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Conserved domains on  [gi|2024430623|ref|XP_040511299|]
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KN motif and ankyrin repeat domain-containing protein 1 isoform X1 [Gallus gallus]

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];
1156-1324 6.22e-43

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 158.96  E-value: 6.22e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024430623 1156 INVADGNGNTALHYSVSHSNFEIVKLLLDANVcNVNHQNKAGYTPIMLAALAaveaeKDMRIVEELFSCG-DVNAKASQa 1234
Cdd:COG0666     80 INAKDDGGNTLLHAAARNGDLEIVKLLLEAGA-DVNARDKDGETPLHLAAYN-----GNLEIVKLLLEAGaDVNAQDND- 152

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024430623 1235 GQTALMLAVSHGRIDMVKALLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLAQpGCNGTLEDNDGSTALSIALEAGH 1314
Cdd:COG0666    153 GNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEA-GADVNAKDNDGKTALDLAAENGN 231

                          170
                   ....*....|
gi 2024430623 1315 KDIAVLLYAH 1324
Cdd:COG0666    232 LEIVKLLLEA 241
KN_motif pfam12075
KN motif; This small motif is found at the N-terminus of Kank proteins and has been called the ...
 39-77 1.64e-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: 77.01  E-value: 1.64e-17
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2024430623   39 PYFVETPYGYQLDLDFLKYVDDIQKGNTIKKLNIQKKRK 77
Cdd:pfam12075    1 PYSVETPYGFHLDLDFLKYVEDIESGQTIRRARVQRRPR 39
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 276-537 5.54e-06

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.21  E-value: 5.54e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024430623  276 KELEEQVKTIPVLQVKISVLQEEKRHmmaeLKSQRKSSQndvygfrkRSYSAGNAEQWEHLSQvrrggelyidcedEMES 355
Cdd:TIGR02168  281 EEIEELQKELYALANEISRLEQQKQI----LRERLANLE--------RQLEELEAQLEELESK-------------LDEL 335

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024430623  356 AEQSSRRVEEFRQLTAEMQALEKKIQDSNYEVP------SNLRESLTKESRSVA---VGADENMNDvVIYNRS------S 420
Cdd:TIGR02168  336 AEELAELEEKLEELKEELESLEAELEELEAELEelesrlEELEEQLETLRSKVAqleLQIASLNNE-IERLEArlerleD 414

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024430623  421 RQHREVAVGTEKEMRESGVGVTEAMLGLStEVEKEIELQQQTIEALKEKIYRLEVQLKETThdREMTKLKQELQAAGSRK 500
Cdd:TIGR02168  415 RRERLQQEIEELLKKLEEAELKELQAELE-ELEEELEELQEELERLEEALEELREELEEAE--QALDAAERELAQLQARL 491

                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 2024430623  501 KVDKAMMAQPLVVSRMVEAVVQMRDQMVGDHVHVADS 537
Cdd:TIGR02168  492 DSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSEL 528
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1156-1324 6.22e-43

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 158.96  E-value: 6.22e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024430623 1156 INVADGNGNTALHYSVSHSNFEIVKLLLDANVcNVNHQNKAGYTPIMLAALAaveaeKDMRIVEELFSCG-DVNAKASQa 1234
Cdd:COG0666     80 INAKDDGGNTLLHAAARNGDLEIVKLLLEAGA-DVNARDKDGETPLHLAAYN-----GNLEIVKLLLEAGaDVNAQDND- 152

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024430623 1235 GQTALMLAVSHGRIDMVKALLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLAQpGCNGTLEDNDGSTALSIALEAGH 1314
Cdd:COG0666    153 GNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEA-GADVNAKDNDGKTALDLAAENGN 231

                          170
                   ....*....|
gi 2024430623 1315 KDIAVLLYAH 1324
Cdd:COG0666    232 LEIVKLLLEA 241
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1239-1324 3.52e-23

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 94.80  E-value: 3.52e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024430623 1239 LMLAVSHGRIDMVKALLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLAQPGCNgtlEDNDGSTALSIALEAGHKDIA 1318
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVN---LKDNGRTALHYAARSGHLEIV 77


                   ....*.
gi 2024430623 1319 VLLYAH 1324
Cdd:pfam12796   78 KLLLEK 83
KN_motif pfam12075
KN motif; This small motif is found at the N-terminus of Kank proteins and has been called the ...
 39-77 1.64e-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: 77.01  E-value: 1.64e-17
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2024430623   39 PYFVETPYGYQLDLDFLKYVDDIQKGNTIKKLNIQKKRK 77
Cdd:pfam12075    1 PYSVETPYGFHLDLDFLKYVEDIESGQTIRRARVQRRPR 39
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 1156-1326 1.36e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 80.86  E-value: 1.36e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024430623 1156 INVADGNGNTALHYSVSHS--NFEIVKLLLDaNVCNVNHQNKAGYTPImlaALAAVEAEKDMRIVEELFSCG-DVNAKas 1232
Cdd:PHA03100    99 VNAPDNNGITPLLYAISKKsnSYSIVEYLLD-NGANVNIKNSDGENLL---HLYLESNKIDLKILKLLIDKGvDINAK-- 172

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024430623 1233 qagqtalmlavshgriDMVKALLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLAQpGCNGTLEDNDGSTALSIALEA 1312
Cdd:PHA03100   173 ----------------NRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDL-GANPNLVNKYGDTPLHIAILN 235

                          170
                   ....*....|....*
gi 2024430623 1313 GHKDI-AVLLYAHVN 1326
Cdd:PHA03100   236 NNKEIfKLLLNNGPS 250
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 1163-1322 1.19e-06

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 53.09  E-value: 1.19e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024430623 1163 GNTALHYSVSHSNFEIVKLLLDANVCNVNhqnkagytpimlaalaaveaekdMRIVEELFscgdvnakasqAGQTALMLA 1242
Cdd:cd22192     51 GETALHVAALYDNLEAAVVLMEAAPELVN-----------------------EPMTSDLY-----------QGETALHIA 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024430623 1243 VSHGRIDMVKALLACGADVNIQDDEGS------TALMCASEH--------GHVEIVKLLLaQPGCNGTLEDNDGSTALSI 1308
Cdd:cd22192     97 VVNQNLNLVRELIARGADVVSPRATGTffrpgpKNLIYYGEHplsfaacvGNEEIVRLLI-EHGADIRAQDSLGNTVLHI 175

                          170
                   ....*....|....
gi 2024430623 1309 ALEAGHKDIAVLLY 1322
Cdd:cd22192    176 LVLQPNKTFACQMY 189
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 276-537 5.54e-06

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.21  E-value: 5.54e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024430623  276 KELEEQVKTIPVLQVKISVLQEEKRHmmaeLKSQRKSSQndvygfrkRSYSAGNAEQWEHLSQvrrggelyidcedEMES 355
Cdd:TIGR02168  281 EEIEELQKELYALANEISRLEQQKQI----LRERLANLE--------RQLEELEAQLEELESK-------------LDEL 335

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024430623  356 AEQSSRRVEEFRQLTAEMQALEKKIQDSNYEVP------SNLRESLTKESRSVA---VGADENMNDvVIYNRS------S 420
Cdd:TIGR02168  336 AEELAELEEKLEELKEELESLEAELEELEAELEelesrlEELEEQLETLRSKVAqleLQIASLNNE-IERLEArlerleD 414

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024430623  421 RQHREVAVGTEKEMRESGVGVTEAMLGLStEVEKEIELQQQTIEALKEKIYRLEVQLKETThdREMTKLKQELQAAGSRK 500
Cdd:TIGR02168  415 RRERLQQEIEELLKKLEEAELKELQAELE-ELEEELEELQEELERLEEALEELREELEEAE--QALDAAERELAQLQARL 491

                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 2024430623  501 KVDKAMMAQPLVVSRMVEAVVQMRDQMVGDHVHVADS 537
Cdd:TIGR02168  492 DSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSEL 528
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 1235-1263 5.83e-06

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: 44.12  E-value: 5.83e-06
                            10        20
                    ....*....|....*....|....*....
gi 2024430623  1235 GQTALMLAVSHGRIDMVKALLACGADVNI 1263
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
270-497 7.01e-06

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 50.54  E-value: 7.01e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024430623  270 IALKRLKELEEQVKTIPVLQVKISVLQEEK---RHMMAELKSQRKSSQNDVygfRKRSYSAGNAEQWEHLSQVRRggELy 346
Cdd:COG4717     68 LNLKELKELEEELKEAEEKEEEYAELQEELeelEEELEELEAELEELREEL---EKLEKLLQLLPLYQELEALEA--EL- 141

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024430623  347 idcEDEMESAEQSSRRVEEFRQLTAEMQALEKKIQdsnyevpsNLRESLTKESRSVAVGADENMNDVViynrssRQHREV 426
Cdd:COG4717    142 ---AELPERLEELEERLEELRELEEELEELEAELA--------ELQEELEELLEQLSLATEEELQDLA------EELEEL 204

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024430623  427 avgtEKEMRESgvgvteamlglstevEKEIELQQQTIEALKEKIYRLEVQLKETTHDREMTKLKQELQAAG 497
Cdd:COG4717    205 ----QQRLAEL---------------EEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAA 256
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
261-479 1.04e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 50.06  E-value: 1.04e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024430623  261 LQQIREQMAIALKRLKELEEQVKTIPVLQVKISVLQEEKRHMMAELKSQRKSSQNDVYG-------FRKRSYSAGNAEqw 333
Cdd:PRK03918   534 LIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEErlkelepFYNEYLELKDAE-- 611

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024430623  334 ehlSQVRRGGELYIDCEDEMESAEQSSRRVE-EFRQLTAEMQALEKKIQDSNYEvpsNLRESLTKESRSVAvGADENMnd 412
Cdd:PRK03918   612 ---KELEREEKELKKLEEELDKAFEELAETEkRLEELRKELEELEKKYSEEEYE---ELREEYLELSRELA-GLRAEL-- 682

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024430623  413 vviynRSSRQHREVAVGTEKEMRESgvgvteamLGLSTEVEKEIELQQQTI---EALKEKIYRLEVQLKE 479
Cdd:PRK03918   683 -----EELEKRREEIKKTLEKLKEE--------LEEREKAKKELEKLEKALervEELREKVKKYKALLKE 739
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1156-1324 6.22e-43

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 158.96  E-value: 6.22e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024430623 1156 INVADGNGNTALHYSVSHSNFEIVKLLLDANVcNVNHQNKAGYTPIMLAALAaveaeKDMRIVEELFSCG-DVNAKASQa 1234
Cdd:COG0666     80 INAKDDGGNTLLHAAARNGDLEIVKLLLEAGA-DVNARDKDGETPLHLAAYN-----GNLEIVKLLLEAGaDVNAQDND- 152

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024430623 1235 GQTALMLAVSHGRIDMVKALLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLAQpGCNGTLEDNDGSTALSIALEAGH 1314
Cdd:COG0666    153 GNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEA-GADVNAKDNDGKTALDLAAENGN 231

                          170
                   ....*....|
gi 2024430623 1315 KDIAVLLYAH 1324
Cdd:COG0666    232 LEIVKLLLEA 241
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1156-1321 1.17e-37

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 143.56  E-value: 1.17e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024430623 1156 INVADGNGNTALHYSVSHSNFEIVKLLLDANVcNVNHQNKAGYTPIMLAALAaveaeKDMRIVEELFSCG-DVNAKaSQA 1234
Cdd:COG0666    113 VNARDKDGETPLHLAAYNGNLEIVKLLLEAGA-DVNAQDNDGNTPLHLAAAN-----GNLEIVKLLLEAGaDVNAR-DND 185

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024430623 1235 GQTALMLAVSHGRIDMVKALLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLAQpGCNGTLEDNDGSTALSIALEAGH 1314
Cdd:COG0666    186 GETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA-GADLNAKDKDGLTALLLAAAAGA 264


                   ....*..
gi 2024430623 1315 KDIAVLL 1321
Cdd:COG0666    265 ALIVKLL 271
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1145-1324 3.83e-35

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 136.24  E-value: 3.83e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024430623 1145 EEISPAVLRHIINVADGNGNTALHYSVSHSNFEIVKLLLDANVcNVNHQNKAGYTPIMLAALAaveaeKDMRIVEELFSC 1224
Cdd:COG0666     36 LLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGA-DINAKDDGGNTLLHAAARN-----GDLEIVKLLLEA 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024430623 1225 G-DVNAKASQaGQTALMLAVSHGRIDMVKALLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLAQpGCNGTLEDNDGS 1303
Cdd:COG0666    110 GaDVNARDKD-GETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEA-GADVNARDNDGE 187

                          170       180
                   ....*....|....*....|.
gi 2024430623 1304 TALSIALEAGHKDIAVLLYAH 1324
Cdd:COG0666    188 TPLHLAAENGHLEIVKLLLEA 208
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1144-1324 3.60e-26

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 110.04  E-value: 3.60e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024430623 1144 FEEISPAVLRHIINVADGNGNTALHYSVSHSNFEIVKLLLDANVCNVNHQNKAGYTPIMLAALAaveaeKDMRIVEELFS 1223
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALA-----GDLLVALLLLA 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024430623 1224 CGDVNAKASQAGQTALMLAVSHGRIDMVKALLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLAQpGCNGTLEDNDGS 1303
Cdd:COG0666     76 AGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA-GADVNAQDNDGN 154

                          170       180
                   ....*....|....*....|.
gi 2024430623 1304 TALSIALEAGHKDIAVLLYAH 1324
Cdd:COG0666    155 TPLHLAAANGNLEIVKLLLEA 175
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1156-1301 5.65e-24

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 103.88  E-value: 5.65e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024430623 1156 INVADGNGNTALHYSVSHSNFEIVKLLLDANVcNVNHQNKAGYTPIMLAALAaveaeKDMRIVEELFSCG-DVNAKaSQA 1234
Cdd:COG0666    146 VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGA-DVNARDNDGETPLHLAAEN-----GHLEIVKLLLEAGaDVNAK-DND 218

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024430623 1235 GQTALMLAVSHGRIDMVKALLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLAQPGCNGTLEDND 1301
Cdd:COG0666    219 GKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDL 285
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1239-1324 3.52e-23

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 94.80  E-value: 3.52e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024430623 1239 LMLAVSHGRIDMVKALLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLAQPGCNgtlEDNDGSTALSIALEAGHKDIA 1318
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVN---LKDNGRTALHYAARSGHLEIV 77


                   ....*.
gi 2024430623 1319 VLLYAH 1324
Cdd:pfam12796   78 KLLLEK 83
KN_motif pfam12075
KN motif; This small motif is found at the N-terminus of Kank proteins and has been called the ...
 39-77 1.64e-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: 77.01  E-value: 1.64e-17
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2024430623   39 PYFVETPYGYQLDLDFLKYVDDIQKGNTIKKLNIQKKRK 77
Cdd:pfam12075    1 PYSVETPYGFHLDLDFLKYVEDIESGQTIRRARVQRRPR 39
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1167-1265 2.68e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 78.23  E-value: 2.68e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024430623 1167 LHYSVSHSNFEIVKLLLDANvCNVNHQNKAGYTPIMLAALAaveaeKDMRIVEELFSCGDVNAKASqaGQTALMLAVSHG 1246
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENG-ADANLQDKNGRTALHLAAKN-----GHLEIVKLLLEHADVNLKDN--GRTALHYAARSG 72

                           90
                   ....*....|....*....
gi 2024430623 1247 RIDMVKALLACGADVNIQD 1265
Cdd:pfam12796   73 HLEIVKLLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 1156-1326 1.36e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 80.86  E-value: 1.36e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024430623 1156 INVADGNGNTALHYSVSHS--NFEIVKLLLDaNVCNVNHQNKAGYTPImlaALAAVEAEKDMRIVEELFSCG-DVNAKas 1232
Cdd:PHA03100    99 VNAPDNNGITPLLYAISKKsnSYSIVEYLLD-NGANVNIKNSDGENLL---HLYLESNKIDLKILKLLIDKGvDINAK-- 172

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024430623 1233 qagqtalmlavshgriDMVKALLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLAQpGCNGTLEDNDGSTALSIALEA 1312
Cdd:PHA03100   173 ----------------NRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDL-GANPNLVNKYGDTPLHIAILN 235

                          170
                   ....*....|....*
gi 2024430623 1313 GHKDI-AVLLYAHVN 1326
Cdd:PHA03100   236 NNKEIfKLLLNNGPS 250
Ank_4 pfam13637
Ankyrin repeats (many copies);
1237-1288 1.52e-12

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 63.45  E-value: 1.52e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2024430623 1237 TALMLAVSHGRIDMVKALLACGADVNIQDDEGSTALMCASEHGHVEIVKLLL 1288
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
 1139-1320 2.87e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 67.36  E-value: 2.87e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024430623 1139 DYITAFEEISPAVLRHII------NVADGNGNTALHYSVSHSN---FEIVKLLLDANVcNVNHQNKAGYTPIMLAALAAV 1209
Cdd:PHA03095    17 DYLLNASNVTVEEVRRLLaagadvNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGA-DVNAPERCGFTPLHLYLYNAT 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024430623 1210 EAekdmRIVEELFSCG-DVNAKaSQAGQTALMLAVSHGRID--MVKALLACGADVNIQDDEGSTALMC--ASEHGHVEIV 1284
Cdd:PHA03095    96 TL----DVIKLLIKAGaDVNAK-DKVGRTPLHVYLSGFNINpkVIRLLLRKGADVNALDLYGMTPLAVllKSRNANVELL 170

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 2024430623 1285 KLLLAQpGCNGTLEDNDGSTALSIALEAGHKDIAVL 1320
Cdd:PHA03095   171 RLLIDA-GADVYAVDDRFRSLLHHHLQSFKPRARIV 205
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 1156-1288 4.85e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 63.75  E-value: 4.85e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024430623 1156 INVADGNGNTALHYSVSHSNFEIVKLLLDaNVCNVNHQNKAGYTPImlaaLAAVEAEKDMRIVEELFSCG-DVNAKASQA 1234
Cdd:PHA02878   194 VNIPDKTNNSPLHHAVKHYNKPIVHILLE-NGASTDARDKCGNTPL----HISVGYCKDYDILKLLLEHGvDVNAKSYIL 268

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2024430623 1235 GQTALMLAVSHGRIdmVKALLACGADVNIQDDEGSTAL-MCASEHGHVEIVKLLL 1288
Cdd:PHA02878   269 GLTALHSSIKSERK--LKLLLEYGADINSLNSYKLTPLsSAVKQYLCINIGRILI 321
PHA03095 PHA03095
ankyrin-like protein; Provisional
 1156-1320 5.74e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 63.51  E-value: 5.74e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024430623 1156 INVADGNGNTALH-YSVSHS-NFEIVKLLLDANVcNVNHQNKAGYTPI---------------MLAALAAVEAEKDMR-- 1216
Cdd:PHA03095   110 VNAKDKVGRTPLHvYLSGFNiNPKVIRLLLRKGA-DVNALDLYGMTPLavllksrnanvellrLLIDAGADVYAVDDRfr 188

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024430623 1217 ---------------IVEELFSCGDVNAKASQAGQTALMLAVSHG---RIDMVKaLLACGADVNIQDDEGSTALMCASEH 1278
Cdd:PHA03095   189 sllhhhlqsfkprarIVRELIRAGCDPAATDMLGNTPLHSMATGSsckRSLVLP-LLIAGISINARNRYGQTPLHYAAVF 267

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 2024430623 1279 GHVEIVKLLLAQpGCNGTLEDNDGSTALSIALEAGHKDI--AVL 1320
Cdd:PHA03095   268 NNPRACRRLIAL-GADINAVSSDGNTPLSLMVRNNNGRAvrAAL 310
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 1177-1326 1.97e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 61.52  E-value: 1.97e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024430623 1177 EIVKLLLDANVcnvnhqnKAGYTPImlaalaaVEAEKDMriVEELFSCG-DVNAKASQAgQTALMLAVSHGRIDMVKALL 1255
Cdd:PHA02874    82 DIIKLLIDNGV-------DTSILPI-------PCIEKDM--IKTILDCGiDVNIKDAEL-KTFLHYAIKKGDLESIKMLF 144

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024430623 1256 ACGADVNIQDDEGSTALMCASEHGHVEIVKLLLaQPGCNGTLEDNDGSTALSIALEAGHKDIAVLLYAHVN 1326
Cdd:PHA02874   145 EYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLL-EKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGN 214
Ank_5 pfam13857
Ankyrin repeats (many copies);
1254-1309 5.37e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 53.50  E-value: 5.37e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2024430623 1254 LLACG-ADVNIQDDEGSTALMCASEHGHVEIVKLLLAqPGCNGTLEDNDGSTALSIA 1309
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLA-YGVDLNLKDEEGLTALDLA 56
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 1157-1288 6.63e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 60.65  E-value: 6.63e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024430623 1157 NVADGNGNTALHYSVSHSNFEIVKLLLDaNVCNVNHQNKAGYTPIMLAALAaveaeKDMRIVEELFSCgdvnAKAS--QA 1234
Cdd:PLN03192   552 DIGDSKGRTPLHIAASKGYEDCVLVLLK-HACNVHIRDANGNTALWNAISA-----KHHKIFRILYHF----ASISdpHA 621

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2024430623 1235 GQTALMLAVSHGRIDMVKALLACGADVNIQDDEGSTALMCASEHGHVEIVKLLL 1288
Cdd:PLN03192   622 AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLI 675
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1272-1336 6.74e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 54.35  E-value: 6.74e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024430623 1272 LMCASEHGHVEIVKLLLaQPGCNGTLEDNDGSTALSIALEAGHKDIAVLLYAHVNFSKTQSPGTP 1336
Cdd:pfam12796    1 LHLAAKNGNLELVKLLL-ENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGRTA 64
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 1251-1324 3.16e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 57.99  E-value: 3.16e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024430623 1251 VKALLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLaQPGCNGTLEDNDGSTALSIALEAGHKDIAVLLYAH 1324
Cdd:PTZ00322    98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLL-EFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
Ank_5 pfam13857
Ankyrin repeats (many copies);
1226-1272 3.77e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 51.19  E-value: 3.77e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 2024430623 1226 DVNAKaSQAGQTALMLAVSHGRIDMVKALLACGADVNIQDDEGSTAL 1272
Cdd:pfam13857    8 DLNRL-DGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 1213-1334 5.64e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 57.57  E-value: 5.64e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024430623 1213 KDMRIVEELFSCGDVNAKASQAGQtaLMLAVSHGRIDMVKALLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLAQpG 1292
Cdd:PLN03192   505 HDLNVGDLLGDNGGEHDDPNMASN--LLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKH-A 581

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 2024430623 1293 CNGTLEDNDGSTALSIALEAGHKDIAVLLYAHVNFSKTQSPG 1334
Cdd:PLN03192   582 CNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHAAG 623
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 1162-1319 9.38e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 56.15  E-value: 9.38e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024430623 1162 NGNTALHYSVSHSNFEIVKLLLDAN-VCNVNHqnkagytPIMLAALAAVEAEKDMRIVEELFSCGD-VNAKASQAGQTAL 1239
Cdd:PHA02875    34 DGISPIKLAMKFRDSEAIKLLMKHGaIPDVKY-------PDIESELHDAVEEGDVKAVEELLDLGKfADDVFYKDGMTPL 106

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024430623 1240 MLAVSHGRIDMVKALLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLAQPGCNgTLEDNDGSTALSIALeaGHKDIAV 1319
Cdd:PHA02875   107 HLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACL-DIEDCCGCTPLIIAM--AKGDIAI 183
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 1167-1321 1.79e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 56.03  E-value: 1.79e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024430623 1167 LHYSVSHSNFEIVKLLLDANVCNVNhqnkagytPIMLAALAAVEAEKDMRIVEELFSCGDVNAKASQAGQTALMLAVSHG 1246
Cdd:PLN03192   498 LQHHKELHDLNVGDLLGDNGGEHDD--------PNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKG 569

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024430623 1247 RIDMVKALLACGADVNIQDDEGSTALMCASEHGHVEIVKLL------------------------------LAQPGCNGT 1296
Cdd:PLN03192   570 YEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILyhfasisdphaagdllctaakrndltamkeLLKQGLNVD 649

                          170       180
                   ....*....|....*....|....*
gi 2024430623 1297 LEDNDGSTALSIALEAGHKDIAVLL 1321
Cdd:PLN03192   650 SEDHQGATALQVAMAEDHVDMVRLL 674
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 1235-1266 3.75e-07

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: 47.67  E-value: 3.75e-07
                           10        20        30
                   ....*....|....*....|....*....|...
gi 2024430623 1235 GQTALMLAVSH-GRIDMVKALLACGADVNIQDD 1266
Cdd:pfam00023    2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 1156-1316 4.77e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 53.81  E-value: 4.77e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024430623 1156 INVADGNGNTALHYSVSHSNFEIVKLLLDaNVCNVNHQNKAGYTPImlaalAAVEAEKDMRIVEELFSCGDVNAKASQAG 1235
Cdd:PHA02874   150 VNIEDDNGCYPIHIAIKHNFFDIIKLLLE-KGAYANVKDNNGESPL-----HNAAEYGDYACIKLLIDHGNHIMNKCKNG 223

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024430623 1236 QTALMLAVSHGRidMVKALLACGADVNIQDDEGSTALMCASEHG-HVEIVKLLLAQPGcNGTLEDNDGSTALSIALEAGH 1314
Cdd:PHA02874   224 FTPLHNAIIHNR--SAIELLINNASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKA-DISIKDNKGENPIDTAFKYIN 300


                   ..
gi 2024430623 1315 KD 1316
Cdd:PHA02874   301 KD 302
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 1156-1317 6.35e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 53.43  E-value: 6.35e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024430623 1156 INVADGNGNTALHYSVSHSNFEIVKLLLDaNVCNVNHQNKAGYTPImlaalaAVEAEKDMRIVEELFSCGDVNAKASQaG 1235
Cdd:PHA02874   183 ANVKDNNGESPLHNAAEYGDYACIKLLID-HGNHIMNKCKNGFTPL------HNAIIHNRSAIELLINNASINDQDID-G 254

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024430623 1236 QTALMLAVSHG-RIDMVKALLACGADVNIQDDEGSTALMCASEH-GHVEIVKLLLAqpgcNGTLEDNDGSTALSIALEag 1313
Cdd:PHA02874   255 STPLHHAINPPcDIDIIDILLYHKADISIKDNKGENPIDTAFKYiNKDPVIKDIIA----NAVLIKEADKLKDSDFLE-- 328


                   ....
gi 2024430623 1314 HKDI 1317
Cdd:PHA02874   329 HIEI 332
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 1235-1263 8.47e-07

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: 46.48  E-value: 8.47e-07
                           10        20
                   ....*....|....*....|....*....
gi 2024430623 1235 GQTALMLAVSHGRIDMVKALLACGADVNI 1263
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 1163-1322 1.19e-06

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 53.09  E-value: 1.19e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024430623 1163 GNTALHYSVSHSNFEIVKLLLDANVCNVNhqnkagytpimlaalaaveaekdMRIVEELFscgdvnakasqAGQTALMLA 1242
Cdd:cd22192     51 GETALHVAALYDNLEAAVVLMEAAPELVN-----------------------EPMTSDLY-----------QGETALHIA 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024430623 1243 VSHGRIDMVKALLACGADVNIQDDEGS------TALMCASEH--------GHVEIVKLLLaQPGCNGTLEDNDGSTALSI 1308
Cdd:cd22192     97 VVNQNLNLVRELIARGADVVSPRATGTffrpgpKNLIYYGEHplsfaacvGNEEIVRLLI-EHGADIRAQDSLGNTVLHI 175

                          170
                   ....*....|....
gi 2024430623 1309 ALEAGHKDIAVLLY 1322
Cdd:cd22192    176 LVLQPNKTFACQMY 189
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 276-537 5.54e-06

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.21  E-value: 5.54e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024430623  276 KELEEQVKTIPVLQVKISVLQEEKRHmmaeLKSQRKSSQndvygfrkRSYSAGNAEQWEHLSQvrrggelyidcedEMES 355
Cdd:TIGR02168  281 EEIEELQKELYALANEISRLEQQKQI----LRERLANLE--------RQLEELEAQLEELESK-------------LDEL 335

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024430623  356 AEQSSRRVEEFRQLTAEMQALEKKIQDSNYEVP------SNLRESLTKESRSVA---VGADENMNDvVIYNRS------S 420
Cdd:TIGR02168  336 AEELAELEEKLEELKEELESLEAELEELEAELEelesrlEELEEQLETLRSKVAqleLQIASLNNE-IERLEArlerleD 414

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024430623  421 RQHREVAVGTEKEMRESGVGVTEAMLGLStEVEKEIELQQQTIEALKEKIYRLEVQLKETThdREMTKLKQELQAAGSRK 500
Cdd:TIGR02168  415 RRERLQQEIEELLKKLEEAELKELQAELE-ELEEELEELQEELERLEEALEELREELEEAE--QALDAAERELAQLQARL 491

                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 2024430623  501 KVDKAMMAQPLVVSRMVEAVVQMRDQMVGDHVHVADS 537
Cdd:TIGR02168  492 DSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSEL 528
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 1235-1263 5.83e-06

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: 44.12  E-value: 5.83e-06
                            10        20
                    ....*....|....*....|....*....
gi 2024430623  1235 GQTALMLAVSHGRIDMVKALLACGADVNI 1263
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_4 pfam13637
Ankyrin repeats (many copies);
1268-1321 7.00e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.57  E-value: 7.00e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2024430623 1268 GSTALMCASEHGHVEIVKLLLaQPGCNGTLEDNDGSTALSIALEAGHKDIAVLL 1321
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLL-EKGADINAVDGNGETALHFAASNGNVEVLKLL 53
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
270-497 7.01e-06

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 50.54  E-value: 7.01e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024430623  270 IALKRLKELEEQVKTIPVLQVKISVLQEEK---RHMMAELKSQRKSSQNDVygfRKRSYSAGNAEQWEHLSQVRRggELy 346
Cdd:COG4717     68 LNLKELKELEEELKEAEEKEEEYAELQEELeelEEELEELEAELEELREEL---EKLEKLLQLLPLYQELEALEA--EL- 141

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024430623  347 idcEDEMESAEQSSRRVEEFRQLTAEMQALEKKIQdsnyevpsNLRESLTKESRSVAVGADENMNDVViynrssRQHREV 426
Cdd:COG4717    142 ---AELPERLEELEERLEELRELEEELEELEAELA--------ELQEELEELLEQLSLATEEELQDLA------EELEEL 204

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024430623  427 avgtEKEMRESgvgvteamlglstevEKEIELQQQTIEALKEKIYRLEVQLKETTHDREMTKLKQELQAAG 497
Cdd:COG4717    205 ----QQRLAEL---------------EEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAA 256
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 1235-1333 7.21e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 50.67  E-value: 7.21e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024430623 1235 GQTALMLAVSHGRIDMVKALLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLAQPGCNGTLEDNdgSTALSIALEAGH 1314
Cdd:PTZ00322   115 GRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFELGAN--AKPDSFTGKPPS 192

                           90
                   ....*....|....*....
gi 2024430623 1315 KDIAVLLYAHVNFSKTQSP 1333
Cdd:PTZ00322   193 LEDSPISSHHPDFSAVPQP 211
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
261-479 1.04e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 50.06  E-value: 1.04e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024430623  261 LQQIREQMAIALKRLKELEEQVKTIPVLQVKISVLQEEKRHMMAELKSQRKSSQNDVYG-------FRKRSYSAGNAEqw 333
Cdd:PRK03918   534 LIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEErlkelepFYNEYLELKDAE-- 611

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024430623  334 ehlSQVRRGGELYIDCEDEMESAEQSSRRVE-EFRQLTAEMQALEKKIQDSNYEvpsNLRESLTKESRSVAvGADENMnd 412
Cdd:PRK03918   612 ---KELEREEKELKKLEEELDKAFEELAETEkRLEELRKELEELEKKYSEEEYE---ELREEYLELSRELA-GLRAEL-- 682

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024430623  413 vviynRSSRQHREVAVGTEKEMRESgvgvteamLGLSTEVEKEIELQQQTI---EALKEKIYRLEVQLKE 479
Cdd:PRK03918   683 -----EELEKRREEIKKTLEKLKEE--------LEEREKAKKELEKLEKALervEELREKVKKYKALLKE 739
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 1157-1263 1.83e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 48.83  E-value: 1.83e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024430623 1157 NVADGNGNTALHYSVSHSNFEIVKLLLDANVCnVNHQNKAGYTPIMLAALAaveaeKDMRIVEELFSCG-DVNAKASQAG 1235
Cdd:PHA02875   129 DIPNTDKFSPLHLAVMMGDIKGIELLIDHKAC-LDIEDCCGCTPLIIAMAK-----GDIAICKMLLDSGaNIDYFGKNGC 202

                           90       100
                   ....*....|....*....|....*...
gi 2024430623 1236 QTALMLAVSHGRIDMVKALLACGADVNI 1263
Cdd:PHA02875   203 VAALCYAIENNKIDIVRLFIKRGADCNI 230
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 1151-1309 3.34e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 47.95  E-value: 3.34e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024430623 1151 VLRHIINVADGNGNTALHYSVSHSNFEIVKLLLdanvcnVNHQNKAGYTPIMLAALAAVEAEKDMRIVEELFSCG-DVNA 1229
Cdd:PHA02878    89 MIRSINKCSVFYTLVAIKDAFNNRNVEIFKIIL------TNRYKNIQTIDLVYIDKKSKDDIIEAEITKLLLSYGaDINM 162

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024430623 1230 KASQAGQTALMLAVSHGRIDMVKALLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLaQPGCNGTLEDNDGSTALSIA 1309
Cdd:PHA02878   163 KDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILL-ENGASTDARDKCGNTPLHIS 241
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1152-1194 3.92e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 43.57  E-value: 3.92e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 2024430623 1152 LRHIINVADGNGNTALHYSVSHSNFEIVKLLLDANvCNVNHQN 1194
Cdd:pfam12796   50 LEHADVNLKDNGRTALHYAARSGHLEIVKLLLEKG-ADINVKD 91
Ank_4 pfam13637
Ankyrin repeats (many copies);
1156-1183 4.02e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 42.26  E-value: 4.02e-05
                           10        20
                   ....*....|....*....|....*...
gi 2024430623 1156 INVADGNGNTALHYSVSHSNFEIVKLLL 1183
Cdd:pfam13637   27 INAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 1144-1272 4.20e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 47.94  E-value: 4.20e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024430623 1144 FEEISPAVLRHI--INVADGNGNTALHYSVSHSNFEIVKLLldanvcnvnHQNKAGYTP-IMLAALAAVEAEKDMRIVEE 1220
Cdd:PLN03192   570 YEDCVLVLLKHAcnVHIRDANGNTALWNAISAKHHKIFRIL---------YHFASISDPhAAGDLLCTAAKRNDLTAMKE 640

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2024430623 1221 LFSCG-DVNAKASQaGQTALMLAVSHGRIDMVKALLACGADV---NIQDDEGSTAL 1272
Cdd:PLN03192   641 LLKQGlNVDSEDHQ-GATALQVAMAEDHVDMVRLLIMNGADVdkaNTDDDFSPTEL 695
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 1217-1306 4.40e-05

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 47.83  E-value: 4.40e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024430623 1217 IVEELFSCGD--------VNAKASQA---GQTALMLAVSHGRIDMVKALLACGADVNIQ----------DDE----GSTA 1271
Cdd:cd22194    112 IVRILLAFAEengildrfINAEYTEEayeGQTALNIAIERRQGDIVKLLIAKGADVNAHakgvffnpkyKHEgfyfGETP 191

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2024430623 1272 LMCASEHGHVEIVKLLLAQPGCNGTLEDNDGSTAL 1306
Cdd:cd22194    192 LALAACTNQPEIVQLLMEKESTDITSQDSRGNTVL 226
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 1167-1321 4.59e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 47.68  E-value: 4.59e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024430623 1167 LHYSVSHSNFEIVKLLLDANVCNVNHQNKAGYTPImlaalAAVEAEKDMRIVEELFSCGDVNAKASQAGQTALMLAVSHG 1246
Cdd:PHA02875    72 LHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPL-----HLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMG 146

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024430623 1247 RIDMVKALLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLAQPGCNGTLEDNDGSTALSIALEAGHKDIAVLL 1321
Cdd:PHA02875   147 DIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIDIVRLF 221
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 1162-1195 5.80e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 41.51  E-value: 5.80e-05
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 2024430623 1162 NGNTALHYSVSHS-NFEIVKLLLDANvCNVNHQNK 1195
Cdd:pfam00023    1 DGNTPLHLAAGRRgNLEIVKLLLSKG-ADVNARDK 34
PHA03095 PHA03095
ankyrin-like protein; Provisional
 1147-1290 1.14e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 46.17  E-value: 1.14e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024430623 1147 ISPAVLRHIINV------ADGNGNTALHY--SVSHSNFEIVKLLLDANvCNVNHQNKAGYTPIMLAALAAVEAEKDMR-- 1216
Cdd:PHA03095   165 ANVELLRLLIDAgadvyaVDDRFRSLLHHhlQSFKPRARIVRELIRAG-CDPAATDMLGNTPLHSMATGSSCKRSLVLpl 243

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024430623 1217 IVEELfscgDVNAKaSQAGQTALMLAVSHGRIDMVKALLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLAQ 1290
Cdd:PHA03095   244 LIAGI----SINAR-NRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAK 312
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 1156-1328 1.71e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 45.72  E-value: 1.71e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024430623 1156 INVADGNGNTALHYSVSHSNFEIVKLLLDANVcNVNHQNKAGYTPImlaalAAVEAEKDMRIVEELFSCGDVNAKASQAG 1235
Cdd:PHA02874   117 VNIKDAELKTFLHYAIKKGDLESIKMLFEYGA-DVNIEDDNGCYPI-----HIAIKHNFFDIIKLLLEKGAYANVKDNNG 190

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024430623 1236 QTALMLAVSHGRIDMVKALLACGADVNIQDDEGSTALMCASEHGHvEIVKLLLAQPGCNGTleDNDGSTALSIALE-AGH 1314
Cdd:PHA02874   191 ESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIELLINNASINDQ--DIDGSTPLHHAINpPCD 267

                          170
                   ....*....|....*
gi 2024430623 1315 KDIA-VLLYAHVNFS 1328
Cdd:PHA02874   268 IDIIdILLYHKADIS 282
Ank_5 pfam13857
Ankyrin repeats (many copies);
1156-1201 2.23e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.41  E-value: 2.23e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 2024430623 1156 INVADGNGNTALHYSVSHSNFEIVKLLLdANVCNVNHQNKAGYTPI 1201
Cdd:pfam13857    9 LNRLDGEGYTPLHVAAKYGALEIVRVLL-AYGVDLNLKDEEGLTAL 53
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 1162-1191 3.29e-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: 3.29e-04
                            10        20        30
                    ....*....|....*....|....*....|
gi 2024430623  1162 NGNTALHYSVSHSNFEIVKLLLDANVcNVN 1191
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGA-DIN 29
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 1239-1324 3.71e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 44.66  E-value: 3.71e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024430623 1239 LMLAVSHGRIDMVKALLACGADVNIQDDEGSTALMCASEHGHV-----EIVKLLLaQPGCNGTLEDNDGSTALSIALEA- 1312
Cdd:PHA03100    39 LYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLL-EYGANVNAPDNNGITPLLYAISKk 117

                           90
                   ....*....|...
gi 2024430623 1313 -GHKDIAVLLYAH 1324
Cdd:PHA03100   118 sNSYSIVEYLLDN 130
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 1156-1326 5.25e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 44.10  E-value: 5.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024430623 1156 INVADGN-GNTALHYSVSHSNFEIVKLLLDANVcNVNHQNKAGYTPimlaalaaveaekdmriveelfscgdvnakasqa 1234
Cdd:PHA02878   160 INMKDRHkGNTALHYATENKDQRLTELLLSYGA-NVNIPDKTNNSP---------------------------------- 204

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024430623 1235 gqtaLMLAVSHGRIDMVKALLACGADVNIQDDEGSTALMCASEH-GHVEIVKLLLAQPGCNGTLEDNDGSTALSIALEAG 1313
Cdd:PHA02878   205 ----LHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSYILGLTALHSSIKSE 280

                          170
                   ....*....|....
gi 2024430623 1314 HKDIAVLLY-AHVN 1326
Cdd:PHA02878   281 RKLKLLLEYgADIN 294
PHA02798 PHA02798
ankyrin-like protein; Provisional
 1217-1320 6.93e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 43.67  E-value: 6.93e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024430623 1217 IVEELFSCG-DVNAKASQAgQTALMLAVSH-----GRIDMVKALLACGADVNIQDDEGSTALMCASEHGHV---EIVkLL 1287
Cdd:PHA02798    53 IVKLFINLGaNVNGLDNEY-STPLCTILSNikdykHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYInnlEIL-LF 130

                           90       100       110
                   ....*....|....*....|....*....|....
gi 2024430623 1288 LAQPGCNGTLEDNDGSTALSIALEAGHK-DIAVL 1320
Cdd:PHA02798   131 MIENGADTTLLDKDGFTMLQVYLQSNHHiDIEII 164
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 261-501 1.06e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 43.21  E-value: 1.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024430623  261 LQQIREQMAIALKRLKELEEQVKTIP----VLQVKISVLQEEKRhmmaELKSQRKSSQNDVYGFRKR--SYSAGNAEQWE 334
Cdd:COG4942     29 LEQLQQEIAELEKELAALKKEEKALLkqlaALERRIAALARRIR----ALEQELAALEAELAELEKEiaELRAELEAQKE 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024430623  335 HLSQV-----RRGGELYIDCEDEMESAEQSSRRVEEFRQLTAEMQALEKKIQDSNYEVpSNLRESLTKESRSVAVGADEn 409
Cdd:COG4942    105 ELAELlralyRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAEL-AALRAELEAERAELEALLAE- 182

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024430623  410 mndvviynrssRQHREVAVGTEKEMRESgvgvteamlgLSTEVEKEIELQQQTIEALKEKIYRLEvqlketthdREMTKL 489
Cdd:COG4942    183 -----------LEEERAALEALKAERQK----------LLARLEKELAELAAELAELQQEAEELE---------ALIARL 232

                          250
                   ....*....|..
gi 2024430623  490 KQELQAAGSRKK 501
Cdd:COG4942    233 EAEAAAAAERTP 244
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 1214-1288 1.08e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 43.51  E-value: 1.08e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024430623 1214 DMRIVEELFSCG-DVNAKASQAgQTALMLAVSHGRIDMVKALLACGADVNIQDDEGSTALMCASEHGHVEIVKLLL 1288
Cdd:PHA02876   157 ELLIAEMLLEGGaDVNAKDIYC-ITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAII 231
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
261-378 2.10e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.45  E-value: 2.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024430623  261 LQQIREQMAIALKRLKELEEQVKTIPVLQVKISVLQEEKRHMMAELKSQRKSSQndvygFRKRSYSAGNAEQWEHLSQ-V 339
Cdd:COG4717    134 LEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLS-----LATEEELQDLAEELEELQQrL 208

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2024430623  340 RRGGELYIDCEDEMESAEQSSRRVEEFRQLTAEMQALEK 378
Cdd:COG4717    209 AELEEELEEAQEELEELEEELEQLENELEAAALEERLKE 247
Ank_4 pfam13637
Ankyrin repeats (many copies);
1163-1201 2.14e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 37.64  E-value: 2.14e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2024430623 1163 GNTALHYSVSHSNFEIVKLLLDANVcNVNHQNKAGYTPI 1201
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGA-DINAVDGNGETAL 38
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 1267-1288 2.21e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.80  E-value: 2.21e-03
                            10        20
                    ....*....|....*....|..
gi 2024430623  1267 EGSTALMCASEHGHVEIVKLLL 1288
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLL 22
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
261-479 2.37e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.36  E-value: 2.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024430623  261 LQQIREQMAIALKRLKELEEQVKTIPVLQVKISVLQEEKRHMMAELKSQRKSSQndvygfRKRSYSAGNAEQWEHLSQVR 340
Cdd:PRK03918   216 LPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIE------ELKKEIEELEEKVKELKELK 289

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024430623  341 RGGELYIDCEDEMESAEQSSRRVE-EFRQLTAEMQALEKKIQDSNyEVPSNLREsLTKESRSVAVGADENMNDVVIYNRs 419
Cdd:PRK03918   290 EKAEEYIKLSEFYEEYLDELREIEkRLSRLEEEINGIEERIKELE-EKEERLEE-LKKKLKELEKRLEELEERHELYEE- 366

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024430623  420 SRQHREVAVGTEKEMRESGVGVTEAMLglsTEVEKEIELQQQTIEALKEKIYRLEVQLKE 479
Cdd:PRK03918   367 AKAKKEELERLKKRLTGLTPEKLEKEL---EELEKAKEEIEEEISKITARIGELKKEIKE 423
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 1162-1192 3.03e-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: 3.03e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 2024430623 1162 NGNTALHYSVSHSNFEIVKLLLDANVcNVNH 1192
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGA-DINA 30
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
330-501 8.26e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.52  E-value: 8.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024430623  330 AEQWEHLSQvrrggELYIDCEDEMESAEQSSRRVEEFRQLTAEMQALEKKIQDSNYEvpsNLRESLTKES--------RS 401
Cdd:COG4717    318 EEELEELLA-----ALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELE---QEIAALLAEAgvedeeelRA 389

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024430623  402 VAVGADENMNDVVIYNRSSRQHREVAVGTEKEMRESGVGVTEAMLGlstEVEKEIELQQQTIEALKEKIYRLEVQLKETT 481
Cdd:COG4717    390 ALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELE---ELEEELEELEEELEELREELAELEAELEQLE 466

                          170       180
                   ....*....|....*....|
gi 2024430623  482 HDREMTKLKQELQAAGSRKK 501
Cdd:COG4717    467 EDGELAELLQELEELKAELR 486
 
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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