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Conserved domains on  [gi|1034607132|ref|XP_016882052|]
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KN motif and ankyrin repeat domain-containing protein 3 isoform X1 [Homo sapiens]

Protein Classification

ankyrin repeat domain-containing protein( domain architecture ID 13778391)

ankyrin (ANK) repeat domain-containing protein may be involved in mediating protein-protein interactions; ankyrin (ANK) repeat domain-containing protein may be involved in mediating protein-protein interactions; similar to Homo sapiens ankyrin repeat and SOCS box protein 7 isoform 1; ankyrin repeat (ANK) domain-containing protein may be involved in mediating protein-protein interactions

Gene Ontology:  GO:0005515
PubMed:  15152081|17176038

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
648-837 4.48e-40

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 149.72  E-value: 4.48e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034607132 648 VARMLEGVRRLGPELLAHVVNLADGNGNTALHYSVSHGNLAIASLLLDTGAcEVNRQNRAGYSALMLAAltsvrqEEEDM 727
Cdd:COG0666    61 AALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGA-DVNARDKDGETPLHLAA------YNGNL 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034607132 728 AVVQRLFCMG-DVNAKASQtGQTALMLAISHGRQDMVATLLACGADVNAQDADGATALMCASEYGRLDTVRLLLTQpGCD 806
Cdd:COG0666   134 EIVKLLLEAGaDVNAQDND-GNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEA-GAD 211

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1034607132 807 PAILDNEGTSALAIALEAEQDEVAALLHAHL 837
Cdd:COG0666   212 VNAKDNDGKTALDLAAENGNLEIVKLLLEAG 242
KN_motif pfam12075
KN motif; This small motif is found at the N-terminus of Kank proteins and has been called the ...
 84-125 8.21e-17

KN motif; This small motif is found at the N-terminus of Kank proteins and has been called the KN (for Kank N-terminal) motif. This protein is found in eukaryotes. Proteins in this family are typically between 413 to 1202 amino acids in length. This protein is found associated with pfam00023. This protein has two conserved sequence motifs: TPYG and LDLDF. Kank1 was obtained by positional cloning of a tumor suppressor gene in renal cell carcinoma, while the other members were found by homology search. The family is involved in the regulation of actin polymerization and cell motility through signaling pathways containing PI3K/Akt and/or unidentified modulators/effectors.


:

Pssm-ID: 432311  Cd Length: 39  Bit Score: 74.69  E-value: 8.21e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1034607132  84 PYSVETPYGFHLDLDFLKYIEELERGPAARRAPGPptsRRPR 125
Cdd:pfam12075   1 PYSVETPYGFHLDLDFLKYVEDIESGQTIRRARVQ---RRPR 39
PksD super family cl43841
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
 109-637 3.45e-06

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


The actual alignment was detected with superfamily member COG3321:

Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 51.03  E-value: 3.45e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034607132  109 GPAARRAPGPPTS--RRPRAPRPGLAGARSPGAWTSSESLASDDGGAPGILSQGAPSGLLMQPLSPRAPVRNPRVEHTLR 186
Cdd:COG3321    854 PGRGRRRVPLPTYpfQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALV 933

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034607132  187 ETSRRLELAQTHERAPSPGRGVPRSPRGSGRSSPAPNLAPASPGPAQLQLVREQMAAALRRLRELEDQARTLPELQEQVR 266
Cdd:COG3321    934 ALAAAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLA 1013

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034607132  267 ALRAEKARLLAGRAQPEPDGEAETRPDKLAQLRRLTERLATSERGGRARASPRADSPDGLAAGRSEGALQVLDGEVGSLD 346
Cdd:COG3321   1014 AAAAAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAA 1093

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034607132  347 GTPQTREVAAEAVPETREAGAQAVPETREAGVEAAPETVEADAWVTEALLGLPAAAERELELLRASLEHQRGVSELLRGR 426
Cdd:COG3321   1094 ALALALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAAL 1173

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034607132  427 LRELEEAREAAEEAAAGARAQLREATTQTPWSCAEKAAQTESPAEAPSLTQESSPGSMDGDRAVAPAGILKSIMKKRDGT 506
Cdd:COG3321   1174 LLALALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAA 1253

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034607132  507 PGAQPSSGPKSLQFVGVLNGEYESSSSEDASDSDGDSENGGAEPPGSSSGSGDDSGGGSDSGTPGPPSGGDIRDPEPEAE 586
Cdd:COG3321   1254 ALLAALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAAALAAL 1333

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1034607132  587 AEPQQVAQGRCELSPRLREACVALQRQLSRPRGVASDGGAVRLVAQEWFRV 637
Cdd:COG3321   1334 AAAVAAALALAAAAAAAAAAAAAAAAAAALAAAAGAAAAAAALALAALAAA 1384
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
648-837 4.48e-40

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 149.72  E-value: 4.48e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034607132 648 VARMLEGVRRLGPELLAHVVNLADGNGNTALHYSVSHGNLAIASLLLDTGAcEVNRQNRAGYSALMLAAltsvrqEEEDM 727
Cdd:COG0666    61 AALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGA-DVNARDKDGETPLHLAA------YNGNL 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034607132 728 AVVQRLFCMG-DVNAKASQtGQTALMLAISHGRQDMVATLLACGADVNAQDADGATALMCASEYGRLDTVRLLLTQpGCD 806
Cdd:COG0666   134 EIVKLLLEAGaDVNAQDND-GNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEA-GAD 211

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1034607132 807 PAILDNEGTSALAIALEAEQDEVAALLHAHL 837
Cdd:COG0666   212 VNAKDNDGKTALDLAAENGNLEIVKLLLEAG 242
KN_motif pfam12075
KN motif; This small motif is found at the N-terminus of Kank proteins and has been called the ...
 84-125 8.21e-17

KN motif; This small motif is found at the N-terminus of Kank proteins and has been called the KN (for Kank N-terminal) motif. This protein is found in eukaryotes. Proteins in this family are typically between 413 to 1202 amino acids in length. This protein is found associated with pfam00023. This protein has two conserved sequence motifs: TPYG and LDLDF. Kank1 was obtained by positional cloning of a tumor suppressor gene in renal cell carcinoma, while the other members were found by homology search. The family is involved in the regulation of actin polymerization and cell motility through signaling pathways containing PI3K/Akt and/or unidentified modulators/effectors.


Pssm-ID: 432311  Cd Length: 39  Bit Score: 74.69  E-value: 8.21e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1034607132  84 PYSVETPYGFHLDLDFLKYIEELERGPAARRAPGPptsRRPR 125
Cdd:pfam12075   1 PYSVETPYGFHLDLDFLKYVEDIESGQTIRRARVQ---RRPR 39
Ank_2 pfam12796
Ankyrin repeats (3 copies);
678-777 1.17e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.92  E-value: 1.17e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034607132 678 LHYSVSHGNLAIASLLLDTGaCEVNRQNRAGYSALMLAALTSVRQeeedmaVVQRLFCMGDVNAKASqtGQTALMLAISH 757
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENG-ADANLQDKNGRTALHLAAKNGHLE------IVKLLLEHADVNLKDN--GRTALHYAARS 71

                          90       100
                  ....*....|....*....|
gi 1034607132 758 GRQDMVATLLACGADVNAQD 777
Cdd:pfam12796  72 GHLEIVKLLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 667-823 5.41e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 62.73  E-value: 5.41e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034607132 667 VNLADGNGNTALHYSVSHGN---LAIASLLLDTGAcEVNRQNRAGYSALMLAALTSVRQEeedmaVVQRLFCMG-DVNAK 742
Cdd:PHA03095   40 VNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGA-DVNAPERCGFTPLHLYLYNATTLD-----VIKLLIKAGaDVNAK 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034607132 743 aSQTGQTAL--MLAISHGRQDMVATLLACGADVNAQDADGATALMCASEYGR--LDTVRLLLTQpGCDPAILDNEGTSAL 818
Cdd:PHA03095  114 -DKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNanVELLRLLIDA-GADVYAVDDRFRSLL 191


                  ....*
gi 1034607132 819 AIALE 823
Cdd:PHA03095  192 HHHLQ 196
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
 109-637 3.45e-06

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 51.03  E-value: 3.45e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034607132  109 GPAARRAPGPPTS--RRPRAPRPGLAGARSPGAWTSSESLASDDGGAPGILSQGAPSGLLMQPLSPRAPVRNPRVEHTLR 186
Cdd:COG3321    854 PGRGRRRVPLPTYpfQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALV 933

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034607132  187 ETSRRLELAQTHERAPSPGRGVPRSPRGSGRSSPAPNLAPASPGPAQLQLVREQMAAALRRLRELEDQARTLPELQEQVR 266
Cdd:COG3321    934 ALAAAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLA 1013

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034607132  267 ALRAEKARLLAGRAQPEPDGEAETRPDKLAQLRRLTERLATSERGGRARASPRADSPDGLAAGRSEGALQVLDGEVGSLD 346
Cdd:COG3321   1014 AAAAAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAA 1093

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034607132  347 GTPQTREVAAEAVPETREAGAQAVPETREAGVEAAPETVEADAWVTEALLGLPAAAERELELLRASLEHQRGVSELLRGR 426
Cdd:COG3321   1094 ALALALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAAL 1173

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034607132  427 LRELEEAREAAEEAAAGARAQLREATTQTPWSCAEKAAQTESPAEAPSLTQESSPGSMDGDRAVAPAGILKSIMKKRDGT 506
Cdd:COG3321   1174 LLALALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAA 1253

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034607132  507 PGAQPSSGPKSLQFVGVLNGEYESSSSEDASDSDGDSENGGAEPPGSSSGSGDDSGGGSDSGTPGPPSGGDIRDPEPEAE 586
Cdd:COG3321   1254 ALLAALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAAALAAL 1333

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1034607132  587 AEPQQVAQGRCELSPRLREACVALQRQLSRPRGVASDGGAVRLVAQEWFRV 637
Cdd:COG3321   1334 AAAVAAALALAAAAAAAAAAAAAAAAAAALAAAAGAAAAAAALALAALAAA 1384
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 673-698 2.39e-04

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: 39.11  E-value: 2.39e-04
                           10        20
                   ....*....|....*....|....*.
gi 1034607132  673 NGNTALHYSVSHGNLAIASLLLDTGA 698
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGA 26
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 674-829 5.16e-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: 43.85  E-value: 5.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034607132 674 GNTALHYSVSHGNLAIASLLLDTGACEVNR----QNRAGYSALMLAALTsvrqeeEDMAVVQRLFCMG-DV-NAKASQT- 746
Cdd:cd22192    51 GETALHVAALYDNLEAAVVLMEAAPELVNEpmtsDLYQGETALHIAVVN------QNLNLVRELIARGaDVvSPRATGTf 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034607132 747 -----------GQTALMLAISHGRQDMVATLLACGADVNAQDADGATALmcaseygrldtvRLLLTQPGCDPA--ILDne 813
Cdd:cd22192   125 frpgpknliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL------------HILVLQPNKTFAcqMYD-- 190

                         170
                  ....*....|....*.
gi 1034607132 814 gtsaLAIALEAEQDEV 829
Cdd:cd22192   191 ----LILSYDKEDDLQ 202
HpnN TIGR03480
hopanoid biosynthesis associated RND transporter like protein HpnN; The genomes containing ...
 239-338 2.59e-03

hopanoid biosynthesis associated RND transporter like protein HpnN; The genomes containing members of this family share the machinery for the biosynthesis of hopanoid lipids. Furthermore, the genes of this family are usually located proximal to other components of this biological process. The proteins appear to be related to the RND family of export proteins, particularly the hydrophobe/amphiphile efflux-3 (HAE3) family represented by TIGR00921.


Pssm-ID: 274598 [Multi-domain]  Cd Length: 862  Bit Score: 41.52  E-value: 2.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034607132 239 EQMAAALRRLRELeDQARTL----PELQEQVRALRAEKARLLAGRAQPEPDGEAETRPDKLAQLRRLTERLatserggrA 314
Cdd:TIGR03480 514 RALTERLEALPEV-DQVVTLpdfvPDDQEAKLALIADLALVLGPTLNPGEADPAPSAEEVAAALRRLAARL--------R 584

                          90       100
                  ....*....|....*....|....
gi 1034607132 315 RASPRADSPDGLAAGRSEGALQVL 338
Cdd:TIGR03480 585 AAAAKSQDPDAAAAGRLAASLDRL 608
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
648-837 4.48e-40

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 149.72  E-value: 4.48e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034607132 648 VARMLEGVRRLGPELLAHVVNLADGNGNTALHYSVSHGNLAIASLLLDTGAcEVNRQNRAGYSALMLAAltsvrqEEEDM 727
Cdd:COG0666    61 AALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGA-DVNARDKDGETPLHLAA------YNGNL 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034607132 728 AVVQRLFCMG-DVNAKASQtGQTALMLAISHGRQDMVATLLACGADVNAQDADGATALMCASEYGRLDTVRLLLTQpGCD 806
Cdd:COG0666   134 EIVKLLLEAGaDVNAQDND-GNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEA-GAD 211

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1034607132 807 PAILDNEGTSALAIALEAEQDEVAALLHAHL 837
Cdd:COG0666   212 VNAKDNDGKTALDLAAENGNLEIVKLLLEAG 242
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
661-833 3.58e-34

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 132.77  E-value: 3.58e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034607132 661 ELLAH--VVNLADGNGNTALHYSVSHGNLAIASLLLDTGAcEVNRQNRAGYSALMLAAltsvrqEEEDMAVVQRLFCMG- 737
Cdd:COG0666   105 LLLEAgaDVNARDKDGETPLHLAAYNGNLEIVKLLLEAGA-DVNAQDNDGNTPLHLAA------ANGNLEIVKLLLEAGa 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034607132 738 DVNAKaSQTGQTALMLAISHGRQDMVATLLACGADVNAQDADGATALMCASEYGRLDTVRLLLTQpGCDPAILDNEGTSA 817
Cdd:COG0666   178 DVNAR-DNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA-GADLNAKDKDGLTA 255

                         170
                  ....*....|....*.
gi 1034607132 818 LAIALEAEQDEVAALL 833
Cdd:COG0666   256 LLLAAAAGAALIVKLL 271
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
648-836 3.29e-31

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 124.30  E-value: 3.29e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034607132 648 VARMLEGVRRLGPELLAHVVNLADGNGNTALHYSVSHGNLAIASLLLDTGAcEVNRQNRAGYSALMLAAltsvrqEEEDM 727
Cdd:COG0666    28 AALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGA-DINAKDDGGNTLLHAAA------RNGDL 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034607132 728 AVVQRLFCMG-DVNAKASQtGQTALMLAISHGRQDMVATLLACGADVNAQDADGATALMCASEYGRLDTVRLLLTQpGCD 806
Cdd:COG0666   101 EIVKLLLEAGaDVNARDKD-GETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEA-GAD 178

                         170       180       190
                  ....*....|....*....|....*....|
gi 1034607132 807 PAILDNEGTSALAIALEAEQDEVAALLHAH 836
Cdd:COG0666   179 VNARDNDGETPLHLAAENGHLEIVKLLLEA 208
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
662-815 5.72e-24

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 103.11  E-value: 5.72e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034607132 662 LLAH--VVNLADGNGNTALHYSVSHGNLAIASLLLDTGAcEVNRQNRAGYSALMLAAltsvrqEEEDMAVVQRLFCMG-D 738
Cdd:COG0666   139 LLEAgaDVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGA-DVNARDNDGETPLHLAA------ENGHLEIVKLLLEAGaD 211

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034607132 739 VNAKASQtGQTALMLAISHGRQDMVATLLACGADVNAQDADGATALMCASEYGRLDTVRLLLTQPGCDPAILDNEGT 815
Cdd:COG0666   212 VNAKDND-GKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
661-833 1.94e-22

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 98.49  E-value: 1.94e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034607132 661 ELLAHVVNLADGNGNTALHYSVSHGNLAIASLLLDTGACEVNRQNRAGYSALMLAAltsvrqEEEDMAVVQRLFCMGDVN 740
Cdd:COG0666     7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAA------LAGDLLVALLLLAAGADI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034607132 741 AKASQTGQTALMLAISHGRQDMVATLLACGADVNAQDADGATALMCASEYGRLDTVRLLLTQpGCDPAILDNEGTSALAI 820
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA-GADVNAQDNDGNTPLHL 159

                         170
                  ....*....|...
gi 1034607132 821 ALEAEQDEVAALL 833
Cdd:COG0666   160 AAANGNLEIVKLL 172
KN_motif pfam12075
KN motif; This small motif is found at the N-terminus of Kank proteins and has been called the ...
 84-125 8.21e-17

KN motif; This small motif is found at the N-terminus of Kank proteins and has been called the KN (for Kank N-terminal) motif. This protein is found in eukaryotes. Proteins in this family are typically between 413 to 1202 amino acids in length. This protein is found associated with pfam00023. This protein has two conserved sequence motifs: TPYG and LDLDF. Kank1 was obtained by positional cloning of a tumor suppressor gene in renal cell carcinoma, while the other members were found by homology search. The family is involved in the regulation of actin polymerization and cell motility through signaling pathways containing PI3K/Akt and/or unidentified modulators/effectors.


Pssm-ID: 432311  Cd Length: 39  Bit Score: 74.69  E-value: 8.21e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1034607132  84 PYSVETPYGFHLDLDFLKYIEELERGPAARRAPGPptsRRPR 125
Cdd:pfam12075   1 PYSVETPYGFHLDLDFLKYVEDIESGQTIRRARVQ---RRPR 39
Ank_2 pfam12796
Ankyrin repeats (3 copies);
678-777 1.17e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.92  E-value: 1.17e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034607132 678 LHYSVSHGNLAIASLLLDTGaCEVNRQNRAGYSALMLAALTSVRQeeedmaVVQRLFCMGDVNAKASqtGQTALMLAISH 757
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENG-ADANLQDKNGRTALHLAAKNGHLE------IVKLLLEHADVNLKDN--GRTALHYAARS 71

                          90       100
                  ....*....|....*....|
gi 1034607132 758 GRQDMVATLLACGADVNAQD 777
Cdd:pfam12796  72 GHLEIVKLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
751-833 1.50e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.54  E-value: 1.50e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034607132 751 LMLAISHGRQDMVATLLACGADVNAQDADGATALMCASEYGRLDTVRLLLTQPGCDpaiLDNEGTSALAIALEAEQDEVA 830
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVN---LKDNGRTALHYAARSGHLEIV 77


                  ...
gi 1034607132 831 ALL 833
Cdd:pfam12796  78 KLL 80
Ank_2 pfam12796
Ankyrin repeats (3 copies);
712-811 3.78e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 71.69  E-value: 3.78e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034607132 712 LMLAAltsvrqEEEDMAVVQRLFCMG-DVNAKaSQTGQTALMLAISHGRQDMVATLLACgADVNAQDaDGATALMCASEY 790
Cdd:pfam12796   1 LHLAA------KNGNLELVKLLLENGaDANLQ-DKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARS 71

                          90       100
                  ....*....|....*....|.
gi 1034607132 791 GRLDTVRLLLtQPGCDPAILD 811
Cdd:pfam12796  72 GHLEIVKLLL-EKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
711-836 1.26e-12

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 69.21  E-value: 1.26e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034607132 711 ALMLAALTSVRQEEEDMAVVQRLFCMGDVNAKASQTGQTALMLAISHGRQDMVATLLACGADVNAQDADGATALMCASEY 790
Cdd:COG0666    18 LLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARN 97

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1034607132 791 GRLDTVRLLLTQpGCDPAILDNEGTSALAIALEAEQDEVAALLHAH 836
Cdd:COG0666    98 GDLEIVKLLLEA-GADVNARDKDGETPLHLAAYNGNLEIVKLLLEA 142
PHA03095 PHA03095
ankyrin-like protein; Provisional
 667-823 5.41e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 62.73  E-value: 5.41e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034607132 667 VNLADGNGNTALHYSVSHGN---LAIASLLLDTGAcEVNRQNRAGYSALMLAALTSVRQEeedmaVVQRLFCMG-DVNAK 742
Cdd:PHA03095   40 VNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGA-DVNAPERCGFTPLHLYLYNATTLD-----VIKLLIKAGaDVNAK 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034607132 743 aSQTGQTAL--MLAISHGRQDMVATLLACGADVNAQDADGATALMCASEYGR--LDTVRLLLTQpGCDPAILDNEGTSAL 818
Cdd:PHA03095  114 -DKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNanVELLRLLIDA-GADVYAVDDRFRSLL 191


                  ....*
gi 1034607132 819 AIALE 823
Cdd:PHA03095  192 HHHLQ 196
Ank_4 pfam13637
Ankyrin repeats (many copies);
749-800 1.11e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.59  E-value: 1.11e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1034607132 749 TALMLAISHGRQDMVATLLACGADVNAQDADGATALMCASEYGRLDTVRLLL 800
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 766-861 1.71e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 61.45  E-value: 1.71e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034607132 766 LLACGADVNAQDADGATALMCASEYGRLDTVRLLLtQPGCDPAILDNEGTSALAIALEAEQDEVAALLHAHlSSGQPDTQ 845
Cdd:PTZ00322  101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLL-EFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH-SQCHFELG 178

                          90
                  ....*....|....*.
gi 1034607132 846 SESPPGSQTATPGEGE 861
Cdd:PTZ00322  179 ANAKPDSFTGKPPSLE 194
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 667-823 2.35e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 57.28  E-value: 2.35e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034607132 667 VNLADGNGNTALHYSVSHGNLAIASLLLDTGAcEVNRQNRAGYSALMLAAltsvrqEEEDMAVVQRLFCMGDVNAKASQT 746
Cdd:PHA02874  150 VNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGA-YANVKDNNGESPLHNAA------EYGDYACIKLLIDHGNHIMNKCKN 222

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034607132 747 GQTALMLAISHGRQdmVATLLACGADVNAQDADGATALMCASEYG-RLDTVRLLLTQPGcDPAILDNEGTSALAIALE 823
Cdd:PHA02874  223 GFTPLHNAIIHNRS--AIELLINNASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKA-DISIKDNKGENPIDTAFK 297
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 668-862 4.47e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 53.72  E-value: 4.47e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034607132 668 NLADGNGNTALHYSVSHGNLAIASLLLDTgACEVNRQNRAGYSALMLAAltsvrqeeedMAVVQRLFCMGDVNAKAS--Q 745
Cdd:PLN03192  552 DIGDSKGRTPLHIAASKGYEDCVLVLLKH-ACNVHIRDANGNTALWNAI----------SAKHHKIFRILYHFASISdpH 620

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034607132 746 TGQTALMLAISHGRQDMVATLLACGADVNAQDADGATALMCASEYGRLDTVRLLLTQ-PGCDPAILDNEGTSA-LAIALE 823
Cdd:PLN03192  621 AAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNgADVDKANTDDDFSPTeLRELLQ 700

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1034607132 824 AEQDEVAALLHAHLSSGQPDTQSE--SPPGSQTATPGEGEC 862
Cdd:PLN03192  701 KRELGHSITIVDSVPADEPDLGRDggSRPGRLQGTSSDNQC 741
Ank_5 pfam13857
Ankyrin repeats (many copies);
766-821 6.51e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.96  E-value: 6.51e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034607132 766 LLACG-ADVNAQDADGATALMCASEYGRLDTVRLLLTqPGCDPAILDNEGTSALAIA 821
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLA-YGVDLNLKDEEGLTALDLA 56
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 667-800 1.50e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 51.59  E-value: 1.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034607132 667 VNLADGNGNTALHYSVSH--GNLAIASLLLDTGaCEVNRQNRAGYSALMLAaltsVRQEEEDMAVVQRLFCMG-DVNAKA 743
Cdd:PHA03100   99 VNAPDNNGITPLLYAISKksNSYSIVEYLLDNG-ANVNIKNSDGENLLHLY----LESNKIDLKILKLLIDKGvDINAKN 173

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034607132 744 S---------------QTGQTALMLAISHGRQDMVATLLACGADVNAQDADGATALMCASEYGRLDTVRLLL 800
Cdd:PHA03100  174 RvnyllsygvpinikdVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLL 245
Ank_5 pfam13857
Ankyrin repeats (many copies);
738-784 1.56e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.80  E-value: 1.56e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1034607132 738 DVNAKaSQTGQTALMLAISHGRQDMVATLLACGADVNAQDADGATAL 784
Cdd:pfam13857   8 DLNRL-DGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 662-822 2.16e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 51.03  E-value: 2.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034607132 662 LLAH--VVNLADGN-GNTALHYSVSHGNLAIASLLLDTGAcEVNRQNRAGYSALMLAaltsVRQEEEDmaVVQRLFCMGD 738
Cdd:PHA02878  153 LLSYgaDINMKDRHkGNTALHYATENKDQRLTELLLSYGA-NVNIPDKTNNSPLHHA----VKHYNKP--IVHILLENGA 225

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034607132 739 VNAKASQTGQTALMLAISHGRQ-DMVATLLACGADVNAQDA-DGATALMCA--SEygrlDTVRLLLtQPGCDPAILDNEG 814
Cdd:PHA02878  226 STDARDKCGNTPLHISVGYCKDyDILKLLLEHGVDVNAKSYiLGLTALHSSikSE----RKLKLLL-EYGADINSLNSYK 300


                  ....*...
gi 1034607132 815 TSALAIAL 822
Cdd:PHA02878  301 LTPLSSAV 308
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
 109-637 3.45e-06

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 51.03  E-value: 3.45e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034607132  109 GPAARRAPGPPTS--RRPRAPRPGLAGARSPGAWTSSESLASDDGGAPGILSQGAPSGLLMQPLSPRAPVRNPRVEHTLR 186
Cdd:COG3321    854 PGRGRRRVPLPTYpfQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALV 933

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034607132  187 ETSRRLELAQTHERAPSPGRGVPRSPRGSGRSSPAPNLAPASPGPAQLQLVREQMAAALRRLRELEDQARTLPELQEQVR 266
Cdd:COG3321    934 ALAAAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLA 1013

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034607132  267 ALRAEKARLLAGRAQPEPDGEAETRPDKLAQLRRLTERLATSERGGRARASPRADSPDGLAAGRSEGALQVLDGEVGSLD 346
Cdd:COG3321   1014 AAAAAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAA 1093

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034607132  347 GTPQTREVAAEAVPETREAGAQAVPETREAGVEAAPETVEADAWVTEALLGLPAAAERELELLRASLEHQRGVSELLRGR 426
Cdd:COG3321   1094 ALALALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAAL 1173

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034607132  427 LRELEEAREAAEEAAAGARAQLREATTQTPWSCAEKAAQTESPAEAPSLTQESSPGSMDGDRAVAPAGILKSIMKKRDGT 506
Cdd:COG3321   1174 LLALALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAA 1253

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034607132  507 PGAQPSSGPKSLQFVGVLNGEYESSSSEDASDSDGDSENGGAEPPGSSSGSGDDSGGGSDSGTPGPPSGGDIRDPEPEAE 586
Cdd:COG3321   1254 ALLAALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAAALAAL 1333

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1034607132  587 AEPQQVAQGRCELSPRLREACVALQRQLSRPRGVASDGGAVRLVAQEWFRV 637
Cdd:COG3321   1334 AAAVAAALALAAAAAAAAAAAAAAAAAAALAAAAGAAAAAAALALAALAAA 1384
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 667-814 4.17e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 50.26  E-value: 4.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034607132 667 VNLADGNGNTALHYSVSHGNLAIASLLLDTGAcEVNRQNRAGYSALMLAALTSVrqeeeDMAVVQRLFCMG-DVNAKASQ 745
Cdd:PHA02878  194 VNIPDKTNNSPLHHAVKHYNKPIVHILLENGA-STDARDKCGNTPLHISVGYCK-----DYDILKLLLEHGvDVNAKSYI 267

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034607132 746 TGQTALMLAISHgrQDMVATLLACGADVNAQDADGATAL-MCASEYGRLDTVRLLLTQPGC----DPAILDNEG 814
Cdd:PHA02878  268 LGLTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLsSAVKQYLCINIGRILISNICLlkriKPDIKNSEG 339
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 747-777 7.21e-06

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: 43.43  E-value: 7.21e-06
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1034607132 747 GQTALMLAISH-GRQDMVATLLACGADVNAQD 777
Cdd:pfam00023   2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
Ank_2 pfam12796
Ankyrin repeats (3 copies);
661-705 8.66e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 44.72  E-value: 8.66e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1034607132 661 ELLAHVVNLADGNGNTALHYSVSHGNLAIASLLLDTGAcEVNRQN 705
Cdd:pfam12796  48 LLLEHADVNLKDNGRTALHYAARSGHLEIVKLLLEKGA-DINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 678-833 8.90e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 48.89  E-value: 8.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034607132 678 LHYSVSHGNLAIASLLLDTGACE-------------------------------------VNRQNRAGYSALMLAALTSV 720
Cdd:PHA03100   39 LYLAKEARNIDVVKILLDNGADInsstknnstplhylsnikynltdvkeivkllleyganVNAPDNNGITPLLYAISKKS 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034607132 721 rqeeEDMAVVQRLFCMG-DVNAKASqTGQTALMLAISHGRQD--MVATLLACGADVNAQ----------------DADGA 781
Cdd:PHA03100  119 ----NSYSIVEYLLDNGaNVNIKNS-DGENLLHLYLESNKIDlkILKLLIDKGVDINAKnrvnyllsygvpinikDVYGF 193

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1034607132 782 TALMCASEYGRLDTVRLLLTQpGCDPAILDNEGTSALAIALEAEQDEVAALL 833
Cdd:PHA03100  194 TPLHYAVYNNNPEFVKYLLDL-GANPNLVNKYGDTPLHIAILNNNKEIFKLL 244
Ank_2 pfam12796
Ankyrin repeats (3 copies);
784-836 2.66e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 43.57  E-value: 2.66e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1034607132 784 LMCASEYGRLDTVRLLLtQPGCDPAILDNEGTSALAIALEAEQDEVAALLHAH 836
Cdd:pfam12796   1 LHLAAKNGNLELVKLLL-ENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH 52
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 667-833 6.79e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 46.11  E-value: 6.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034607132 667 VNLADGNGNTALHYSVSHGNLAIASLLLDTGAcEVNRQNRAGYSALmlaaLTSVRQEEEDMAvvqRLFCMGDVNAKasqt 746
Cdd:PHA02874   28 INISVDETTTPLIDAIRSGDAKIVELFIKHGA-DINHINTKIPHPL----LTAIKIGAHDII---KLLIDNGVDTS---- 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034607132 747 gqtalMLAISHGRQDMVATLLACGADVNAQDADGATALMCASEYGRLDTVRLLLtQPGCDPAILDNEGTSALAIALEAEQ 826
Cdd:PHA02874   96 -----ILPIPCIEKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLF-EYGADVNIEDDNGCYPIHIAIKHNF 169


                  ....*..
gi 1034607132 827 DEVAALL 833
Cdd:PHA02874  170 FDIIKLL 176
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 747-806 9.81e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.04  E-value: 9.81e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034607132 747 GQTALMLAISHGRQDMVATLLACGADVNAQDADGATALMCASEYGRLDTVRLLLTQPGCD 806
Cdd:PTZ00322  115 GRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCH 174
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 673-810 1.09e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 45.75  E-value: 1.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034607132 673 NGNTALHYSVSHGNLAIASLLLDTGAcEVNRQNRAGYSALMLAALtsvrqeeedmavvqrlfcMGDVNA-------KASQ 745
Cdd:PHA02875  101 DGMTPLHLATILKKLDIMKLLIARGA-DPDIPNTDKFSPLHLAVM------------------MGDIKGiellidhKACL 161

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034607132 746 T-----GQTALMLAISHGRQDMVATLLACGADVNAQDADGATALMC-ASEYGRLDTVRLLLTQpGCDPAIL 810
Cdd:PHA02875  162 DiedccGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCyAIENNKIDIVRLFIKR-GADCNIM 231
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 662-779 1.13e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 46.01  E-value: 1.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034607132 662 LLAHV--VNLADGNGNTALHYSVSHGNLAIASLLLDtgaCEVNRQNRAGYSALMLAAltsvrqEEEDMAVVQRLFCMG-D 738
Cdd:PLN03192  577 LLKHAcnVHIRDANGNTALWNAISAKHHKIFRILYH---FASISDPHAAGDLLCTAA------KRNDLTAMKELLKQGlN 647

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1034607132 739 VNAKASQtGQTALMLAISHGRQDMVATLLACGADVNAQDAD 779
Cdd:PLN03192  648 VDSEDHQ-GATALQVAMAEDHVDMVRLLIMNGADVDKANTD 687
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 693-801 1.85e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 44.95  E-value: 1.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034607132 693 LLDTGAcEVNRQNRAGYSALMLAAltsvrqEEEDMAVVQRLFCMG-DVNAKaSQTGQTALMLAISHGRQDMVATLLACGA 771
Cdd:PHA02874  110 ILDCGI-DVNIKDAELKTFLHYAI------KKGDLESIKMLFEYGaDVNIE-DDNGCYPIHIAIKHNFFDIIKLLLEKGA 181

                          90       100       110
                  ....*....|....*....|....*....|
gi 1034607132 772 DVNAQDADGATALMCASEYGRLDTVRLLLT 801
Cdd:PHA02874  182 YANVKDNNGESPLHNAAEYGDYACIKLLID 211
Ank_4 pfam13637
Ankyrin repeats (many copies);
674-717 1.98e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.95  E-value: 1.98e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1034607132 674 GNTALHYSVSHGNLAIASLLLDTGAcEVNRQNRAGYSALMLAAL 717
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGA-DINAVDGNGETALHFAAS 43
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 721-857 1.99e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 45.05  E-value: 1.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034607132 721 RQEEEDMAVVQRLFCMG-DVNAKASQTgQTALMLAISHGRQDMVATLLACGADVNAQDADGATALMCASEYGRLDTVRll 799
Cdd:PHA02876  152 RIQQDELLIAEMLLEGGaDVNAKDIYC-ITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIK-- 228

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034607132 800 ltqpgcdpAILDNEGTS-----ALAIALEAEQDEVAALLH-AHLSSGQPDTQSESPPGSQTATP 857
Cdd:PHA02876  229 --------AIIDNRSNInkndlSLLKAIRNEDLETSLLLYdAGFSVNSIDDCKNTPLHHASQAP 284
PHA03095 PHA03095
ankyrin-like protein; Provisional
 670-803 2.21e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 44.63  E-value: 2.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034607132 670 ADGNGNTALHY--SVSHGNLAIASLLLDTGaCEVNRQNRAGYSAL-MLAALTSVRQeeedmAVVQRLFCMG-DVNAKaSQ 745
Cdd:PHA03095  183 VDDRFRSLLHHhlQSFKPRARIVRELIRAG-CDPAATDMLGNTPLhSMATGSSCKR-----SLVLPLLIAGiSINAR-NR 255

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034607132 746 TGQTALMLAISHGRQDMVATLLACGADVNAQDADGAT--ALMCASEYGRLdtVRLLL-TQP 803
Cdd:PHA03095  256 YGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTplSLMVRNNNGRA--VRAALaKNP 314
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 673-698 2.39e-04

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: 39.11  E-value: 2.39e-04
                           10        20
                   ....*....|....*....|....*.
gi 1034607132  673 NGNTALHYSVSHGNLAIASLLLDTGA 698
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGA 26
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 673-706 2.81e-04

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: 38.81  E-value: 2.81e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1034607132 673 NGNTALHYSVSH-GNLAIASLLLDTGAcEVNRQNR 706
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGA-DVNARDK 34
Ank_4 pfam13637
Ankyrin repeats (many copies);
667-694 3.33e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.18  E-value: 3.33e-04
                          10        20
                  ....*....|....*....|....*...
gi 1034607132 667 VNLADGNGNTALHYSVSHGNLAIASLLL 694
Cdd:pfam13637  27 INAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 674-829 5.16e-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: 43.85  E-value: 5.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034607132 674 GNTALHYSVSHGNLAIASLLLDTGACEVNR----QNRAGYSALMLAALTsvrqeeEDMAVVQRLFCMG-DV-NAKASQT- 746
Cdd:cd22192    51 GETALHVAALYDNLEAAVVLMEAAPELVNEpmtsDLYQGETALHIAVVN------QNLNLVRELIARGaDVvSPRATGTf 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034607132 747 -----------GQTALMLAISHGRQDMVATLLACGADVNAQDADGATALmcaseygrldtvRLLLTQPGCDPA--ILDne 813
Cdd:cd22192   125 frpgpknliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL------------HILVLQPNKTFAcqMYD-- 190

                         170
                  ....*....|....*.
gi 1034607132 814 gtsaLAIALEAEQDEV 829
Cdd:cd22192   191 ----LILSYDKEDDLQ 202
Ank_5 pfam13857
Ankyrin repeats (many copies);
662-715 7.84e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.10  E-value: 7.84e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034607132 662 LLAHV---VNLADGNGNTALHYSVSHGNLAIASLLLDTGaCEVNRQNRAGYSALMLA 715
Cdd:pfam13857   1 LLEHGpidLNRLDGEGYTPLHVAAKYGALEIVRVLLAYG-VDLNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 747-775 9.28e-04

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: 37.18  E-value: 9.28e-04
                           10        20
                   ....*....|....*....|....*....
gi 1034607132  747 GQTALMLAISHGRQDMVATLLACGADVNA 775
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 673-849 1.00e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 42.67  E-value: 1.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034607132 673 NGNTALHYSVSHGNLAIASLLLDTGAcEVNRQNRAGYSALMLA----------------ALTSVRQ-----------EEE 725
Cdd:PHA02875    1 MDQVALCDAILFGELDIARRLLDIGI-NPNFEIYDGISPIKLAmkfrdseaikllmkhgAIPDVKYpdieselhdavEEG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034607132 726 DMAVVQRLFCMGD-VNAKASQTGQTALMLAISHGRQDMVATLLACGADVNAQDADGATALMCASEYGRLDTVRLLLTQPG 804
Cdd:PHA02875   80 DVKAVEELLDLGKfADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKA 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1034607132 805 CdPAILDNEGTSALAIALEAEQDEVAALLhahLSSG-QPDTQSESP 849
Cdd:PHA02875  160 C-LDIEDCCGCTPLIIAMAKGDIAICKML---LDSGaNIDYFGKNG 201
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
239-460 1.38e-03

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 42.31  E-value: 1.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034607132 239 EQMAAALRRLRELEDQARTLPELQEQVRALRAEKARLLAGRAQPEPDGEAETRPDKLAQLRRLTERLATSERGGRARASP 318
Cdd:COG0515   259 AELAAALRAVLRSLAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAPAAAAAAAAAAAALAA 338

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034607132 319 RADSPDGLAAGRSEGALQVLDGEVGSLDGTPQTREVAAEAVPETREAGAQAVPETREAGVEAAPETVEADAWVTEALLGL 398
Cdd:COG0515   339 AAAAAAAAAAAALLAAAAALAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAA 418

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034607132 399 PAAAERELELLRASLEHQRGVSELLRGRLRELEEAREAAEEAAAGARAQLREATTQTPWSCA 460
Cdd:COG0515   419 ALAAAAAAAAAAAAAAAAAAAAAARLLAAAAAAAAAAAAAPLLAALLAAAALAAAAAAAALA 480
PHA03095 PHA03095
ankyrin-like protein; Provisional
 721-800 1.66e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 41.93  E-value: 1.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034607132 721 RQEEEDMAVVQRLFCMG-DVNAKAS--QTGQTALMLAISHGRQDMVATLLACGADVNAQDADGATALMCASEYG-RLDTV 796
Cdd:PHA03095   21 NASNVTVEEVRRLLAAGaDVNFRGEygKTPLHLYLHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNAtTLDVI 100


                  ....
gi 1034607132 797 RLLL 800
Cdd:PHA03095  101 KLLI 104
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 747-775 1.71e-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: 36.47  E-value: 1.71e-03
                          10        20
                  ....*....|....*....|....*....
gi 1034607132 747 GQTALMLAISHGRQDMVATLLACGADVNA 775
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
HpnN TIGR03480
hopanoid biosynthesis associated RND transporter like protein HpnN; The genomes containing ...
 239-338 2.59e-03

hopanoid biosynthesis associated RND transporter like protein HpnN; The genomes containing members of this family share the machinery for the biosynthesis of hopanoid lipids. Furthermore, the genes of this family are usually located proximal to other components of this biological process. The proteins appear to be related to the RND family of export proteins, particularly the hydrophobe/amphiphile efflux-3 (HAE3) family represented by TIGR00921.


Pssm-ID: 274598 [Multi-domain]  Cd Length: 862  Bit Score: 41.52  E-value: 2.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034607132 239 EQMAAALRRLRELeDQARTL----PELQEQVRALRAEKARLLAGRAQPEPDGEAETRPDKLAQLRRLTERLatserggrA 314
Cdd:TIGR03480 514 RALTERLEALPEV-DQVVTLpdfvPDDQEAKLALIADLALVLGPTLNPGEADPAPSAEEVAAALRRLAARL--------R 584

                          90       100
                  ....*....|....*....|....
gi 1034607132 315 RASPRADSPDGLAAGRSEGALQVL 338
Cdd:TIGR03480 585 AAAAKSQDPDAAAAGRLAASLDRL 608
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 232-424 3.49e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.08  E-value: 3.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034607132 232 AQLQLVREQMAAALRRLRELEDQARtlpELQEQVRALRAEKARLLAGRAQPEPDGEA--ETRPDKLAQLRRLTERLATSE 309
Cdd:COG1196   302 QDIARLEERRRELEERLEELEEELA---ELEEELEELEEELEELEEELEEAEEELEEaeAELAEAEEALLEAEAELAEAE 378

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034607132 310 RGGRARASpradspdglAAGRSEGALQVLDGEVGSLDGTPQTREVAAEAVPETREAGAQAVPETREAGVEAAPETVEADA 389
Cdd:COG1196   379 EELEELAE---------ELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAE 449

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1034607132 390 WVTEALLGLPAAAERELELLRASLEHQRGVSELLR 424
Cdd:COG1196   450 EEAELEEEEEALLELLAELLEEAALLEAALAELLE 484
PutA COG0506
Proline dehydrogenase [Amino acid transport and metabolism]; Proline dehydrogenase is part of ...
 241-414 3.62e-03

Proline dehydrogenase [Amino acid transport and metabolism]; Proline dehydrogenase is part of the Pathway/BioSystem: Proline degradation


Pssm-ID: 440272 [Multi-domain]  Cd Length: 975  Bit Score: 41.19  E-value: 3.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034607132 241 MAAALRRLRELE--------------DQARTLPELQEQVRALRAEKARLLAGRAQPEPDGEAETRPDKLAQLRRLTERLA 306
Cdd:COG0506   397 DAALAYLLRRLLennsflnffvadfdDDEDLLEFPREPPRFLAALAAPTPPPPPPLRRQRRRRRRARGGALAAALAAAAA 476

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034607132 307 TSERGGRARASPRADSPDGLAAGRSEGALQVLDGEVGSLDGTPQTREVAAEAVPETREAGAQAVPETREAGVEAAPETVE 386
Cdd:COG0506   477 AAALAAAAAAAAALAAAAAGAAAAAAAAAVAVVPAAAAAVVAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 556

                         170       180
                  ....*....|....*....|....*...
gi 1034607132 387 ADAWVTEALLGLPAAAERELELLRASLE 414
Cdd:COG0506   557 AAAAEAAEAALLLAAAAAEAAAAAALAA 584
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 637-721 6.42e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 39.97  E-value: 6.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034607132 637 VSSQRRSQAEPVARMLEGVRrlGPELLAH---VVNLADGNGNTALHYSVSHGNLAIASLLLDTGAcEVNRQNRAGYSALM 713
Cdd:PHA02875  130 IPNTDKFSPLHLAVMMGDIK--GIELLIDhkaCLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGA-NIDYFGKNGCVAAL 206


                  ....*...
gi 1034607132 714 LAALTSVR 721
Cdd:PHA02875  207 CYAIENNK 214
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 649-821 8.18e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 39.48  E-value: 8.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034607132 649 ARMLEGVRrlgpELLA--HVVNLADGNGNTALHYSVSHGN-LAIASLLLDTGACEVNRQ---------NRAGYSALMLaa 716
Cdd:PHA02878   47 ARNLDVVK----SLLTrgHNVNQPDHRDLTPLHIICKEPNkLGMKEMIRSINKCSVFYTlvaikdafnNRNVEIFKII-- 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034607132 717 LTSVRQEEEDMAVVQ----------------RLFCMG-DVNAKASQTGQTALMLAISHGRQDMVATLLACGADVNAQDAD 779
Cdd:PHA02878  121 LTNRYKNIQTIDLVYidkkskddiieaeitkLLLSYGaDINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKT 200

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1034607132 780 GATALMCASEYGRLDTVRLLLtQPGCDPAILDNEGTSALAIA 821
Cdd:PHA02878  201 NNSPLHHAVKHYNKPIVHILL-ENGASTDARDKCGNTPLHIS 241
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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