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Conserved domains on  [gi|768001791|ref|XP_011526186|]
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KN motif and ankyrin repeat domain-containing protein 3 isoform X2 [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];
597-786 1.36e-39

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 148.18  E-value: 1.36e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768001791 597 VARMLEGVRRLGPELLAHVVNLADGNGNTALHYSVSHGNLAIASLLLDTGAcEVNRQNRAGYSALMLAAltsvrqEEEDM 676
Cdd:COG0666   61 AALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGA-DVNARDKDGETPLHLAA------YNGNL 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768001791 677 AVVQRLFCMG-DVNAKASQtGQTALMLAISHGRQDMVATLLACGADVNAQDADGATALMCASEYGRLDTVRLLLTQpGCD 755
Cdd:COG0666  134 EIVKLLLEAGaDVNAQDND-GNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEA-GAD 211

                        170       180       190
                 ....*....|....*....|....*....|.
gi 768001791 756 PAILDNEGTSALAIALEAEQDEVAALLHAHL 786
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 ...
 33-74 9.68e-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: 74.31  E-value: 9.68e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 768001791   33 PYSVETPYGFHLDLDFLKYIEELERGPAARRAPGPptsRRPR 74
Cdd:pfam12075   1 PYSVETPYGFHLDLDFLKYVEDIESGQTIRRARVQ---RRPR 39
PksD super family cl43841
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
 58-586 4.22e-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: 50.64  E-value: 4.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768001791   58 GPAARRAPGPPTS--RRPRAPRPGLAGARSPGAWTSSESLASDDGGAPGILSQGAPSGLLMQPLSPRAPVRNPRVEHTLR 135
Cdd:COG3321   854 PGRGRRRVPLPTYpfQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALV 933

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768001791  136 ETSRRLELAQTHERAPSPGRGVPRSPRGSGRSSPAPNLAPASPGPAQLQLVREQMAAALRRLRELEDQARTLPELQEQVR 215
Cdd:COG3321   934 ALAAAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLA 1013

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768001791  216 ALRAEKARLLAGRAQPEPDGEAETRPDKLAQLRRLTERLATSERGGRARASPRADSPDGLAAGRSEGALQVLDGEVGSLD 295
Cdd:COG3321  1014 AAAAAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAA 1093

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768001791  296 GTPQTREVAAEAVPETREAGAQAVPETREAGVEAAPETVEADAWVTEALLGLPAAAERELELLRASLEHQRGVSELLRGR 375
Cdd:COG3321  1094 ALALALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAAL 1173

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768001791  376 LRELEEAREAAEEAAAGARAQLREATTQTPWSCAEKAAQTESPAEAPSLTQESSPGSMDGDRAVAPAGILKSIMKKRDGT 455
Cdd:COG3321  1174 LLALALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAA 1253

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768001791  456 PGAQPSSGPKSLQFVGVLNGEYESSSSEDASDSDGDSENGGAEPPGSSSGSGDDSGGGSDSGTPGPPSGGDIRDPEPEAE 535
Cdd:COG3321  1254 ALLAALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAAALAAL 1333

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|.
gi 768001791  536 AEPQQVAQGRCELSPRLREACVALQRQLSRPRGVASDGGAVRLVAQEWFRV 586
Cdd:COG3321  1334 AAAVAAALALAAAAAAAAAAAAAAAAAAALAAAAGAAAAAAALALAALAAA 1384
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
597-786 1.36e-39

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 148.18  E-value: 1.36e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768001791 597 VARMLEGVRRLGPELLAHVVNLADGNGNTALHYSVSHGNLAIASLLLDTGAcEVNRQNRAGYSALMLAAltsvrqEEEDM 676
Cdd:COG0666   61 AALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGA-DVNARDKDGETPLHLAA------YNGNL 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768001791 677 AVVQRLFCMG-DVNAKASQtGQTALMLAISHGRQDMVATLLACGADVNAQDADGATALMCASEYGRLDTVRLLLTQpGCD 755
Cdd:COG0666  134 EIVKLLLEAGaDVNAQDND-GNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEA-GAD 211

                        170       180       190
                 ....*....|....*....|....*....|.
gi 768001791 756 PAILDNEGTSALAIALEAEQDEVAALLHAHL 786
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 ...
 33-74 9.68e-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: 74.31  E-value: 9.68e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 768001791   33 PYSVETPYGFHLDLDFLKYIEELERGPAARRAPGPptsRRPR 74
Cdd:pfam12075   1 PYSVETPYGFHLDLDFLKYVEDIESGQTIRRARVQ---RRPR 39
Ank_2 pfam12796
Ankyrin repeats (3 copies);
627-726 1.10e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.92  E-value: 1.10e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768001791  627 LHYSVSHGNLAIASLLLDTGaCEVNRQNRAGYSALMLAALTSVRQeeedmaVVQRLFCMGDVNAKASqtGQTALMLAISH 706
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENG-ADANLQDKNGRTALHLAAKNGHLE------IVKLLLEHADVNLKDN--GRTALHYAARS 71

                          90       100
                  ....*....|....*....|
gi 768001791  707 GRQDMVATLLACGADVNAQD 726
Cdd:pfam12796  72 GHLEIVKLLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 616-772 4.97e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 62.73  E-value: 4.97e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768001791 616 VNLADGNGNTALHYSVSHGN---LAIASLLLDTGAcEVNRQNRAGYSALMLAALTSVRQEeedmaVVQRLFCMG-DVNAK 691
Cdd:PHA03095  40 VNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGA-DVNAPERCGFTPLHLYLYNATTLD-----VIKLLIKAGaDVNAK 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768001791 692 aSQTGQTAL--MLAISHGRQDMVATLLACGADVNAQDADGATALMCASEYGR--LDTVRLLLTQpGCDPAILDNEGTSAL 767
Cdd:PHA03095 114 -DKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNanVELLRLLIDA-GADVYAVDDRFRSLL 191


                 ....*
gi 768001791 768 AIALE 772
Cdd:PHA03095 192 HHHLQ 196
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
 58-586 4.22e-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: 50.64  E-value: 4.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768001791   58 GPAARRAPGPPTS--RRPRAPRPGLAGARSPGAWTSSESLASDDGGAPGILSQGAPSGLLMQPLSPRAPVRNPRVEHTLR 135
Cdd:COG3321   854 PGRGRRRVPLPTYpfQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALV 933

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768001791  136 ETSRRLELAQTHERAPSPGRGVPRSPRGSGRSSPAPNLAPASPGPAQLQLVREQMAAALRRLRELEDQARTLPELQEQVR 215
Cdd:COG3321   934 ALAAAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLA 1013

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768001791  216 ALRAEKARLLAGRAQPEPDGEAETRPDKLAQLRRLTERLATSERGGRARASPRADSPDGLAAGRSEGALQVLDGEVGSLD 295
Cdd:COG3321  1014 AAAAAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAA 1093

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768001791  296 GTPQTREVAAEAVPETREAGAQAVPETREAGVEAAPETVEADAWVTEALLGLPAAAERELELLRASLEHQRGVSELLRGR 375
Cdd:COG3321  1094 ALALALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAAL 1173

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768001791  376 LRELEEAREAAEEAAAGARAQLREATTQTPWSCAEKAAQTESPAEAPSLTQESSPGSMDGDRAVAPAGILKSIMKKRDGT 455
Cdd:COG3321  1174 LLALALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAA 1253

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768001791  456 PGAQPSSGPKSLQFVGVLNGEYESSSSEDASDSDGDSENGGAEPPGSSSGSGDDSGGGSDSGTPGPPSGGDIRDPEPEAE 535
Cdd:COG3321  1254 ALLAALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAAALAAL 1333

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|.
gi 768001791  536 AEPQQVAQGRCELSPRLREACVALQRQLSRPRGVASDGGAVRLVAQEWFRV 586
Cdd:COG3321  1334 AAAVAAALALAAAAAAAAAAAAAAAAAAALAAAAGAAAAAAALALAALAAA 1384
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 622-647 2.25e-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: 2.25e-04
                           10        20
                   ....*....|....*....|....*.
gi 768001791   622 NGNTALHYSVSHGNLAIASLLLDTGA 647
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGA 26
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 623-778 4.79e-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: 4.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768001791 623 GNTALHYSVSHGNLAIASLLLDTGACEVNR----QNRAGYSALMLAALTsvrqeeEDMAVVQRLFCMG-DV-NAKASQT- 695
Cdd:cd22192   51 GETALHVAALYDNLEAAVVLMEAAPELVNEpmtsDLYQGETALHIAVVN------QNLNLVRELIARGaDVvSPRATGTf 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768001791 696 -----------GQTALMLAISHGRQDMVATLLACGADVNAQDADGATALmcaseygrldtvRLLLTQPGCDPA--ILDne 762
Cdd:cd22192  125 frpgpknliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL------------HILVLQPNKTFAcqMYD-- 190

                        170
                 ....*....|....*.
gi 768001791 763 gtsaLAIALEAEQDEV 778
Cdd:cd22192  191 ----LILSYDKEDDLQ 202
HpnN TIGR03480
hopanoid biosynthesis associated RND transporter like protein HpnN; The genomes containing ...
 188-287 3.08e-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: 41.14  E-value: 3.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768001791  188 EQMAAALRRLRELeDQARTL----PELQEQVRALRAEKARLLAGRAQPEPDGEAETRPDKLAQLRRLTERLatserggrA 263
Cdd:TIGR03480 514 RALTERLEALPEV-DQVVTLpdfvPDDQEAKLALIADLALVLGPTLNPGEADPAPSAEEVAAALRRLAARL--------R 584

                          90       100
                  ....*....|....*....|....
gi 768001791  264 RASPRADSPDGLAAGRSEGALQVL 287
Cdd:TIGR03480 585 AAAAKSQDPDAAAAGRLAASLDRL 608
PHA03247 PHA03247
large tegument protein UL36; Provisional
 59-181 9.75e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 39.92  E-value: 9.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768001791   59 PAARRAPGPPTSRRPRAPRPGlagarSPGAWTSSESLASDDGGAPGILSQGAPSGLLMQPLSPRAPVRNPRVEHTLRETS 138
Cdd:PHA03247 2619 PDTHAPDPPPPSPSPAANEPD-----PHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVG 2693

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 768001791  139 RRLELAQTHERAPSP---------GRGVPRSPRGSGRSSPAPNLAPASPGPA 181
Cdd:PHA03247 2694 SLTSLADPPPPPPTPepaphalvsATPLPPGPAAARQASPALPAAPAPPAVP 2745
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
597-786 1.36e-39

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 148.18  E-value: 1.36e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768001791 597 VARMLEGVRRLGPELLAHVVNLADGNGNTALHYSVSHGNLAIASLLLDTGAcEVNRQNRAGYSALMLAAltsvrqEEEDM 676
Cdd:COG0666   61 AALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGA-DVNARDKDGETPLHLAA------YNGNL 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768001791 677 AVVQRLFCMG-DVNAKASQtGQTALMLAISHGRQDMVATLLACGADVNAQDADGATALMCASEYGRLDTVRLLLTQpGCD 755
Cdd:COG0666  134 EIVKLLLEAGaDVNAQDND-GNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEA-GAD 211

                        170       180       190
                 ....*....|....*....|....*....|.
gi 768001791 756 PAILDNEGTSALAIALEAEQDEVAALLHAHL 786
Cdd:COG0666  212 VNAKDNDGKTALDLAAENGNLEIVKLLLEAG 242
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
610-782 9.25e-34

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 131.61  E-value: 9.25e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768001791 610 ELLAH--VVNLADGNGNTALHYSVSHGNLAIASLLLDTGAcEVNRQNRAGYSALMLAAltsvrqEEEDMAVVQRLFCMG- 686
Cdd:COG0666  105 LLLEAgaDVNARDKDGETPLHLAAYNGNLEIVKLLLEAGA-DVNAQDNDGNTPLHLAA------ANGNLEIVKLLLEAGa 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768001791 687 DVNAKaSQTGQTALMLAISHGRQDMVATLLACGADVNAQDADGATALMCASEYGRLDTVRLLLTQpGCDPAILDNEGTSA 766
Cdd:COG0666  178 DVNAR-DNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA-GADLNAKDKDGLTA 255

                        170
                 ....*....|....*.
gi 768001791 767 LAIALEAEQDEVAALL 782
Cdd:COG0666  256 LLLAAAAGAALIVKLL 271
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
597-785 7.68e-31

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 123.14  E-value: 7.68e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768001791 597 VARMLEGVRRLGPELLAHVVNLADGNGNTALHYSVSHGNLAIASLLLDTGAcEVNRQNRAGYSALMLAAltsvrqEEEDM 676
Cdd:COG0666   28 AALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGA-DINAKDDGGNTLLHAAA------RNGDL 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768001791 677 AVVQRLFCMG-DVNAKASQtGQTALMLAISHGRQDMVATLLACGADVNAQDADGATALMCASEYGRLDTVRLLLTQpGCD 755
Cdd:COG0666  101 EIVKLLLEAGaDVNARDKD-GETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEA-GAD 178

                        170       180       190
                 ....*....|....*....|....*....|
gi 768001791 756 PAILDNEGTSALAIALEAEQDEVAALLHAH 785
Cdd:COG0666  179 VNARDNDGETPLHLAAENGHLEIVKLLLEA 208
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
611-764 1.25e-23

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 101.95  E-value: 1.25e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768001791 611 LLAH--VVNLADGNGNTALHYSVSHGNLAIASLLLDTGAcEVNRQNRAGYSALMLAAltsvrqEEEDMAVVQRLFCMG-D 687
Cdd:COG0666  139 LLEAgaDVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGA-DVNARDNDGETPLHLAA------ENGHLEIVKLLLEAGaD 211

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768001791 688 VNAKASQtGQTALMLAISHGRQDMVATLLACGADVNAQDADGATALMCASEYGRLDTVRLLLTQPGCDPAILDNEGT 764
Cdd:COG0666  212 VNAKDND-GKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
610-782 3.80e-22

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 97.72  E-value: 3.80e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768001791 610 ELLAHVVNLADGNGNTALHYSVSHGNLAIASLLLDTGACEVNRQNRAGYSALMLAAltsvrqEEEDMAVVQRLFCMGDVN 689
Cdd:COG0666    7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAA------LAGDLLVALLLLAAGADI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768001791 690 AKASQTGQTALMLAISHGRQDMVATLLACGADVNAQDADGATALMCASEYGRLDTVRLLLTQpGCDPAILDNEGTSALAI 769
Cdd:COG0666   81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA-GADVNAQDNDGNTPLHL 159

                        170
                 ....*....|...
gi 768001791 770 ALEAEQDEVAALL 782
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 ...
 33-74 9.68e-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: 74.31  E-value: 9.68e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 768001791   33 PYSVETPYGFHLDLDFLKYIEELERGPAARRAPGPptsRRPR 74
Cdd:pfam12075   1 PYSVETPYGFHLDLDFLKYVEDIESGQTIRRARVQ---RRPR 39
Ank_2 pfam12796
Ankyrin repeats (3 copies);
627-726 1.10e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.92  E-value: 1.10e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768001791  627 LHYSVSHGNLAIASLLLDTGaCEVNRQNRAGYSALMLAALTSVRQeeedmaVVQRLFCMGDVNAKASqtGQTALMLAISH 706
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENG-ADANLQDKNGRTALHLAAKNGHLE------IVKLLLEHADVNLKDN--GRTALHYAARS 71

                          90       100
                  ....*....|....*....|
gi 768001791  707 GRQDMVATLLACGADVNAQD 726
Cdd:pfam12796  72 GHLEIVKLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
700-782 1.41e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.54  E-value: 1.41e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768001791  700 LMLAISHGRQDMVATLLACGADVNAQDADGATALMCASEYGRLDTVRLLLTQPGCDpaiLDNEGTSALAIALEAEQDEVA 779
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVN---LKDNGRTALHYAARSGHLEIV 77


                  ...
gi 768001791  780 ALL 782
Cdd:pfam12796  78 KLL 80
Ank_2 pfam12796
Ankyrin repeats (3 copies);
661-760 3.55e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 71.69  E-value: 3.55e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768001791  661 LMLAAltsvrqEEEDMAVVQRLFCMG-DVNAKaSQTGQTALMLAISHGRQDMVATLLACgADVNAQDaDGATALMCASEY 739
Cdd:pfam12796   1 LHLAA------KNGNLELVKLLLENGaDANLQ-DKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARS 71

                          90       100
                  ....*....|....*....|.
gi 768001791  740 GRLDTVRLLLtQPGCDPAILD 760
Cdd:pfam12796  72 GHLEIVKLLL-EKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
660-785 1.82e-12

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 68.83  E-value: 1.82e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768001791 660 ALMLAALTSVRQEEEDMAVVQRLFCMGDVNAKASQTGQTALMLAISHGRQDMVATLLACGADVNAQDADGATALMCASEY 739
Cdd:COG0666   18 LLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARN 97

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 768001791 740 GRLDTVRLLLTQpGCDPAILDNEGTSALAIALEAEQDEVAALLHAH 785
Cdd:COG0666   98 GDLEIVKLLLEA-GADVNARDKDGETPLHLAAYNGNLEIVKLLLEA 142
PHA03095 PHA03095
ankyrin-like protein; Provisional
 616-772 4.97e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 62.73  E-value: 4.97e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768001791 616 VNLADGNGNTALHYSVSHGN---LAIASLLLDTGAcEVNRQNRAGYSALMLAALTSVRQEeedmaVVQRLFCMG-DVNAK 691
Cdd:PHA03095  40 VNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGA-DVNAPERCGFTPLHLYLYNATTLD-----VIKLLIKAGaDVNAK 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768001791 692 aSQTGQTAL--MLAISHGRQDMVATLLACGADVNAQDADGATALMCASEYGR--LDTVRLLLTQpGCDPAILDNEGTSAL 767
Cdd:PHA03095 114 -DKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNanVELLRLLIDA-GADVYAVDDRFRSLL 191


                 ....*
gi 768001791 768 AIALE 772
Cdd:PHA03095 192 HHHLQ 196
Ank_4 pfam13637
Ankyrin repeats (many copies);
698-749 1.04e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.59  E-value: 1.04e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 768001791  698 TALMLAISHGRQDMVATLLACGADVNAQDADGATALMCASEYGRLDTVRLLL 749
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 715-810 1.87e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 61.07  E-value: 1.87e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768001791 715 LLACGADVNAQDADGATALMCASEYGRLDTVRLLLtQPGCDPAILDNEGTSALAIALEAEQDEVAALLHAHlSSGQPDTQ 794
Cdd:PTZ00322 101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLL-EFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH-SQCHFELG 178

                         90
                 ....*....|....*.
gi 768001791 795 SESPPGSQTATPGEGE 810
Cdd:PTZ00322 179 ANAKPDSFTGKPPSLE 194
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 616-772 2.17e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 57.28  E-value: 2.17e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768001791 616 VNLADGNGNTALHYSVSHGNLAIASLLLDTGAcEVNRQNRAGYSALMLAAltsvrqEEEDMAVVQRLFCMGDVNAKASQT 695
Cdd:PHA02874 150 VNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGA-YANVKDNNGESPLHNAA------EYGDYACIKLLIDHGNHIMNKCKN 222

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768001791 696 GQTALMLAISHGRQdmVATLLACGADVNAQDADGATALMCASEYG-RLDTVRLLLTQPGcDPAILDNEGTSALAIALE 772
Cdd:PHA02874 223 GFTPLHNAIIHNRS--AIELLINNASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKA-DISIKDNKGENPIDTAFK 297
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 617-811 4.12e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 53.72  E-value: 4.12e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768001791 617 NLADGNGNTALHYSVSHGNLAIASLLLDTgACEVNRQNRAGYSALMLAAltsvrqeeedMAVVQRLFCMGDVNAKAS--Q 694
Cdd:PLN03192 552 DIGDSKGRTPLHIAASKGYEDCVLVLLKH-ACNVHIRDANGNTALWNAI----------SAKHHKIFRILYHFASISdpH 620

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768001791 695 TGQTALMLAISHGRQDMVATLLACGADVNAQDADGATALMCASEYGRLDTVRLLLTQ-PGCDPAILDNEGTSA-LAIALE 772
Cdd:PLN03192 621 AAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNgADVDKANTDDDFSPTeLRELLQ 700

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 768001791 773 AEQDEVAALLHAHLSSGQPDTQSE--SPPGSQTATPGEGEC 811
Cdd:PLN03192 701 KRELGHSITIVDSVPADEPDLGRDggSRPGRLQGTSSDNQC 741
Ank_5 pfam13857
Ankyrin repeats (many copies);
715-770 6.37e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.96  E-value: 6.37e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 768001791  715 LLACG-ADVNAQDADGATALMCASEYGRLDTVRLLLTqPGCDPAILDNEGTSALAIA 770
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLA-YGVDLNLKDEEGLTALDLA 56
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 616-749 1.39e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 51.59  E-value: 1.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768001791 616 VNLADGNGNTALHYSVSH--GNLAIASLLLDTGaCEVNRQNRAGYSALMLAaltsVRQEEEDMAVVQRLFCMG-DVNAKA 692
Cdd:PHA03100  99 VNAPDNNGITPLLYAISKksNSYSIVEYLLDNG-ANVNIKNSDGENLLHLY----LESNKIDLKILKLLIDKGvDINAKN 173

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768001791 693 S---------------QTGQTALMLAISHGRQDMVATLLACGADVNAQDADGATALMCASEYGRLDTVRLLL 749
Cdd:PHA03100 174 RvnyllsygvpinikdVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLL 245
Ank_5 pfam13857
Ankyrin repeats (many copies);
687-733 1.52e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.80  E-value: 1.52e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 768001791  687 DVNAKaSQTGQTALMLAISHGRQDMVATLLACGADVNAQDADGATAL 733
Cdd:pfam13857   8 DLNRL-DGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 611-771 2.00e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 51.03  E-value: 2.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768001791 611 LLAH--VVNLADGN-GNTALHYSVSHGNLAIASLLLDTGAcEVNRQNRAGYSALMLAaltsVRQEEEDmaVVQRLFCMGD 687
Cdd:PHA02878 153 LLSYgaDINMKDRHkGNTALHYATENKDQRLTELLLSYGA-NVNIPDKTNNSPLHHA----VKHYNKP--IVHILLENGA 225

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768001791 688 VNAKASQTGQTALMLAISHGRQ-DMVATLLACGADVNAQDA-DGATALMCA--SEygrlDTVRLLLtQPGCDPAILDNEG 763
Cdd:PHA02878 226 STDARDKCGNTPLHISVGYCKDyDILKLLLEHGVDVNAKSYiLGLTALHSSikSE----RKLKLLL-EYGADINSLNSYK 300


                 ....*...
gi 768001791 764 TSALAIAL 771
Cdd:PHA02878 301 LTPLSSAV 308
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 616-763 3.86e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 50.26  E-value: 3.86e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768001791 616 VNLADGNGNTALHYSVSHGNLAIASLLLDTGAcEVNRQNRAGYSALMLAALTSVrqeeeDMAVVQRLFCMG-DVNAKASQ 694
Cdd:PHA02878 194 VNIPDKTNNSPLHHAVKHYNKPIVHILLENGA-STDARDKCGNTPLHISVGYCK-----DYDILKLLLEHGvDVNAKSYI 267

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768001791 695 TGQTALMLAISHgrQDMVATLLACGADVNAQDADGATAL-MCASEYGRLDTVRLLLTQPGC----DPAILDNEG 763
Cdd:PHA02878 268 LGLTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLsSAVKQYLCINIGRILISNICLlkriKPDIKNSEG 339
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
 58-586 4.22e-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: 50.64  E-value: 4.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768001791   58 GPAARRAPGPPTS--RRPRAPRPGLAGARSPGAWTSSESLASDDGGAPGILSQGAPSGLLMQPLSPRAPVRNPRVEHTLR 135
Cdd:COG3321   854 PGRGRRRVPLPTYpfQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALV 933

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768001791  136 ETSRRLELAQTHERAPSPGRGVPRSPRGSGRSSPAPNLAPASPGPAQLQLVREQMAAALRRLRELEDQARTLPELQEQVR 215
Cdd:COG3321   934 ALAAAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLA 1013

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768001791  216 ALRAEKARLLAGRAQPEPDGEAETRPDKLAQLRRLTERLATSERGGRARASPRADSPDGLAAGRSEGALQVLDGEVGSLD 295
Cdd:COG3321  1014 AAAAAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAA 1093

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768001791  296 GTPQTREVAAEAVPETREAGAQAVPETREAGVEAAPETVEADAWVTEALLGLPAAAERELELLRASLEHQRGVSELLRGR 375
Cdd:COG3321  1094 ALALALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAAL 1173

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768001791  376 LRELEEAREAAEEAAAGARAQLREATTQTPWSCAEKAAQTESPAEAPSLTQESSPGSMDGDRAVAPAGILKSIMKKRDGT 455
Cdd:COG3321  1174 LLALALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAA 1253

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768001791  456 PGAQPSSGPKSLQFVGVLNGEYESSSSEDASDSDGDSENGGAEPPGSSSGSGDDSGGGSDSGTPGPPSGGDIRDPEPEAE 535
Cdd:COG3321  1254 ALLAALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAAALAAL 1333

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|.
gi 768001791  536 AEPQQVAQGRCELSPRLREACVALQRQLSRPRGVASDGGAVRLVAQEWFRV 586
Cdd:COG3321  1334 AAAVAAALALAAAAAAAAAAAAAAAAAAALAAAAGAAAAAAALALAALAAA 1384
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 696-726 6.80e-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: 6.80e-06
                          10        20        30
                  ....*....|....*....|....*....|..
gi 768001791  696 GQTALMLAISH-GRQDMVATLLACGADVNAQD 726
Cdd:pfam00023   2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
Ank_2 pfam12796
Ankyrin repeats (3 copies);
610-654 8.13e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 44.72  E-value: 8.13e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 768001791  610 ELLAHVVNLADGNGNTALHYSVSHGNLAIASLLLDTGAcEVNRQN 654
Cdd:pfam12796  48 LLLEHADVNLKDNGRTALHYAARSGHLEIVKLLLEKGA-DINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 627-782 8.25e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 48.89  E-value: 8.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768001791 627 LHYSVSHGNLAIASLLLDTGACE-------------------------------------VNRQNRAGYSALMLAALTSV 669
Cdd:PHA03100  39 LYLAKEARNIDVVKILLDNGADInsstknnstplhylsnikynltdvkeivkllleyganVNAPDNNGITPLLYAISKKS 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768001791 670 rqeeEDMAVVQRLFCMG-DVNAKASqTGQTALMLAISHGRQD--MVATLLACGADVNAQ----------------DADGA 730
Cdd:PHA03100 119 ----NSYSIVEYLLDNGaNVNIKNS-DGENLLHLYLESNKIDlkILKLLIDKGVDINAKnrvnyllsygvpinikDVYGF 193

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 768001791 731 TALMCASEYGRLDTVRLLLTQpGCDPAILDNEGTSALAIALEAEQDEVAALL 782
Cdd:PHA03100 194 TPLHYAVYNNNPEFVKYLLDL-GANPNLVNKYGDTPLHIAILNNNKEIFKLL 244
Ank_2 pfam12796
Ankyrin repeats (3 copies);
733-785 2.50e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 43.57  E-value: 2.50e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 768001791  733 LMCASEYGRLDTVRLLLtQPGCDPAILDNEGTSALAIALEAEQDEVAALLHAH 785
Cdd:pfam12796   1 LHLAAKNGNLELVKLLL-ENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH 52
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 616-782 6.30e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 46.11  E-value: 6.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768001791 616 VNLADGNGNTALHYSVSHGNLAIASLLLDTGAcEVNRQNRAGYSALmlaaLTSVRQEEEDMAvvqRLFCMGDVNAKasqt 695
Cdd:PHA02874  28 INISVDETTTPLIDAIRSGDAKIVELFIKHGA-DINHINTKIPHPL----LTAIKIGAHDII---KLLIDNGVDTS---- 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768001791 696 gqtalMLAISHGRQDMVATLLACGADVNAQDADGATALMCASEYGRLDTVRLLLtQPGCDPAILDNEGTSALAIALEAEQ 775
Cdd:PHA02874  96 -----ILPIPCIEKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLF-EYGADVNIEDDNGCYPIHIAIKHNF 169


                 ....*..
gi 768001791 776 DEVAALL 782
Cdd:PHA02874 170 FDIIKLL 176
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 622-759 1.01e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 45.75  E-value: 1.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768001791 622 NGNTALHYSVSHGNLAIASLLLDTGAcEVNRQNRAGYSALMLAALtsvrqeeedmavvqrlfcMGDVNA-------KASQ 694
Cdd:PHA02875 101 DGMTPLHLATILKKLDIMKLLIARGA-DPDIPNTDKFSPLHLAVM------------------MGDIKGiellidhKACL 161

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768001791 695 T-----GQTALMLAISHGRQDMVATLLACGADVNAQDADGATALMC-ASEYGRLDTVRLLLTQpGCDPAIL 759
Cdd:PHA02875 162 DiedccGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCyAIENNKIDIVRLFIKR-GADCNIM 231
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 696-755 1.03e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.04  E-value: 1.03e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 768001791 696 GQTALMLAISHGRQDMVATLLACGADVNAQDADGATALMCASEYGRLDTVRLLLTQPGCD 755
Cdd:PTZ00322 115 GRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCH 174
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 611-728 1.04e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 46.01  E-value: 1.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768001791 611 LLAHV--VNLADGNGNTALHYSVSHGNLAIASLLLDtgaCEVNRQNRAGYSALMLAAltsvrqEEEDMAVVQRLFCMG-D 687
Cdd:PLN03192 577 LLKHAcnVHIRDANGNTALWNAISAKHHKIFRILYH---FASISDPHAAGDLLCTAA------KRNDLTAMKELLKQGlN 647

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 768001791 688 VNAKASQtGQTALMLAISHGRQDMVATLLACGADVNAQDAD 728
Cdd:PLN03192 648 VDSEDHQ-GATALQVAMAEDHVDMVRLLIMNGADVDKANTD 687
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 642-750 1.72e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 44.95  E-value: 1.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768001791 642 LLDTGAcEVNRQNRAGYSALMLAAltsvrqEEEDMAVVQRLFCMG-DVNAKaSQTGQTALMLAISHGRQDMVATLLACGA 720
Cdd:PHA02874 110 ILDCGI-DVNIKDAELKTFLHYAI------KKGDLESIKMLFEYGaDVNIE-DDNGCYPIHIAIKHNFFDIIKLLLEKGA 181

                         90       100       110
                 ....*....|....*....|....*....|
gi 768001791 721 DVNAQDADGATALMCASEYGRLDTVRLLLT 750
Cdd:PHA02874 182 YANVKDNNGESPLHNAAEYGDYACIKLLID 211
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 670-806 1.84e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 45.05  E-value: 1.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768001791 670 RQEEEDMAVVQRLFCMG-DVNAKASQTgQTALMLAISHGRQDMVATLLACGADVNAQDADGATALMCASEYGRLDTVRll 748
Cdd:PHA02876 152 RIQQDELLIAEMLLEGGaDVNAKDIYC-ITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIK-- 228

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768001791 749 ltqpgcdpAILDNEGTS-----ALAIALEAEQDEVAALLH-AHLSSGQPDTQSESPPGSQTATP 806
Cdd:PHA02876 229 --------AIIDNRSNInkndlSLLKAIRNEDLETSLLLYdAGFSVNSIDDCKNTPLHHASQAP 284
Ank_4 pfam13637
Ankyrin repeats (many copies);
623-666 1.86e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.95  E-value: 1.86e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 768001791  623 GNTALHYSVSHGNLAIASLLLDTGAcEVNRQNRAGYSALMLAAL 666
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGA-DINAVDGNGETALHFAAS 43
PHA03095 PHA03095
ankyrin-like protein; Provisional
 619-752 2.05e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 44.63  E-value: 2.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768001791 619 ADGNGNTALHY--SVSHGNLAIASLLLDTGaCEVNRQNRAGYSAL-MLAALTSVRQeeedmAVVQRLFCMG-DVNAKaSQ 694
Cdd:PHA03095 183 VDDRFRSLLHHhlQSFKPRARIVRELIRAG-CDPAATDMLGNTPLhSMATGSSCKR-----SLVLPLLIAGiSINAR-NR 255

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768001791 695 TGQTALMLAISHGRQDMVATLLACGADVNAQDADGAT--ALMCASEYGRLdtVRLLL-TQP 752
Cdd:PHA03095 256 YGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTplSLMVRNNNGRA--VRAALaKNP 314
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 622-647 2.25e-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: 2.25e-04
                           10        20
                   ....*....|....*....|....*.
gi 768001791   622 NGNTALHYSVSHGNLAIASLLLDTGA 647
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGA 26
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 622-655 2.65e-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: 2.65e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 768001791  622 NGNTALHYSVSH-GNLAIASLLLDTGAcEVNRQNR 655
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGA-DVNARDK 34
Ank_4 pfam13637
Ankyrin repeats (many copies);
616-643 3.13e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.18  E-value: 3.13e-04
                          10        20
                  ....*....|....*....|....*...
gi 768001791  616 VNLADGNGNTALHYSVSHGNLAIASLLL 643
Cdd:pfam13637  27 INAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 623-778 4.79e-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: 4.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768001791 623 GNTALHYSVSHGNLAIASLLLDTGACEVNR----QNRAGYSALMLAALTsvrqeeEDMAVVQRLFCMG-DV-NAKASQT- 695
Cdd:cd22192   51 GETALHVAALYDNLEAAVVLMEAAPELVNEpmtsDLYQGETALHIAVVN------QNLNLVRELIARGaDVvSPRATGTf 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768001791 696 -----------GQTALMLAISHGRQDMVATLLACGADVNAQDADGATALmcaseygrldtvRLLLTQPGCDPA--ILDne 762
Cdd:cd22192  125 frpgpknliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL------------HILVLQPNKTFAcqMYD-- 190

                        170
                 ....*....|....*.
gi 768001791 763 gtsaLAIALEAEQDEV 778
Cdd:cd22192  191 ----LILSYDKEDDLQ 202
Ank_5 pfam13857
Ankyrin repeats (many copies);
611-664 7.90e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.10  E-value: 7.90e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 768001791  611 LLAHV---VNLADGNGNTALHYSVSHGNLAIASLLLDTGaCEVNRQNRAGYSALMLA 664
Cdd:pfam13857   1 LLEHGpidLNRLDGEGYTPLHVAAKYGALEIVRVLLAYG-VDLNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 696-724 8.74e-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: 8.74e-04
                           10        20
                   ....*....|....*....|....*....
gi 768001791   696 GQTALMLAISHGRQDMVATLLACGADVNA 724
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 622-798 9.30e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 42.67  E-value: 9.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768001791 622 NGNTALHYSVSHGNLAIASLLLDTGAcEVNRQNRAGYSALMLA----------------ALTSVRQ-----------EEE 674
Cdd:PHA02875   1 MDQVALCDAILFGELDIARRLLDIGI-NPNFEIYDGISPIKLAmkfrdseaikllmkhgAIPDVKYpdieselhdavEEG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768001791 675 DMAVVQRLFCMGD-VNAKASQTGQTALMLAISHGRQDMVATLLACGADVNAQDADGATALMCASEYGRLDTVRLLLTQPG 753
Cdd:PHA02875  80 DVKAVEELLDLGKfADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKA 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 768001791 754 CdPAILDNEGTSALAIALEAEQDEVAALLhahLSSG-QPDTQSESP 798
Cdd:PHA02875 160 C-LDIEDCCGCTPLIIAMAKGDIAICKML---LDSGaNIDYFGKNG 201
PHA03095 PHA03095
ankyrin-like protein; Provisional
 670-749 1.54e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 41.93  E-value: 1.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768001791 670 RQEEEDMAVVQRLFCMG-DVNAKAS--QTGQTALMLAISHGRQDMVATLLACGADVNAQDADGATALMCASEYG-RLDTV 745
Cdd:PHA03095  21 NASNVTVEEVRRLLAAGaDVNFRGEygKTPLHLYLHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNAtTLDVI 100


                 ....
gi 768001791 746 RLLL 749
Cdd:PHA03095 101 KLLI 104
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 696-724 1.61e-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: 1.61e-03
                          10        20
                  ....*....|....*....|....*....
gi 768001791  696 GQTALMLAISHGRQDMVATLLACGADVNA 724
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
188-409 1.82e-03

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 41.54  E-value: 1.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768001791 188 EQMAAALRRLRELEDQARTLPELQEQVRALRAEKARLLAGRAQPEPDGEAETRPDKLAQLRRLTERLATSERGGRARASP 267
Cdd:COG0515  259 AELAAALRAVLRSLAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAPAAAAAAAAAAAALAA 338

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768001791 268 RADSPDGLAAGRSEGALQVLDGEVGSLDGTPQTREVAAEAVPETREAGAQAVPETREAGVEAAPETVEADAWVTEALLGL 347
Cdd:COG0515  339 AAAAAAAAAAAALLAAAAALAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAA 418

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768001791 348 PAAAERELELLRASLEHQRGVSELLRGRLRELEEAREAAEEAAAGARAQLREATTQTPWSCA 409
Cdd:COG0515  419 ALAAAAAAAAAAAAAAAAAAAAAARLLAAAAAAAAAAAAAPLLAALLAAAALAAAAAAAALA 480
HpnN TIGR03480
hopanoid biosynthesis associated RND transporter like protein HpnN; The genomes containing ...
 188-287 3.08e-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: 41.14  E-value: 3.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768001791  188 EQMAAALRRLRELeDQARTL----PELQEQVRALRAEKARLLAGRAQPEPDGEAETRPDKLAQLRRLTERLatserggrA 263
Cdd:TIGR03480 514 RALTERLEALPEV-DQVVTLpdfvPDDQEAKLALIADLALVLGPTLNPGEADPAPSAEEVAAALRRLAARL--------R 584

                          90       100
                  ....*....|....*....|....
gi 768001791  264 RASPRADSPDGLAAGRSEGALQVL 287
Cdd:TIGR03480 585 AAAAKSQDPDAAAAGRLAASLDRL 608
PutA COG0506
Proline dehydrogenase [Amino acid transport and metabolism]; Proline dehydrogenase is part of ...
 190-363 5.51e-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: 40.42  E-value: 5.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768001791 190 MAAALRRLRELE--------------DQARTLPELQEQVRALRAEKARLLAGRAQPEPDGEAETRPDKLAQLRRLTERLA 255
Cdd:COG0506  397 DAALAYLLRRLLennsflnffvadfdDDEDLLEFPREPPRFLAALAAPTPPPPPPLRRQRRRRRRARGGALAAALAAAAA 476

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768001791 256 TSERGGRARASPRADSPDGLAAGRSEGALQVLDGEVGSLDGTPQTREVAAEAVPETREAGAQAVPETREAGVEAAPETVE 335
Cdd:COG0506  477 AAALAAAAAAAAALAAAAAGAAAAAAAAAVAVVPAAAAAVVAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 556

                        170       180
                 ....*....|....*....|....*...
gi 768001791 336 ADAWVTEALLGLPAAAERELELLRASLE 363
Cdd:COG0506  557 AAAAEAAEAALLLAAAAAEAAAAAALAA 584
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 586-670 5.98e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 39.97  E-value: 5.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768001791 586 VSSQRRSQAEPVARMLEGVRrlGPELLAH---VVNLADGNGNTALHYSVSHGNLAIASLLLDTGAcEVNRQNRAGYSALM 662
Cdd:PHA02875 130 IPNTDKFSPLHLAVMMGDIK--GIELLIDhkaCLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGA-NIDYFGKNGCVAAL 206


                 ....*...
gi 768001791 663 LAALTSVR 670
Cdd:PHA02875 207 CYAIENNK 214
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 181-373 6.08e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.31  E-value: 6.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768001791 181 AQLQLVREQMAAALRRLRELEDQARtlpELQEQVRALRAEKARLLAGRAQPEPDGEA--ETRPDKLAQLRRLTERLATSE 258
Cdd:COG1196  302 QDIARLEERRRELEERLEELEEELA---ELEEELEELEEELEELEEELEEAEEELEEaeAELAEAEEALLEAEAELAEAE 378

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768001791 259 RGGRARASpradspdglAAGRSEGALQVLDGEVGSLDGTPQTREVAAEAVPETREAGAQAVPETREAGVEAAPETVEADA 338
Cdd:COG1196  379 EELEELAE---------ELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAE 449

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 768001791 339 WVTEALLGLPAAAERELELLRASLEHQRGVSELLR 373
Cdd:COG1196  450 EEAELEEEEEALLELLAELLEEAALLEAALAELLE 484
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 598-770 7.61e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 39.48  E-value: 7.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768001791 598 ARMLEGVRrlgpELLA--HVVNLADGNGNTALHYSVSHGN-LAIASLLLDTGACEVNRQ---------NRAGYSALMLaa 665
Cdd:PHA02878  47 ARNLDVVK----SLLTrgHNVNQPDHRDLTPLHIICKEPNkLGMKEMIRSINKCSVFYTlvaikdafnNRNVEIFKII-- 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768001791 666 LTSVRQEEEDMAVVQ----------------RLFCMG-DVNAKASQTGQTALMLAISHGRQDMVATLLACGADVNAQDAD 728
Cdd:PHA02878 121 LTNRYKNIQTIDLVYidkkskddiieaeitkLLLSYGaDINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKT 200

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 768001791 729 GATALMCASEYGRLDTVRLLLtQPGCDPAILDNEGTSALAIA 770
Cdd:PHA02878 201 NNSPLHHAVKHYNKPIVHILL-ENGASTDARDKCGNTPLHIS 241
PHA03247 PHA03247
large tegument protein UL36; Provisional
 59-181 9.75e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 39.92  E-value: 9.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768001791   59 PAARRAPGPPTSRRPRAPRPGlagarSPGAWTSSESLASDDGGAPGILSQGAPSGLLMQPLSPRAPVRNPRVEHTLRETS 138
Cdd:PHA03247 2619 PDTHAPDPPPPSPSPAANEPD-----PHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVG 2693

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 768001791  139 RRLELAQTHERAPSP---------GRGVPRSPRGSGRSSPAPNLAPASPGPA 181
Cdd:PHA03247 2694 SLTSLADPPPPPPTPepaphalvsATPLPPGPAAARQASPALPAAPAPPAVP 2745
 
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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