDDAQKPVEESEQ-AEKTAEPVKSEDpaaPVAETAegtaetAEPQS---KEQEPTSTD 753
Cdd:PTZ00459   175 LTTGNGENTLPA--GIVEGNPSPPPPQDGIHSREQdGEGTTSEGQKNV---PLPETA------ATPQShhdKGSEGTGED 243

                          250       260
                   ....*....|....*....|....*.
gi 2037976975  754 EGATAaeVTAPEVTPGETMSGDAVPA 779
Cdd:PTZ00459   244 TKATT--VTANTTDTTNTQNSDGSTA 267
rne PRK10811
ribonuclease E; Reviewed
 686-828 5.50e-06

ribonuclease E; Reviewed


Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 51.19  E-value: 5.50e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  686 VLMATETVIQENLVPDDAQ-KPVEESEQAEKTAEPVKSEDPAAPVAETAEGTAETAEPQSKEQEPTSTDEGATAAE--VT 762
Cdd:PRK10811   847 VVRPQDVQVEEQREAEEVQvQPVVAEVPVAAAVEPVVSAPVVEAVAEVVEEPVVVAEPQPEEVVVVETTHPEVIAApvTE 926

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2037976975  763 APEVTPGETMSGDAVPAEIAGGEKEKTEEGTRDQAAPGAEETQAGEDKLDELTSAKDRATLQPTTA 828
Cdd:PRK10811   927 QPQVITESDVAVAQEVAEHAEPVVEPQDETADIEEAAETAEVVVAEPEVVAQPAAPVVAEVAAEVE 992
MDN1 COG5271
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ...
 424-855 2.07e-04

Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444083 [Multi-domain]  Cd Length: 1028  Bit Score: 46.16  E-value: 2.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  424 VIELTETDDTESLISEGSSISSVKSSMKESEPTAPSEGTVQEETTGEVGAAPVVDGGEAPEEGIKDEVKQDDGPTVGEGE 503
Cdd:COG5271    256 ESAGATAEVGGTPDTDDEATDDADGLEAAEDDALDAELTAAQAADPESDDDADDSTLAALEGAAEDTEIATADELAAADD 335

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  504 GSKSEGVA-------PGGEGVTTGGEGVAPGGEGVAPSGEGVAPSEMDATVNGEGVATGDEGSKESVEKEGGEDTKEGEA 576
Cdd:COG5271    336 EDDDDSAAedaaeeaATAEDSAAEDTQDAEDEAAGEAADESEGADTDAAADEADAAADDSADDEEASADGGTSPTSDTDE 415

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  577 TLVDENNAKEATDnSNKETADDTNTRVEENKDSETQDSAEQQVesepakEESASGAGTGSDDKPVETTEGKETTKPEEAT 656
Cdd:COG5271    416 EEEEADEDASAGE-TEDESTDVTSAEDDIATDEEADSLADEEE------EAEAELDTEEDTESAEEDADGDEATDEDDAS 488

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  657 EVTAKEDTPRAEEASSAEEEKMKDGGGDEVLMATEtviQENLVPDDAQKPVEESEQAEktaEPVKSEDPAAPVAETAEGT 736
Cdd:COG5271    489 DDGDEEEAEEDAEAEADSDELTAEETSADDGADTD---AAADPEDSDEDALEDETEGE---ENAPGSDQDADETDEPEAT 562

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  737 AETAEPQSKEQEPTSTDEGATAAEVTAPEVTPGETMSGDAVPAEIAGGEKEKTEEGTRDQAAPGAEETQAGEDKLDELTS 816
Cdd:COG5271    563 AEEDEPDEAEAETEDATENADADETEESADESEEAEASEDEAAEEEEADDDEADADADGAADEEETEEEAAEDEAAEPET 642

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|.
gi 2037976975  817 AKDRATLQPTTANTLTGRS--TSVSFHEDAIKLKEEKADSE 855
Cdd:COG5271    643 DASEAADEDADAETEAEASadESEEEAEDESETSSEDAEED 683
Treacle pfam03546
Treacher Collins syndrome protein Treacle;
472-871 2.22e-04

Treacher Collins syndrome protein Treacle;


Pssm-ID: 460967 [Multi-domain]  Cd Length: 531  Bit Score: 45.83  E-value: 2.22e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  472 GAAPVVDGGEAPEEGIKDEVKQDDGPTvGEGEGSKSEGVAPGGEGVTTGGEGVAPGGE----------GVAPSGEGVAPS 541
Cdd:pfam03546   70 GAPPVPPGKTGPAAAQAQAGKPEEDSE-SSSEESDSDGETPAAATLTTSPAQVKPLGKnsqvrpastvGKGPSGKGANPA 148

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  542 EMDATvnGEGVATGDEGSKESVEKEGGEDTKEGEATLVDENNAKEATDNSNKETADDTN---------------TRVEEN 606
Cdd:pfam03546  149 PPGKA--GSAAPLVQVGKKEEDSESSSEESDSEGEAPPAATQAKPSGKILQVRPASGPAkgaapappqkagpvaTQVKAE 226

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  607 KDSETQDSAEQQVESEpakeESASGAGTGSDDKP-VETTEGKETtkPEEATEVTAkedTPRAEEASSAEEEKMKDGGGde 685
Cdd:pfam03546  227 RSKEDSESSEESSDSE----EEAPAAATPAQAKPaLKTPQTKAS--PRKGTPITP---TSAKVPPVRVGTPAPWKAGT-- 295

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  686 vlMATETVIQENLVPDDAQKP------VEESEQAEKTAePVKSEDPAAPVAETAEGTAETA------------------- 740
Cdd:pfam03546  296 --VTSPACASSPAVARGAQRPeedsssSEESESEEETA-PAAAVGQAKSVGKGLQGKAASAptkgpsgqgtapvppgktg 372

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  741 ------------EPQSKEQEPTSTDEGATAAEVTAPEVTPGETMSGDAVPAEIAGGEkekteegtrdQAAPGAEETQAGE 808
Cdd:pfam03546  373 pavaqvkaeaqeDSESSEEESDSEEAAATPAQVKASGKTPQAKANPAPTKASSAKGA----------ASAPGKVVAAAAQ 442

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  809 DKLDELTSAKDRATLQPTTANTLTGRSTSVSF------------------HEDAIKLKEEKADSEDRPKTPV----KTPT 866
Cdd:pfam03546  443 AKQGSPAKVKPPARTPQNSAISVRGQASVPAVgkavataaqaqkgpvggpQEEDSESSEEESDSEEEAPAQAkpsgKTPQ 522


                   ....*
gi 2037976975  867 VRSGS 871
Cdd:pfam03546  523 VRAAS 527
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 942-969 1.16e-03

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: 1.16e-03
                            10        20
                    ....*....|....*....|....*...
gi 2037976975   942 VDQLFDKWDNDGSGYLDLEEFHSIMAKF 969
Cdd:smart00054    2 LKEAFRLFDKDGDGKIDFEEFKDLLKAL 29
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
 942-969 1.32e-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: 1.32e-03
                           10        20
                   ....*....|....*....|....*...
gi 2037976975  942 VDQLFDKWDNDGSGYLDLEEFHSIMAKF 969
Cdd:pfam00036    2 LKEIFRLFDKDGDGKIDFEEFKELLKKL 29
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
936-1005 2.27e-03

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 39.78  E-value: 2.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  936 AKRRQMVDQLFDKWDNDGSGYLDLEEFHSIMAKFKDNMESRIMAKAKQKLEKEEL------------------------- 990
Cdd:COG5126      1 DLQRRKLDRRFDLLDADGDGVLERDDFEALFRRLWATLFSEADTDGDGRISREEFvagmeslfeatvepfaraafdlldt 80

                           90
                   ....*....|....*..
gi 2037976975  991 --DNRLSKPEFKAYIEA 1005
Cdd:COG5126     81 dgDGKISADEFRRLLTA 97
EFh_PRIP cd16206
EF-hand motif found in phospholipase C-related but catalytically inactive proteins (PRIP); ...
 944-1009 2.52e-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: 2.52e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2037976975  944 QLFDKWDNDGSGYLDLEEFHSIMAKFKDNM-ESRIMAKAKQKLEKEE-LDNRLSKPEFkayIEAVCSL 1009
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 3.85e-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: 3.85e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2037976975  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 5.14e-28

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: 107.67  E-value: 5.14e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  151 DARAYLLDKLLPTLILGIEKLLMEAERRDL---TEKNEANPNFNPLNYLAQYLMRNNPRY 207
Cdd:cd22968      1 ETRAYLVEKVLPTLVPGLEKLLKEVERRGLleeEGRPEPAPRFNPINWLAQYLMRNNPRY 60
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
 453-725 6.44e-09

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


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 60.78  E-value: 6.44e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  453 SEPTAPSEGTVQEETTGEVGAAPVVD--GGEAPEEGIKDEV--KQDDGPTVGEGEG-SKSEGVAPGGEGVTTGGEGVAPG 527
Cdd:TIGR00927  636 AEAEHTGERTGEEGERPTEAEGENGEesGGEAEQEGETETKgeNESEGEIPAERKGeQEGEGEIEAKEADHKGETEAEEV 715

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  528 GEGVAPSGEGvAPSEMDATVNGEGVATGDEGSKESVEKEGGEdtKEGEAtlvDENNAKEATDNSNKETADDTNTRVEENK 607
Cdd:TIGR00927  716 EHEGETEAEG-TEDEGEIETGEEGEEVEDEGEGEAEGKHEVE--TEGDR---KETEHEGETEAEGKEDEDEGEIQAGEDG 789

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  608 DSETQDSAEQQVESEPAKEESASGAGTGSDDKPVETTEGKETTKPEEAT---EVTAKEDtpraeeassaeEEKMKDGGGD 684
Cdd:TIGR00927  790 EMKGDEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQELNaenQGEAKQD-----------EKGVDGGGGS 858

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 2037976975  685 EVLMATETVIQENLVPDDAQKPVEESEQAEKTAEPVKSEDP 725
Cdd:TIGR00927  859 DGGDSEEEEEEEEEEEEEEEEEEEEEEEEEENEEPLSLEWP 899
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
 452-663 1.35e-07

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


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 56.54  E-value: 1.35e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  452 ESEPTAPSEGTVQEETTGEVGAAPVVDGGEAPEEGIKDEVKQDDGPTVGEGEGSKSEGvapgGEGVTTGGEGVAPGGEGV 531
Cdd:TIGR00927  680 ESEGEIPAERKGEQEGEGEIEAKEADHKGETEAEEVEHEGETEAEGTEDEGEIETGEE----GEEVEDEGEGEAEGKHEV 755

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  532 APSGEgvaPSEMDATVNGEGVATGDEGSKESVEKEGGE-DTKEGEATLVDENNAKEATDNSNKETADDTNTRVEENKDSE 610
Cdd:TIGR00927  756 ETEGD---RKETEHEGETEAEGKEDEDEGEIQAGEDGEmKGDEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDET 832

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2037976975  611 TQDSAEQQVESEPAKEESASGAGTGSDDKPVETTEGKETTKPEEATEVTAKED 663
Cdd:TIGR00927  833 GEQELNAENQGEAKQDEKGVDGGGGSDGGDSEEEEEEEEEEEEEEEEEEEEEE 885
PTZ00459 PTZ00459
mucin-associated surface protein (MASP); Provisional
 527-779 3.94e-07

mucin-associated surface protein (MASP); Provisional


Pssm-ID: 185638 [Multi-domain]  Cd Length: 291  Bit Score: 53.64  E-value: 3.94e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  527 GGEGVAPSGEGVAPSEMDATVNGEGVATGDEGSKESveKEGGEDTKEGEATLVDENNAKEATDNSNKETADDTNTRVEEN 606
Cdd:PTZ00459    23 GGRCEAGVGVGAQQDGGKSPPESKGLETSSQGTQDL--KGGAAGAKENSPPLPTEEDDEDVDDDSEEGDDDDGGAEDEEE 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  607 KDSETQDSAEQQVESEPAKEESASgagTGSDDKPVETTEGKETTKPEEA---------TEVTAKEDTPRAEEASSAEeek 677
Cdd:PTZ00459   101 EKVRGQSGQEGTVALGSGSTEKKL---IGSEKQTELSISSAESISPSGSrelnvnltqTEVEGKKETDKNTPAVENP--- 174

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  678 MKDGGGDEVLMAteTVIQENLVPDDAQKPVEESEQ-AEKTAEPVKSEDpaaPVAETAegtaetAEPQS---KEQEPTSTD 753
Cdd:PTZ00459   175 LTTGNGENTLPA--GIVEGNPSPPPPQDGIHSREQdGEGTTSEGQKNV---PLPETA------ATPQShhdKGSEGTGED 243

                          250       260
                   ....*....|....*....|....*.
gi 2037976975  754 EGATAaeVTAPEVTPGETMSGDAVPA 779
Cdd:PTZ00459   244 TKATT--VTANTTDTTNTQNSDGSTA 267
DD_DPY30_SDC1-like cd22958
dimerization/docking (D/D) domain found in the DPY30/SDC1-like family; The DPY30/SDC1-like ...
 152-204 1.75e-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: 1.75e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2037976975  152 ARAYLLDKLLPTLILGIEKLLMeaerrdltekneANPNfNPLNYLAQYLMRNN 204
Cdd:cd22958      1 AREYLSETVLPTLIPALAELLK------------ARPE-DPLEWLAEYLLRNN 40
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
 534-805 5.30e-06

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


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 51.53  E-value: 5.30e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  534 SGEGVAPSEMDATVNGEGVATGDEGSKESVEKEGGEDTKEGEATLVDENNAKEATDNSNK-ETADDTNTRVEENKDSETQ 612
Cdd:TIGR00927  631 SKGDVAEAEHTGERTGEEGERPTEAEGENGEESGGEAEQEGETETKGENESEGEIPAERKgEQEGEGEIEAKEADHKGET 710

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  613 DSAEQQVESEPAKEESasgagtgSDDKPVETTEGKETTKPEEATEVTAKEDTPRAEEASSAEEEKMKDGGGDEVLMATET 692
Cdd:TIGR00927  711 EAEEVEHEGETEAEGT-------EDEGEIETGEEGEEVEDEGEGEAEGKHEVETEGDRKETEHEGETEAEGKEDEDEGEI 783

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  693 VIQEN--LVPDDAQKPVEESEQAEKTAEPVKSEDPAAPVAETAEGTAETAepqskEQEPTSTDEGATAAEVTAPEvTPGE 770
Cdd:TIGR00927  784 QAGEDgeMKGDEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETG-----EQELNAENQGEAKQDEKGVD-GGGG 857

                          250       260       270
                   ....*....|....*....|....*....|....*
gi 2037976975  771 TMSGDAVPAEIAGGEKEKTEEGTRDQAAPGAEETQ 805
Cdd:TIGR00927  858 SDGGDSEEEEEEEEEEEEEEEEEEEEEEEEEENEE 892
rne PRK10811
ribonuclease E; Reviewed
 686-828 5.50e-06

ribonuclease E; Reviewed


Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 51.19  E-value: 5.50e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  686 VLMATETVIQENLVPDDAQ-KPVEESEQAEKTAEPVKSEDPAAPVAETAEGTAETAEPQSKEQEPTSTDEGATAAE--VT 762
Cdd:PRK10811   847 VVRPQDVQVEEQREAEEVQvQPVVAEVPVAAAVEPVVSAPVVEAVAEVVEEPVVVAEPQPEEVVVVETTHPEVIAApvTE 926

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2037976975  763 APEVTPGETMSGDAVPAEIAGGEKEKTEEGTRDQAAPGAEETQAGEDKLDELTSAKDRATLQPTTA 828
Cdd:PRK10811   927 QPQVITESDVAVAQEVAEHAEPVVEPQDETADIEEAAETAEVVVAEPEVVAQPAAPVVAEVAAEVE 992
PRK13108 PRK13108
prolipoprotein diacylglyceryl transferase; Reviewed
 615-821 8.12e-06

prolipoprotein diacylglyceryl transferase; Reviewed


Pssm-ID: 237284 [Multi-domain]  Cd Length: 460  Bit Score: 50.36  E-value: 8.12e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  615 AEQQVESEPAKEESASGAGTGSDDKPVettEGKETTKPEEATEVTAKEDTPRAEEASSAEEEKMKDGGGDEVLMatetvi 694
Cdd:PRK13108   292 VDEALEREPAELAAAAVASAASAVGPV---GPGEPNQPDDVAEAVKAEVAEVTDEVAAESVVQVADRDGESTPA------ 362

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  695 qenlvPDDAQKPVEESEQAEKTAepvkSEDPAAPVAETAEGTAETAEPQSKEQEPTSTDEgATAAEVTAPEVTPGEtmsg 774
Cdd:PRK13108   363 -----VEETSEADIEREQPGDLA----GQAPAAHQVDAEAASAAPEEPAALASEAHDETE-PEVPEKAAPIPDPAK---- 428

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 2037976975  775 davpaeiaggEKEKTEEGTRDQAApgaeeTQAGEDKLDELTSAKDRA 821
Cdd:PRK13108   429 ----------PDELAVAGPGDDPA-----EPDGIRRQDDFSSRRRRW 460
DD_IQCK cd22969
dimerization/docking (D/D) domain found in IQ domain-containing protein K (IQCK) and similar ...
 152-205 8.33e-06

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: 44.42  E-value: 8.33e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2037976975  152 ARAYLLDKLLPTLILGIEKLLMEAERRD-LTEKNEAnpnFNPLNYLAQYLMRNNP 205
Cdd:cd22969      7 PVEYLEEYIFPVLLPALEEMLEEAKKEDcFERKRTK---FNGLDFLTEYLYNNNP 58
PTZ00121 PTZ00121
MAEBL; Provisional
 550-868 1.13e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.52  E-value: 1.13e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  550 EGVATGDEGSKESVEKEGGEDTKEGEATLVDENNAKEATDNsnKETADDTNTRVEENKDSETQDSAEQQVESEPAK--EE 627
Cdd:PTZ00121  1287 EEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEA--KKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEaaEE 1364

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  628 SASGAGTGSDDKPVETTEGK----ETTKPEEATEvTAKEDTPRAEEASSAEEEKMKdggGDEVLMATETVIQenlvPDDA 703
Cdd:PTZ00121  1365 KAEAAEKKKEEAKKKADAAKkkaeEKKKADEAKK-KAEEDKKKADELKKAAAAKKK---ADEAKKKAEEKKK----ADEA 1436

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  704 QKPVEESEQAE----KTAEPVKSEDpaapVAETAEGTAETAEPQSKEQEPTSTDEGATAAEVTAPEvtpgetmsgdAVPA 779
Cdd:PTZ00121  1437 KKKAEEAKKADeakkKAEEAKKAEE----AKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKK----------ADEA 1502

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  780 EIAGGEKEKTEEGTRDQAAPGAEETQAGED--KLDELTSAKDRATLQPTTantltgRSTSVSFHEDAIKLKEEKADSEDR 857
Cdd:PTZ00121  1503 KKAAEAKKKADEAKKAEEAKKADEAKKAEEakKADEAKKAEEKKKADELK------KAEELKKAEEKKKAEEAKKAEEDK 1576

                          330
                   ....*....|.
gi 2037976975  858 PKTPVKTPTVR 868
Cdd:PTZ00121  1577 NMALRKAEEAK 1587
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
 579-812 1.51e-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: 49.99  E-value: 1.51e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  579 VDENNAKEATDNSNKETADDTNTRVEENKDSETQDSAEQQVESEPAKEESASGAGTGSDDKPVET-TEGKETTKPEEATE 657
Cdd:TIGR00927  635 VAEAEHTGERTGEEGERPTEAEGENGEESGGEAEQEGETETKGENESEGEIPAERKGEQEGEGEIeAKEADHKGETEAEE 714

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  658 VTAKEDTpraeeassaeeekmkDGGGDEVLMATETVIQENLVPDDAQKPVEESEQAEKTAEPVKSEDPAAPVAETAEGTA 737
Cdd:TIGR00927  715 VEHEGET---------------EAEGTEDEGEIETGEEGEEVEDEGEGEAEGKHEVETEGDRKETEHEGETEAEGKEDED 779

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2037976975  738 EtAEPQSKEQEPTSTDEGATAAEVTAPEVTPGETMSGDAVPAEIAGGEKEKTEEGTRDQAAPGAEETQAGEDKLD 812
Cdd:TIGR00927  780 E-GEIQAGEDGEMKGDEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQELNAENQGEAKQDEKGVD 853
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
 553-754 3.25e-05

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 48.63  E-value: 3.25e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  553 ATGDEGSKESVEKEGGEDTKEGEATLVDENNAKEATDNSNKETADDTNTRVEENKDSETQDSAEQQVesepakEESASGA 632
Cdd:PTZ00341   945 ANIEEDAEENVEEDAEENVEENVEENVEENVEENVEENVEENVEENVEENVEENVEENIEENVEENV------EENIEEN 1018

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  633 GTGSDDKPVETTEGKETTKPEEATEVTAKEDTPRAEEASSAEEEKMKDGGGDEVlmatETVIQENlVPDDAQKPVEES-E 711
Cdd:PTZ00341  1019 VEEYDEENVEEVEENVEEYDEENVEEIEENAEENVEENIEENIEEYDEENVEEI----EENIEEN-IEENVEENVEENvE 1093

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 2037976975  712 QAEKTAEPVKSEDPAAPVAETAEGTAETAEPQSKEQEPTSTDE 754
Cdd:PTZ00341  1094 EIEENVEENVEENAEENAEENAEENAEEYDDENPEEHNEEYDE 1136
PHA03169 PHA03169
hypothetical protein; Provisional
 584-808 3.36e-05

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 48.04  E-value: 3.36e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  584 AKEATDNSNKETADDTNTRVEENKDSETQDSAEQQVESEPAKEESASGAGTGSDDKPVETTEGKETTKPEEATEVTAKED 663
Cdd:PHA03169    43 AAKPAPPAPTTSGPQVRAVAEQGHRQTESDTETAEESRHGEKEERGQGGPSGSGSESVGSPTPSPSGSAEELASGLSPEN 122

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  664 TpraeeassaeeekmkDGGGDEvlmatetviqenlvpddaqKPVEESEQAEKTAEPVKSEDPAAPVAETAEGTAETAEPQ 743
Cdd:PHA03169   123 T---------------SGSSPE-------------------SPASHSPPPSPPSHPGPHEPAPPESHNPSPNQQPSSFLQ 168

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2037976975  744 -SKEQEPTSTDEGATAAEVTAPEvtPGETMSGDAVPAEIAGGEKEKTEEGTRDQAAPGAEETQAGE 808
Cdd:PHA03169   169 pSHEDSPEEPEPPTSEPEPDSPG--PPQSETPTSSPPPQSPPDEPGEPQSPTPQQAPSPNTQQAVE 232
PTZ00121 PTZ00121
MAEBL; Provisional
 560-859 5.90e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.21  E-value: 5.90e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  560 KESVEKEGGEDTKEGEATLVDEN--NAKEATDNSNKETADDTNTRVEENKDSETQDSAEQ-QVESEPAKEESASGAGTGS 636
Cdd:PTZ00121  1188 RKAEELRKAEDARKAEAARKAEEerKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEeRNNEEIRKFEEARMAHFAR 1267

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  637 DDKPVETTEGKETTKPEEATEVTAKEDTPRAEEASSAEEEKMKDGGGDEVLMATETVIQENLVPDDAQKPVEESEQAEKT 716
Cdd:PTZ00121  1268 RQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEA 1347

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  717 AEpvKSEDPAAPVAETAEGTAETAEPQSKEQEptstdEGATAAEVTAPEVTPGETMSGDAVPAEIAGGEKEKTEEGTR-- 794
Cdd:PTZ00121  1348 AK--AEAEAAADEAEAAEEKAEAAEKKKEEAK-----KKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKka 1420

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2037976975  795 DQAAPGAEETQAGEDkldeltsAKDRATlQPTTANTLTGRSTSVSFHEDAIKLKEEKADSEDRPK 859
Cdd:PTZ00121  1421 DEAKKKAEEKKKADE-------AKKKAE-EAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKK 1477
PTZ00121 PTZ00121
MAEBL; Provisional
 565-859 5.90e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.21  E-value: 5.90e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  565 KEGGEDTKEGEATLVDENNAKEATDNSNKETADDTNTRVEENKDSETQDSAEQQVESEPAKEESASGAGTGSDDKPVETT 644
Cdd:PTZ00121  1236 KKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAK 1315

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  645 EGKETTKPEEATEVTAKEDTPRAEEASSAEEEKMK--DGGGDEVLMATETVIQENLVPDDAQKPVEEseqAEKTAEPVKS 722
Cdd:PTZ00121  1316 KADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAeaEAAADEAEAAEEKAEAAEKKKEEAKKKADA---AKKKAEEKKK 1392

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  723 EDPAAPVAETAEGTAEtaEPQSKEQEPTSTDEGATAAEvtapEVTPGETMSGDAVPAEIAGGEKEKTEEGTRDQAAPGAE 802
Cdd:PTZ00121  1393 ADEAKKKAEEDKKKAD--ELKKAAAAKKKADEAKKKAE----EKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKA 1466

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2037976975  803 ETQAGEDKLDELTSAKDRATLQPTTANTLTGRSTSVSFHEDAIKLKEEKADSEDRPK 859
Cdd:PTZ00121  1467 EEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKK 1523
PTZ00121 PTZ00121
MAEBL; Provisional
 534-859 1.44e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.67  E-value: 1.44e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  534 SGEGVAPSEMDATVNGEGVATGDEGSKEsvEKEGGEDTKEGEATLVDE-NNAKEATDNSNKETADDTNTRVEENKDSETQ 612
Cdd:PTZ00121  1068 QDEGLKPSYKDFDFDAKEDNRADEATEE--AFGKAEEAKKTETGKAEEaRKAEEAKKKAEDARKAEEARKAEDARKAEEA 1145

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  613 DSAEQQVESEPAK--EES--ASGAGTGSDDKPVEttEGKETTKPEEATEVTAKEDTPRAEEASSAEEEKMkdggGDEVLM 688
Cdd:PTZ00121  1146 RKAEDAKRVEIARkaEDArkAEEARKAEDAKKAE--AARKAEEVRKAEELRKAEDARKAEAARKAEEERK----AEEARK 1219

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  689 ATET-VIQENLVPDDAQKPVEESEQAEK--TAEPVKSEDPAAPVAETAEGTAETAEPQSKEQEPTSTDEGATAAEV-TAP 764
Cdd:PTZ00121  1220 AEDAkKAEAVKKAEEAKKDAEEAKKAEEerNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAkKAE 1299

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  765 EVTPGETMSGDAVPAEIAGGEKEKTEEGTR--DQAAPGAEET-QAGEDKLDELTSAKDRATLQPTTANTLTGRSTSVSFH 841
Cdd:PTZ00121  1300 EKKKADEAKKKAEEAKKADEAKKKAEEAKKkaDAAKKKAEEAkKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKK 1379

                          330
                   ....*....|....*...
gi 2037976975  842 EDAIKLKEEKADSEDRPK 859
Cdd:PTZ00121  1380 ADAAKKKAEEKKKADEAK 1397
PHA03169 PHA03169
hypothetical protein; Provisional
 434-666 1.93e-04

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 45.73  E-value: 1.93e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  434 ESLISEGSSISSVKSSMKESEPTAPSEGTVQEETTGEVGAAPVVDGGEAPEEGIKDEVKQDDGPTVGEGEgsksEGVAPG 513
Cdd:PHA03169    28 GTREQAGRRRGTAARAAKPAPPAPTTSGPQVRAVAEQGHRQTESDTETAEESRHGEKEERGQGGPSGSGS----ESVGSP 103

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  514 GEGVTTGGEGVAPGGEGVAPSGEGVAPSEMDATVNGEGVATGD-EGSKESVEKEGGEDTKEGEATLVDENNAKEAtDNSN 592
Cdd:PHA03169   104 TPSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGPhEPAPPESHNPSPNQQPSSFLQPSHEDSPEEP-EPPT 182

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2037976975  593 KETADDTntrvEENKDSETQDSAEQqvESEPAKEESASGAGTGSD-DKPVETTEGKETTKPEEATEVTAKEDTPR 666
Cdd:PHA03169   183 SEPEPDS----PGPPQSETPTSSPP--PQSPPDEPGEPQSPTPQQaPSPNTQQAVEHEDEPTEPEREGPPFPGHR 251
MDN1 COG5271
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ...
 424-855 2.07e-04

Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444083 [Multi-domain]  Cd Length: 1028  Bit Score: 46.16  E-value: 2.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  424 VIELTETDDTESLISEGSSISSVKSSMKESEPTAPSEGTVQEETTGEVGAAPVVDGGEAPEEGIKDEVKQDDGPTVGEGE 503
Cdd:COG5271    256 ESAGATAEVGGTPDTDDEATDDADGLEAAEDDALDAELTAAQAADPESDDDADDSTLAALEGAAEDTEIATADELAAADD 335

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  504 GSKSEGVA-------PGGEGVTTGGEGVAPGGEGVAPSGEGVAPSEMDATVNGEGVATGDEGSKESVEKEGGEDTKEGEA 576
Cdd:COG5271    336 EDDDDSAAedaaeeaATAEDSAAEDTQDAEDEAAGEAADESEGADTDAAADEADAAADDSADDEEASADGGTSPTSDTDE 415

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  577 TLVDENNAKEATDnSNKETADDTNTRVEENKDSETQDSAEQQVesepakEESASGAGTGSDDKPVETTEGKETTKPEEAT 656
Cdd:COG5271    416 EEEEADEDASAGE-TEDESTDVTSAEDDIATDEEADSLADEEE------EAEAELDTEEDTESAEEDADGDEATDEDDAS 488

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  657 EVTAKEDTPRAEEASSAEEEKMKDGGGDEVLMATEtviQENLVPDDAQKPVEESEQAEktaEPVKSEDPAAPVAETAEGT 736
Cdd:COG5271    489 DDGDEEEAEEDAEAEADSDELTAEETSADDGADTD---AAADPEDSDEDALEDETEGE---ENAPGSDQDADETDEPEAT 562

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  737 AETAEPQSKEQEPTSTDEGATAAEVTAPEVTPGETMSGDAVPAEIAGGEKEKTEEGTRDQAAPGAEETQAGEDKLDELTS 816
Cdd:COG5271    563 AEEDEPDEAEAETEDATENADADETEESADESEEAEASEDEAAEEEEADDDEADADADGAADEEETEEEAAEDEAAEPET 642

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|.
gi 2037976975  817 AKDRATLQPTTANTLTGRS--TSVSFHEDAIKLKEEKADSE 855
Cdd:COG5271    643 DASEAADEDADAETEAEASadESEEEAEDESETSSEDAEED 683
Treacle pfam03546
Treacher Collins syndrome protein Treacle;
472-871 2.22e-04

Treacher Collins syndrome protein Treacle;


Pssm-ID: 460967 [Multi-domain]  Cd Length: 531  Bit Score: 45.83  E-value: 2.22e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  472 GAAPVVDGGEAPEEGIKDEVKQDDGPTvGEGEGSKSEGVAPGGEGVTTGGEGVAPGGE----------GVAPSGEGVAPS 541
Cdd:pfam03546   70 GAPPVPPGKTGPAAAQAQAGKPEEDSE-SSSEESDSDGETPAAATLTTSPAQVKPLGKnsqvrpastvGKGPSGKGANPA 148

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  542 EMDATvnGEGVATGDEGSKESVEKEGGEDTKEGEATLVDENNAKEATDNSNKETADDTN---------------TRVEEN 606
Cdd:pfam03546  149 PPGKA--GSAAPLVQVGKKEEDSESSSEESDSEGEAPPAATQAKPSGKILQVRPASGPAkgaapappqkagpvaTQVKAE 226

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  607 KDSETQDSAEQQVESEpakeESASGAGTGSDDKP-VETTEGKETtkPEEATEVTAkedTPRAEEASSAEEEKMKDGGGde 685
Cdd:pfam03546  227 RSKEDSESSEESSDSE----EEAPAAATPAQAKPaLKTPQTKAS--PRKGTPITP---TSAKVPPVRVGTPAPWKAGT-- 295

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  686 vlMATETVIQENLVPDDAQKP------VEESEQAEKTAePVKSEDPAAPVAETAEGTAETA------------------- 740
Cdd:pfam03546  296 --VTSPACASSPAVARGAQRPeedsssSEESESEEETA-PAAAVGQAKSVGKGLQGKAASAptkgpsgqgtapvppgktg 372

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  741 ------------EPQSKEQEPTSTDEGATAAEVTAPEVTPGETMSGDAVPAEIAGGEkekteegtrdQAAPGAEETQAGE 808
Cdd:pfam03546  373 pavaqvkaeaqeDSESSEEESDSEEAAATPAQVKASGKTPQAKANPAPTKASSAKGA----------ASAPGKVVAAAAQ 442

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  809 DKLDELTSAKDRATLQPTTANTLTGRSTSVSF------------------HEDAIKLKEEKADSEDRPKTPV----KTPT 866
Cdd:pfam03546  443 AKQGSPAKVKPPARTPQNSAISVRGQASVPAVgkavataaqaqkgpvggpQEEDSESSEEESDSEEEAPAQAkpsgKTPQ 522


                   ....*
gi 2037976975  867 VRSGS 871
Cdd:pfam03546  523 VRAAS 527
MDN1 COG5271
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ...
 426-866 3.00e-04

Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444083 [Multi-domain]  Cd Length: 1028  Bit Score: 45.78  E-value: 3.00e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  426 ELTETDDTESLISEGSSISSVKSSMKESEPTAPSEGTVQEETTGEVGAAPVVDGGEAPEEGIKDEVKQDDGPTVGEGegs 505
Cdd:COG5271    204 GATVTTDPGDSVAADDDLAAEEGASAVVEEEDASEDAVAAADETLLADDDDTESAGATAEVGGTPDTDDEATDDADG--- 280

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  506 kseGVAPGGEGVTTGGEGVAPGGEGVAPSGEGVAPSEMDATVNGEGVATGDEGSKESVEKEGGEDTKEGEATLVDENNAK 585
Cdd:COG5271    281 ---LEAAEDDALDAELTAAQAADPESDDDADDSTLAALEGAAEDTEIATADELAAADDEDDDDSAAEDAAEEAATAEDSA 357

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  586 EATDNSNKETADDTNTRVEENKDSETQDSAEQQVESEPAKEESASGAGTGSDDKPVETTEGKETTKPEEATEVTAKEDTP 665
Cdd:COG5271    358 AEDTQDAEDEAAGEAADESEGADTDAAADEADAAADDSADDEEASADGGTSPTSDTDEEEEEADEDASAGETEDESTDVT 437

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  666 RAEEASSAeeekmkDGGGDEVLMATETVIQENLVPDDAQKPVEESEQAEKTaepvKSEDPAAPVAETAEGTAETAEPQS- 744
Cdd:COG5271    438 SAEDDIAT------DEEADSLADEEEEAEAELDTEEDTESAEEDADGDEAT----DEDDASDDGDEEEAEEDAEAEADSd 507

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  745 -KEQEPTSTDEGATAAEVTAPEVTPGETmSGDAVPAEIAGGEKEKTEEGTRDQAAPGAEET--QAGEDKLDELTSAKDRA 821
Cdd:COG5271    508 eLTAEETSADDGADTDAAADPEDSDEDA-LEDETEGEENAPGSDQDADETDEPEATAEEDEpdEAEAETEDATENADADE 586

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*
gi 2037976975  822 TLQPTTANTLTGRSTSVSFHEDAIKLKEEKADSEDRPKTPVKTPT 866
Cdd:COG5271    587 TEESADESEEAEASEDEAAEEEEADDDEADADADGAADEEETEEE 631
rne PRK10811
ribonuclease E; Reviewed
 640-811 4.81e-04

ribonuclease E; Reviewed


Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 45.03  E-value: 4.81e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  640 PVETTEGKETTKPEEATEVTAKEDTPRAEEASSaeeekmkdgggdevlMATETVIQEnlVPDDAQKPVEESEQAEKTAEP 719
Cdd:PRK10811   849 RPQDVQVEEQREAEEVQVQPVVAEVPVAAAVEP---------------VVSAPVVEA--VAEVVEEPVVVAEPQPEEVVV 911

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  720 VKSEDP---AAPVAE----TAEGTAETAEPQSKEQEPTSTD----EGATAAEVTAPEVTPGETMSGDAVPAEIAGGEKEK 788
Cdd:PRK10811   912 VETTHPeviAAPVTEqpqvITESDVAVAQEVAEHAEPVVEPqdetADIEEAAETAEVVVAEPEVVAQPAAPVVAEVAAEV 991

                          170       180
                   ....*....|....*....|...
gi 2037976975  789 TEEGTRDQAAPGAEETQAGEDKL 811
Cdd:PRK10811   992 ETVTAVEPEVAPAQVPEATVEHN 1014
rne PRK10811
ribonuclease E; Reviewed
 607-768 7.53e-04

ribonuclease E; Reviewed


Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 44.26  E-value: 7.53e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  607 KDSETQDSAE-QQVESEPAKEESASGAgTGSDDKPVETTEGKETTKPEEATEVTAKEDTPRAEEASsaeeekmkdgggdE 685
Cdd:PRK10811   851 QDVQVEEQREaEEVQVQPVVAEVPVAA-AVEPVVSAPVVEAVAEVVEEPVVVAEPQPEEVVVVETT-------------H 916

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  686 VLMATETVIQENLVPDDAQKPVEES--EQAEKTAEPVKSEDPAAPVAETAEGTAETAEPQSKEQEPTSTDEGATAAEVTA 763
Cdd:PRK10811   917 PEVIAAPVTEQPQVITESDVAVAQEvaEHAEPVVEPQDETADIEEAAETAEVVVAEPEVVAQPAAPVVAEVAAEVETVTA 996


                   ....*
gi 2037976975  764 PEVTP 768
Cdd:PRK10811   997 VEPEV 1001
PRK14949 PRK14949
DNA polymerase III subunits gamma and tau; Provisional
 423-785 7.74e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237863 [Multi-domain]  Cd Length: 944  Bit Score: 44.33  E-value: 7.74e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  423 PVIELTETDDTESLISEgssissvkSSMKESEptAPSEGTVQEETTGEVGAAPVVDGGEAPEEGIKDEVKQDDgpTVGEG 502
Cdd:PRK14949   443 EQALDDESELLAALNAE--------QAVILSQ--AQSQGFEASSSLDADNSAVPEQIDSTAEQSVVNPSVTDT--QVDDT 510

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  503 EGSKSEGVAPGGEGVTTGGEGVAPGGEGVAPSGEGVAPSEMDATVNGEGVATGDEGSKESVEKEGGEDTKEGEATLVDEN 582
Cdd:PRK14949   511 SASNNSAADNTVDDNYSAEDTLESNGLDEGDYAQDSAPLDAYQDDYVAFSSESYNALSDDEQHSANVQSAQSAAEAQPSS 590

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  583 NAKEATDNSNKETA----DDTNTRVEENKDSETQDSAEQQVESEPAKEESAsgagtgsDDKPVETTEGKETTKPEEATEV 658
Cdd:PRK14949   591 QSLSPISAVTTAAAsladDDILDAVLAARDSLLSDLDALSPKEGDGKKSSA-------DRKPKTPPSRAPPASLSKPASS 663

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  659 TAKEDTPrAEEASSAEEEKMKDGGGDEVLMATETVIQENLVPDDAQKP--VEESEQAEKTAEPVKSEDPAAPVAETAEGT 736
Cdd:PRK14949   664 PDASQTS-ASFDLDPDFELATHQSVPEAALASGSAPAPPPVPDPYDRPpwEEAPEVASANDGPNNAAEGNLSESVEDASN 742

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2037976975  737 AET------AEPQSKEQEPTSTDEGATAAEVTAPEVTPGETMSGDAVPAEIAGGE 785
Cdd:PRK14949   743 SELqaveqqATHQPQVQAEAQSPASTTALTQTSSEVQDTELNLVLLSSGSITGHP 797
MDN1 COG5271
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ...
 452-856 1.10e-03

Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444083 [Multi-domain]  Cd Length: 1028  Bit Score: 43.85  E-value: 1.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  452 ESEPTAPSEGTVQEET-TGEVGAAPVVDGGEAPEEGIKDEVKQDDGPTVGEGEGSKSEGVAPGGEGVTTGGEGVAPGGEG 530
Cdd:COG5271    556 TDEPEATAEEDEPDEAeAETEDATENADADETEESADESEEAEASEDEAAEEEEADDDEADADADGAADEEETEEEAAED 635

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  531 VAPSGEGVAPSEMDATVNGEGVATGDEGSKESVEKEGGEDTKEGEATLVDENNAKEATDNSNKETADDTNTRVEENKDSE 610
Cdd:COG5271    636 EAAEPETDASEAADEDADAETEAEASADESEEEAEDESETSSEDAEEDADAAAAEASDDEEETEEADEDAETASEEADAE 715

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  611 TQDSAEQqvesEPAKEESASGAGTGSDDKPVETTEGKETTKPEEATEVTAKEDtpraeeassaeeekmkDGGGDEVLMAT 690
Cdd:COG5271    716 EADTEAD----GTAEEAEEAAEEAESADEEAASLPDEADAEEEAEEAEEAEED----------------DADGLEEALEE 775

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  691 ETVIQENLVPDDAQKPVEESEQAEKTAEPVKSEDPAAPVAETAEGTAETAEPQSKEQEPTSTDEgataAEVTAPEVTPGE 770
Cdd:COG5271    776 EKADAEEAATDEEAEAAAEEKEKVADEDQDTDEDALLDEAEADEEEDLDGEDEETADEALEDIE----AGIAEDDEEDDD 851

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  771 TMSGDAVPAEIAGGEKEKTEEGTRDQAAPGAEETQAGEDKLDELTSAKDRATLQPTTANTLTGRSTSVSFHEDAIKLKEE 850
Cdd:COG5271    852 AAAAKDVDADLDLDADLAADEHEAEEAQEAETDADADADAGEADSSGESSAAAEDDDAAEDADSDDGANDEDDDDDAEEE 931


                   ....*.
gi 2037976975  851 KADSED 856
Cdd:COG5271    932 RKDAEE 937
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 942-969 1.16e-03

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: 1.16e-03
                            10        20
                    ....*....|....*....|....*...
gi 2037976975   942 VDQLFDKWDNDGSGYLDLEEFHSIMAKF 969
Cdd:smart00054    2 LKEAFRLFDKDGDGKIDFEEFKDLLKAL 29
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
 942-969 1.32e-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: 1.32e-03
                           10        20
                   ....*....|....*....|....*...
gi 2037976975  942 VDQLFDKWDNDGSGYLDLEEFHSIMAKF 969
Cdd:pfam00036    2 LKEIFRLFDKDGDGKIDFEEFKELLKKL 29
PRK13108 PRK13108
prolipoprotein diacylglyceryl transferase; Reviewed
 709-878 2.01e-03

prolipoprotein diacylglyceryl transferase; Reviewed


Pssm-ID: 237284 [Multi-domain]  Cd Length: 460  Bit Score: 42.66  E-value: 2.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  709 ESEQAEKTAEPVKSEDPAAPVAETAEGTAETAEPQSKEQEPTSTDEGATAAEVTAPEVTPGETMSGDAVPAEIAG---GE 785
Cdd:PRK13108   283 GALRGSEYVVDEALEREPAELAAAAVASAASAVGPVGPGEPNQPDDVAEAVKAEVAEVTDEVAAESVVQVADRDGestPA 362

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  786 KEKTEEGTRDQAAPGAEETQA-GEDKLDELTSAKdratlQPTTANTLTGRSTSVSFHEDAIKlKEEKADSeDRPKTPV-- 862
Cdd:PRK13108   363 VEETSEADIEREQPGDLAGQApAAHQVDAEAASA-----APEEPAALASEAHDETEPEVPEK-AAPIPDP-AKPDELAva 435

                          170
                   ....*....|....*....
gi 2037976975  863 ---KTPTVRSGSRSGSAFD 878
Cdd:PRK13108   436 gpgDDPAEPDGIRRQDDFS 454
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
936-1005 2.27e-03

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 39.78  E-value: 2.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  936 AKRRQMVDQLFDKWDNDGSGYLDLEEFHSIMAKFKDNMESRIMAKAKQKLEKEEL------------------------- 990
Cdd:COG5126      1 DLQRRKLDRRFDLLDADGDGVLERDDFEALFRRLWATLFSEADTDGDGRISREEFvagmeslfeatvepfaraafdlldt 80

                           90
                   ....*....|....*..
gi 2037976975  991 --DNRLSKPEFKAYIEA 1005
Cdd:COG5126     81 dgDGKISADEFRRLLTA 97
EFh_PRIP cd16206
EF-hand motif found in phospholipase C-related but catalytically inactive proteins (PRIP); ...
 944-1009 2.52e-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: 2.52e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2037976975  944 QLFDKWDNDGSGYLDLEEFHSIMAKFKDNM-ESRIMAKAKQKLEKEE-LDNRLSKPEFkayIEAVCSL 1009
Cdd:cd16206      4 SVFEEADTNKSGFLDEEEAVQLIKQLNPGLsTSRIKQKLKELQKKKDgARGRVSSDEF---VELFKEL 68
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 703-881 2.63e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 42.28  E-value: 2.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  703 AQKPVEESEQAEKTAEPVKSEDPAAPVAETAEGTAETAEPQSKEQEPTSTDEGATAAEVTAPEVTPGetmsGDAVPAEIA 782
Cdd:PRK07764   599 GPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDG----GDGWPAKAG 674

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  783 GGEKEKTEEGTRDQA-APGAEETQAGEDKLDELTSAKDRATLQPTT-ANTLTGRSTSVSFHEDAIKLKEEKADSEDRPKT 860
Cdd:PRK07764   675 GAAPAAPPPAPAPAApAAPAGAAPAQPAPAPAATPPAGQADDPAAQpPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGA 754

                          170       180
                   ....*....|....*....|.
gi 2037976975  861 PVKTPTVRSGSRSGSAFDESA 881
Cdd:PRK07764   755 PAQPPPPPAPAPAAAPAAAPP 775
MDN1 COG5271
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ...
 423-866 3.04e-03

Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444083 [Multi-domain]  Cd Length: 1028  Bit Score: 42.31  E-value: 3.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  423 PVIELTETDDTESLISEGSSISSVKSSMKESEPTAPSEGTVQEETTGEVGAAPVVDGGEAPEEGIKDEVKQDDGPTVGEG 502
Cdd:COG5271    317 GAAEDTEIATADELAAADDEDDDDSAAEDAAEEAATAEDSAAEDTQDAEDEAAGEAADESEGADTDAAADEADAAADDSA 396

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  503 EGSKSE----GVAPGGEGVTTGGEGVAPGGEGVAPSGEGVAPSEMDATVNGEGVATGDEGSKESVEKEGGEDTkegeatl 578
Cdd:COG5271    397 DDEEASadggTSPTSDTDEEEEEADEDASAGETEDESTDVTSAEDDIATDEEADSLADEEEEAEAELDTEEDT------- 469

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  579 vDENNAKEATDNSNKETADDTNTRVEENKDSETQDSAEQQVESEPAKEESasgagtGSDDKPVETTEGKETTKPEEATEV 658
Cdd:COG5271    470 -ESAEEDADGDEATDEDDASDDGDEEEAEEDAEAEADSDELTAEETSADD------GADTDAAADPEDSDEDALEDETEG 542

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  659 TAKEDTPRAEEASSAEEEKMKDGGGDEVLMATETVIQENLVPDDAQKPVEESEQAEKTAEpvKSEDPAAPVAETAEGTAE 738
Cdd:COG5271    543 EENAPGSDQDADETDEPEATAEEDEPDEAEAETEDATENADADETEESADESEEAEASED--EAAEEEEADDDEADADAD 620

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  739 TAEPQSKEQEPTSTDEGATA-AEVTAPEVTPGETMSGDAVPAEIAGGEKEKTEEGTRDQAAPGAEETQAGEDKLDELTSA 817
Cdd:COG5271    621 GAADEEETEEEAAEDEAAEPeTDASEAADEDADAETEAEASADESEEEAEDESETSSEDAEEDADAAAAEASDDEEETEE 700

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*....
gi 2037976975  818 KDRATLQPTTANTLTGRSTSVSFHEDAIKLKEEKADSEDRPKTPVKTPT 866
Cdd:COG5271    701 ADEDAETASEEADAEEADTEADGTAEEAEEAAEEAESADEEAASLPDEA 749
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
907-1004 3.33e-03

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 39.39  E-value: 3.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  907 LVKFITDGYVETEQEKFLRLQQARREAqsaKRRQMVDQLFDKWDNDGSGYLDLEEFHSIMAKFKDNMESriMAKAKQKLE 986
Cdd:COG5126     39 FSEADTDGDGRISREEFVAGMESLFEA---TVEPFARAAFDLLDTDGDGKISADEFRRLLTALGVSEEE--ADELFARLD 113

                           90
                   ....*....|....*...
gi 2037976975  987 KEElDNRLSKPEFKAYIE 1004
Cdd:COG5126    114 TDG-DGKISFEEFVAAVR 130
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 913-967 3.56e-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: 37.14  E-value: 3.56e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2037976975  913 DGYVeTEQEkflrLQQARREAQSAKRRQMVDQLFDKWDNDGSGYLDLEEFHSIMA 967
Cdd:cd00051     14 DGTI-SADE----LKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
Dpy-30 pfam05186
Dpy-30 motif; This motif is found in a wide variety of domain contexts. It is found in the ...
 152-205 3.85e-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: 3.85e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2037976975  152 ARAYLLDKLLPTLILGiekllmeaerrdLTEKNEANPNfNPLNYLAQYLMRNNP 205
Cdd:pfam05186    2 ARQYLNKTVAPILLQG------------LTELAKERPE-DPIEYLADYLLKNNP 42
PRK13108 PRK13108
prolipoprotein diacylglyceryl transferase; Reviewed
 540-666 4.09e-03

prolipoprotein diacylglyceryl transferase; Reviewed


Pssm-ID: 237284 [Multi-domain]  Cd Length: 460  Bit Score: 41.50  E-value: 4.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  540 PSEMDATvnGEGVATGDEGSKESVEKEGGEDTKEGEATLVDENNAKEATdNSNKETADD---TNTRVEENK--DSETQDS 614
Cdd:PRK13108   300 PAELAAA--AVASAASAVGPVGPGEPNQPDDVAEAVKAEVAEVTDEVAA-ESVVQVADRdgeSTPAVEETSeaDIEREQP 376

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2037976975  615 AEQQVESEPAKEESASGAGTGSDDKPVETTEGKETTKPEEATEVTAKEDTPR 666
Cdd:PRK13108   377 GDLAGQAPAAHQVDAEAASAAPEEPAALASEAHDETEPEVPEKAAPIPDPAK 428
DD_DPY30_SDC1 cd22965
dimerization/docking (D/D) domain found in the DPY30/SDC1 family; This family includes DPY30 ...
 152-205 4.72e-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: 36.25  E-value: 4.72e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2037976975  152 ARAYLLDKLLPTLILGIEKLLMEaerRdltekneanPNfNPLNYLAQYLMRNNP 205
Cdd:cd22965      1 TRQYLDKTVVPVLLEGLKELAKE---R---------PE-DPLEFLAEYLLKNSP 41
PTZ00121 PTZ00121
MAEBL; Provisional
 553-813 5.02e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.67  E-value: 5.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  553 ATGDEGSKESVEKEGGEDTKEGEATLVDENNAKEATDNsnKETADDTNTRVEENKDS-ETQDSAEQQVESEPAKEESASG 631
Cdd:PTZ00121  1366 AEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEED--KKKADELKKAAAAKKKAdEAKKKAEEKKKADEAKKKAEEA 1443

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  632 AGTGSDDKPVETTEGKETTKPEEATEVTAKEDTPRAEEASSAEEEKMKdgggdevlmatetviqenlvpddAQKPVEESE 711
Cdd:PTZ00121  1444 KKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKK-----------------------AEEAKKKAD 1500

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2037976975  712 QAEKTAEPVKSEDPAAPVAEtaegtAETAEPQSKEQEPTSTDEGATAAEV-TAPEVTPGETMSGdavPAEIAGGEKEKTE 790
Cdd:PTZ00121  1501 EAKKAAEAKKKADEAKKAEE-----AKKADEAKKAEEAKKADEAKKAEEKkKADELKKAEELKK---AEEKKKAEEAKKA 1572

                          250       260
                   ....*....|....*....|...
gi 2037976975  791 EGTRDQAAPGAEETQAGEDKLDE 813
Cdd:PTZ00121  1573 EEDKNMALRKAEEAKKAEEARIE 1595
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 941-1003 5.49e-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: 5.49e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2037976975  941 MVDQLFDKWDNDGSGYLDLEEFHSIMAKFKDNMESRIMAKAKQKLEKEElDNRLSKPEFKAYI 1003
Cdd:cd00051      1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDG-DGKIDFEEFLELM 62
EF-hand_6 pfam13405
EF-hand domain;
944-969 6.46e-03

EF-hand domain;


Pssm-ID: 463869 [Multi-domain]  Cd Length: 30  Bit Score: 35.62  E-value: 6.46e-03
                           10        20
                   ....*....|....*....|....*.
gi 2037976975  944 QLFDKWDNDGSGYLDLEEFHSIMAKF 969
Cdd:pfam13405    4 EAFKLFDKDGDGKISLEELRKALRSL 29
DD_AK7 cd22967
dimerization/docking (D/D) domain found in adenylate kinase 7 and similar proteins; Adenylate ...
 153-204 6.78e-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: 6.78e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2037976975  153 RAYLLDKLLPTLILGiekllmeaerrdLTEKNEANPNfNPLNYLAQYLMRNN 204
Cdd:cd22967      3 RNYLMKYVMPTLTEG------------LVEVCKVRPE-DPVDFLAEYLFKHN 41
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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