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Conserved domains on  [gi|157822091|ref|NP_001101417|]
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KN motif and ankyrin repeat domain-containing protein 4 [Rattus norvegicus]

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];
826-994 8.94e-29

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 117.36  E-value: 8.94e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822091  826 VNLADRSGNTALHYSVSHSNFAIAKLLLDTGVcNVDHQNKAGYTAVMitpLASpkTKEDMAVVWKLLREG-NVNIQaTQG 904
Cdd:COG0666   113 VNARDKDGETPLHLAAYNGNLEIVKLLLEAGA-DVNAQDNDGNTPLH---LAA--ANGNLEIVKLLLEAGaDVNAR-DND 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822091  905 GQTALMLGVSHDREDMVQALLSCKADVNLQDHDGSSALMLACHQGNADLVRLLLAHADcNSNLTDKAGQTALSIVLNSPA 984
Cdd:COG0666   186 GETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA-DLNAKDKDGLTALLLAAAAGA 264

                         170
                  ....*....|
gi 157822091  985 HVEIAELLRA 994
Cdd:COG0666   265 ALIVKLLLLA 274
KN_motif pfam12075
KN motif; This small motif is found at the N-terminus of Kank proteins and has been called the ...
 24-62 1.68e-20

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: 85.09  E-value: 1.68e-20
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 157822091    24 PYSVETPYGFHLDLDFLKYVDDIEKGHTIKRIPIHRRAK 62
Cdd:pfam12075    1 PYSVETPYGFHLDLDFLKYVEDIESGQTIRRARVQRRPR 39
COG4913 super family cl25907
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
338-428 4.48e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


The actual alignment was detected with superfamily member COG4913:

Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.05  E-value: 4.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822091  338 VETATSSISSLKSQVLDLE---DKLSGRTEELAQVRAALEQQEEETKAREQRIQELECTVAHLEEKlsQEKASDALDRTD 414
Cdd:COG4913   663 VASAEREIAELEAELERLDassDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEE--LDELQDRLEAAE 740

                          90
                  ....*....|....
gi 157822091  415 AMVNTDPLRELIPR 428
Cdd:COG4913   741 DLARLELRALLEER 754
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
826-994 8.94e-29

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 117.36  E-value: 8.94e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822091  826 VNLADRSGNTALHYSVSHSNFAIAKLLLDTGVcNVDHQNKAGYTAVMitpLASpkTKEDMAVVWKLLREG-NVNIQaTQG 904
Cdd:COG0666   113 VNARDKDGETPLHLAAYNGNLEIVKLLLEAGA-DVNAQDNDGNTPLH---LAA--ANGNLEIVKLLLEAGaDVNAR-DND 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822091  905 GQTALMLGVSHDREDMVQALLSCKADVNLQDHDGSSALMLACHQGNADLVRLLLAHADcNSNLTDKAGQTALSIVLNSPA 984
Cdd:COG0666   186 GETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA-DLNAKDKDGLTALLLAAAAGA 264

                         170
                  ....*....|
gi 157822091  985 HVEIAELLRA 994
Cdd:COG0666   265 ALIVKLLLLA 274
KN_motif pfam12075
KN motif; This small motif is found at the N-terminus of Kank proteins and has been called the ...
 24-62 1.68e-20

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: 85.09  E-value: 1.68e-20
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 157822091    24 PYSVETPYGFHLDLDFLKYVDDIEKGHTIKRIPIHRRAK 62
Cdd:pfam12075    1 PYSVETPYGFHLDLDFLKYVEDIESGQTIRRARVQRRPR 39
Ank_2 pfam12796
Ankyrin repeats (3 copies);
909-995 1.93e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.54  E-value: 1.93e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822091   909 LMLGVSHDREDMVQALLSCKADVNLQDHDGSSALMLACHQGNADLVRLLLAHADCNSNLtdkAGQTAL--SIVLNspaHV 986
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKD---NGRTALhyAARSG---HL 74


                   ....*....
gi 157822091   987 EIAELLRAH 995
Cdd:pfam12796   75 EIVKLLLEK 83
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 826-948 2.54e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 57.58  E-value: 2.54e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822091  826 VNLADRSGNTALHYSVSHSNFAIAKLLLDTGvCNVDHQNKAGYTAVMItplaSPKTKEDMAVVWKLLREG-NVNIQATQG 904
Cdd:PHA02878  194 VNIPDKTNNSPLHHAVKHYNKPIVHILLENG-ASTDARDKCGNTPLHI----SVGYCKDYDILKLLLEHGvDVNAKSYIL 268

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 157822091  905 GQTALMLGVsHDrEDMVQALLSCKADVNLQDHDGSSALMLACHQ 948
Cdd:PHA02878  269 GLTALHSSI-KS-ERKLKLLLEYGADINSLNSYKLTPLSSAVKQ 310
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 937-964 2.50e-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: 36.41  E-value: 2.50e-03
                            10        20
                    ....*....|....*....|....*....
gi 157822091    937 DGSSALMLACHQGNADLVRLLLAH-ADCN 964
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKgADIN 29
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
338-428 4.48e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.05  E-value: 4.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822091  338 VETATSSISSLKSQVLDLE---DKLSGRTEELAQVRAALEQQEEETKAREQRIQELECTVAHLEEKlsQEKASDALDRTD 414
Cdd:COG4913   663 VASAEREIAELEAELERLDassDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEE--LDELQDRLEAAE 740

                          90
                  ....*....|....
gi 157822091  415 AMVNTDPLRELIPR 428
Cdd:COG4913   741 DLARLELRALLEER 754
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 333-432 6.17e-03

chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 40.82  E-value: 6.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822091   333 ESLGLVETATSSISSLKSQVLDLEDKLSGRTEELAQVRAALEQQEEETKAREQRIQELECTVAHLEEKLSQEKAsdALDR 412
Cdd:TIGR02169  706 ELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEE--ALND 783

                           90       100
                   ....*....|....*....|
gi 157822091   413 TDAMVNTDPLRElIPRESQD 432
Cdd:TIGR02169  784 LEARLSHSRIPE-IQAELSK 802
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
826-994 8.94e-29

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 117.36  E-value: 8.94e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822091  826 VNLADRSGNTALHYSVSHSNFAIAKLLLDTGVcNVDHQNKAGYTAVMitpLASpkTKEDMAVVWKLLREG-NVNIQaTQG 904
Cdd:COG0666   113 VNARDKDGETPLHLAAYNGNLEIVKLLLEAGA-DVNAQDNDGNTPLH---LAA--ANGNLEIVKLLLEAGaDVNAR-DND 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822091  905 GQTALMLGVSHDREDMVQALLSCKADVNLQDHDGSSALMLACHQGNADLVRLLLAHADcNSNLTDKAGQTALSIVLNSPA 984
Cdd:COG0666   186 GETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA-DLNAKDKDGLTALLLAAAAGA 264

                         170
                  ....*....|
gi 157822091  985 HVEIAELLRA 994
Cdd:COG0666   265 ALIVKLLLLA 274
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
821-995 4.20e-26

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 109.66  E-value: 4.20e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822091  821 LLKLLVNLADRSGNTALHYSVSHSNFAIAKLLLDTGVCNVDHQNKAGYTAVMITplaspKTKEDMAVVWKLLREG-NVNI 899
Cdd:COG0666    41 LLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAA-----ARNGDLEIVKLLLEAGaDVNA 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822091  900 QaTQGGQTALMLGVSHDREDMVQALLSCKADVNLQDHDGSSALMLACHQGNADLVRLLLAH-ADCnsNLTDKAGQTALSI 978
Cdd:COG0666   116 R-DKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAgADV--NARDNDGETPLHL 192

                         170
                  ....*....|....*...
gi 157822091  979 -VLNSpaHVEIAELLRAH 995
Cdd:COG0666   193 aAENG--HLEIVKLLLEA 208
KN_motif pfam12075
KN motif; This small motif is found at the N-terminus of Kank proteins and has been called the ...
 24-62 1.68e-20

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: 85.09  E-value: 1.68e-20
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 157822091    24 PYSVETPYGFHLDLDFLKYVDDIEKGHTIKRIPIHRRAK 62
Cdd:pfam12075    1 PYSVETPYGFHLDLDFLKYVEDIESGQTIRRARVQRRPR 39
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
821-995 1.83e-20

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 93.09  E-value: 1.83e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822091  821 LLKLLVNLADRSGNTALHYSVSHSNFAIAKLLLDTGVCNVDHQNKAGYTAVMITPLASPKTKEDMAVVWKLLREGNVNIQ 900
Cdd:COG0666     3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822091  901 ATQGGQTALMLGVSHDREDMVQALLSCKADVNLQDHDGSSALMLACHQGNADLVRLLLAH-ADcnSNLTDKAGQTALSI- 978
Cdd:COG0666    83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAgAD--VNAQDNDGNTPLHLa 160

                         170
                  ....*....|....*..
gi 157822091  979 VLNSpaHVEIAELLRAH 995
Cdd:COG0666   161 AANG--NLEIVKLLLEA 175
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
818-971 3.70e-19

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 89.24  E-value: 3.70e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822091  818 SPHLLKLL------VNLADRSGNTALHYSVSHSNFAIAKLLLDTGVcNVDHQNKAGYTAVMItplASpkTKEDMAVVWKL 891
Cdd:COG0666   132 NLEIVKLLleagadVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGA-DVNARDNDGETPLHL---AA--ENGHLEIVKLL 205

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822091  892 LREG-NVNIQaTQGGQTALMLGVSHDREDMVQALLSCKADVNLQDHDGSSALMLACHQGNADLVRLLLAHADCNSNLTDK 970
Cdd:COG0666   206 LEAGaDVNAK-DNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLD 284


                  .
gi 157822091  971 A 971
Cdd:COG0666   285 L 285
Ank_2 pfam12796
Ankyrin repeats (3 copies);
909-995 1.93e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.54  E-value: 1.93e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822091   909 LMLGVSHDREDMVQALLSCKADVNLQDHDGSSALMLACHQGNADLVRLLLAHADCNSNLtdkAGQTAL--SIVLNspaHV 986
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKD---NGRTALhyAARSG---HL 74


                   ....*....
gi 157822091   987 EIAELLRAH 995
Cdd:pfam12796   75 EIVKLLLEK 83
Ank_2 pfam12796
Ankyrin repeats (3 copies);
837-935 2.93e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 63.60  E-value: 2.93e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822091   837 LHYSVSHSNFAIAKLLLDTGvCNVDHQNKAGYTAVMITplASpktKEDMAVVWKLLREGNVNIQAtqGGQTALMLGVSHD 916
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENG-ADANLQDKNGRTALHLA--AK---NGHLEIVKLLLEHADVNLKD--NGRTALHYAARSG 72

                           90
                   ....*....|....*....
gi 157822091   917 REDMVQALLSCKADVNLQD 935
Cdd:pfam12796   73 HLEIVKLLLEKGADINVKD 91
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 826-948 2.54e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 57.58  E-value: 2.54e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822091  826 VNLADRSGNTALHYSVSHSNFAIAKLLLDTGvCNVDHQNKAGYTAVMItplaSPKTKEDMAVVWKLLREG-NVNIQATQG 904
Cdd:PHA02878  194 VNIPDKTNNSPLHHAVKHYNKPIVHILLENG-ASTDARDKCGNTPLHI----SVGYCKDYDILKLLLEHGvDVNAKSYIL 268

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 157822091  905 GQTALMLGVsHDrEDMVQALLSCKADVNLQDHDGSSALMLACHQ 948
Cdd:PHA02878  269 GLTALHSSI-KS-ERKLKLLLEYGADINSLNSYKLTPLSSAVKQ 310
Ank_5 pfam13857
Ankyrin repeats (many copies);
924-979 4.81e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 50.42  E-value: 4.81e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 157822091   924 LLSCK-ADVNLQDHDGSSALMLACHQGNADLVRLLLAHaDCNSNLTDKAGQTALSIV 979
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAY-GVDLNLKDEEGLTALDLA 56
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 821-990 4.10e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 53.81  E-value: 4.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822091  821 LLKLLV------NLADRSGNTALHYSVSHSNFAIAKLLLDTGvCNVDHQNKAGYtavmiTPLASpKTKEDMAVVWKLLRE 894
Cdd:PHA02874  172 IIKLLLekgayaNVKDNNGESPLHNAAEYGDYACIKLLIDHG-NHIMNKCKNGF-----TPLHN-AIIHNRSAIELLINN 244

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822091  895 GNVNIQATQgGQTALMLGVSHD-REDMVQALLSCKADVNLQDHDGSSALMLACHQGNAD-LVRLLLAhadcNSNLTDKAG 972
Cdd:PHA02874  245 ASINDQDID-GSTPLHHAINPPcDIDIIDILLYHKADISIKDNKGENPIDTAFKYINKDpVIKDIIA----NAVLIKEAD 319

                         170
                  ....*....|....*...
gi 157822091  973 QTALSIVLNspaHVEIAE 990
Cdd:PHA02874  320 KLKDSDFLE---HIEIKD 334
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 814-962 5.68e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 53.13  E-value: 5.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822091  814 VQPQSPHLLKLL------VNLADRSGNTALHYSVSHS--NFAIAKLLLDTGvCNVDHQNKAGYTAVMITpLASPKTKEDM 885
Cdd:PHA03100   81 NLTDVKEIVKLLleyganVNAPDNNGITPLLYAISKKsnSYSIVEYLLDNG-ANVNIKNSDGENLLHLY-LESNKIDLKI 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822091  886 AvvwKLLREGNVNIQA--------TQG---------GQTALMLGVSHDREDMVQALLSCKADVNLQDHDGSSALMLACHQ 948
Cdd:PHA03100  159 L---KLLIDKGVDINAknrvnyllSYGvpinikdvyGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILN 235

                         170
                  ....*....|....
gi 157822091  949 GNADLVRLLLAHAD 962
Cdd:PHA03100  236 NNKEIFKLLLNNGP 249
Ank_4 pfam13637
Ankyrin repeats (many copies);
907-958 1.22e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.11  E-value: 1.22e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 157822091   907 TALMLGVSHDREDMVQALLSCKADVNLQDHDGSSALMLACHQGNADLVRLLL 958
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
 884-992 3.71e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 50.79  E-value: 3.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822091  884 DMAVVWKLLREG-NVNiQATQGGQTAL---MLGVSHDREDMVQALLSCKADVNLQDHDGSSALML-ACHQGNADLVRLLL 958
Cdd:PHA03095   26 TVEEVRRLLAAGaDVN-FRGEYGKTPLhlyLHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLyLYNATTLDVIKLLI 104

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 157822091  959 AH-ADCNSnlTDKAGQTALSIVLNSP-AHVEIAELL 992
Cdd:PHA03095  105 KAgADVNA--KDKVGRTPLHVYLSGFnINPKVIRLL 138
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 823-1010 5.80e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 50.25  E-value: 5.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822091  823 KLLVNLADRSGNTALHYSVSHSNFAIAKLLLDTGvCNVDHQNKAGYTAvMITPLASpKTKEDMAVVWKLLREGNvniqaT 902
Cdd:PLN03192  548 KLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHA-CNVHIRDANGNTA-LWNAISA-KHHKIFRILYHFASISD-----P 619

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822091  903 QGGQTALMLGVSHDREDMVQALLSCKADVNLQDHDGSSALMLACHQGNADLVRLLL---AHADCnSNLTDKAGQTALSIV 979
Cdd:PLN03192  620 HAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLImngADVDK-ANTDDDFSPTELREL 698

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 157822091  980 L------------NSPAHVEIAELLRAHSEQGRSLGLKELQKN 1010
Cdd:PLN03192  699 LqkrelghsitivDSVPADEPDLGRDGGSRPGRLQGTSSDNQC 741
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 826-980 6.22e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 49.96  E-value: 6.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822091  826 VNLADRSGNTALHYSVSHSNFAIAKLLLDTGV-CNVDHQNKAgytavmiTPLASPKTKEDMAVVWKLLREGNVNIQATQG 904
Cdd:PHA02874  150 VNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAyANVKDNNGE-------SPLHNAAEYGDYACIKLLIDHGNHIMNKCKN 222

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157822091  905 GQTALMLGVSHDREdmVQALLSCKADVNLQDHDGSSALMLACHQG-NADLVRLLLAHaDCNSNLTDKAGQTALSIVL 980
Cdd:PHA02874  223 GFTPLHNAIIHNRS--AIELLINNASINDQDIDGSTPLHHAINPPcDIDIIDILLYH-KADISIKDNKGENPIDTAF 296
PHA03095 PHA03095
ankyrin-like protein; Provisional
 826-983 9.84e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 49.25  E-value: 9.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822091  826 VNLADRSGNTALHYSVSHSN-FAIAKLLLDTGVcNVDHQNKAGYTAVMITpLASPKTkedmavvwkllregnvniqatqg 904
Cdd:PHA03095   76 VNAPERCGFTPLHLYLYNATtLDVIKLLIKAGA-DVNAKDKVGRTPLHVY-LSGFNI----------------------- 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822091  905 gqtalmlgvshdREDMVQALLSCKADVNLQDHDGSSAL--MLACHQGNADLVRLLLAhADCNSNLTDKAGQTALSIVLNS 982
Cdd:PHA03095  131 ------------NPKVIRLLLRKGADVNALDLYGMTPLavLLKSRNANVELLRLLID-AGADVYAVDDRFRSLLHHHLQS 197


                  .
gi 157822091  983 P 983
Cdd:PHA03095  198 F 198
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 921-1003 1.62e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 48.74  E-value: 1.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822091  921 VQALLSCKADVNLQDHDGSSALMLACHQGNADLVRLLLAHAdCNSNLTDKAGQTALSIVLNSPAHvEIAELLRAHSEQGR 1000
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFG-ADPTLLDKDGKTPLELAEENGFR-EVVQLLSRHSQCHF 175


                  ...
gi 157822091 1001 SLG 1003
Cdd:PTZ00322  176 ELG 178
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 826-995 4.87e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 47.18  E-value: 4.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822091  826 VNLADR-SGNTALHYSVSHSNFAIAKLLLDTGVcNVDHQNKAGYtavmiTPLASPKTKEDMAVVWKLLREG-NVNIQaTQ 903
Cdd:PHA02878  160 INMKDRhKGNTALHYATENKDQRLTELLLSYGA-NVNIPDKTNN-----SPLHHAVKHYNKPIVHILLENGaSTDAR-DK 232

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822091  904 GGQTALMLGVSHDRE-DMVQALLSCKADVNLQDH-DGSSALMLACHqgNADLVRLLLAH-ADCNSNLTDKagQTALSIVL 980
Cdd:PHA02878  233 CGNTPLHISVGYCKDyDILKLLLEHGVDVNAKSYiLGLTALHSSIK--SERKLKLLLEYgADINSLNSYK--LTPLSSAV 308

                         170
                  ....*....|....*
gi 157822091  981 NSPAHVEIAELLRAH 995
Cdd:PHA02878  309 KQYLCINIGRILISN 323
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 837-992 6.08e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 46.58  E-value: 6.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822091  837 LHYSVSHSNFAIAKLLLDTGvCNVDHQNKAGYTAVM---------------------------------ITPL--ASPKT 881
Cdd:PHA03100   39 LYLAKEARNIDVVKILLDNG-ADINSSTKNNSTPLHylsnikynltdvkeivkllleyganvnapdnngITPLlyAISKK 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822091  882 KEDMAVVWKLLREG-NVNIQaTQGGQTALMLGVS--HDREDMVQALLSCKADVN----------------LQDHDGSSAL 942
Cdd:PHA03100  118 SNSYSIVEYLLDNGaNVNIK-NSDGENLLHLYLEsnKIDLKILKLLIDKGVDINaknrvnyllsygvpinIKDVYGFTPL 196

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 157822091  943 MLACHQGNADLVRLLLaHADCNSNLTDKAGQTALSIVLNSpAHVEIAELL 992
Cdd:PHA03100  197 HYAVYNNNPEFVKYLL-DLGANPNLVNKYGDTPLHIAILN-NNKEIFKLL 244
Ank_5 pfam13857
Ankyrin repeats (many copies);
891-945 8.58e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.18  E-value: 8.58e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 157822091   891 LLREGNVNIQATQG-GQTALMLGVSHDREDMVQALLSCKADVNLQDHDGSSALMLA 945
Cdd:pfam13857    1 LLEHGPIDLNRLDGeGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 874-992 3.91e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 44.21  E-value: 3.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822091  874 TPLASPKTKEDMAVVWKLLREGN-VNIQATQGGQTALMLGVSHDREDMVQALLSCKADVNLQDHDGSSALMLACHQGNAD 952
Cdd:PHA02875   70 SELHDAVEEGDVKAVEELLDLGKfADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIK 149

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 157822091  953 LVRLLLAHADCnSNLTDKAGQTALSIVLnSPAHVEIAELL 992
Cdd:PHA02875  150 GIELLIDHKAC-LDIEDCCGCTPLIIAM-AKGDIAICKML 187
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 905-967 1.15e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 42.96  E-value: 1.15e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157822091  905 GQTALMLGVSHDREDMVQALLSCKADVNLQDHDGSSALMLACHQGNADLVRLLLAHADCNSNL 967
Cdd:PTZ00322  115 GRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFEL 177
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 905-936 1.20e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 37.27  E-value: 1.20e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 157822091   905 GQTALMLGVSH-DREDMVQALLSCKADVNLQDH 936
Cdd:pfam00023    2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
Ank_4 pfam13637
Ankyrin repeats (many copies);
821-853 1.21e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.02  E-value: 1.21e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 157822091   821 LLKLL------VNLADRSGNTALHYSVSHSNFAIAKLLL 853
Cdd:pfam13637   16 LLRLLlekgadINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 833-865 2.23e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 36.50  E-value: 2.23e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 157822091   833 GNTALHYSVSHS-NFAIAKLLLDTGvCNVDHQNK 865
Cdd:pfam00023    2 GNTPLHLAAGRRgNLEIVKLLLSKG-ADVNARDK 34
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 937-964 2.50e-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: 36.41  E-value: 2.50e-03
                            10        20
                    ....*....|....*....|....*....
gi 157822091    937 DGSSALMLACHQGNADLVRLLLAH-ADCN 964
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKgADIN 29
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 831-933 2.62e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 41.52  E-value: 2.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822091  831 RSGNTALHYSVSHSNFAIAKLLL----DTGVCNVDHQNKAgYTAVMI------------------------TPLASPKTK 882
Cdd:PHA02875  100 KDGMTPLHLATILKKLDIMKLLIargaDPDIPNTDKFSPL-HLAVMMgdikgiellidhkacldiedccgcTPLIIAMAK 178

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 157822091  883 EDMAVVWKLLREG-NVNIQATQGGQTALMLGVSHDREDMVQALLSCKADVNL 933
Cdd:PHA02875  179 GDIAICKMLLDSGaNIDYFGKNGCVAALCYAIENNKIDIVRLFIKRGADCNI 230
Ank_4 pfam13637
Ankyrin repeats (many copies);
833-873 3.18e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.48  E-value: 3.18e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 157822091   833 GNTALHYSVSHSNFAIAKLLLDTGVcNVDHQNKAGYTAVMI 873
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGA-DINAVDGNGETALHF 40
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 826-995 3.75e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 41.02  E-value: 3.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822091  826 VNLADRSGNTALHYSVSHSN-FAIAKLLLDTGVCNVDHQNKAGYTA-----------VMITPLASPKTKEDM-------- 885
Cdd:PHA02878   63 VNQPDHRDLTPLHIICKEPNkLGMKEMIRSINKCSVFYTLVAIKDAfnnrnveifkiILTNRYKNIQTIDLVyidkkskd 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822091  886 ----AVVWKLLRE--GNVNIQATQGGQTALMLGVSHDREDMVQALLSCKADVNLQDHDGSSALMLACHQGNADLVRLLLA 959
Cdd:PHA02878  143 diieAEITKLLLSygADINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLE 222

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 157822091  960 HAdCNSNLTDKAGQTALSIVLNSPAHVEIAELLRAH 995
Cdd:PHA02878  223 NG-ASTDARDKCGNTPLHISVGYCKDYDILKLLLEH 257
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
338-428 4.48e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.05  E-value: 4.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822091  338 VETATSSISSLKSQVLDLE---DKLSGRTEELAQVRAALEQQEEETKAREQRIQELECTVAHLEEKlsQEKASDALDRTD 414
Cdd:COG4913   663 VASAEREIAELEAELERLDassDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEE--LDELQDRLEAAE 740

                          90
                  ....*....|....
gi 157822091  415 AMVNTDPLRELIPR 428
Cdd:COG4913   741 DLARLELRALLEER 754
Ank_5 pfam13857
Ankyrin repeats (many copies);
824-871 4.71e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.17  E-value: 4.71e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 157822091   824 LLVNLADRSGNTALHYSVSHSNFAIAKLLLDTGV-CNVdhQNKAGYTAV 871
Cdd:pfam13857    7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVdLNL--KDEEGLTAL 53
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 905-932 5.61e-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: 35.31  E-value: 5.61e-03
                           10        20
                   ....*....|....*....|....*...
gi 157822091   905 GQTALMLGVSHDREDMVQALLSCKADVN 932
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADIN 29
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 333-432 6.17e-03

chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 40.82  E-value: 6.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822091   333 ESLGLVETATSSISSLKSQVLDLEDKLSGRTEELAQVRAALEQQEEETKAREQRIQELECTVAHLEEKLSQEKAsdALDR 412
Cdd:TIGR02169  706 ELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEE--ALND 783

                           90       100
                   ....*....|....*....|
gi 157822091   413 TDAMVNTDPLRElIPRESQD 432
Cdd:TIGR02169  784 LEARLSHSRIPE-IQAELSK 802
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 937-970 9.41e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 34.96  E-value: 9.41e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 157822091   937 DGSSALMLAC-HQGNADLVRLLLAHaDCNSNLTDK 970
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSK-GADVNARDK 34
 
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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