NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|675378395|gb|KFM71297|]
View 

Tankyrase-1, partial [Stegodyphus mimosarum]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PHA03095 super family cl33707
ankyrin-like protein; Provisional
 84-368 1.48e-15

ankyrin-like protein; Provisional


The actual alignment was detected with superfamily member PHA03095:

Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 81.22  E-value: 1.48e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675378395   84 CRDHMGASPMHKAVLFSQKP---IIDYLLDrYPSVVHARDHKGRTPLHYAAVLSDGGEIYKMLLDHGADTKATDVYGNRP 160
Cdd:PHA03095   42 FRGEYGKTPLHLYLHYSSEKvkdIVRLLLE-AGADVNAPERCGFTPLHLYLYNATTLDVIKLLIKAGADVNAKDKVGRTP 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675378395  161 eyyMHArdemdiqalkegHDTGKS--PKMTKM---KHFQSNDGNKKDtvarsakpagtRTQIREMLTSGNLEAleELVlq 235
Cdd:PHA03095  121 ---LHV------------YLSGFNinPKVIRLllrKGADVNALDLYG-----------MTPLAVLLKSRNANV--ELL-- 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675378395  236 ghgdKLLGESSNNPLVRDFIRMVPIymeriyEIHRAVARGRLRDVQTLLDRKKLALARDPLGATPLHKAVMYG---HNDV 312
Cdd:PHA03095  171 ----RLLIDAGADVYAVDDRFRSLL------HHHLQSFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSsckRSLV 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 675378395  313 AEYITLNfpLAKDTKDLDGRTPLHYAAALkDNHELYNMLISLGANPLVLDYRGKTA 368
Cdd:PHA03095  241 LPLLIAG--ISINARNRYGQTPLHYAAVF-NNPRACRRLIALGADINAVSSDGNTP 293
DD_DYDC-like cd22966
dimerization/docking (D/D) domain found in the DPY30 domain-containing protein (DYDC)-like ...
 1277-1319 2.44e-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: 68.17  E-value: 2.44e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 675378395 1277 DSRYLATVLGDALIKGLTQVAARRPRDPIGYLATYLYQYAARK 1319
Cdd:cd22966     1 DSAYLKETVGDVLTKALAEVALKRPADPIEFLANWLLKYRENE 43
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1072-1165 3.77e-13

Ankyrin repeats (3 copies);


:

Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 66.29  E-value: 3.77e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675378395  1072 HDAVVRGNLGEVESVLTRKRFALSRDHLGASPLHLAVLHGHTDIVKYIIDNFpeALDGPDNeGRTPLHYAAVMrdgGSY- 1150
Cdd:pfam12796    2 HLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA--DVNLKDN-GRTALHYAARS---GHLe 75

                           90
                   ....*....|....*.
gi 675378395  1151 -YRILLMAGADETVKD 1165
Cdd:pfam12796   76 iVKLLLEKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
511-848 3.15e-12

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 68.83  E-value: 3.15e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675378395  511 NAKLQEYINDQVPLLVKKIEAIHSAVSNDDLNELQAQLHETDHMVLAKDHFGMAPIHRAVLMNKPETLAFLIDRfPETVN 590
Cdd:COG0666    36 LLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEA-GADVN 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675378395  591 ARDKEGRTALHYAAAMsrepGASNYFKILLEAGADSRIRDNQGRSPeyyrthhvpiphklnLHqkmlkklrsksepppqn 670
Cdd:COG0666   115 ARDKDGETPLHLAAYN----GNLEIVKLLLEAGADVNAQDNDGNTP---------------LH----------------- 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675378395  671 rvkklpgingigslpqvtmdkinqwlqngdlehikefamdgygqhlvgktswsedvrqylkslplflmtlgsafHAVERG 750
Cdd:COG0666   159 --------------------------------------------------------------------------LAAANG 164

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675378395  751 DVESLDKLIASEENLLRsKNSDGSTLMHHAVLHDQLDVLNYFLhKYPTLVNIKDRNGRTPLHVAGQQKNQYVYTILTAAG 830
Cdd:COG0666   165 NLEIVKLLLEAGADVNA-RDNDGETPLHLAAENGHLEIVKLLL-EAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAG 242

                         330
                  ....*....|....*...
gi 675378395  831 ADPMILDQKGRSAEYYYT 848
Cdd:COG0666   243 ADLNAKDKDGLTALLLAA 260
SEEEED pfam14797
Serine-rich region of AP3B1, clathrin-adaptor complex; This short low-complexity, highly ...
 859-952 8.40e-05

Serine-rich region of AP3B1, clathrin-adaptor complex; This short low-complexity, highly serine-rich region lies on clathrin-adaptor complex 3 beta-1 subunit proteins, between family Adaptin_N, pfam01602 and a C-terminal domain, AP3B1_C,pfam14796.


:

Pssm-ID: 434218 [Multi-domain]  Cd Length: 111  Bit Score: 43.38  E-value: 8.40e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675378395   859 SPSSSTPEDSSGNE-----KISSSPEENKKD-------EQGNEAEQQSKDSKNSKSpdkEEESDTKTEVKiaENEEKKDA 926
Cdd:pfam14797   16 SDSSSDSESESGSEseeegKEGSSSEDSSEDssseqesESGSESEKKRTAKRNSKA---KGKSDSEDGEK--KNEKSKTS 90

                           90       100
                   ....*....|....*....|....*.
gi 675378395   927 EGSTTATAEKaktpvpEGKSTDSEQE 952
Cdd:pfam14797   91 DSSDTESSSS------EESSSDSESE 110
 
Name Accession Description Interval E-value
PHA03095 PHA03095
ankyrin-like protein; Provisional
 84-368 1.48e-15

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 81.22  E-value: 1.48e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675378395   84 CRDHMGASPMHKAVLFSQKP---IIDYLLDrYPSVVHARDHKGRTPLHYAAVLSDGGEIYKMLLDHGADTKATDVYGNRP 160
Cdd:PHA03095   42 FRGEYGKTPLHLYLHYSSEKvkdIVRLLLE-AGADVNAPERCGFTPLHLYLYNATTLDVIKLLIKAGADVNAKDKVGRTP 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675378395  161 eyyMHArdemdiqalkegHDTGKS--PKMTKM---KHFQSNDGNKKDtvarsakpagtRTQIREMLTSGNLEAleELVlq 235
Cdd:PHA03095  121 ---LHV------------YLSGFNinPKVIRLllrKGADVNALDLYG-----------MTPLAVLLKSRNANV--ELL-- 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675378395  236 ghgdKLLGESSNNPLVRDFIRMVPIymeriyEIHRAVARGRLRDVQTLLDRKKLALARDPLGATPLHKAVMYG---HNDV 312
Cdd:PHA03095  171 ----RLLIDAGADVYAVDDRFRSLL------HHHLQSFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSsckRSLV 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 675378395  313 AEYITLNfpLAKDTKDLDGRTPLHYAAALkDNHELYNMLISLGANPLVLDYRGKTA 368
Cdd:PHA03095  241 LPLLIAG--ISINARNRYGQTPLHYAAVF-NNPRACRRLIALGADINAVSSDGNTP 293
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
57-400 5.24e-15

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 77.30  E-value: 5.24e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675378395   57 IDEIHKAVSTGNLRDVQHLIDRKKLAFCRDHMGASPMHKAVLFSQKPIIDYLLDRYPSVvHARDHKGRTPLHYAAvLSDG 136
Cdd:COG0666    55 ALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADV-NARDKDGETPLHLAA-YNGN 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675378395  137 GEIYKMLLDHGADTKATDVYGNRPeyymhardemdiqalkeghdtgkspkmtkmkhfqsndgnkkdtvarsakpagtrtq 216
Cdd:COG0666   133 LEIVKLLLEAGADVNAQDNDGNTP-------------------------------------------------------- 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675378395  217 iremltsgnlealeelvlqghgdkllgessnnplvrdfirmvpiymeriyeIHRAVARGRLRDVQTLLDRKKLALARDPL 296
Cdd:COG0666   157 ---------------------------------------------------LHLAAANGNLEIVKLLLEAGADVNARDND 185

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675378395  297 GATPLHKAVMYGHNDVAEYItLNFPLAKDTKDLDGRTPLHYAAAlKDNHELYNMLISLGANPLVLDYRGKTAEYYLQFPE 376
Cdd:COG0666   186 GETPLHLAAENGHLEIVKLL-LEAGADVNAKDNDGKTALDLAAE-NGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAG 263

                         330       340
                  ....*....|....*....|....
gi 675378395  377 HLHLEQMIKQSQRLNANYMANHAN 400
Cdd:COG0666   264 AALIVKLLLLALLLLAAALLDLLT 287
DD_DYDC-like cd22966
dimerization/docking (D/D) domain found in the DPY30 domain-containing protein (DYDC)-like ...
 1277-1319 2.44e-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: 68.17  E-value: 2.44e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 675378395 1277 DSRYLATVLGDALIKGLTQVAARRPRDPIGYLATYLYQYAARK 1319
Cdd:cd22966     1 DSAYLKETVGDVLTKALAEVALKRPADPIEFLANWLLKYRENE 43
Ank_2 pfam12796
Ankyrin repeats (3 copies);
268-362 9.74e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 68.22  E-value: 9.74e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675378395   268 IHRAVARGRLRDVQTLLDRKKLALARDPLGATPLHKAVMYGHNDVAEYItLNFPLAKDtkDLDGRTPLHYaAALKDNHEL 347
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLL-LEHADVNL--KDNGRTALHY-AARSGHLEI 76

                           90
                   ....*....|....*
gi 675378395   348 YNMLISLGANPLVLD 362
Cdd:pfam12796   77 VKLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1072-1165 3.77e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 66.29  E-value: 3.77e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675378395  1072 HDAVVRGNLGEVESVLTRKRFALSRDHLGASPLHLAVLHGHTDIVKYIIDNFpeALDGPDNeGRTPLHYAAVMrdgGSY- 1150
Cdd:pfam12796    2 HLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA--DVNLKDN-GRTALHYAARS---GHLe 75

                           90
                   ....*....|....*.
gi 675378395  1151 -YRILLMAGADETVKD 1165
Cdd:pfam12796   76 iVKLLLEKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
511-848 3.15e-12

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 68.83  E-value: 3.15e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675378395  511 NAKLQEYINDQVPLLVKKIEAIHSAVSNDDLNELQAQLHETDHMVLAKDHFGMAPIHRAVLMNKPETLAFLIDRfPETVN 590
Cdd:COG0666    36 LLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEA-GADVN 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675378395  591 ARDKEGRTALHYAAAMsrepGASNYFKILLEAGADSRIRDNQGRSPeyyrthhvpiphklnLHqkmlkklrsksepppqn 670
Cdd:COG0666   115 ARDKDGETPLHLAAYN----GNLEIVKLLLEAGADVNAQDNDGNTP---------------LH----------------- 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675378395  671 rvkklpgingigslpqvtmdkinqwlqngdlehikefamdgygqhlvgktswsedvrqylkslplflmtlgsafHAVERG 750
Cdd:COG0666   159 --------------------------------------------------------------------------LAAANG 164

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675378395  751 DVESLDKLIASEENLLRsKNSDGSTLMHHAVLHDQLDVLNYFLhKYPTLVNIKDRNGRTPLHVAGQQKNQYVYTILTAAG 830
Cdd:COG0666   165 NLEIVKLLLEAGADVNA-RDNDGETPLHLAAENGHLEIVKLLL-EAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAG 242

                         330
                  ....*....|....*...
gi 675378395  831 ADPMILDQKGRSAEYYYT 848
Cdd:COG0666   243 ADLNAKDKDGLTALLLAA 260
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1096-1199 5.03e-12

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 68.44  E-value: 5.03e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675378395 1096 RDHLGASPLHLAVLHGHTDIVKYIIDNfPEALDGPDNEGRTPLHYAAvmrDGGSYY--RILLMAGADETVKDKAGHTPDY 1173
Cdd:COG0666   149 QDNDGNTPLHLAAANGNLEIVKLLLEA-GADVNARDNDGETPLHLAA---ENGHLEivKLLLEAGADVNAKDNDGKTALD 224

                          90       100
                  ....*....|....*....|....*.
gi 675378395 1174 YLTHAGVLTIRDLLEGYRIRDAQNRR 1199
Cdd:COG0666   225 LAAENGNLEIVKLLLEAGADLNAKDK 250
Ank_2 pfam12796
Ankyrin repeats (3 copies);
744-837 1.35e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 56.28  E-value: 1.35e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675378395   744 FHAVERGDVESLDKLIASEENLlRSKNSDGSTLMHHAVLHDQLDVLNYFLHKYPtlVNIKDrNGRTPLHVAGQQKNQYVY 823
Cdd:pfam12796    2 HLAAKNGNLELVKLLLENGADA-NLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKD-NGRTALHYAARSGHLEIV 77

                           90
                   ....*....|....
gi 675378395   824 TILTAAGADPMILD 837
Cdd:pfam12796   78 KLLLEKGADINVKD 91
Dpy-30 pfam05186
Dpy-30 motif; This motif is found in a wide variety of domain contexts. It is found in the ...
 1277-1317 3.89e-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: 50.69  E-value: 3.89e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 675378395  1277 DSRYLATVLGDALIKGLTQVAARRPRDPIGYLATYLYQYAA 1317
Cdd:pfam05186    2 ARQYLNKTVAPILLQGLTELAKERPEDPIEYLADYLLKNNP 42
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 532-636 4.57e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 50.73  E-value: 4.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675378395  532 IHSAVSNDDLNELQAQLHETDHmVLAKDHFGMAPIHRAVLMNKpETLAFLIDRfpETVNARDKEGRTALHYAAamsREPG 611
Cdd:PHA02874  194 LHNAAEYGDYACIKLLIDHGNH-IMNKCKNGFTPLHNAIIHNR-SAIELLINN--ASINDQDIDGSTPLHHAI---NPPC 266

                          90       100
                  ....*....|....*....|....*
gi 675378395  612 ASNYFKILLEAGADSRIRDNQGRSP 636
Cdd:PHA02874  267 DIDIIDILLYHKADISIKDNKGENP 291
PHA03095 PHA03095
ankyrin-like protein; Provisional
 1093-1171 5.01e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 50.79  E-value: 5.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675378395 1093 ALSRDHLGASPLHLAVLHG---HTDIVKYIIDNFpeALDGPDNEGRTPLHYAAVMRDGGSYYRiLLMAGADETVKDKAGH 1169
Cdd:PHA03095  215 PAATDMLGNTPLHSMATGSsckRSLVLPLLIAGI--SINARNRYGQTPLHYAAVFNNPRACRR-LIALGADINAVSSDGN 291


                  ..
gi 675378395 1170 TP 1171
Cdd:PHA03095  292 TP 293
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 732-832 9.45e-06

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: 50.01  E-value: 9.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675378395  732 SLPLFLmtlgsafhAVERGDVESLDKLIASEENLLRSKNSDGSTLMHHAVLHDQLDVLNYFLHKYPTLVNIKDRN----G 807
Cdd:cd22192    18 ESPLLL--------AAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNEPMTSdlyqG 89

                          90       100
                  ....*....|....*....|....*
gi 675378395  808 RTPLHVAGQQKNQYVYTILTAAGAD 832
Cdd:cd22192    90 ETALHIAVVNQNLNLVRELIARGAD 114
SEEEED pfam14797
Serine-rich region of AP3B1, clathrin-adaptor complex; This short low-complexity, highly ...
 859-952 8.40e-05

Serine-rich region of AP3B1, clathrin-adaptor complex; This short low-complexity, highly serine-rich region lies on clathrin-adaptor complex 3 beta-1 subunit proteins, between family Adaptin_N, pfam01602 and a C-terminal domain, AP3B1_C,pfam14796.


Pssm-ID: 434218 [Multi-domain]  Cd Length: 111  Bit Score: 43.38  E-value: 8.40e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675378395   859 SPSSSTPEDSSGNE-----KISSSPEENKKD-------EQGNEAEQQSKDSKNSKSpdkEEESDTKTEVKiaENEEKKDA 926
Cdd:pfam14797   16 SDSSSDSESESGSEseeegKEGSSSEDSSEDssseqesESGSESEKKRTAKRNSKA---KGKSDSEDGEK--KNEKSKTS 90

                           90       100
                   ....*....|....*....|....*.
gi 675378395   927 EGSTTATAEKaktpvpEGKSTDSEQE 952
Cdd:pfam14797   91 DSSDTESSSS------EESSSDSESE 110
ftsN TIGR02223
cell division protein FtsN; FtsN is a poorly conserved protein active in cell division in a ...
 818-970 3.38e-04

cell division protein FtsN; FtsN is a poorly conserved protein active in cell division in a number of Proteobacteria. The N-terminal 30 residue region tends to by Lys/Arg-rich, and is followed by a membrane-spanning region. This is followed by an acidic low-complexity region of variable length and a well-conserved C-terminal domain of two tandem regions matched by pfam05036 (Sporulation related repeat), found in several cell division and sporulation proteins. The role of FtsN as a suppressor for other cell division mutations is poorly understood; it may involve cell wall hydrolysis. [Cellular processes, Cell division]


Pssm-ID: 274041 [Multi-domain]  Cd Length: 298  Bit Score: 44.30  E-value: 3.38e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675378395   818 KNQYVYTILTAAGADPMILDQKGRSAEYYYTSSIKPTKPQISPSSSTPEDSSGNEKISSSPEE----------------- 880
Cdd:TIGR02223   19 KNRRLVRATVLIAAILILLFIGGSSGLYLLTESKQANEPETLQPKNQTENGETAADLPPKPEErwsyieelearevlind 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675378395   881 NKKDEQGNEAEQQSKDSKNSKSPDKEEESDTKTEVKIA--ENEEKKDAEGSTTATAEKAKTPVP--EGKSTDSEQEEKQG 956
Cdd:TIGR02223   99 PEEPSNGGGVEESAQLTAEQRQLLEQMQADMRAAEKVLatAPSEQTVAVEARKQTAEKKPQKARtaEAQKTPVETEKIAS 178

                          170
                   ....*....|....
gi 675378395   957 NDDKENNSDKEEGK 970
Cdd:TIGR02223  179 KVKEAKQKQKALPK 192
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 263-356 5.34e-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: 44.23  E-value: 5.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675378395  263 ERIYEI--HRAVARGRLRDVQTLLDRKKLAL-ARDPLGATPLHKAVMYGHNDVAEYITLNFP-LAKD--TKDL-DGRTPL 335
Cdd:cd22192    14 KRISESplLLAAKENDVQAIKKLLKCPSCDLfQRGALGETALHVAALYDNLEAAVVLMEAAPeLVNEpmTSDLyQGETAL 93

                          90       100
                  ....*....|....*....|.
gi 675378395  336 HYAAAlKDNHELYNMLISLGA 356
Cdd:cd22192    94 HIAVV-NQNLNLVRELIARGA 113
PTZ00121 PTZ00121
MAEBL; Provisional
 879-968 1.11e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.59  E-value: 1.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675378395  879 EENKKDEQGNEAEQQSKDSKNSKSPDKEEESDTKTEVKIAENEEKKDAEGSTTATAEKAKTPVPEGKSTDSEQEEKQGND 958
Cdd:PTZ00121 1644 EEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKK 1723

                          90
                  ....*....|
gi 675378395  959 DKENNSDKEE 968
Cdd:PTZ00121 1724 AEEENKIKAE 1733
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 1100-1122 1.14e-03

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.57  E-value: 1.14e-03
                            10        20
                    ....*....|....*....|...
gi 675378395   1100 GASPLHLAVLHGHTDIVKYIIDN 1122
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDK 24
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 1096-1160 2.29e-03

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: 2.29e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 675378395 1096 RDHLGASPLHLAVLHGHTDIVKYIIDNFPEALDGPDN----EGRTPLHyAAVMRDGGSYYRILLMAGAD 1160
Cdd:cd22192    47 RGALGETALHVAALYDNLEAAVVLMEAAPELVNEPMTsdlyQGETALH-IAVVNQNLNLVRELIARGAD 114
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 330-358 4.57e-03

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.03  E-value: 4.57e-03
                            10        20
                    ....*....|....*....|....*....
gi 675378395    330 DGRTPLHYAAAlKDNHELYNMLISLGANP 358
Cdd:smart00248    1 DGRTPLHLAAE-NGNLEVVKLLLDKGADI 28
 
Name Accession Description Interval E-value
PHA03095 PHA03095
ankyrin-like protein; Provisional
 84-368 1.48e-15

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 81.22  E-value: 1.48e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675378395   84 CRDHMGASPMHKAVLFSQKP---IIDYLLDrYPSVVHARDHKGRTPLHYAAVLSDGGEIYKMLLDHGADTKATDVYGNRP 160
Cdd:PHA03095   42 FRGEYGKTPLHLYLHYSSEKvkdIVRLLLE-AGADVNAPERCGFTPLHLYLYNATTLDVIKLLIKAGADVNAKDKVGRTP 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675378395  161 eyyMHArdemdiqalkegHDTGKS--PKMTKM---KHFQSNDGNKKDtvarsakpagtRTQIREMLTSGNLEAleELVlq 235
Cdd:PHA03095  121 ---LHV------------YLSGFNinPKVIRLllrKGADVNALDLYG-----------MTPLAVLLKSRNANV--ELL-- 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675378395  236 ghgdKLLGESSNNPLVRDFIRMVPIymeriyEIHRAVARGRLRDVQTLLDRKKLALARDPLGATPLHKAVMYG---HNDV 312
Cdd:PHA03095  171 ----RLLIDAGADVYAVDDRFRSLL------HHHLQSFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSsckRSLV 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 675378395  313 AEYITLNfpLAKDTKDLDGRTPLHYAAALkDNHELYNMLISLGANPLVLDYRGKTA 368
Cdd:PHA03095  241 LPLLIAG--ISINARNRYGQTPLHYAAVF-NNPRACRRLIALGADINAVSSDGNTP 293
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
57-400 5.24e-15

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 77.30  E-value: 5.24e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675378395   57 IDEIHKAVSTGNLRDVQHLIDRKKLAFCRDHMGASPMHKAVLFSQKPIIDYLLDRYPSVvHARDHKGRTPLHYAAvLSDG 136
Cdd:COG0666    55 ALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADV-NARDKDGETPLHLAA-YNGN 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675378395  137 GEIYKMLLDHGADTKATDVYGNRPeyymhardemdiqalkeghdtgkspkmtkmkhfqsndgnkkdtvarsakpagtrtq 216
Cdd:COG0666   133 LEIVKLLLEAGADVNAQDNDGNTP-------------------------------------------------------- 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675378395  217 iremltsgnlealeelvlqghgdkllgessnnplvrdfirmvpiymeriyeIHRAVARGRLRDVQTLLDRKKLALARDPL 296
Cdd:COG0666   157 ---------------------------------------------------LHLAAANGNLEIVKLLLEAGADVNARDND 185

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675378395  297 GATPLHKAVMYGHNDVAEYItLNFPLAKDTKDLDGRTPLHYAAAlKDNHELYNMLISLGANPLVLDYRGKTAEYYLQFPE 376
Cdd:COG0666   186 GETPLHLAAENGHLEIVKLL-LEAGADVNAKDNDGKTALDLAAE-NGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAG 263

                         330       340
                  ....*....|....*....|....
gi 675378395  377 HLHLEQMIKQSQRLNANYMANHAN 400
Cdd:COG0666   264 AALIVKLLLLALLLLAAALLDLLT 287
DD_DYDC-like cd22966
dimerization/docking (D/D) domain found in the DPY30 domain-containing protein (DYDC)-like ...
 1277-1319 2.44e-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: 68.17  E-value: 2.44e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 675378395 1277 DSRYLATVLGDALIKGLTQVAARRPRDPIGYLATYLYQYAARK 1319
Cdd:cd22966     1 DSAYLKETVGDVLTKALAEVALKRPADPIEFLANWLLKYRENE 43
Ank_2 pfam12796
Ankyrin repeats (3 copies);
268-362 9.74e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 68.22  E-value: 9.74e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675378395   268 IHRAVARGRLRDVQTLLDRKKLALARDPLGATPLHKAVMYGHNDVAEYItLNFPLAKDtkDLDGRTPLHYaAALKDNHEL 347
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLL-LEHADVNL--KDNGRTALHY-AARSGHLEI 76

                           90
                   ....*....|....*
gi 675378395   348 YNMLISLGANPLVLD 362
Cdd:pfam12796   77 VKLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1072-1165 3.77e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 66.29  E-value: 3.77e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675378395  1072 HDAVVRGNLGEVESVLTRKRFALSRDHLGASPLHLAVLHGHTDIVKYIIDNFpeALDGPDNeGRTPLHYAAVMrdgGSY- 1150
Cdd:pfam12796    2 HLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA--DVNLKDN-GRTALHYAARS---GHLe 75

                           90
                   ....*....|....*.
gi 675378395  1151 -YRILLMAGADETVKD 1165
Cdd:pfam12796   76 iVKLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
60-154 6.26e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 65.91  E-value: 6.26e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675378395    60 IHKAVSTGNLRDVQHLIDRKKLAFCRDHMGASPMHKAVLFSQKPIIDYLLDRYPSvvhARDHKGRTPLHYAAvLSDGGEI 139
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV---NLKDNGRTALHYAA-RSGHLEI 76

                           90
                   ....*....|....*
gi 675378395   140 YKMLLDHGADTKATD 154
Cdd:pfam12796   77 VKLLLEKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
511-848 3.15e-12

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 68.83  E-value: 3.15e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675378395  511 NAKLQEYINDQVPLLVKKIEAIHSAVSNDDLNELQAQLHETDHMVLAKDHFGMAPIHRAVLMNKPETLAFLIDRfPETVN 590
Cdd:COG0666    36 LLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEA-GADVN 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675378395  591 ARDKEGRTALHYAAAMsrepGASNYFKILLEAGADSRIRDNQGRSPeyyrthhvpiphklnLHqkmlkklrsksepppqn 670
Cdd:COG0666   115 ARDKDGETPLHLAAYN----GNLEIVKLLLEAGADVNAQDNDGNTP---------------LH----------------- 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675378395  671 rvkklpgingigslpqvtmdkinqwlqngdlehikefamdgygqhlvgktswsedvrqylkslplflmtlgsafHAVERG 750
Cdd:COG0666   159 --------------------------------------------------------------------------LAAANG 164

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675378395  751 DVESLDKLIASEENLLRsKNSDGSTLMHHAVLHDQLDVLNYFLhKYPTLVNIKDRNGRTPLHVAGQQKNQYVYTILTAAG 830
Cdd:COG0666   165 NLEIVKLLLEAGADVNA-RDNDGETPLHLAAENGHLEIVKLLL-EAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAG 242

                         330
                  ....*....|....*...
gi 675378395  831 ADPMILDQKGRSAEYYYT 848
Cdd:COG0666   243 ADLNAKDKDGLTALLLAA 260
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1096-1199 5.03e-12

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 68.44  E-value: 5.03e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675378395 1096 RDHLGASPLHLAVLHGHTDIVKYIIDNfPEALDGPDNEGRTPLHYAAvmrDGGSYY--RILLMAGADETVKDKAGHTPDY 1173
Cdd:COG0666   149 QDNDGNTPLHLAAANGNLEIVKLLLEA-GADVNARDNDGETPLHLAA---ENGHLEivKLLLEAGADVNAKDNDGKTALD 224

                          90       100
                  ....*....|....*....|....*.
gi 675378395 1174 YLTHAGVLTIRDLLEGYRIRDAQNRR 1199
Cdd:COG0666   225 LAAENGNLEIVKLLLEAGADLNAKDK 250
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1072-1171 8.24e-11

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 64.59  E-value: 8.24e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675378395 1072 HDAVVRGNLGEVESVLTRKRFALSRDHLGASPLHLAVLHGHTDIVKYIIDNfpEA-LDGPDNEGRTPLHYAAvmrDGGSY 1150
Cdd:COG0666    92 HAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA--GAdVNAQDNDGNTPLHLAA---ANGNL 166

                          90       100
                  ....*....|....*....|...
gi 675378395 1151 Y--RILLMAGADETVKDKAGHTP 1171
Cdd:COG0666   167 EivKLLLEAGADVNARDNDGETP 189
Ank_2 pfam12796
Ankyrin repeats (3 copies);
744-837 1.35e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 56.28  E-value: 1.35e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675378395   744 FHAVERGDVESLDKLIASEENLlRSKNSDGSTLMHHAVLHDQLDVLNYFLHKYPtlVNIKDrNGRTPLHVAGQQKNQYVY 823
Cdd:pfam12796    2 HLAAKNGNLELVKLLLENGADA-NLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKD-NGRTALHYAARSGHLEIV 77

                           90
                   ....*....|....
gi 675378395   824 TILTAAGADPMILD 837
Cdd:pfam12796   78 KLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
532-630 1.57e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 56.28  E-value: 1.57e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675378395   532 IHSAVSNDDLNELQaQLHETDHMVLAKDHFGMAPIHRAVLMNKPETLAFLIDRFPetVNARDkEGRTALHYAAAMsrepG 611
Cdd:pfam12796    1 LHLAAKNGNLELVK-LLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKD-NGRTALHYAARS----G 72

                           90
                   ....*....|....*....
gi 675378395   612 ASNYFKILLEAGADSRIRD 630
Cdd:pfam12796   73 HLEIVKLLLEKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1072-1199 5.16e-09

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 59.20  E-value: 5.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675378395 1072 HDAVVRGNLGEVESVLTRKRFALSRDHLGASPLHLAVLHGHTDIVKYIIDNfpEA-LDGPDNEGRTPLHYAAVMRDGGSy 1150
Cdd:COG0666   158 HLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEA--GAdVNAKDNDGKTALDLAAENGNLEI- 234

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 675378395 1151 YRILLMAGADETVKDKAGHTPDYYLTHAGVLTIRDLLEGYRIRDAQNRR 1199
Cdd:COG0666   235 VKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALL 283
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1072-1171 1.32e-08

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 58.04  E-value: 1.32e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675378395 1072 HDAVVRGNLGEVESVLTRKRFALSRDHLGASPLHLAVLHGHTDIVKYIIDNfPEALDGPDNEGRTPLHYAAvMRDGGSYY 1151
Cdd:COG0666    59 LAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEA-GADVNARDKDGETPLHLAA-YNGNLEIV 136

                          90       100
                  ....*....|....*....|
gi 675378395 1152 RILLMAGADETVKDKAGHTP 1171
Cdd:COG0666   137 KLLLEAGADVNAQDNDGNTP 156
DD_CrRSP2-like cd22982
dimerization/docking (D/D) domain found in Chlamydomonas reinhardtii flagellar radial spoke ...
 1277-1320 3.46e-08

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: 51.21  E-value: 3.46e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 675378395 1277 DSRYLATVLGDALIKGLTQVAARRPRDPIGYLATYLYQYAARKS 1320
Cdd:cd22982     1 DTEYLKETVGEALAKGCAAVALAQPEDPVEYLGLWLLQHVRNKE 44
Dpy-30 pfam05186
Dpy-30 motif; This motif is found in a wide variety of domain contexts. It is found in the ...
 1277-1317 3.89e-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: 50.69  E-value: 3.89e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 675378395  1277 DSRYLATVLGDALIKGLTQVAARRPRDPIGYLATYLYQYAA 1317
Cdd:pfam05186    2 ARQYLNKTVAPILLQGLTELAKERPEDPIEYLADYLLKNNP 42
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
531-659 2.58e-07

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 53.80  E-value: 2.58e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675378395  531 AIHSAVSNDDLNELQAQL-HETDhmVLAKDHFGMAPIHRAVLMNKPETLAFLIDRFPEtVNARDKEGRTALHYAAAMsre 609
Cdd:COG0666   156 PLHLAAANGNLEIVKLLLeAGAD--VNARDNDGETPLHLAAENGHLEIVKLLLEAGAD-VNAKDNDGKTALDLAAEN--- 229

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 675378395  610 pGASNYFKILLEAGADSRIRDNQGRSPEYYRTHHVPIPHKLNLHQKMLKK 659
Cdd:COG0666   230 -GNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLL 278
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1104-1142 1.05e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 48.19  E-value: 1.05e-06
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 675378395  1104 LHLAVLHGHTDIVKYIIDNFPEAlDGPDNEGRTPLHYAA 1142
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADA-NLQDKNGRTALHLAA 38
Ank_4 pfam13637
Ankyrin repeats (many copies);
1102-1142 1.21e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.88  E-value: 1.21e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 675378395  1102 SPLHLAVLHGHTDIVKYIIDNFPEaLDGPDNEGRTPLHYAA 1142
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGAD-INAVDGNGETALHFAA 42
DD_DPY30_SDC1-like cd22958
dimerization/docking (D/D) domain found in the DPY30/SDC1-like family; The DPY30/SDC1-like ...
 1280-1316 1.87e-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: 1.87e-06
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 675378395 1280 YLATVLGDALIKGLTQVAARRPRDPIGYLATYLYQYA 1316
Cdd:cd22958     4 YLSETVLPTLIPALAELLKARPEDPLEWLAEYLLRNN 40
DD_AK7 cd22967
dimerization/docking (D/D) domain found in adenylate kinase 7 and similar proteins; Adenylate ...
 1279-1316 3.41e-06

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: 45.17  E-value: 3.41e-06
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 675378395 1279 RYLATVLGDALIKGLTQVAARRPRDPIGYLATYLYQYA 1316
Cdd:cd22967     4 NYLMKYVMPTLTEGLVEVCKVRPEDPVDFLAEYLFKHN 41
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 532-636 4.57e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 50.73  E-value: 4.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675378395  532 IHSAVSNDDLNELQAQLHETDHmVLAKDHFGMAPIHRAVLMNKpETLAFLIDRfpETVNARDKEGRTALHYAAamsREPG 611
Cdd:PHA02874  194 LHNAAEYGDYACIKLLIDHGNH-IMNKCKNGFTPLHNAIIHNR-SAIELLINN--ASINDQDIDGSTPLHHAI---NPPC 266

                          90       100
                  ....*....|....*....|....*
gi 675378395  612 ASNYFKILLEAGADSRIRDNQGRSP 636
Cdd:PHA02874  267 DIDIIDILLYHKADISIKDNKGENP 291
Ank_4 pfam13637
Ankyrin repeats (many copies);
562-609 5.00e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.96  E-value: 5.00e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 675378395   562 GMAPIHRAVLMNKPETLAFLIDRFPEtVNARDKEGRTALHYAAAMSRE 609
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGAD-INAVDGNGETALHFAASNGNV 47
PHA03095 PHA03095
ankyrin-like protein; Provisional
 1093-1171 5.01e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 50.79  E-value: 5.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675378395 1093 ALSRDHLGASPLHLAVLHG---HTDIVKYIIDNFpeALDGPDNEGRTPLHYAAVMRDGGSYYRiLLMAGADETVKDKAGH 1169
Cdd:PHA03095  215 PAATDMLGNTPLHSMATGSsckRSLVLPLLIAGI--SINARNRYGQTPLHYAAVFNNPRACRR-LIALGADINAVSSDGN 291


                  ..
gi 675378395 1170 TP 1171
Cdd:PHA03095  292 TP 293
Ank_5 pfam13857
Ankyrin repeats (many copies);
1100-1141 5.98e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 44.64  E-value: 5.98e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 675378395  1100 GASPLHLAVLHGHTDIVKYIIDNfPEALDGPDNEGRTPLHYA 1141
Cdd:pfam13857   16 GYTPLHVAAKYGALEIVRVLLAY-GVDLNLKDEEGLTALDLA 56
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 732-832 9.45e-06

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: 50.01  E-value: 9.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675378395  732 SLPLFLmtlgsafhAVERGDVESLDKLIASEENLLRSKNSDGSTLMHHAVLHDQLDVLNYFLHKYPTLVNIKDRN----G 807
Cdd:cd22192    18 ESPLLL--------AAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNEPMTSdlyqG 89

                          90       100
                  ....*....|....*....|....*
gi 675378395  808 RTPLHVAGQQKNQYVYTILTAAGAD 832
Cdd:cd22192    90 ETALHIAVVNQNLNLVRELIARGAD 114
Ank_5 pfam13857
Ankyrin repeats (many copies);
283-338 1.20e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.87  E-value: 1.20e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 675378395   283 LLDRKKLAL-ARDPLGATPLHKAVMYGHNDVAEYItLNFPLAKDTKDLDGRTPLHYA 338
Cdd:pfam13857    1 LLEHGPIDLnRLDGEGYTPLHVAAKYGALEIVRVL-LAYGVDLNLKDEEGLTALDLA 56
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 116-357 1.66e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 49.29  E-value: 1.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675378395  116 VHARDHKGRTPLHYAAVLSDGGEIYKMLLDHGADTKATDVYGNRPEYYMhardemdiqaLKEGHDTgkspkmtkmkhfqs 195
Cdd:PHA02876  266 VNSIDDCKNTPLHHASQAPSLSRLVPKLLERGADVNAKNIKGETPLYLM----------AKNGYDT-------------- 321

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675378395  196 ndGNKKDTVARSAK-PAGTRTQIREMLTSGNLEALEELVLQghgdklLGESSNNPLVRDFIRMVPiymeriyeIHRAVAR 274
Cdd:PHA02876  322 --ENIRTLIMLGADvNAADRLYITPLHQASTLDRNKDIVIT------LLELGANVNARDYCDKTP--------IHYAAVR 385

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675378395  275 GRLRDVQTLLDRKKLALARDPLGATPLHKAvMYGHNDVAEYITLNFPLAK-DTKDLDGRTPLHYAAALKDNHELYNMLIS 353
Cdd:PHA02876  386 NNVVIINTLLDYGADIEALSQKIGTALHFA-LCGTNPYMSVKTLIDRGANvNSKNKDLSTPLHYACKKNCKLDVIEMLLD 464


                  ....
gi 675378395  354 LGAN 357
Cdd:PHA02876  465 NGAD 468
Ank_5 pfam13857
Ankyrin repeats (many copies);
581-636 2.00e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.49  E-value: 2.00e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 675378395   581 LIDRFPETVNARDKEGRTALHYAAamsrEPGASNYFKILLEAGADSRIRDNQGRSP 636
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAA----KYGALEIVRVLLAYGVDLNLKDEEGLTA 52
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 122-154 2.44e-05

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: 42.28  E-value: 2.44e-05
                           10        20        30
                   ....*....|....*....|....*....|...
gi 675378395   122 KGRTPLHYAAVLSDGGEIYKMLLDHGADTKATD 154
Cdd:pfam00023    1 DGNTPLHLAAGRRGNLEIVKLLLSKGADVNARD 33
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 330-362 2.59e-05

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: 42.28  E-value: 2.59e-05
                           10        20        30
                   ....*....|....*....|....*....|...
gi 675378395   330 DGRTPLHYAAALKDNHELYNMLISLGANPLVLD 362
Cdd:pfam00023    1 DGNTPLHLAAGRRGNLEIVKLLLSKGADVNARD 33
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 1071-1200 2.86e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 48.06  E-value: 2.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675378395 1071 VHDAVVRGNLGEVESVLTRKRFA---LSRDhlGASPLHLAVLHGHTDIVKYIIDNFPEAlDGPDNEGRTPLHYAAVMRDg 1147
Cdd:PHA02875   72 LHDAVEEGDVKAVEELLDLGKFAddvFYKD--GMTPLHLATILKKLDIMKLLIARGADP-DIPNTDKFSPLHLAVMMGD- 147

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 675378395 1148 GSYYRILLMAGADETVKDKAGHTPDYYLTHAGVLTI-RDLLEGYRIRDAQNRRP 1200
Cdd:PHA02875  148 IKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAIcKMLLDSGANIDYFGKNG 201
PHA03095 PHA03095
ankyrin-like protein; Provisional
 555-843 3.59e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 48.10  E-value: 3.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675378395  555 VLAKDHFGMAPIHrAVLMNK--PETLAFLIDRFPEtVNARDKEGRTALH-YAAAMSREPGAsnyFKILLEAGADSRIRDN 631
Cdd:PHA03095   76 VNAPERCGFTPLH-LYLYNAttLDVIKLLIKAGAD-VNAKDKVGRTPLHvYLSGFNINPKV---IRLLLRKGADVNALDL 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675378395  632 QGRSP--EYYRTHHVPIphklnlhqKMLKKLRSKSEPPpqnrvkklpgingigslpqVTMDKINQWLqngdLEHIKEFAm 709
Cdd:PHA03095  151 YGMTPlaVLLKSRNANV--------ELLRLLIDAGADV-------------------YAVDDRFRSL----LHHHLQSF- 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675378395  710 dgygqhlvgktswsedvrqylkslplflmtlgsafhaveRGDVESLDKLIASEENlLRSKNSDGSTLMHHAVLHD---QL 786
Cdd:PHA03095  199 ---------------------------------------KPRARIVRELIRAGCD-PAATDMLGNTPLHSMATGSsckRS 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 675378395  787 DVLNYFLHKypTLVNIKDRNGRTPLHVAGQQKNQYVYTILTAAGADPMILDQKGRSA 843
Cdd:PHA03095  239 LVLPLLIAG--ISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTP 293
Ank_4 pfam13637
Ankyrin repeats (many copies);
299-352 4.05e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 42.26  E-value: 4.05e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 675378395   299 TPLHKAVMYGHNDVAEYItLNFPLAKDTKDLDGRTPLHYaAALKDNHELYNMLI 352
Cdd:pfam13637    3 TALHAAAASGHLELLRLL-LEKGADINAVDGNGETALHF-AASNGNVEVLKLLL 54
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 280-367 5.52e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 47.35  E-value: 5.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675378395  280 VQTLLDRKKLALARDPLGATPLHKAVMYGHND-------------------VAEYITLNFPLakDTKDLDGRTPLHYAAA 340
Cdd:PHA03100  124 VEYLLDNGANVNIKNSDGENLLHLYLESNKIDlkilkllidkgvdinaknrVNYLLSYGVPI--NIKDVYGFTPLHYAVY 201

                          90       100
                  ....*....|....*....|....*..
gi 675378395  341 lKDNHELYNMLISLGANPLVLDYRGKT 367
Cdd:PHA03100  202 -NNNPEFVKYLLDLGANPNLVNKYGDT 227
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 85-156 5.97e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 47.35  E-value: 5.97e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 675378395   85 RDHMGASPMHKAVLFSQKPIIDYLLDrYPSVVHARDHKGRTPLHYaAVLSDGGEIYKMLLDHGADTKATDVY 156
Cdd:PHA03100  188 KDVYGFTPLHYAVYNNNPEFVKYLLD-LGANPNLVNKYGDTPLHI-AILNNNKEIFKLLLNNGPSIKTIIET 257
Ank_2 pfam12796
Ankyrin repeats (3 copies);
566-639 7.03e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 42.80  E-value: 7.03e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 675378395   566 IHRAVLMNKPETLAFLIDRFPEtVNARDKEGRTALHYAAAMsrepGASNYFKILLEaGADSRIRDNqGRSPEYY 639
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGAD-ANLQDKNGRTALHLAAKN----GHLEIVKLLLE-HADVNLKDN-GRTALHY 67
SEEEED pfam14797
Serine-rich region of AP3B1, clathrin-adaptor complex; This short low-complexity, highly ...
 859-952 8.40e-05

Serine-rich region of AP3B1, clathrin-adaptor complex; This short low-complexity, highly serine-rich region lies on clathrin-adaptor complex 3 beta-1 subunit proteins, between family Adaptin_N, pfam01602 and a C-terminal domain, AP3B1_C,pfam14796.


Pssm-ID: 434218 [Multi-domain]  Cd Length: 111  Bit Score: 43.38  E-value: 8.40e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675378395   859 SPSSSTPEDSSGNE-----KISSSPEENKKD-------EQGNEAEQQSKDSKNSKSpdkEEESDTKTEVKiaENEEKKDA 926
Cdd:pfam14797   16 SDSSSDSESESGSEseeegKEGSSSEDSSEDssseqesESGSESEKKRTAKRNSKA---KGKSDSEDGEK--KNEKSKTS 90

                           90       100
                   ....*....|....*....|....*.
gi 675378395   927 EGSTTATAEKaktpvpEGKSTDSEQE 952
Cdd:pfam14797   91 DSSDTESSSS------EESSSDSESE 110
Ank_4 pfam13637
Ankyrin repeats (many copies);
268-315 9.25e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.49  E-value: 9.25e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 675378395   268 IHRAVARGRLRDVQTLLDRKKLALARDPLGATPLHKAVMYGHNDVAEY 315
Cdd:pfam13637    5 LHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKL 52
PHA03095 PHA03095
ankyrin-like protein; Provisional
 1100-1205 9.25e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 46.56  E-value: 9.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675378395 1100 GASPLHLAVLHGHT-DIVKYIIDNFPEALDGpDNEGRTPLH-YAAVMRDGGSYYRILLMAGADETVKDKAGHTP-DYYL- 1175
Cdd:PHA03095   83 GFTPLHLYLYNATTlDVIKLLIKAGADVNAK-DKVGRTPLHvYLSGFNINPKVIRLLLRKGADVNALDLYGMTPlAVLLk 161

                          90       100       110
                  ....*....|....*....|....*....|..
gi 675378395 1176 -THAGVLTIRDLLE-GYRIRDAQNRRPSQVNI 1205
Cdd:PHA03095  162 sRNANVELLRLLIDaGADVYAVDDRFRSLLHH 193
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 105-160 1.05e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 46.58  E-value: 1.05e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 675378395  105 IDYLLDrYPSVVHARDHKGRTPLHYAaVLSDGGEIYKMLLDHGADTKATDVYGNRP 160
Cdd:PHA03100  175 VNYLLS-YGVPINIKDVYGFTPLHYA-VYNNNPEFVKYLLDLGANPNLVNKYGDTP 228
Ank_5 pfam13857
Ankyrin repeats (many copies);
758-814 1.21e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.18  E-value: 1.21e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 675378395   758 LIASEENLLRSKNSDGSTLMHHAVLHDQLDVLNYfLHKYPTLVNIKDRNGRTPLHVA 814
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRV-LLAYGVDLNLKDEEGLTALDLA 56
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 548-832 1.30e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 46.20  E-value: 1.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675378395  548 LHETDHMVLAKDHFGMAPIHRAVLMNKPETLAFLIDRFPETVNARDKEgRTALHYAA-AMSREPGASNYFKILLEAGADS 626
Cdd:PHA03100   21 IIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNN-STPLHYLSnIKYNLTDVKEIVKLLLEYGANV 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675378395  627 RIRDNQGRSPEYYrthhvPIPHKLNlHQKMLKKLRSksepppqnrvkklpgiNGIgslpqvtmdKINqwLQNGDLEHIke 706
Cdd:PHA03100  100 NAPDNNGITPLLY-----AISKKSN-SYSIVEYLLD----------------NGA---------NVN--IKNSDGENL-- 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675378395  707 famdgygQHLVGKTSWSEdvrqyLKSLPLFLmtlgsafhavERG-DVESLDKLiaseeNLLRSKNSD-------GSTLMH 778
Cdd:PHA03100  145 -------LHLYLESNKID-----LKILKLLI----------DKGvDINAKNRV-----NYLLSYGVPinikdvyGFTPLH 197

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 675378395  779 HAVLHDQLDVLNYFLHKyPTLVNIKDRNGRTPLHVAGQQKNQYVYTILTAAGAD 832
Cdd:PHA03100  198 YAVYNNNPEFVKYLLDL-GANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPS 250
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 8-185 2.07e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 45.37  E-value: 2.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675378395    8 PITLWLKLGALEKLeqvvldgygdQLYGKTSRIPQVNkflrqVPLFQSkidEIHKAVSTGNLRDVQHLIDRKKLA---FC 84
Cdd:PHA02875   38 PIKLAMKFRDSEAI----------KLLMKHGAIPDVK-----YPDIES---ELHDAVEEGDVKAVEELLDLGKFAddvFY 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675378395   85 RDhmGASPMHKAVLfSQKPIIDYLLDRYPSVVHARDHKGRTPLHYAAVLSDGGEIyKMLLDHGADTKATDVYGNRPEYYM 164
Cdd:PHA02875  100 KD--GMTPLHLATI-LKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGI-ELLIDHKACLDIEDCCGCTPLIIA 175

                         170       180
                  ....*....|....*....|.
gi 675378395  165 HARDemDIQALKEGHDTGKSP 185
Cdd:PHA02875  176 MAKG--DIAICKMLLDSGANI 194
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 1071-1171 2.32e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 45.34  E-value: 2.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675378395 1071 VHDAVVRGNLGEVESVLTRKRFALSRDHLGASPLHLAVLHGHTdIVKYIIDNfpEALDGPDNEGRTPLHYAAVMRDGGSY 1150
Cdd:PHA02874  194 LHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRS-AIELLINN--ASINDQDIDGSTPLHHAINPPCDIDI 270

                          90       100
                  ....*....|....*....|.
gi 675378395 1151 YRILLMAGADETVKDKAGHTP 1171
Cdd:PHA02874  271 IDILLYHKADISIKDNKGENP 291
ftsN TIGR02223
cell division protein FtsN; FtsN is a poorly conserved protein active in cell division in a ...
 818-970 3.38e-04

cell division protein FtsN; FtsN is a poorly conserved protein active in cell division in a number of Proteobacteria. The N-terminal 30 residue region tends to by Lys/Arg-rich, and is followed by a membrane-spanning region. This is followed by an acidic low-complexity region of variable length and a well-conserved C-terminal domain of two tandem regions matched by pfam05036 (Sporulation related repeat), found in several cell division and sporulation proteins. The role of FtsN as a suppressor for other cell division mutations is poorly understood; it may involve cell wall hydrolysis. [Cellular processes, Cell division]


Pssm-ID: 274041 [Multi-domain]  Cd Length: 298  Bit Score: 44.30  E-value: 3.38e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675378395   818 KNQYVYTILTAAGADPMILDQKGRSAEYYYTSSIKPTKPQISPSSSTPEDSSGNEKISSSPEE----------------- 880
Cdd:TIGR02223   19 KNRRLVRATVLIAAILILLFIGGSSGLYLLTESKQANEPETLQPKNQTENGETAADLPPKPEErwsyieelearevlind 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675378395   881 NKKDEQGNEAEQQSKDSKNSKSPDKEEESDTKTEVKIA--ENEEKKDAEGSTTATAEKAKTPVP--EGKSTDSEQEEKQG 956
Cdd:TIGR02223   99 PEEPSNGGGVEESAQLTAEQRQLLEQMQADMRAAEKVLatAPSEQTVAVEARKQTAEKKPQKARtaEAQKTPVETEKIAS 178

                          170
                   ....*....|....
gi 675378395   957 NDDKENNSDKEEGK 970
Cdd:TIGR02223  179 KVKEAKQKQKALPK 192
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 1071-1188 3.54e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 44.57  E-value: 3.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675378395 1071 VHDAVVRGNLGEVESVLTRKRFALSRDHLGASPLHLAVLHGHTDIVKYIIDNfPEALDGPDNEGRTPLHYAAVMRDGGSy 1150
Cdd:PHA02874  128 LHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEK-GAYANVKDNNGESPLHNAAEYGDYAC- 205

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 675378395 1151 YRILLMAGADETVKDKAGHTPdyylTHAGVLTIRDLLE 1188
Cdd:PHA02874  206 IKLLIDHGNHIMNKCKNGFTP----LHNAIIHNRSAIE 239
DD_NDKH5-like cd22970
dimerization/docking (D/D) domain found in nucleoside diphosphate kinase homolog 5 (NDKH5) ...
 1280-1312 3.81e-04

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: 39.44  E-value: 3.81e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 675378395 1280 YLATVLGDALIKGLTQVAARRPRDPIGYLATYL 1312
Cdd:cd22970     8 YLSKHVNPTLLKGLTELCKEKPADPVTWLADWL 40
Ank_5 pfam13857
Ankyrin repeats (many copies);
1119-1171 3.82e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.64  E-value: 3.82e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 675378395  1119 IIDNFPEALDGPDNEGRTPLHYAAvmrdggsYY------RILLMAGADETVKDKAGHTP 1171
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAA-------KYgaleivRVLLAYGVDLNLKDEEGLTA 52
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 263-356 5.34e-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: 44.23  E-value: 5.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675378395  263 ERIYEI--HRAVARGRLRDVQTLLDRKKLAL-ARDPLGATPLHKAVMYGHNDVAEYITLNFP-LAKD--TKDL-DGRTPL 335
Cdd:cd22192    14 KRISESplLLAAKENDVQAIKKLLKCPSCDLfQRGALGETALHVAALYDNLEAAVVLMEAAPeLVNEpmTSDLyQGETAL 93

                          90       100
                  ....*....|....*....|.
gi 675378395  336 HYAAAlKDNHELYNMLISLGA 356
Cdd:cd22192    94 HIAVV-NQNLNLVRELIARGA 113
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 769-846 6.57e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 43.80  E-value: 6.57e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 675378395  769 KNSDGSTLMHHAVLHDQLDVLNYFLhKYPTLVNIKDRNGRTPLHVAGQQKNQYVYTILTAAGADPMILDQKGRSAEYY 846
Cdd:PHA02874  120 KDAELKTFLHYAIKKGDLESIKMLF-EYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHN 196
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 60-367 9.27e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 43.33  E-value: 9.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675378395   60 IHKAVSTGNLRDVQHLIDRKKLAFCRDHMGASPMHKAVLFSQKPIIDYLLDRYPSV-VHARDHKGRTPLHYAAVlsdggE 138
Cdd:PHA02878   41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCsVFYTLVAIKDAFNNRNV-----E 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675378395  139 IYKMLLdhgadtkatdvygnrPEYYMHARDEMDIQALKEGHDTGKSPKMTKMKHFQSNDGNKKDTVARSakpagtrTQIR 218
Cdd:PHA02878  116 IFKIIL---------------TNRYKNIQTIDLVYIDKKSKDDIIEAEITKLLLSYGADINMKDRHKGN-------TALH 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675378395  219 EMLTSGNLEALEELVLQGHGDKLLGESSNNPLvrdfirmvpiymeriyeiHRAVARGRLRDVQTLLDRKKLALARDPLGA 298
Cdd:PHA02878  174 YATENKDQRLTELLLSYGANVNIPDKTNNSPL------------------HHAVKHYNKPIVHILLENGASTDARDKCGN 235

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 675378395  299 TPLHKAVMYghndVAEYITLNFPLAKDT-----KDLDGRTPLHyaAALKDNHELyNMLISLGANPLVLDYRGKT 367
Cdd:PHA02878  236 TPLHISVGY----CKDYDILKLLLEHGVdvnakSYILGLTALH--SSIKSERKL-KLLLEYGADINSLNSYKLT 302
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 1100-1125 1.09e-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.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 37.62  E-value: 1.09e-03
                           10        20
                   ....*....|....*....|....*.
gi 675378395  1100 GASPLHLAVLHGHTDIVKYIIDNFPE 1125
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGAD 27
PTZ00121 PTZ00121
MAEBL; Provisional
 879-968 1.11e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.59  E-value: 1.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675378395  879 EENKKDEQGNEAEQQSKDSKNSKSPDKEEESDTKTEVKIAENEEKKDAEGSTTATAEKAKTPVPEGKSTDSEQEEKQGND 958
Cdd:PTZ00121 1644 EEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKK 1723

                          90
                  ....*....|
gi 675378395  959 DKENNSDKEE 968
Cdd:PTZ00121 1724 AEEENKIKAE 1733
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 1100-1122 1.14e-03

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.57  E-value: 1.14e-03
                            10        20
                    ....*....|....*....|...
gi 675378395   1100 GASPLHLAVLHGHTDIVKYIIDN 1122
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDK 24
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 60-160 1.24e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 43.03  E-value: 1.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675378395   60 IHKAVSTGNLRDVQHLIDRKKLAFCRDHMGASPMHKAVLFSqKPIIDYLLDRypSVVHARDHKGRTPLHYAAVLSDGGEI 139
Cdd:PHA02874  194 LHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHN-RSAIELLINN--ASINDQDIDGSTPLHHAINPPCDIDI 270

                          90       100
                  ....*....|....*....|.
gi 675378395  140 YKMLLDHGADTKATDVYGNRP 160
Cdd:PHA02874  271 IDILLYHKADISIKDNKGENP 291
PTZ00372 PTZ00372
endonuclease 4-like protein; Provisional
 851-962 1.38e-03

endonuclease 4-like protein; Provisional


Pssm-ID: 240388  Cd Length: 413  Bit Score: 42.78  E-value: 1.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675378395  851 IKPTKPQISPSSSTPEDS-SGNEKISSSPEENKKDEqgNEAEQQSKDSKNSKSPDKEEESDTKTEVKIAENEEKKDaEGS 929
Cdd:PTZ00372    9 LSFFSGTTQKSKLQPISYiYSNVLVLSKEILSTFSE--EENKVATTSTKKDKKEDKNNESKKKSEKKKKKKKEKKE-PKS 85

                          90       100       110
                  ....*....|....*....|....*....|...
gi 675378395  930 TTATAEKAKTPVPEgKSTDSEQEEKQGNDDKEN 962
Cdd:PTZ00372   86 EGETKLGFKTPKKS-KKTKKKPPKPKPNEDVDN 117
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 589-842 1.44e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 42.64  E-value: 1.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675378395  589 VNARDKEGRTALHYAAamsrEPGASNYFKILLEAGADSRIRDNQGRSPEyyrthHVPIPHKlnlhqkmlkklrskseppp 668
Cdd:PHA02874  117 VNIKDAELKTFLHYAI----KKGDLESIKMLFEYGADVNIEDDNGCYPI-----HIAIKHN------------------- 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675378395  669 qnrvkklpgingigslpqvTMDKINQWLQNGDLEHIKefamDGYGQHlvgktswsedvrqylkslPLFlmtlgsafHAVE 748
Cdd:PHA02874  169 -------------------FFDIIKLLLEKGAYANVK----DNNGES------------------PLH--------NAAE 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675378395  749 RGDVESLdKLIASEENLLRSKNSDGSTLMHHAVLHDQlDVLNYFLHKypTLVNIKDRNGRTPLHVAGQQK-NQYVYTILT 827
Cdd:PHA02874  200 YGDYACI-KLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIELLINN--ASINDQDIDGSTPLHHAINPPcDIDIIDILL 275

                         250
                  ....*....|....*
gi 675378395  828 AAGADPMILDQKGRS 842
Cdd:PHA02874  276 YHKADISIKDNKGEN 290
Ank_4 pfam13637
Ankyrin repeats (many copies);
744-793 1.62e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.02  E-value: 1.62e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 675378395   744 FHAVERGDVESLDKLIASEENLLRSkNSDGSTLMHHAVLHDQLDVLNYFL 793
Cdd:pfam13637    6 HAAAASGHLELLRLLLEKGADINAV-DGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
773-814 1.64e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.02  E-value: 1.64e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 675378395   773 GSTLMHHAVLHDQLDVLNYfLHKYPTLVNIKDRNGRTPLHVA 814
Cdd:pfam13637    1 ELTALHAAAASGHLELLRL-LLEKGADINAVDGNGETALHFA 41
Ank_4 pfam13637
Ankyrin repeats (many copies);
91-131 1.74e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 37.64  E-value: 1.74e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 675378395    91 SPMHKAVLFSQKPIIDYLLDrYPSVVHARDHKGRTPLHYAA 131
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLE-KGADINAVDGNGETALHFAA 42
Ank_4 pfam13637
Ankyrin repeats (many copies);
60-109 1.99e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 37.64  E-value: 1.99e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 675378395    60 IHKAVSTGNLRDVQHLIDRKKLAFCRDHMGASPMHKAVLFSQKPIIDYLL 109
Cdd:pfam13637    5 LHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 595-631 2.05e-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: 36.88  E-value: 2.05e-03
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 675378395   595 EGRTALHYAAAMSrepGASNYFKILLEAGADSRIRDN 631
Cdd:pfam00023    1 DGNTPLHLAAGRR---GNLEIVKLLLSKGADVNARDK 34
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 1133-1166 2.26e-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: 36.88  E-value: 2.26e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 675378395  1133 EGRTPLHYAAVMRDGGSYYRILLMAGADETVKDK 1166
Cdd:pfam00023    1 DGNTPLHLAAGRRGNLEIVKLLLSKGADVNARDK 34
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 1096-1160 2.29e-03

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: 2.29e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 675378395 1096 RDHLGASPLHLAVLHGHTDIVKYIIDNFPEALDGPDN----EGRTPLHyAAVMRDGGSYYRILLMAGAD 1160
Cdd:cd22192    47 RGALGETALHVAALYDNLEAAVVLMEAAPELVNEPMTsdlyQGETALH-IAVVNQNLNLVRELIARGAD 114
DD_DPY30_SDC1 cd22965
dimerization/docking (D/D) domain found in the DPY30/SDC1 family; This family includes DPY30 ...
 1280-1312 2.38e-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: 37.02  E-value: 2.38e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 675378395 1280 YLATVLGDALIKGLTQVAARRPRDPIGYLATYL 1312
Cdd:cd22965     4 YLDKTVVPVLLEGLKELAKERPEDPLEFLAEYL 36
Ank_4 pfam13637
Ankyrin repeats (many copies);
530-582 2.50e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 37.25  E-value: 2.50e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 675378395   530 EAIHSAVSNDDLNELQAqLHETDHMVLAKDHFGMAPIHRAVLMNKPETLAFLI 582
Cdd:pfam13637    3 TALHAAAASGHLELLRL-LLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
 773-850 2.63e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 41.93  E-value: 2.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675378395  773 GSTLMHHAVLHDQ-LDVLNyFLHKYPTLVNIKDRNGRTPLHV--AGQQKNQYVYTILTAAGADPMILDQKGRSAEYYYTS 849
Cdd:PHA03095   83 GFTPLHLYLYNATtLDVIK-LLIKAGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLK 161


                  .
gi 675378395  850 S 850
Cdd:PHA03095  162 S 162
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 116-435 3.03e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 41.97  E-value: 3.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675378395  116 VHARDHKGRTPLHYAAVLSDGgEIYKMLLDHGADTKATDVYG-NRPEYYMHARDEMDIQALKEGHdtgkspkmtkmkhfq 194
Cdd:PHA02876  171 VNAKDIYCITPIHYAAERGNA-KMVNLLLSYGADVNIIALDDlSVLECAVDSKNIDTIKAIIDNR--------------- 234

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675378395  195 sNDGNKKDTVARSAkpagtrtqiremLTSGNLEALEELVLQGHGDKLLGESSNNPLvrdfirmvpiymeriyeiHRAVAR 274
Cdd:PHA02876  235 -SNINKNDLSLLKA------------IRNEDLETSLLLYDAGFSVNSIDDCKNTPL------------------HHASQA 283

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675378395  275 GRL-RDVQTLLDRKKLALARDPLGATPLHKAVMYGHNdvAEYITLNFPLAKDTKDLDG--RTPLHYAAALKDNHELYNML 351
Cdd:PHA02876  284 PSLsRLVPKLLERGADVNAKNIKGETPLYLMAKNGYD--TENIRTLIMLGADVNAADRlyITPLHQASTLDRNKDIVITL 361

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675378395  352 ISLGANPLVLDYRGKTAEYYLQFPEHLHLeqmikqsqrlnANYMANHANRMKAVSPK----------RKSPYPTRATLaL 421
Cdd:PHA02876  362 LELGANVNARDYCDKTPIHYAAVRNNVVI-----------INTLLDYGADIEALSQKigtalhfalcGTNPYMSVKTL-I 429

                         330
                  ....*....|....
gi 675378395  422 DFNANIRPMNGELS 435
Cdd:PHA02876  430 DRGANVNSKNKDLS 443
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 60-147 3.71e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 41.49  E-value: 3.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675378395   60 IHKAVSTGNLRDVQHLIDRKKLAFCRDHMGASPMHKAVLFSQKPIIDYLLDRyPSVVHARDHKGRTPLHYAAVLSDGGEI 139
Cdd:PHA02874  128 LHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEK-GAYANVKDNNGESPLHNAAEYGDYACI 206


                  ....*...
gi 675378395  140 yKMLLDHG 147
Cdd:PHA02874  207 -KLLIDHG 213
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
743-843 4.37e-03

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 40.71  E-value: 4.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675378395  743 AFHAVERGDVESLDKLIASEENLLRSKNSDGSTLMHHAVLHDQLDVLNYFLHKYPTLVNIKDRNGRTPLHVAGQQKNQYV 822
Cdd:COG0666    23 LLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEI 102

                          90       100
                  ....*....|....*....|.
gi 675378395  823 YTILTAAGADPMILDQKGRSA 843
Cdd:COG0666   103 VKLLLEAGADVNARDKDGETP 123
Ank_5 pfam13857
Ankyrin repeats (many copies);
548-603 4.39e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.56  E-value: 4.39e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 675378395   548 LHETDHM-VLAKDHFGMAPIHRAVLMNKPETLAFLIDRfPETVNARDKEGRTALHYA 603
Cdd:pfam13857    1 LLEHGPIdLNRLDGEGYTPLHVAAKYGALEIVRVLLAY-GVDLNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 330-358 4.57e-03

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.03  E-value: 4.57e-03
                            10        20
                    ....*....|....*....|....*....
gi 675378395    330 DGRTPLHYAAAlKDNHELYNMLISLGANP 358
Cdd:smart00248    1 DGRTPLHLAAE-NGNLEVVKLLLDKGADI 28
Ank_4 pfam13637
Ankyrin repeats (many copies);
1071-1120 4.88e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.48  E-value: 4.88e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 675378395  1071 VHDAVVRGNLGEVESVLTRKRFALSRDHLGASPLHLAVLHGHTDIVKYII 1120
Cdd:pfam13637    5 LHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00121 PTZ00121
MAEBL; Provisional
 872-970 4.96e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.67  E-value: 4.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675378395  872 EKISSSPEENKKDEQGNEAEQQSKDSKNSKSPDKEEESDTKTEVKIAENEEKKDAEGSTTA------TAEKAKTPVPEGK 945
Cdd:PTZ00121 1664 AEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAeeenkiKAEEAKKEAEEDK 1743

                          90       100
                  ....*....|....*....|....*
gi 675378395  946 STDSEQEEKQGNDDKENNSDKEEGK 970
Cdd:PTZ00121 1744 KKAEEAKKDEEEKKKIAHLKKEEEK 1768
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1074-1187 6.67e-03

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 40.32  E-value: 6.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675378395 1074 AVVRGNLGEVESVLTRKRFALSRDHLGASPLHLAVLHGHTDIVKYIIDNFPEALDGPDNEGRTPLHYAAVMRDGGSYyRI 1153
Cdd:COG0666    27 AAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIV-KL 105

                          90       100       110
                  ....*....|....*....|....*....|....
gi 675378395 1154 LLMAGADETVKDKAGHTPDYYLTHAGVLTIRDLL 1187
Cdd:COG0666   106 LLEAGADVNARDKDGETPLHLAAYNGNLEIVKLL 139
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 89-160 7.31e-03

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: 40.77  E-value: 7.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675378395   89 GASPMHKAVLFSQKPIIDYLLDRYPSVVHARD-------------HKGRTPLHYAAVLSDGgEIYKMLLDHGADTKATDV 155
Cdd:cd22192    89 GETALHIAVVNQNLNLVRELIARGADVVSPRAtgtffrpgpknliYYGEHPLSFAACVGNE-EIVRLLIEHGADIRAQDS 167


                  ....*
gi 675378395  156 YGNRP 160
Cdd:cd22192   168 LGNTV 172
PRK08581 PRK08581
amidase domain-containing protein;
848-967 7.60e-03

amidase domain-containing protein;


Pssm-ID: 236304 [Multi-domain]  Cd Length: 619  Bit Score: 40.54  E-value: 7.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675378395  848 TSSIKPTKPQISPSSSTPEDSSGNEKISSSpeeNKKDEQGNEAEQQSKDSKNSKSPDKEEESDTKTevkiaeneeKKDAE 927
Cdd:PRK08581  151 KNSDSSIKNDTDTQSSKQDKADNQKAPSSN---NTKPSTSNKQPNSPKPTQPNQSNSQPASDDTAN---------QKSSS 218

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 675378395  928 GSTTATAEKAKTPVPEGKSTDSEQEEKQGNDDKENNSDKE 967
Cdd:PRK08581  219 KDNQSMSDSALDSILDQYSEDAKKTQKDYASQSKKDKTET 258
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 268-366 8.32e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 40.33  E-value: 8.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675378395  268 IHRAVARGRLRDVQTLLDRKKLALARDPLGATPLHKAVMygHNDVAEYITLNFPLAKDTkDLDGRTPLHYAAALKDNHEL 347
Cdd:PHA02874  194 LHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII--HNRSAIELLINNASINDQ-DIDGSTPLHHAINPPCDIDI 270

                          90
                  ....*....|....*....
gi 675378395  348 YNMLISLGANPLVLDYRGK 366
Cdd:PHA02874  271 IDILLYHKADISIKDNKGE 289
Ank_5 pfam13857
Ankyrin repeats (many copies);
108-158 8.58e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.79  E-value: 8.58e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 675378395   108 LLDRYPSVVHARDHKGRTPLHYAAvlSDGG-EIYKMLLDHGADTKATDVYGN 158
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAA--KYGAlEIVRVLLAYGVDLNLKDEEGL 50
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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