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Conserved domains on  [gi|922580217|ref|NP_001254880|]
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ANK_REP_REGION domain-containing protein [Caenorhabditis elegans]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DD_DYDC-like cd22966
dimerization/docking (D/D) domain found in the DPY30 domain-containing protein (DYDC)-like ...
 657-693 3.84e-14

dimerization/docking (D/D) domain found in the DPY30 domain-containing protein (DYDC)-like family; The DYDC-like family includes DYDC1 and DYDC2, as well as Chlamydomonas reinhardtii flagellar radial spoke protein 2 (RSP2) and similar proteins. DYDC1 plays a crucial role during acrosome biogenesis. RSP2 is a calmodulin binding spoke stalk protein required for motility in Chlamydomonas reinhardtii. It binds calmodulin in a calcium-dependent manner. Members of this family contain an N-terminal domain that shows high sequence similarity to the dimerization/docking (D/D) domain of protein DPY-30/SDC1.


:

Pssm-ID: 438535  Cd Length: 44  Bit Score: 66.63  E-value: 3.84e-14
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 922580217 657 YLARTVAPVLTKALAEVLLRRPADPIGFIAEWLSKYV 693
Cdd:cd22966    4 YLKETVGDVLTKALAEVALKRPADPIEFLANWLLKYR 40
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
84-189 2.59e-13

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 71.14  E-value: 2.59e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580217  84 DAIHKAVEEGDVRRVKSLIDRPLLSTARDNYGMTPIHKALLHGQTNTVRFLLGRFPScVNATDHAGRTPLHYAAADPNGE 163
Cdd:COG0666   89 TLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGAD-VNAQDNDGNTPLHLAAANGNLE 167

                         90       100
                 ....*....|....*....|....*.
gi 922580217 164 hMIKVLQKSGGDAFIEDKHGHTPFYY 189
Cdd:COG0666  168 -IVKLLLEAGADVNARDNDGETPLHL 192
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
280-416 1.41e-12

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 68.83  E-value: 1.41e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580217 280 IHKAVETGNLRAVKLLTDRKKLSLCRDTRGLSPLHKAIVFERTDIAKYLIRNYPQsVNAMDQKKRTPLHYAAAlkdGGYL 359
Cdd:COG0666  124 LHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGAD-VNARDNDGETPLHLAAE---NGHL 199

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 922580217 360 Y--KVMRKSGADPNIYDCNGRPAKYYLKHTGEIDLSAMRLDTRAALKQVLHNRVAPSYL 416
Cdd:COG0666  200 EivKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLL 258
Ank_2 pfam12796
Ankyrin repeats (3 copies);
471-565 6.70e-12

Ankyrin repeats (3 copies);


:

Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 62.06  E-value: 6.70e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580217  471 IHKSIKEGNLDKVKELMKTKKLAIARDRFGCTPLHSAVVHEHTEIVRYIAGHYNsvLNAPDYNkRTAMHYAAAArdgGHY 550
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNG-RTALHYAARS---GHL 74

                          90
                  ....*....|....*..
gi 922580217  551 --LKILGKAGADPMAVD 565
Cdd:pfam12796  75 eiVKLLLEKGADINVKD 91
PTZ00322 super family cl31426
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 528-633 4.46e-03

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


The actual alignment was detected with superfamily member PTZ00322:

Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 40.27  E-value: 4.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580217 528 NAPDYNKRTAMHYAAAArdgGHY--LKILGKAGADPMAVDNEGRTPdyyrrnavIDLKLIKDRDEDFETINEEYLEDGPL 605
Cdd:PTZ00322 109 NCRDYDGRTPLHIACAN---GHVqvVRVLLEFGADPTLLDKDGKTP--------LELAEENGFREVVQLLSRHSQCHFEL 177

                         90       100       110
                 ....*....|....*....|....*....|
gi 922580217 606 iDSPATPDS--GSEGSFIDSARMLDDEDES 633
Cdd:PTZ00322 178 -GANAKPDSftGKPPSLEDSPISSHHPDFS 206
 
Name Accession Description Interval E-value
DD_DYDC-like cd22966
dimerization/docking (D/D) domain found in the DPY30 domain-containing protein (DYDC)-like ...
 657-693 3.84e-14

dimerization/docking (D/D) domain found in the DPY30 domain-containing protein (DYDC)-like family; The DYDC-like family includes DYDC1 and DYDC2, as well as Chlamydomonas reinhardtii flagellar radial spoke protein 2 (RSP2) and similar proteins. DYDC1 plays a crucial role during acrosome biogenesis. RSP2 is a calmodulin binding spoke stalk protein required for motility in Chlamydomonas reinhardtii. It binds calmodulin in a calcium-dependent manner. Members of this family contain an N-terminal domain that shows high sequence similarity to the dimerization/docking (D/D) domain of protein DPY-30/SDC1.


Pssm-ID: 438535  Cd Length: 44  Bit Score: 66.63  E-value: 3.84e-14
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 922580217 657 YLARTVAPVLTKALAEVLLRRPADPIGFIAEWLSKYV 693
Cdd:cd22966    4 YLKETVGDVLTKALAEVALKRPADPIEFLANWLLKYR 40
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
84-189 2.59e-13

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 71.14  E-value: 2.59e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580217  84 DAIHKAVEEGDVRRVKSLIDRPLLSTARDNYGMTPIHKALLHGQTNTVRFLLGRFPScVNATDHAGRTPLHYAAADPNGE 163
Cdd:COG0666   89 TLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGAD-VNAQDNDGNTPLHLAAANGNLE 167

                         90       100
                 ....*....|....*....|....*.
gi 922580217 164 hMIKVLQKSGGDAFIEDKHGHTPFYY 189
Cdd:COG0666  168 -IVKLLLEAGADVNARDNDGETPLHL 192
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
280-416 1.41e-12

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 68.83  E-value: 1.41e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580217 280 IHKAVETGNLRAVKLLTDRKKLSLCRDTRGLSPLHKAIVFERTDIAKYLIRNYPQsVNAMDQKKRTPLHYAAAlkdGGYL 359
Cdd:COG0666  124 LHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGAD-VNARDNDGETPLHLAAE---NGHL 199

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 922580217 360 Y--KVMRKSGADPNIYDCNGRPAKYYLKHTGEIDLSAMRLDTRAALKQVLHNRVAPSYL 416
Cdd:COG0666  200 EivKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLL 258
Ank_2 pfam12796
Ankyrin repeats (3 copies);
471-565 6.70e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 62.06  E-value: 6.70e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580217  471 IHKSIKEGNLDKVKELMKTKKLAIARDRFGCTPLHSAVVHEHTEIVRYIAGHYNsvLNAPDYNkRTAMHYAAAArdgGHY 550
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNG-RTALHYAARS---GHL 74

                          90
                  ....*....|....*..
gi 922580217  551 --LKILGKAGADPMAVD 565
Cdd:pfam12796  75 eiVKLLLEKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
456-571 6.95e-12

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 66.90  E-value: 6.95e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580217 456 AFLDRLPDYMDKIDGIHKSIKEGNLDKVKELMKTKKLAIARDRFGCTPLHSAVVHEHTEIVRYIAGHyNSVLNAPDYNKR 535
Cdd:COG0666   76 AGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA-GADVNAQDNDGN 154

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 922580217 536 TAMHYAAAArdgGHY--LKILGKAGADPMAVDNEGRTP 571
Cdd:COG0666  155 TPLHLAAAN---GNLeiVKLLLEAGADVNARDNDGETP 189
Ank_2 pfam12796
Ankyrin repeats (3 copies);
86-180 1.20e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 61.29  E-value: 1.20e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580217   86 IHKAVEEGDVRRVKSLIDRPLLSTARDNYGMTPIHKALLHGQTNTVRFLLGRFpsCVNATDHaGRTPLHYAAAdpNGEH- 164
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA--DVNLKDN-GRTALHYAAR--SGHLe 75

                          90
                  ....*....|....*.
gi 922580217  165 MIKVLQKSGGDAFIED 180
Cdd:pfam12796  76 IVKLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
280-374 1.11e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 58.59  E-value: 1.11e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580217  280 IHKAVETGNLRAVKLLTDRKKLSLCRDTRGLSPLHKAIVFERTDIAKYLIRNYPQSvnaMDQKKRTPLHYAAALKDGGYL 359
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVN---LKDNGRTALHYAARSGHLEIV 77

                          90
                  ....*....|....*
gi 922580217  360 yKVMRKSGADPNIYD 374
Cdd:pfam12796  78 -KLLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 64-378 5.20e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 62.35  E-value: 5.20e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580217  64 TVNASSNEFLSGLTQYLtkidaiHKAVEEgDVRRVKSLIDRPLLSTARDNYGMTPIHKALLHGQT-NTVRFLLGRFPScV 142
Cdd:PHA03095  39 DVNFRGEYGKTPLHLYL------HYSSEK-VKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIKAGAD-V 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580217 143 NATDHAGRTPLHYAAADPN-GEHMIKVLQKSGGDAFIEDKHGHTPFyyrthgqrlnvrsmkdnavmnqlisgqlsrpllq 221
Cdd:PHA03095 111 NAKDKVGRTPLHVYLSGFNiNPKVIRLLLRKGADVNALDLYGMTPL---------------------------------- 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580217 222 dleeDIYDWIHTGNIGKLEELVLTGyADLllgrnHEVDDadsigFLEVLPQYQAkiQSIHKavetgNLRAVKLLTDRKKL 301
Cdd:PHA03095 157 ----AVLLKSRNANVELLRLLIDAG-ADV-----YAVDD-----RFRSLLHHHL--QSFKP-----RARIVRELIRAGCD 214

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580217 302 SLCRDTRGLSPLHKAIVF---ERTDIAKYLIRNYpqSVNAMDQKKRTPLHYAAALKDGGYLYKVMrKSGADPNIYDCNGR 378
Cdd:PHA03095 215 PAATDMLGNTPLHSMATGsscKRSLVLPLLIAGI--SINARNRYGQTPLHYAAVFNNPRACRRLI-ALGADINAVSSDGN 291
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 86-186 1.71e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 57.28  E-value: 1.71e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580217  86 IHKAVEEGDVRRVKSLIDRPLLSTARDNYGMTPIHKALLHGQTnTVRFLLGRfpSCVNATDHAGRTPLHYAAADPNGEHM 165
Cdd:PHA02874 194 LHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRS-AIELLINN--ASINDQDIDGSTPLHHAINPPCDIDI 270

                         90       100
                 ....*....|....*....|.
gi 922580217 166 IKVLQKSGGDAFIEDKHGHTP 186
Cdd:PHA02874 271 IDILLYHKADISIKDNKGENP 291
Dpy-30 pfam05186
Dpy-30 motif; This motif is found in a wide variety of domain contexts. It is found in the ...
 657-692 2.62e-08

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: 50.30  E-value: 2.62e-08
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 922580217  657 YLARTVAPVLTKALAEVLLRRPADPIGFIAEWLSKY 692
Cdd:pfam05186   5 YLNKTVAPILLQGLTELAKERPEDPIEYLADYLLKN 40
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 280-411 1.69e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 54.20  E-value: 1.69e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580217 280 IHKAVETGNLRAVKLLTDRKKLSLCRDTRGLSPLHKAIVFERTDIaKYLIRNypQSVNAMDQKKRTPLHYAAALKDGGYL 359
Cdd:PHA02874 194 LHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAI-ELLINN--ASINDQDIDGSTPLHHAINPPCDIDI 270

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 922580217 360 YKVMRKSGADPNIYDCNGRpakyylkhtGEIDLSAMRLDTRAALKQVLHNRV 411
Cdd:PHA02874 271 IDILLYHKADISIKDNKGE---------NPIDTAFKYINKDPVIKDIIANAV 313
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 471-594 7.39e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 48.81  E-value: 7.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580217 471 IHKSIKEGNLDKVKELMKTKKLAIARDRFGCTPLHSAVVHEHTEIVRYIA--GHYnsvLNAPDYNKRTAMHYAAaarDGG 548
Cdd:PHA02874 128 LHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLekGAY---ANVKDNNGESPLHNAA---EYG 201

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 922580217 549 HY--LKILGKAGADPMAVDNEGRTPDY----YRRNAV---IDLKLIKDRDEDFET 594
Cdd:PHA02874 202 DYacIKLLIDHGNHIMNKCKNGFTPLHnaiiHNRSAIellINNASINDQDIDGST 256
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 89-192 9.20e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 42.31  E-value: 9.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580217  89 AVEEGDVRRVKSLIDRPllST---ARDNYGMTPIHKALLHGQTNTVRFLLGRFPSCVN--ATD--HAGRTPLHYAAADPN 161
Cdd:cd22192   24 AAKENDVQAIKKLLKCP--SCdlfQRGALGETALHVAALYDNLEAAVVLMEAAPELVNepMTSdlYQGETALHIAVVNQN 101

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 922580217 162 gEHMIKVLQKSGGD---------AFIedKHGHTPFYYRTH 192
Cdd:cd22192  102 -LNLVRELIARGADvvspratgtFFR--PGPKNLIYYGEH 138
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 528-633 4.46e-03

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 40.27  E-value: 4.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580217 528 NAPDYNKRTAMHYAAAArdgGHY--LKILGKAGADPMAVDNEGRTPdyyrrnavIDLKLIKDRDEDFETINEEYLEDGPL 605
Cdd:PTZ00322 109 NCRDYDGRTPLHIACAN---GHVqvVRVLLEFGADPTLLDKDGKTP--------LELAEENGFREVVQLLSRHSQCHFEL 177

                         90       100       110
                 ....*....|....*....|....*....|
gi 922580217 606 iDSPATPDS--GSEGSFIDSARMLDDEDES 633
Cdd:PTZ00322 178 -GANAKPDSftGKPPSLEDSPISSHHPDFS 206
 
Name Accession Description Interval E-value
DD_DYDC-like cd22966
dimerization/docking (D/D) domain found in the DPY30 domain-containing protein (DYDC)-like ...
 657-693 3.84e-14

dimerization/docking (D/D) domain found in the DPY30 domain-containing protein (DYDC)-like family; The DYDC-like family includes DYDC1 and DYDC2, as well as Chlamydomonas reinhardtii flagellar radial spoke protein 2 (RSP2) and similar proteins. DYDC1 plays a crucial role during acrosome biogenesis. RSP2 is a calmodulin binding spoke stalk protein required for motility in Chlamydomonas reinhardtii. It binds calmodulin in a calcium-dependent manner. Members of this family contain an N-terminal domain that shows high sequence similarity to the dimerization/docking (D/D) domain of protein DPY-30/SDC1.


Pssm-ID: 438535  Cd Length: 44  Bit Score: 66.63  E-value: 3.84e-14
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 922580217 657 YLARTVAPVLTKALAEVLLRRPADPIGFIAEWLSKYV 693
Cdd:cd22966    4 YLKETVGDVLTKALAEVALKRPADPIEFLANWLLKYR 40
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
84-189 2.59e-13

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 71.14  E-value: 2.59e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580217  84 DAIHKAVEEGDVRRVKSLIDRPLLSTARDNYGMTPIHKALLHGQTNTVRFLLGRFPScVNATDHAGRTPLHYAAADPNGE 163
Cdd:COG0666   89 TLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGAD-VNAQDNDGNTPLHLAAANGNLE 167

                         90       100
                 ....*....|....*....|....*.
gi 922580217 164 hMIKVLQKSGGDAFIEDKHGHTPFYY 189
Cdd:COG0666  168 -IVKLLLEAGADVNARDNDGETPLHL 192
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
83-410 4.50e-13

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 70.37  E-value: 4.50e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580217  83 IDAIHKAVEEGDVRRVKSLIDRPLLSTARDNYGMTPIHKALLHGQTNTVRFLLGRFPScVNATDHAGRTPLHYAAADPNG 162
Cdd:COG0666   55 ALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGAD-VNARDKDGETPLHLAAYNGNL 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580217 163 EhMIKVLQKSGGDAFIEDKHGHTPFyyrthgqrlnvrsmkdnavmnqlisgqlsrpllqdleediydwihtgnigkleel 242
Cdd:COG0666  134 E-IVKLLLEAGADVNAQDNDGNTPL------------------------------------------------------- 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580217 243 vltgyadlllgrnhevddadsigflevlpqyqakiqsiHKAVETGNLRAVKLLTDRKKLSLCRDTRGLSPLHKAIVFERT 322
Cdd:COG0666  158 --------------------------------------HLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHL 199

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580217 323 DIAKYLIRNYPqSVNAMDQKKRTPLHYAAALKDGGYLyKVMRKSGADPNIYDCNGRPAKYYLKHTGEIDLSAMRLDTRAA 402
Cdd:COG0666  200 EIVKLLLEAGA-DVNAKDNDGKTALDLAAENGNLEIV-KLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLL 277


                 ....*...
gi 922580217 403 LKQVLHNR 410
Cdd:COG0666  278 LAAALLDL 285
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
280-416 1.41e-12

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 68.83  E-value: 1.41e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580217 280 IHKAVETGNLRAVKLLTDRKKLSLCRDTRGLSPLHKAIVFERTDIAKYLIRNYPQsVNAMDQKKRTPLHYAAAlkdGGYL 359
Cdd:COG0666  124 LHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGAD-VNARDNDGETPLHLAAE---NGHL 199

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 922580217 360 Y--KVMRKSGADPNIYDCNGRPAKYYLKHTGEIDLSAMRLDTRAALKQVLHNRVAPSYL 416
Cdd:COG0666  200 EivKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLL 258
Ank_2 pfam12796
Ankyrin repeats (3 copies);
471-565 6.70e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 62.06  E-value: 6.70e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580217  471 IHKSIKEGNLDKVKELMKTKKLAIARDRFGCTPLHSAVVHEHTEIVRYIAGHYNsvLNAPDYNkRTAMHYAAAArdgGHY 550
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNG-RTALHYAARS---GHL 74

                          90
                  ....*....|....*..
gi 922580217  551 --LKILGKAGADPMAVD 565
Cdd:pfam12796  75 eiVKLLLEKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
456-571 6.95e-12

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 66.90  E-value: 6.95e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580217 456 AFLDRLPDYMDKIDGIHKSIKEGNLDKVKELMKTKKLAIARDRFGCTPLHSAVVHEHTEIVRYIAGHyNSVLNAPDYNKR 535
Cdd:COG0666   76 AGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA-GADVNAQDNDGN 154

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 922580217 536 TAMHYAAAArdgGHY--LKILGKAGADPMAVDNEGRTP 571
Cdd:COG0666  155 TPLHLAAAN---GNLeiVKLLLEAGADVNARDNDGETP 189
Ank_2 pfam12796
Ankyrin repeats (3 copies);
86-180 1.20e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 61.29  E-value: 1.20e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580217   86 IHKAVEEGDVRRVKSLIDRPLLSTARDNYGMTPIHKALLHGQTNTVRFLLGRFpsCVNATDHaGRTPLHYAAAdpNGEH- 164
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA--DVNLKDN-GRTALHYAAR--SGHLe 75

                          90
                  ....*....|....*.
gi 922580217  165 MIKVLQKSGGDAFIED 180
Cdd:pfam12796  76 IVKLLLEKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
235-596 3.66e-11

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 64.59  E-value: 3.66e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580217 235 NIGKLEELVLTGYADLLLGRNHEVDDADSIGFLEVLPQYQAKIQSIHKAVETGNLRAVKLLTDRKKLSLCRDTRGLSPLH 314
Cdd:COG0666   13 AALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLH 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580217 315 KAIVFERTDIAKYLIRNYPqSVNAMDQKKRTPLHYAAALKDggylYKVMR---KSGADPNIYDCNGRPAkyylkhtgeid 391
Cdd:COG0666   93 AAARNGDLEIVKLLLEAGA-DVNARDKDGETPLHLAAYNGN----LEIVKlllEAGADVNAQDNDGNTP----------- 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580217 392 lsamrldtraalkqvlhnrvapsylessiqqwlrdgqlakleqlvlsgcgdllqsrtsthtetqafldrlpdymdkidgI 471
Cdd:COG0666  157 -------------------------------------------------------------------------------L 157

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580217 472 HKSIKEGNLDKVKELMKTKKLAIARDRFGCTPLHSAVVHEHTEIVRYIAGHyNSVLNAPDYNKRTAMHYAAAARDGGHyL 551
Cdd:COG0666  158 HLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEA-GADVNAKDNDGKTALDLAAENGNLEI-V 235

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 922580217 552 KILGKAGADPMAVDNEGRTPDYYRRNAVIDLKLIKDRDEDFETIN 596
Cdd:COG0666  236 KLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAA 280
Ank_2 pfam12796
Ankyrin repeats (3 copies);
280-374 1.11e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 58.59  E-value: 1.11e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580217  280 IHKAVETGNLRAVKLLTDRKKLSLCRDTRGLSPLHKAIVFERTDIAKYLIRNYPQSvnaMDQKKRTPLHYAAALKDGGYL 359
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVN---LKDNGRTALHYAARSGHLEIV 77

                          90
                  ....*....|....*
gi 922580217  360 yKVMRKSGADPNIYD 374
Cdd:pfam12796  78 -KLLLEKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
201-570 4.28e-10

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 61.51  E-value: 4.28e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580217 201 MKDNAVMNQLISGQLSRPLLQDLEEDIYDWIHTGNIGKLEELVLTGYADLLLGRNHEVDDADSIGFLEVLPQYQAKIQSI 280
Cdd:COG0666   12 LAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLL 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580217 281 HKAVETGNLRAVKLLTDRKKLSLCRDTRGLSPLHKAIVFERTDIAKYLIRNYPqSVNAMDQKKRTPLHYAAALKDggylY 360
Cdd:COG0666   92 HAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGA-DVNAQDNDGNTPLHLAAANGN----L 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580217 361 KVMR---KSGADPNIYDCNGRPAkyylkhtgeidlsamrldtraalkqvlhnrvapsylessiqqwlrdgqlakleqlvl 437
Cdd:COG0666  167 EIVKlllEAGADVNARDNDGETP--------------------------------------------------------- 189

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580217 438 sgcgdllqsrtsthtetqafldrlpdymdkidgIHKSIKEGNLDKVKELMKTKKLAIARDRFGCTPLHSAVVHEHTEIVR 517
Cdd:COG0666  190 ---------------------------------LHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVK 236

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 922580217 518 YIAGHYNSVlNAPDYNKRTAMHYAAAARDGGHYLKILGKAGADPMAVDNEGRT 570
Cdd:COG0666  237 LLLEAGADL-NAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
PHA03095 PHA03095
ankyrin-like protein; Provisional
 64-378 5.20e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 62.35  E-value: 5.20e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580217  64 TVNASSNEFLSGLTQYLtkidaiHKAVEEgDVRRVKSLIDRPLLSTARDNYGMTPIHKALLHGQT-NTVRFLLGRFPScV 142
Cdd:PHA03095  39 DVNFRGEYGKTPLHLYL------HYSSEK-VKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIKAGAD-V 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580217 143 NATDHAGRTPLHYAAADPN-GEHMIKVLQKSGGDAFIEDKHGHTPFyyrthgqrlnvrsmkdnavmnqlisgqlsrpllq 221
Cdd:PHA03095 111 NAKDKVGRTPLHVYLSGFNiNPKVIRLLLRKGADVNALDLYGMTPL---------------------------------- 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580217 222 dleeDIYDWIHTGNIGKLEELVLTGyADLllgrnHEVDDadsigFLEVLPQYQAkiQSIHKavetgNLRAVKLLTDRKKL 301
Cdd:PHA03095 157 ----AVLLKSRNANVELLRLLIDAG-ADV-----YAVDD-----RFRSLLHHHL--QSFKP-----RARIVRELIRAGCD 214

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580217 302 SLCRDTRGLSPLHKAIVF---ERTDIAKYLIRNYpqSVNAMDQKKRTPLHYAAALKDGGYLYKVMrKSGADPNIYDCNGR 378
Cdd:PHA03095 215 PAATDMLGNTPLHSMATGsscKRSLVLPLLIAGI--SINARNRYGQTPLHYAAVFNNPRACRRLI-ALGADINAVSSDGN 291
DD_DPY30_SDC1-like cd22958
dimerization/docking (D/D) domain found in the DPY30/SDC1-like family; The DPY30/SDC1-like ...
 657-689 4.41e-09

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: 52.45  E-value: 4.41e-09
                         10        20        30
                 ....*....|....*....|....*....|...
gi 922580217 657 YLARTVAPVLTKALAEVLLRRPADPIGFIAEWL 689
Cdd:cd22958    4 YLSETVLPTLIPALAELLKARPEDPLEWLAEYL 36
PHA03095 PHA03095
ankyrin-like protein; Provisional
 305-571 8.38e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 58.50  E-value: 8.38e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580217 305 RDTRGLSPLHKAIVFERT-DIAKYLIRnYPQSVNAMDQKKRTPLHYaaalkdggYL------YKVMR---KSGADPNIYD 374
Cdd:PHA03095  79 PERCGFTPLHLYLYNATTlDVIKLLIK-AGADVNAKDKVGRTPLHV--------YLsgfninPKVIRlllRKGADVNALD 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580217 375 CNGR-PAKYYLKHTGeIDLSAMRLdtraalkqvlhnrvapsylessiqqwlrdgqlakleqLVLSGCGDllqsrtsthTE 453
Cdd:PHA03095 150 LYGMtPLAVLLKSRN-ANVELLRL-------------------------------------LIDAGADV---------YA 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580217 454 TQAFLDRLPDYmdkidgiHK-SIKEGNlDKVKELMKTKKLAIARDRFGCTPLHSAVVH---EHTEIVRYIAGhyNSVLNA 529
Cdd:PHA03095 183 VDDRFRSLLHH-------HLqSFKPRA-RIVRELIRAGCDPAATDMLGNTPLHSMATGsscKRSLVLPLLIA--GISINA 252

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 922580217 530 PDYNKRTAMHYAAAARDGGHYLKILgKAGADPMAVDNEGRTP 571
Cdd:PHA03095 253 RNRYGQTPLHYAAVFNNPRACRRLI-ALGADINAVSSDGNTP 293
DD_AK7 cd22967
dimerization/docking (D/D) domain found in adenylate kinase 7 and similar proteins; Adenylate ...
 657-692 1.05e-08

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: 51.33  E-value: 1.05e-08
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 922580217 657 YLARTVAPVLTKALAEVLLRRPADPIGFIAEWLSKY 692
Cdd:cd22967    5 YLMKYVMPTLTEGLVEVCKVRPEDPVDFLAEYLFKH 40
DD_NDKH5-like cd22970
dimerization/docking (D/D) domain found in nucleoside diphosphate kinase homolog 5 (NDKH5) ...
 657-689 1.16e-08

dimerization/docking (D/D) domain found in nucleoside diphosphate kinase homolog 5 (NDKH5)-like family; The NDKH5 family includes NDKH5, Chlamydomonas reinhardtii flagellar radial spoke protein 23 (RSP23) and similar proteins. 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. 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 C-terminal domain that shows high sequence similarity to the dimerization/docking (D/D) domain of protein DPY-30/SDC1.


Pssm-ID: 438539  Cd Length: 45  Bit Score: 51.38  E-value: 1.16e-08
                         10        20        30
                 ....*....|....*....|....*....|...
gi 922580217 657 YLARTVAPVLTKALAEVLLRRPADPIGFIAEWL 689
Cdd:cd22970    8 YLSKHVNPTLLKGLTELCKEKPADPVTWLADWL 40
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 86-186 1.71e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 57.28  E-value: 1.71e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580217  86 IHKAVEEGDVRRVKSLIDRPLLSTARDNYGMTPIHKALLHGQTnTVRFLLGRfpSCVNATDHAGRTPLHYAAADPNGEHM 165
Cdd:PHA02874 194 LHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRS-AIELLINN--ASINDQDIDGSTPLHHAINPPCDIDI 270

                         90       100
                 ....*....|....*....|.
gi 922580217 166 IKVLQKSGGDAFIEDKHGHTP 186
Cdd:PHA02874 271 IDILLYHKADISIKDNKGENP 291
Dpy-30 pfam05186
Dpy-30 motif; This motif is found in a wide variety of domain contexts. It is found in the ...
 657-692 2.62e-08

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: 50.30  E-value: 2.62e-08
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 922580217  657 YLARTVAPVLTKALAEVLLRRPADPIGFIAEWLSKY 692
Cdd:pfam05186   5 YLNKTVAPILLQGLTELAKERPEDPIEYLADYLLKN 40
Ank_4 pfam13637
Ankyrin repeats (many copies);
84-135 7.51e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.20  E-value: 7.51e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 922580217   84 DAIHKAVEEGDVRRVKSLIDRPLLSTARDNYGMTPIHKALLHGQTNTVRFLL 135
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 118-372 1.06e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 54.89  E-value: 1.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580217 118 PIHKALLHGQTNTVRFLLGRFPScVNATDHAGRTPLHYAAADPNGEHMIKVL-QKSGGDAFIEDKHGHTPFYYRthgqrl 196
Cdd:PHA02878  40 PLHQAVEARNLDVVKSLLTRGHN-VNQPDHRDLTPLHIICKEPNKLGMKEMIrSINKCSVFYTLVAIKDAFNNR------ 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580217 197 NVRSMKdnAVMNQLISGQLSRPLLQDLEEDIYDWIHTgnigKLEELVLTGYADLLLGRNHEVDDAdsigflevlpqyqak 276
Cdd:PHA02878 113 NVEIFK--IILTNRYKNIQTIDLVYIDKKSKDDIIEA----EITKLLLSYGADINMKDRHKGNTA--------------- 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580217 277 iqsIHKAVETGNLRAVKLLTDRKKLSLCRDTRGLSPLHKAIVFERTDIAKYLIRNyPQSVNAMDQKKRTPLHYAAALKDG 356
Cdd:PHA02878 172 ---LHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLEN-GASTDARDKCGNTPLHISVGYCKD 247

                        250
                 ....*....|....*.
gi 922580217 357 GYLYKVMRKSGADPNI 372
Cdd:PHA02878 248 YDILKLLLEHGVDVNA 263
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 280-411 1.69e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 54.20  E-value: 1.69e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580217 280 IHKAVETGNLRAVKLLTDRKKLSLCRDTRGLSPLHKAIVFERTDIaKYLIRNypQSVNAMDQKKRTPLHYAAALKDGGYL 359
Cdd:PHA02874 194 LHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAI-ELLINN--ASINDQDIDGSTPLHHAINPPCDIDI 270

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 922580217 360 YKVMRKSGADPNIYDCNGRpakyylkhtGEIDLSAMRLDTRAALKQVLHNRV 411
Cdd:PHA02874 271 IDILLYHKADISIKDNKGE---------NPIDTAFKYINKDPVIKDIIANAV 313
DD_CrRSP2-like cd22982
dimerization/docking (D/D) domain found in Chlamydomonas reinhardtii flagellar radial spoke ...
 657-693 1.88e-07

dimerization/docking (D/D) domain found in Chlamydomonas reinhardtii flagellar radial spoke protein 2 (RSP2) and similar proteins; Flagellar radial spokes contribute to the regulation of dynein arm activity and thus the pattern of flagellar bending. They consist of a thin stalk, which is attached to the a subfiber of the outer doublet microtubule, and a bulbous head, which is attached to the stalk and appears to interact with the projections from the central pair of microtubules. RSP2 is a calmodulin binding spoke stalk protein required for motility in Chlamydomonas reinhardtii. It binds calmodulin in a calcium-dependent manner. This model corresponds to the C-terminal domain of RSP2, which shows high sequence similarity to the dimerization/docking (D/D) domain of protein DPY-30/SDC1.


Pssm-ID: 438551  Cd Length: 53  Bit Score: 48.13  E-value: 1.88e-07
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 922580217 657 YLARTVAPVLTKALAEVLLRRPADPIGFIAEWLSKYV 693
Cdd:cd22982    4 YLKETVGEALAKGCAAVALAQPEDPVEYLGLWLLQHV 40
DD_DPY30_SDC1 cd22965
dimerization/docking (D/D) domain found in the DPY30/SDC1 family; This family includes DPY30 ...
 657-692 3.47e-07

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: 47.03  E-value: 3.47e-07
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 922580217 657 YLARTVAPVLTKALAEVLLRRPADPIGFIAEWLSKY 692
Cdd:cd22965    4 YLDKTVVPVLLEGLKELAKERPEDPLEFLAEYLLKN 39
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 97-307 1.96e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 50.82  E-value: 1.96e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580217  97 RVKSLIDRPLLSTARDNYGMTPIHKALLHGQTNTVRFLL--GRFPscvNATDHAGRTPLHYAAADPNGEhMIKVLQKSGG 174
Cdd:PHA03100 174 RVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLdlGANP---NLVNKYGDTPLHIAILNNNKE-IFKLLLNNGP 249

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580217 175 DAFIEDKH----GHTPFYYRTHGQRLnvrsMKDNAVMNQLISGQLSRPLLQDLEEDIYDWIHT--GNIGKLEELVLTGYA 248
Cdd:PHA03100 250 SIKTIIETllyfKDKDLNTITKIKML----KKSIMYMFLLDPGFYKNRKLIENSKSLKDVINEceKEIERMKEIKLNKVT 325

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 922580217 249 --DLLLGRNHE-----VDDADSIGFLEvLPQYQAKIQ-SIHKAVEtgnlRAVKLLTDRKKL-SLCRDT 307
Cdd:PHA03100 326 vyDIIFNKNINflsryVNNKSVTKYTT-SKIYGKYIKkVINKAIE----RKKLIKKIIKKLnNLCKNT 388
Ank_4 pfam13637
Ankyrin repeats (many copies);
115-169 3.21e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.57  E-value: 3.21e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 922580217  115 GMTPIHKALLHGQTNTVRFLLGrFPSCVNATDHAGRTPLHYAAAdpNG-EHMIKVL 169
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLE-KGADINAVDGNGETALHFAAS--NGnVEVLKLL 53
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 471-594 7.39e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 48.81  E-value: 7.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580217 471 IHKSIKEGNLDKVKELMKTKKLAIARDRFGCTPLHSAVVHEHTEIVRYIA--GHYnsvLNAPDYNKRTAMHYAAaarDGG 548
Cdd:PHA02874 128 LHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLekGAY---ANVKDNNGESPLHNAA---EYG 201

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 922580217 549 HY--LKILGKAGADPMAVDNEGRTPDY----YRRNAV---IDLKLIKDRDEDFET 594
Cdd:PHA02874 202 DYacIKLLIDHGNHIMNKCKNGFTPLHnaiiHNRSAIellINNASINDQDIDGST 256
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 86-189 8.01e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 48.83  E-value: 8.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580217  86 IHKAVEEGDVRRVKSLIDrplLSTARDNY----GMTPIHKALLHGQTNTVRFLLGRFPSC-VNATDHAgrTPLHYA--AA 158
Cdd:PHA02875  72 LHDAVEEGDVKAVEELLD---LGKFADDVfykdGMTPLHLATILKKLDIMKLLIARGADPdIPNTDKF--SPLHLAvmMG 146

                         90       100       110
                 ....*....|....*....|....*....|.
gi 922580217 159 DPNgehMIKVLQKSGGDAFIEDKHGHTPFYY 189
Cdd:PHA02875 147 DIK---GIELLIDHKACLDIEDCCGCTPLII 174
Ank_2 pfam12796
Ankyrin repeats (3 copies);
85-146 2.12e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 43.57  E-value: 2.12e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 922580217   85 AIHKAVEEGDVRRVKSLIDRPLLStaRDNYGMTPIHKALLHGQTNTVRFLLGRFPScVNATD 146
Cdd:pfam12796  33 ALHLAAKNGHLEIVKLLLEHADVN--LKDNGRTALHYAARSGHLEIVKLLLEKGAD-INVKD 91
Ank_4 pfam13637
Ankyrin repeats (many copies);
471-518 2.14e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 42.26  E-value: 2.14e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 922580217  471 IHKSIKEGNLDKVKELMKTKKLAIARDRFGCTPLHSAVVHEHTEIVRY 518
Cdd:pfam13637   5 LHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKL 52
Ank_4 pfam13637
Ankyrin repeats (many copies);
502-546 3.56e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.88  E-value: 3.56e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 922580217  502 TPLHSAVVHEHTEIVRYIAGHYNSVlNAPDYNKRTAMHYAAAARD 546
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADI-NAVDGNGETALHFAASNGN 46
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 86-208 6.09e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 46.11  E-value: 6.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580217  86 IHKAVEEGDVRRVKSLIDRPLLSTARDNYGMTPIHKALLHGQTNTVRFLLGRfPSCVNATDHAGRTPLHYAAAdpNGEH- 164
Cdd:PHA02874 128 LHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEK-GAYANVKDNNGESPLHNAAE--YGDYa 204

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 922580217 165 MIKVLQKSGGDAFIEDKHGHTPFYYRTHGQRLNVRSMKDNAVMN 208
Cdd:PHA02874 205 CIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAIELLINNASIN 248
PHA03095 PHA03095
ankyrin-like protein; Provisional
 495-586 8.37e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 45.79  E-value: 8.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580217 495 ARDRFGCTPLHSAVVHEHTE-IVRYIAGHYNSVlNAPDYNKRTAMH-YAAAARDGGHYLKILGKAGADPMAVDNEGRTP- 571
Cdd:PHA03095  78 APERCGFTPLHLYLYNATTLdVIKLLIKAGADV-NAKDKVGRTPLHvYLSGFNINPKVIRLLLRKGADVNALDLYGMTPl 156

                         90
                 ....*....|....*
gi 922580217 572 DYYRRNAVIDLKLIK 586
Cdd:PHA03095 157 AVLLKSRNANVELLR 171
Ank_4 pfam13637
Ankyrin repeats (many copies);
280-329 1.25e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 40.34  E-value: 1.25e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 922580217  280 IHKAVETGNLRAVKLLTDRKKLSLCRDTRGLSPLHKAIVFERTDIAKYLI 329
Cdd:pfam13637   5 LHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 336-598 1.59e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 45.05  E-value: 1.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580217 336 VNAMDQKKRTPLHYAAAlKDGGYLYKVMRKSGADPNIYDCNGRPAKYYLKHTGEIDLSAMRLDTRAALKQ---VLHNRVA 412
Cdd:PHA02876 171 VNAKDIYCITPIHYAAE-RGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKndlSLLKAIR 249

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580217 413 PSYLESSiqqwlrdgqlakleqLVLSGCGDLLQS-----RTSTHTETQA-FLDRL-PDYMDK-IDGIHKSIKEG------ 478
Cdd:PHA02876 250 NEDLETS---------------LLLYDAGFSVNSiddckNTPLHHASQApSLSRLvPKLLERgADVNAKNIKGEtplylm 314

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580217 479 -----NLDKVKELMKTKKLAIARDRFGCTPLHSAVVHEHTEIVRYIAGHYNSVLNAPDYNKRTAMHYaAAARDGGHYLKI 553
Cdd:PHA02876 315 akngyDTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKDIVITLLELGANVNARDYCDKTPIHY-AAVRNNVVIINT 393

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 922580217 554 LGKAGADPMAVDNEGRTPDY---YRRNAVIDLKLIKDRDEDFETINEE 598
Cdd:PHA02876 394 LLDYGADIEALSQKIGTALHfalCGTNPYMSVKTLIDRGANVNSKNKD 441
Ank_4 pfam13637
Ankyrin repeats (many copies);
309-352 1.79e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.57  E-value: 1.79e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 922580217  309 GLSPLHKAIVFERTDIAKYLIrNYPQSVNAMDQKKRTPLHYAAA 352
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLL-EKGADINAVDGNGETALHFAAS 43
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 98-372 3.35e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 43.50  E-value: 3.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580217  98 VKSLIDR--PLLSTARDNYGMTPIHKALLHGQTNTVRF--LLGRFPSCVNATDHAGRTPLHYAAADPNGE-HMIKVLQKS 172
Cdd:PHA03100  51 VKILLDNgaDINSSTKNNSTPLHYLSNIKYNLTDVKEIvkLLLEYGANVNAPDNNGITPLLYAISKKSNSySIVEYLLDN 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580217 173 GGDAFIEDKHGHTPFYYRTHGQRLNVrsmkdnavmnqlisgqlsrpllqdleediydwihtgNIGKLeelvltgyadlLL 252
Cdd:PHA03100 131 GANVNIKNSDGENLLHLYLESNKIDL------------------------------------KILKL-----------LI 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580217 253 GRNHEVDDADSIgflEVLPQYQAKIQSihkavetgnlravklltdrkklslcRDTRGLSPLHKAIVFERTDIAKYLIrNY 332
Cdd:PHA03100 164 DKGVDINAKNRV---NYLLSYGVPINI-------------------------KDVYGFTPLHYAVYNNNPEFVKYLL-DL 214

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 922580217 333 PQSVNAMDQKKRTPLHYAAALKDgGYLYKVMRKSGADPNI 372
Cdd:PHA03100 215 GANPNLVNKYGDTPLHIAILNNN-KEIFKLLLNNGPSIKT 253
DD_CrRSP_unchar cd22964
dimerization/docking (D/D) domain of an uncharacterized subunit found in Chlamydomonas ...
 657-692 4.18e-04

dimerization/docking (D/D) domain of an uncharacterized subunit found in Chlamydomonas reinhardtii radial spoke 1; Flagellar radial spokes contribute to the regulation of dynein arm activity and thus the pattern of flagellar bending. They consist of a thin stalk, which is attached to a subfiber of the outer doublet microtubule, and a bulbous head, which is attached to the stalk and appears to interact with the projections from the central pair of microtubules. This subfamily includes an uncharacterized protein found in Chlamydomonas reinhardtii radial spoke 1. It contains a conserved domain 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: 438533  Cd Length: 46  Bit Score: 38.36  E-value: 4.18e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 922580217 657 YLARTVA-PVLTKALAEVLLRRPADPIGFIAEWLSKY 692
Cdd:cd22964    8 YLQQKVInPILEQLVTDLLQEKPEDPVPFMIQWLRKK 44
Ank_5 pfam13857
Ankyrin repeats (many copies);
104-156 4.69e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.48  E-value: 4.69e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 922580217  104 RPLLSTARDNYGMTPIHKALLHGQTNTVRFLLGRfPSCVNATDHAGRTPLHYA 156
Cdd:pfam13857   5 GPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAY-GVDLNLKDEEGLTALDLA 56
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 117-596 6.76e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 43.13  E-value: 6.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580217 117 TPIHKALLHGQTNTVRFLLGRFPSCVNATDHAGRTPLHYAAADPNGEHMIKVLQKSGgDAFIEDKHGHTPFYYRTHGQrL 196
Cdd:PHA02876  43 TAIHQALQLRQIDIVEEIIQQNPELIYITDHKCHSTLHTICIIPNVMDIVISLTLDC-DIILDIKYASIILNKHKLDE-A 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580217 197 NVRSMKDNAVMNQLISGQLSRPL--LQDLEEDIydwihtgnigKLEELVLtgyADLLLGRNHEVDDADSIGflevlpqyq 274
Cdd:PHA02876 121 CIHILKEAISGNDIHYDKINESIeyMKLIKERI----------QQDELLI---AEMLLEGGADVNAKDIYC--------- 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580217 275 akIQSIHKAVETGNLRAVKLL------------TDRKKLSLCRDTRGLSPLhKAIVFERTDIAK---------------- 326
Cdd:PHA02876 179 --ITPIHYAAERGNAKMVNLLlsygadvniialDDLSVLECAVDSKNIDTI-KAIIDNRSNINKndlsllkairnedlet 255

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580217 327 -YLIRNYPQSVNAMDQKKRTPLHYAAALKDGGYLYKVMRKSGADPNIYDCNGRPAKYYLKHTGeidlsamrLDTRaalkq 405
Cdd:PHA02876 256 sLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNG--------YDTE----- 322

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580217 406 vlhnrvapsylessiqqwlrdgqlaKLEQLVLSGCG-DLLQSRTSTHTETQAFLDRlpdymdkidgihksikegNLDKVK 484
Cdd:PHA02876 323 -------------------------NIRTLIMLGADvNAADRLYITPLHQASTLDR------------------NKDIVI 359

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580217 485 ELMKTKKLAIARDRFGCTPLHSAVVHEHTEIVRYIAgHYNSVLNAPDYNKRTAMHYAAAARDGGHYLKILGKAGADPMAV 564
Cdd:PHA02876 360 TLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLL-DYGADIEALSQKIGTALHFALCGTNPYMSVKTLIDRGANVNSK 438

                        490       500       510
                 ....*....|....*....|....*....|....*
gi 922580217 565 DNEGRTPDYY--RRNAVID-LKLIKDRDEDFETIN 596
Cdd:PHA02876 439 NKDLSTPLHYacKKNCKLDvIEMLLDNGADVNAIN 473
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 80-363 7.06e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 42.74  E-value: 7.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580217  80 LTKIDAIHKAVEEGDVRRVKSLIDRpllstaRDNYGMTPIhkALLHGQTNT---VRFLLGRFPSCVNATDHAGRTPLHYA 156
Cdd:PHA02876 209 LDDLSVLECAVDSKNIDTIKAIIDN------RSNINKNDL--SLLKAIRNEdleTSLLLYDAGFSVNSIDDCKNTPLHHA 280

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580217 157 AADPNGEHMIKVLQKSGGDAFIEDKHGHTPFYYrthgqrlnvrsMKDNAVMNQLISGQLSRPLLQDLEEDIYDW-IHTGN 235
Cdd:PHA02876 281 SQAPSLSRLVPKLLERGADVNAKNIKGETPLYL-----------MAKNGYDTENIRTLIMLGADVNAADRLYITpLHQAS 349

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580217 236 -IGKLEELVLTgyaDLLLGRNHEVDD------------ADSIGFLEVLPQYQAKIQSIHKAV---------ETGNLRAVK 293
Cdd:PHA02876 350 tLDRNKDIVIT---LLELGANVNARDycdktpihyaavRNNVVIINTLLDYGADIEALSQKIgtalhfalcGTNPYMSVK 426

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580217 294 LLTDRKKLSLCRDTRGLSPLHKAIVFE-RTDIAKYLIRNyPQSVNAMDQKKRTP--------------LHYAAALKDGGY 358
Cdd:PHA02876 427 TLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDN-GADVNAINIQNQYPllialeyhgivnilLHYGAELRDSRV 505


                 ....*
gi 922580217 359 LYKVM 363
Cdd:PHA02876 506 LHKSL 510
Ank_5 pfam13857
Ankyrin repeats (many copies);
134-187 7.52e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.10  E-value: 7.52e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 922580217  134 LLGRFPSCVNATDHAGRTPLHYAAADPNGEhMIKVLQKSGGDAFIEDKHGHTPF 187
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALE-IVRVLLAYGVDLNLKDEEGLTAL 53
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 89-192 9.20e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 42.31  E-value: 9.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580217  89 AVEEGDVRRVKSLIDRPllST---ARDNYGMTPIHKALLHGQTNTVRFLLGRFPSCVN--ATD--HAGRTPLHYAAADPN 161
Cdd:cd22192   24 AAKENDVQAIKKLLKCP--SCdlfQRGALGETALHVAALYDNLEAAVVLMEAAPELVNepMTSdlYQGETALHIAVVNQN 101

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 922580217 162 gEHMIKVLQKSGGD---------AFIedKHGHTPFYYRTH 192
Cdd:cd22192  102 -LNLVRELIARGADvvspratgtFFR--PGPKNLIYYGEH 138
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 363-541 1.30e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 41.90  E-value: 1.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580217 363 MRKSGADPNIYDCNG-RPAKYylkhtgeidlsAMRLDTRAALKQVLHNRVAPSY----LESSIQQWLRDGQLAKLEQLVL 437
Cdd:PHA02875  21 LLDIGINPNFEIYDGiSPIKL-----------AMKFRDSEAIKLLMKHGAIPDVkypdIESELHDAVEEGDVKAVEELLD 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580217 438 SG--CGDLLQSRTSTHTETQAFLDRL------------PDY--MDKIDGIHKSIKEGNLDKVKELMKTKKLAIARDRFGC 501
Cdd:PHA02875  90 LGkfADDVFYKDGMTPLHLATILKKLdimklliargadPDIpnTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGC 169

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 922580217 502 TPLHSAVVHEHTEIVRYIaghYNSVLNaPDYNKR----TAMHYA 541
Cdd:PHA02875 170 TPLIIAMAKGDIAICKML---LDSGAN-IDYFGKngcvAALCYA 209
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 471-571 3.13e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 40.63  E-value: 3.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580217 471 IHKSIKEGNLDKVKELMKTKKLAIARDRFGCTPLHSAVVH-EHTEIVRYIAGHYNSVlNAPDYNKR-TAMHYAAAARDgg 548
Cdd:PHA02878 205 LHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDV-NAKSYILGlTALHSSIKSER-- 281

                         90       100
                 ....*....|....*....|...
gi 922580217 549 hYLKILGKAGADPMAVDNEGRTP 571
Cdd:PHA02878 282 -KLKLLLEYGADINSLNSYKLTP 303
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 149-181 4.43e-03

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 35.34  E-value: 4.43e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 922580217  149 GRTPLHYAAADPNGEHMIKVLQKSGGDAFIEDK 181
Cdd:pfam00023   2 GNTPLHLAAGRRGNLEIVKLLLSKGADVNARDK 34
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 528-633 4.46e-03

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 40.27  E-value: 4.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580217 528 NAPDYNKRTAMHYAAAArdgGHY--LKILGKAGADPMAVDNEGRTPdyyrrnavIDLKLIKDRDEDFETINEEYLEDGPL 605
Cdd:PTZ00322 109 NCRDYDGRTPLHIACAN---GHVqvVRVLLEFGADPTLLDKDGKTP--------LELAEENGFREVVQLLSRHSQCHFEL 177

                         90       100       110
                 ....*....|....*....|....*....|
gi 922580217 606 iDSPATPDS--GSEGSFIDSARMLDDEDES 633
Cdd:PTZ00322 178 -GANAKPDSftGKPPSLEDSPISSHHPDFS 206
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 82-178 4.94e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 39.97  E-value: 4.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580217  82 KIDAIHKAVEEGDVRRVKSLIDRPLLSTARDNYGMTPIHKALLHGQTNTVRFLLGrfpSCVNaTDHAGRTP---LHYAAA 158
Cdd:PHA02875 135 KFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLD---SGAN-IDYFGKNGcvaALCYAI 210

                         90       100
                 ....*....|....*....|
gi 922580217 159 DPNGEHMIKVLQKSGGDAFI 178
Cdd:PHA02875 211 ENNKIDIVRLFIKRGADCNI 230
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 222-372 5.25e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 39.97  E-value: 5.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580217 222 DLEEDIYDWIHTGNIGKLEELVLTG-YADLLLGRN-----HEVDDADSIGFLEVLPQYQA--------KIQSIHKAVETG 287
Cdd:PHA02875  67 DIESELHDAVEEGDVKAVEELLDLGkFADDVFYKDgmtplHLATILKKLDIMKLLIARGAdpdipntdKFSPLHLAVMMG 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580217 288 NLRAVKLLTDRKKLSLCRDTRGLSPLHKAIVFERTDIAKYLIrNYPQSVNAMDQKKRTPLHYAAALKDGGYLYKVMRKSG 367
Cdd:PHA02875 147 DIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLL-DSGANIDYFGKNGCVAALCYAIENNKIDIVRLFIKRG 225


                 ....*
gi 922580217 368 ADPNI 372
Cdd:PHA02875 226 ADCNI 230
PHA03095 PHA03095
ankyrin-like protein; Provisional
 496-571 6.06e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 39.62  E-value: 6.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580217 496 RDRFGCTPLHSAV---VHEHTEIVRYI--AGhynSVLNAPDYNKRTAMHYAAAARDGGHYLKILGKAGADPMAVDNEGRT 570
Cdd:PHA03095  43 RGEYGKTPLHLYLhysSEKVKDIVRLLleAG---ADVNAPERCGFTPLHLYLYNATTLDVIKLLIKAGADVNAKDKVGRT 119


                 .
gi 922580217 571 P 571
Cdd:PHA03095 120 P 120
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 126-187 7.59e-03

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 39.50  E-value: 7.59e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 922580217 126 GQTNTVRFLL--GRFPSCVnatDHAGRTPLHYAAAdpNGE-HMIKVLQKSGGDAFIEDKHGHTPF 187
Cdd:PTZ00322  93 GDAVGARILLtgGADPNCR---DYDGRTPLHIACA--NGHvQVVRVLLEFGADPTLLDKDGKTPL 152
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 280-355 8.54e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 39.18  E-value: 8.54e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 922580217 280 IHKAVETGNLRAVKLLTDRKKLSLCRDTRGLSPLHKAIVFERTDIAKYLIRNyPQSVNAMDQKKRTPLHYAAALKD 355
Cdd:PHA02874 128 LHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEK-GAYANVKDNNGESPLHNAAEYGD 202
 
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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