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Conserved domains on  [gi|359338997|ref|NP_001008650|]
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putative palmitoyltransferase ZDHHC13 [Danio rerio]

Protein Classification

ankyrin repeat domain-containing DHHC palmitoyltransferase family protein( domain architecture ID 12790884)

DHHC family palmitoyltransferase may catalyze the addition of palmitate onto various protein substrates and be involved in a variety of cellular processes; contains N-terminal ankyrin repeats;

EC:  2.3.1.-
Gene Ontology:  GO:0043543|GO:0016747
PubMed:  21388813

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
75-292 1.25e-39

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 147.02  E-value: 1.25e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359338997  75 DIIKATQFGALERCKELVEAGYDVRQPDKENVTLLHWAAINNRADIVKYYISKGAVIDQLGGDLNsTPLHWAIRQGHLSM 154
Cdd:COG0666   24 LLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGN-TLLHAAARNGDLEI 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359338997 155 VIQLMRYGADPSLADGEGYRGLHLAVLFQNMPIAAYLMAKGQEVDLPDLNGQTPLMLAAQK----IIgpeptNFLIKCNA 230
Cdd:COG0666  103 VKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANgnleIV-----KLLLEAGA 177

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 359338997 231 SVNAVDKvNRNSPLHCAVLAGNVDSVHILLEAGASVDMQNDNGHTAIDLAQQVHSPLLIHML 292
Cdd:COG0666  178 DVNARDN-DGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLL 238
DHHC pfam01529
DHHC palmitoyltransferase; This entry refers to the DHHC domain, found in DHHC proteins which ...
 450-580 2.45e-33

DHHC palmitoyltransferase; This entry refers to the DHHC domain, found in DHHC proteins which are palmitoyltransferases. Palmitoylation or, more specifically S-acylation, plays important roles in the regulation of protein localization, stability, and activity. It is a post-translational protein modification that involves the attachment of palmitic acid to Cys residues through a thioester linkage. Protein acyltransferases (PATs), also known as palmitoyltransferases, catalyze this reaction by transferring the palmitoyl group from palmitoyl-CoA to the thiol group of Cys residues. They are characterized by the presence of a 50-residue-long domain called the DHHC domain, which in most but not all cases is also cysteine-rich and gets its name from a highly conserved DHHC signature tetrapeptide (Asp-His-His-Cys). The Cys residue within the DHHC domain forms a stable acyl intermediate and transfers the acyl chain to the Cys residues of a target protein. Some proteins containing a DHHC domain include Drosophila DNZ1 protein, Mouse Abl-philin 2 (Aph2) protein, Mammalian ZDHHC9, Yeast ankyrin repeat-containing protein AKR1, Yeast Erf2 protein, and Arabidopsis thaliana tip growth defective 1.


:

Pssm-ID: 396215  Cd Length: 132  Bit Score: 124.40  E-value: 2.45e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359338997  450 FCTSCMMRKPMRANHCFSCNACVAKQDHHSIWINGCIGARNHPFFVLFLVALNFLCIWMFYGSITYWSRHCPLHYSEEGI 529
Cdd:pfam01529   7 YCSTCNIYKPPRSKHCRVCNRCVLRFDHHCPWLNNCIGKRNHKYFILFLLYLTLYLILYLVLSLYYLVKLIESSTLFFFL 86

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 359338997  530 WGALTAlmgcspWLLYVFCFVFFHTTWASILLVLQLYQIaFLGLTTSERAN 580
Cdd:pfam01529  87 ILFLFS------ISIILLILSLFFLLFLGILLFFHLYLI-SRNLTTYEFMK 130
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
75-292 1.25e-39

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 147.02  E-value: 1.25e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359338997  75 DIIKATQFGALERCKELVEAGYDVRQPDKENVTLLHWAAINNRADIVKYYISKGAVIDQLGGDLNsTPLHWAIRQGHLSM 154
Cdd:COG0666   24 LLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGN-TLLHAAARNGDLEI 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359338997 155 VIQLMRYGADPSLADGEGYRGLHLAVLFQNMPIAAYLMAKGQEVDLPDLNGQTPLMLAAQK----IIgpeptNFLIKCNA 230
Cdd:COG0666  103 VKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANgnleIV-----KLLLEAGA 177

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 359338997 231 SVNAVDKvNRNSPLHCAVLAGNVDSVHILLEAGASVDMQNDNGHTAIDLAQQVHSPLLIHML 292
Cdd:COG0666  178 DVNARDN-DGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLL 238
DHHC pfam01529
DHHC palmitoyltransferase; This entry refers to the DHHC domain, found in DHHC proteins which ...
 450-580 2.45e-33

DHHC palmitoyltransferase; This entry refers to the DHHC domain, found in DHHC proteins which are palmitoyltransferases. Palmitoylation or, more specifically S-acylation, plays important roles in the regulation of protein localization, stability, and activity. It is a post-translational protein modification that involves the attachment of palmitic acid to Cys residues through a thioester linkage. Protein acyltransferases (PATs), also known as palmitoyltransferases, catalyze this reaction by transferring the palmitoyl group from palmitoyl-CoA to the thiol group of Cys residues. They are characterized by the presence of a 50-residue-long domain called the DHHC domain, which in most but not all cases is also cysteine-rich and gets its name from a highly conserved DHHC signature tetrapeptide (Asp-His-His-Cys). The Cys residue within the DHHC domain forms a stable acyl intermediate and transfers the acyl chain to the Cys residues of a target protein. Some proteins containing a DHHC domain include Drosophila DNZ1 protein, Mouse Abl-philin 2 (Aph2) protein, Mammalian ZDHHC9, Yeast ankyrin repeat-containing protein AKR1, Yeast Erf2 protein, and Arabidopsis thaliana tip growth defective 1.


Pssm-ID: 396215  Cd Length: 132  Bit Score: 124.40  E-value: 2.45e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359338997  450 FCTSCMMRKPMRANHCFSCNACVAKQDHHSIWINGCIGARNHPFFVLFLVALNFLCIWMFYGSITYWSRHCPLHYSEEGI 529
Cdd:pfam01529   7 YCSTCNIYKPPRSKHCRVCNRCVLRFDHHCPWLNNCIGKRNHKYFILFLLYLTLYLILYLVLSLYYLVKLIESSTLFFFL 86

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 359338997  530 WGALTAlmgcspWLLYVFCFVFFHTTWASILLVLQLYQIaFLGLTTSERAN 580
Cdd:pfam01529  87 ILFLFS------ISIILLILSLFFLLFLGILLFFHLYLI-SRNLTTYEFMK 130
COG5273 COG5273
Uncharacterized protein containing DHHC-type Zn finger [General function prediction only];
379-568 8.63e-26

Uncharacterized protein containing DHHC-type Zn finger [General function prediction only];


Pssm-ID: 227598 [Multi-domain]  Cd Length: 309  Bit Score: 108.30  E-value: 8.63e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359338997 379 VFWMVVTWVLW----------FLPDEPSAAVQMLFTVNITAVLYYyiRSCRTDPGHV--KATEEEKKKNIVVLAEAGCLD 446
Cdd:COG5273   30 MFIGLFLLSRIvvytllvivkSLSLVVLFIILFIVILVLASFSYL--LLLVSDPGYLgeNITLSGYRETISRLLDDGKFG 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359338997 447 PRIFCTSCMMRKPMRANHCFSCNACVAKQDHHSIWINGCIGARNHPFFVLFLVALNFLCIWMF-----YGSITYWSRHCP 521
Cdd:COG5273  108 TENFCSTCNIYKPPRSHHCSICNRCVLKFDHHCPWINNCVGFRNYRFFYQFLLYTILVALVVLlstayYIAGIFSIRHDT 187

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 359338997 522 LHYSEEGIWGalTALMGCSPWlLYVFCFVFFHT-TWASILLVLQLYQI 568
Cdd:COG5273  188 SLAICFLIFG--CSLLGVVFF-IITTLLLLFLIyLILNNLTTIEFIQI 232
Ank_2 pfam12796
Ankyrin repeats (3 copies);
76-169 9.06e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 78.62  E-value: 9.06e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359338997   76 IIKATQFGALERCKELVEAGYDVRQPDKENVTLLHWAAINNRADIVKYYISKGAVIDQLGGDlnsTPLHWAIRQGHLSMV 155
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGR---TALHYAARSGHLEIV 77

                          90
                  ....*....|....
gi 359338997  156 IQLMRYGADPSLAD 169
Cdd:pfam12796  78 KLLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 115-312 3.49e-15

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 78.53  E-value: 3.49e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359338997 115 NNRADIVKYYISKGAVIDQLGGdLNSTPLHWAIRQGH---LSMVIQLMRYGADPSLADGEGYRGLHLAVLFQN-MPIAAY 190
Cdd:PHA03095  24 NVTVEEVRRLLAAGADVNFRGE-YGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKL 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359338997 191 LMAKGQEVDLPDLNGQTPLML-AAQKIIGPEPTNFLIKCNASVNAVDKVNRNsPLHCAVLAGNVD--SVHILLEAGASVD 267
Cdd:PHA03095 103 LIKAGADVNAKDKVGRTPLHVyLSGFNINPKVIRLLLRKGADVNALDLYGMT-PLAVLLKSRNANveLLRLLIDAGADVY 181

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 359338997 268 MQNDNGHTAIDlaqqvhspllIHMLSvvkterIKANSACLKLLNR 312
Cdd:PHA03095 182 AVDDRFRSLLH----------HHLQS------FKPRARIVRELIR 210
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 141-167 4.13e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.95  E-value: 4.13e-04
                           10        20
                   ....*....|....*....|....*..
gi 359338997   141 TPLHWAIRQGHLSMVIQLMRYGADPSL 167
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
75-292 1.25e-39

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 147.02  E-value: 1.25e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359338997  75 DIIKATQFGALERCKELVEAGYDVRQPDKENVTLLHWAAINNRADIVKYYISKGAVIDQLGGDLNsTPLHWAIRQGHLSM 154
Cdd:COG0666   24 LLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGN-TLLHAAARNGDLEI 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359338997 155 VIQLMRYGADPSLADGEGYRGLHLAVLFQNMPIAAYLMAKGQEVDLPDLNGQTPLMLAAQK----IIgpeptNFLIKCNA 230
Cdd:COG0666  103 VKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANgnleIV-----KLLLEAGA 177

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 359338997 231 SVNAVDKvNRNSPLHCAVLAGNVDSVHILLEAGASVDMQNDNGHTAIDLAQQVHSPLLIHML 292
Cdd:COG0666  178 DVNARDN-DGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLL 238
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
75-310 2.54e-37

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 140.86  E-value: 2.54e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359338997  75 DIIKATQFGALERCKELVEAGYDVRQPDKENVTLLHWAAINNRADIVKYYISKGAVIDQLGGDLNsTPLHWAIRQGHLSM 154
Cdd:COG0666   57 LLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGE-TPLHLAAYNGNLEI 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359338997 155 VIQLMRYGADPSLADGEGYRGLHLAVLFQNMPIAAYLMAKGQEVDLPDLNGQTPLMLAAQK----IIgpeptNFLIKCNA 230
Cdd:COG0666  136 VKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENghleIV-----KLLLEAGA 210

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359338997 231 SVNAVDKvNRNSPLHCAVLAGNVDSVHILLEAGASVDMQNDNGHTAIDLAQQVHSPLLIHMLSVVKTERIKANSACLKLL 310
Cdd:COG0666  211 DVNAKDN-DGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
DHHC pfam01529
DHHC palmitoyltransferase; This entry refers to the DHHC domain, found in DHHC proteins which ...
 450-580 2.45e-33

DHHC palmitoyltransferase; This entry refers to the DHHC domain, found in DHHC proteins which are palmitoyltransferases. Palmitoylation or, more specifically S-acylation, plays important roles in the regulation of protein localization, stability, and activity. It is a post-translational protein modification that involves the attachment of palmitic acid to Cys residues through a thioester linkage. Protein acyltransferases (PATs), also known as palmitoyltransferases, catalyze this reaction by transferring the palmitoyl group from palmitoyl-CoA to the thiol group of Cys residues. They are characterized by the presence of a 50-residue-long domain called the DHHC domain, which in most but not all cases is also cysteine-rich and gets its name from a highly conserved DHHC signature tetrapeptide (Asp-His-His-Cys). The Cys residue within the DHHC domain forms a stable acyl intermediate and transfers the acyl chain to the Cys residues of a target protein. Some proteins containing a DHHC domain include Drosophila DNZ1 protein, Mouse Abl-philin 2 (Aph2) protein, Mammalian ZDHHC9, Yeast ankyrin repeat-containing protein AKR1, Yeast Erf2 protein, and Arabidopsis thaliana tip growth defective 1.


Pssm-ID: 396215  Cd Length: 132  Bit Score: 124.40  E-value: 2.45e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359338997  450 FCTSCMMRKPMRANHCFSCNACVAKQDHHSIWINGCIGARNHPFFVLFLVALNFLCIWMFYGSITYWSRHCPLHYSEEGI 529
Cdd:pfam01529   7 YCSTCNIYKPPRSKHCRVCNRCVLRFDHHCPWLNNCIGKRNHKYFILFLLYLTLYLILYLVLSLYYLVKLIESSTLFFFL 86

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 359338997  530 WGALTAlmgcspWLLYVFCFVFFHTTWASILLVLQLYQIaFLGLTTSERAN 580
Cdd:pfam01529  87 ILFLFS------ISIILLILSLFFLLFLGILLFFHLYLI-SRNLTTYEFMK 130
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
102-280 7.59e-28

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 113.90  E-value: 7.59e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359338997 102 DKENVTLLHWAAINNRADIVKYYISKGAVIDQLGGDLNSTPLHWAIRQGHLSMVIQLMRYGADPSLADGEGYRGLHLAVL 181
Cdd:COG0666   17 LLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAAR 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359338997 182 FQNMPIAAYLMAKGQEVDLPDLNGQTPLMLAAQ----KIIgpeptNFLIKCNASVNAVDKvNRNSPLHCAVLAGNVDSVH 257
Cdd:COG0666   97 NGDLEIVKLLLEAGADVNARDKDGETPLHLAAYngnlEIV-----KLLLEAGADVNAQDN-DGNTPLHLAAANGNLEIVK 170

                        170       180
                 ....*....|....*....|...
gi 359338997 258 ILLEAGASVDMQNDNGHTAIDLA 280
Cdd:COG0666  171 LLLEAGADVNARDNDGETPLHLA 193
COG5273 COG5273
Uncharacterized protein containing DHHC-type Zn finger [General function prediction only];
379-568 8.63e-26

Uncharacterized protein containing DHHC-type Zn finger [General function prediction only];


Pssm-ID: 227598 [Multi-domain]  Cd Length: 309  Bit Score: 108.30  E-value: 8.63e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359338997 379 VFWMVVTWVLW----------FLPDEPSAAVQMLFTVNITAVLYYyiRSCRTDPGHV--KATEEEKKKNIVVLAEAGCLD 446
Cdd:COG5273   30 MFIGLFLLSRIvvytllvivkSLSLVVLFIILFIVILVLASFSYL--LLLVSDPGYLgeNITLSGYRETISRLLDDGKFG 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359338997 447 PRIFCTSCMMRKPMRANHCFSCNACVAKQDHHSIWINGCIGARNHPFFVLFLVALNFLCIWMF-----YGSITYWSRHCP 521
Cdd:COG5273  108 TENFCSTCNIYKPPRSHHCSICNRCVLKFDHHCPWINNCVGFRNYRFFYQFLLYTILVALVVLlstayYIAGIFSIRHDT 187

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 359338997 522 LHYSEEGIWGalTALMGCSPWlLYVFCFVFFHT-TWASILLVLQLYQI 568
Cdd:COG5273  188 SLAICFLIFG--CSLLGVVFF-IITTLLLLFLIyLILNNLTTIEFIQI 232
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
119-280 6.61e-18

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 84.62  E-value: 6.61e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359338997 119 DIVKYYISKGAVIDQLGGDLNSTPLHWAIRQGHLSMVIQLMRYGADPSLADGEGYRGLHLAVLFQNMPIAAYLMAKGQEV 198
Cdd:COG0666    1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359338997 199 DLPDLNGQTPLMLAAQK----IIgpeptNFLIKCNASVNAVDKvNRNSPLHCAVLAGNVDSVHILLEAGASVDMQNDNGH 274
Cdd:COG0666   81 NAKDDGGNTLLHAAARNgdleIV-----KLLLEAGADVNARDK-DGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGN 154


                 ....*.
gi 359338997 275 TAIDLA 280
Cdd:COG0666  155 TPLHLA 160
Ank_2 pfam12796
Ankyrin repeats (3 copies);
76-169 9.06e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 78.62  E-value: 9.06e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359338997   76 IIKATQFGALERCKELVEAGYDVRQPDKENVTLLHWAAINNRADIVKYYISKGAVIDQLGGDlnsTPLHWAIRQGHLSMV 155
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGR---TALHYAARSGHLEIV 77

                          90
                  ....*....|....
gi 359338997  156 IQLMRYGADPSLAD 169
Cdd:pfam12796  78 KLLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 115-312 3.49e-15

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 78.53  E-value: 3.49e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359338997 115 NNRADIVKYYISKGAVIDQLGGdLNSTPLHWAIRQGH---LSMVIQLMRYGADPSLADGEGYRGLHLAVLFQN-MPIAAY 190
Cdd:PHA03095  24 NVTVEEVRRLLAAGADVNFRGE-YGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKL 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359338997 191 LMAKGQEVDLPDLNGQTPLML-AAQKIIGPEPTNFLIKCNASVNAVDKVNRNsPLHCAVLAGNVD--SVHILLEAGASVD 267
Cdd:PHA03095 103 LIKAGADVNAKDKVGRTPLHVyLSGFNINPKVIRLLLRKGADVNALDLYGMT-PLAVLLKSRNANveLLRLLIDAGADVY 181

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 359338997 268 MQNDNGHTAIDlaqqvhspllIHMLSvvkterIKANSACLKLLNR 312
Cdd:PHA03095 182 AVDDRFRSLLH----------HHLQS------FKPRARIVRELIR 210
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 102-280 1.68e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 75.86  E-value: 1.68e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359338997 102 DKENVTLLHWAAINNRADIVKYYISKGAVIDQlGGDLNSTPLHWAIRQGH-----LSMVIQLMRYGADPSLADGEGYRGL 176
Cdd:PHA03100  32 YKKPVLPLYLAKEARNIDVVKILLDNGADINS-STKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGANVNAPDNNGITPL 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359338997 177 HLAV--LFQNMPIAAYLMAKGQEVDLPDLNGQTPLMLAAQ------KIIgpeptNFLIKCNASVNAVDKVNR-------- 240
Cdd:PHA03100 111 LYAIskKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLEsnkidlKIL-----KLLIDKGVDINAKNRVNYllsygvpi 185

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 359338997 241 -------NSPLHCAVLAGNVDSVHILLEAGASVDMQNDNGHTAIDLA 280
Cdd:PHA03100 186 nikdvygFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIA 232
Ank_2 pfam12796
Ankyrin repeats (3 copies);
176-270 3.11e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 68.60  E-value: 3.11e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359338997  176 LHLAVLFQNMPIAAYLMAKGQEVDLPDLNGQTPLMLAAQKiiG-PEPTNFLIKcNASVNAVDkvNRNSPLHCAVLAGNVD 254
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKN--GhLEIVKLLLE-HADVNLKD--NGRTALHYAARSGHLE 75

                          90
                  ....*....|....*.
gi 359338997  255 SVHILLEAGASVDMQN 270
Cdd:pfam12796  76 IVKLLLEKGADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 86-336 1.28e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 73.46  E-value: 1.28e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359338997  86 ERCKELVEAGYDVRQPDKENVTLLHWAAINNRADIVKYYISKGAVIDqLGGDLNSTPLHWAIRQGHLSMVIQLMRYGADP 165
Cdd:PHA02874 105 DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVN-IEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYA 183

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359338997 166 SLADGEGYRGLHLAVLFQNMPIAAYLMAKGQEVDLPDLNGQTPLMLAaqkIIGPEPTNFLIKCNASVNAVDkVNRNSPLH 245
Cdd:PHA02874 184 NVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNA---IIHNRSAIELLINNASINDQD-IDGSTPLH 259

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359338997 246 CAV-LAGNVDSVHILLEAGASVDMQNDNGHTAIDLAQQvhsplLIHMLSVVKteRIKANSACLK---------LLNRYKV 315
Cdd:PHA02874 260 HAInPPCDIDIIDILLYHKADISIKDNKGENPIDTAFK-----YINKDPVIK--DIIANAVLIKeadklkdsdFLEHIEI 332

                        250       260
                 ....*....|....*....|.
gi 359338997 316 CLQSVFSVVVVGAFGAILDMR 336
Cdd:PHA02874 333 KDNKEFSDFIKECNEEIEDMK 353
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 118-362 2.72e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 72.61  E-value: 2.72e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359338997 118 ADIVKYYISKGAVIDQLGGDLNSTPLHWAIRQGHLSMVIQLMRYGADPSLADGEGYRGLHLAVLFQNMPIAAYLMAKGQE 197
Cdd:PHA02878 147 AEITKLLLSYGADINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAS 226

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359338997 198 VDLPDLNGQTPLMLAAQKIIGPEPTNFLIKCNASVNAVDKVNRNSPLHCAVlaGNVDSVHILLEAGASVDMQNDNGHTAI 277
Cdd:PHA02878 227 TDARDKCGNTPLHISVGYCKDYDILKLLLEHGVDVNAKSYILGLTALHSSI--KSERKLKLLLEYGADINSLNSYKLTPL 304

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359338997 278 DlaqqvhspllihmlSVVKTErikansACLKLLNR--YKVCLQSVFSVVVVGAFGAILDMR--TESWLLKGILLACIMAV 353
Cdd:PHA02878 305 S--------------SAVKQY------LCINIGRIliSNICLLKRIKPDIKNSEGFIDNMDciTSNKRLNQIKDKCEDEL 364


                 ....*....
gi 359338997 354 INLASRQLA 362
Cdd:PHA02878 365 NRLASIKIT 373
Ank_2 pfam12796
Ankyrin repeats (3 copies);
143-236 1.67e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 63.60  E-value: 1.67e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359338997  143 LHWAIRQGHLSMVIQLMRYGADPSLADGEGYRGLHLAVLFQNMPIAAYLMAKGQeVDLPDlNGQTPLMLAAQKiiGPEPT 222
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD-VNLKD-NGRTALHYAARS--GHLEI 76

                          90
                  ....*....|....*
gi 359338997  223 -NFLIKCNASVNAVD 236
Cdd:pfam12796  77 vKLLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 91-280 9.53e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 64.28  E-value: 9.53e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359338997  91 LVEAGYDVRQPDKENVTLLHWAAIN-NRADIVKYYISKGAVIDQlGGDLNSTPLHwairqGHLS-------MVIQLMRYG 162
Cdd:PHA03095  69 LLEAGADVNAPERCGFTPLHLYLYNaTTLDVIKLLIKAGADVNA-KDKVGRTPLH-----VYLSgfninpkVIRLLLRKG 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359338997 163 ADPSLADGEGYRGLHLAVLFQNMPIA--AYLMAKGQEVDLPDLNGQTPLMLAAQKIiGPEPTNF--LIKCNASVNAVDkV 238
Cdd:PHA03095 143 ADVNALDLYGMTPLAVLLKSRNANVEllRLLIDAGADVYAVDDRFRSLLHHHLQSF-KPRARIVreLIRAGCDPAATD-M 220

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 359338997 239 NRNSPLHCAVLAGNVDSVHI--LLEAGASVDMQNDNGHTAIDLA 280
Cdd:PHA03095 221 LGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYA 264
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 89-273 1.75e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 63.75  E-value: 1.75e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359338997  89 KELVEAGYDVRQPDKENV-TLLHWAAINNRADIVKYYISKGAVIDQLgGDLNSTPLHWAIRQGHLSMVIQLMRYGADPSL 167
Cdd:PHA02878 151 KLLLSYGADINMKDRHKGnTALHYATENKDQRLTELLLSYGANVNIP-DKTNNSPLHHAVKHYNKPIVHILLENGASTDA 229

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359338997 168 ADGEGYRGLHLAVLF-QNMPIAAYLMAKGQEVDLPD-LNGQTPLMLAaqkIIGPEPTNFLIKCNASVNAVDkVNRNSPLH 245
Cdd:PHA02878 230 RDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSyILGLTALHSS---IKSERKLKLLLEYGADINSLN-SYKLTPLS 305

                        170       180       190
                 ....*....|....*....|....*....|....
gi 359338997 246 CAVLA------GNVDSVHILLEAGASVDMQNDNG 273
Cdd:PHA02878 306 SAVKQylciniGRILISNICLLKRIKPDIKNSEG 339
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 79-292 4.04e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 62.77  E-value: 4.04e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359338997  79 ATQFGALERCKELVEAGYDVRQPDKENVTLLHWAAINNRADIVKYYISKGAVIDQlggdlNSTPLHWAIRQGHLSMviQL 158
Cdd:PHA02876 185 AAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINK-----NDLSLLKAIRNEDLET--SL 257

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359338997 159 MRYGADPSLADGEGYRG--LHLAVLFQNMP-IAAYLMAKGQEVDLPDLNGQTPLMLAAQKIIGPEPTNFLIKCNASVNAV 235
Cdd:PHA02876 258 LLYDAGFSVNSIDDCKNtpLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYLMAKNGYDTENIRTLIMLGADVNAA 337

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 359338997 236 DKVnRNSPLHCA-VLAGNVDSVHILLEAGASVDMQNDNGHTAIDLAQQVHSPLLIHML 292
Cdd:PHA02876 338 DRL-YITPLHQAsTLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTL 394
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 97-279 6.57e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 61.55  E-value: 6.57e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359338997  97 DVRQPDKEnvTLLHWAAINNRADIVKYYISKGAVIDQLGGDLNSTPLHWAIRQGHLSMVIQLMRYGADPSLADGEGYRGL 176
Cdd:PHA02875  62 DVKYPDIE--SELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPL 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359338997 177 HLAVLFQNMPIAAYLMAKGQEVDLPDLNGQTPLMLAAQKiIGPEPTNFLIKCNASVNAVDKvNRNSPLHCAVLAGN-VDS 255
Cdd:PHA02875 140 HLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAK-GDIAICKMLLDSGANIDYFGK-NGCVAALCYAIENNkIDI 217

                        170       180
                 ....*....|....*....|....*..
gi 359338997 256 VHILLEAGAS---VDMQNDNGHTAIDL 279
Cdd:PHA02875 218 VRLFIKRGADcniMFMIEGEECTILDM 244
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 79-256 9.97e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 61.13  E-value: 9.97e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359338997  79 ATQFGALERCKELVEAGYDVRQPDKENVTLLHWAAINNRADIVKYYISKGAVIDQLGGDLNsTPLHWAIRQGHLSMVIQL 158
Cdd:PHA02874 131 AIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGE-SPLHNAAEYGDYACIKLL 209

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359338997 159 MRYGADPSLADGEGYRGLHLAVLFQNMPIAayLMAKGQEVDLPDLNGQTPLMLAAQKIIGPEPTNFLIKCNASVNAVDKV 238
Cdd:PHA02874 210 IDHGNHIMNKCKNGFTPLHNAIIHNRSAIE--LLINNASINDQDIDGSTPLHHAINPPCDIDIIDILLYHKADISIKDNK 287

                        170
                 ....*....|....*...
gi 359338997 239 NRNsPLHCAVLAGNVDSV 256
Cdd:PHA02874 288 GEN-PIDTAFKYINKDPV 304
PHA03095 PHA03095
ankyrin-like protein; Provisional
 91-256 2.31e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 56.96  E-value: 2.31e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359338997  91 LVEAGYDVRQPDKENVTLLHWAAINNRADI--VKYYISKGAviDQLGGDLN-STPLHWairqgHL-------SMVIQLMR 160
Cdd:PHA03095 138 LLRKGADVNALDLYGMTPLAVLLKSRNANVelLRLLIDAGA--DVYAVDDRfRSLLHH-----HLqsfkpraRIVRELIR 210

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359338997 161 YGADPSLADGEGYRGLHLAVLFQNM--PIAAYLMAKGQEVDLPDLNGQTPLMLAAqKIIGPEPTNFLIKCNASVNAVDKv 238
Cdd:PHA03095 211 AGCDPAATDMLGNTPLHSMATGSSCkrSLVLPLLIAGISINARNRYGQTPLHYAA-VFNNPRACRRLIALGADINAVSS- 288

                        170
                 ....*....|....*...
gi 359338997 239 NRNSPLHCAVLAGNVDSV 256
Cdd:PHA03095 289 DGNTPLSLMVRNNNGRAV 306
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 135-279 3.91e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 56.61  E-value: 3.91e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359338997 135 GGDLNS------TPLHWAIRQGHLSMVIQLMRYGADPSLADGEGYRGLHLAVLFQNMPIAAYLMAKGQEVDLPDLNgqtp 208
Cdd:PHA02876 168 GADVNAkdiyciTPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKNDLS---- 243

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 359338997 209 lMLAAQKIIGPEPTNFLIKCNASVNAVDkVNRNSPLHCAVLAGNVDS-VHILLEAGASVDMQNDNGHTAIDL 279
Cdd:PHA02876 244 -LLKAIRNEDLETSLLLYDAGFSVNSID-DCKNTPLHHASQAPSLSRlVPKLLERGADVNAKNIKGETPLYL 313
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 91-237 9.24e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 54.67  E-value: 9.24e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359338997  91 LVEAGYDVRQPDKENVTLLHWAAIN--NRADIVKYYISKGAVIDQLGGDlNSTPLHWAIRQGH--LSMV---IQ------ 157
Cdd:PHA03100  92 LLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSD-GENLLHLYLESNKidLKILkllIDkgvdin 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359338997 158 -------LMRYGADPSLADGEGYRGLHLAVLFQNMPIAAYLMAKGQEVDLPDLNGQTPLMLAAQKIIgPEPTNFLIKCNA 230
Cdd:PHA03100 171 aknrvnyLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNN-KEIFKLLLNNGP 249


                 ....*..
gi 359338997 231 SVNAVDK 237
Cdd:PHA03100 250 SIKTIIE 256
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 141-291 1.43e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 51.15  E-value: 1.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359338997 141 TPLHWAIRQGHLSMVIQLMRYGADPSLADGEGYRGLHLAVLFQNMPIAAYLMAKGQEVDlpDL---NGQTPLMLA--AQK 215
Cdd:PHA02875  37 SPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFAD--DVfykDGMTPLHLAtiLKK 114

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 359338997 216 IigpEPTNFLIKCNASVNaVDKVNRNSPLHCAVLAGNVDSVHILLEAGASVDMQNDNGHTaidlaqqvhsPLLIHM 291
Cdd:PHA02875 115 L---DIMKLLIARGADPD-IPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCT----------PLIIAM 176
Ank_4 pfam13637
Ankyrin repeats (many copies);
105-155 2.37e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.96  E-value: 2.37e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 359338997  105 NVTLLHWAAINNRADIVKYYISKGAVIDQLGGDLNsTPLHWAIRQGHLSMV 155
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGE-TALHFAASNGNVEVL 50
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 146-309 5.89e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 49.22  E-value: 5.89e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359338997 146 AIRQGHLSMVIQLMRYGADPSLADGEGYRGLHLAVLFQNMPIAAYLMAKGQ--EVDLPDLngQTPLMLAAQ--KIIGPEp 221
Cdd:PHA02875   9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAipDVKYPDI--ESELHDAVEegDVKAVE- 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359338997 222 tnFLIKCNASVNAVDKVNRNSPLHCAVLAGNVDSVHILLEAGASVDMQNDNGHTAIDLAqqvhspllIHMLSVVKTERIK 301
Cdd:PHA02875  86 --ELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLA--------VMMGDIKGIELLI 155


                 ....*...
gi 359338997 302 ANSACLKL 309
Cdd:PHA02875 156 DHKACLDI 163
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 137-292 6.03e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 49.19  E-value: 6.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359338997 137 DLNSTPLHWAIRQGHLSMVIQLMRYGADPSLADGEGYRGLHLAVLFQNMPIAAYLMAKGQEVDL---PDLNGQTplmlaa 213
Cdd:PHA02874  33 DETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSIlpiPCIEKDM------ 106

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 359338997 214 qkiigpepTNFLIKCNASVNAVDKVNRnSPLHCAVLAGNVDSVHILLEAGASVDMQNDNGHTAIDLAQQVHSPLLIHML 292
Cdd:PHA02874 107 --------IKTILDCGIDVNIKDAELK-TFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLL 176
Ank_4 pfam13637
Ankyrin repeats (many copies);
240-280 1.52e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 42.65  E-value: 1.52e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 359338997  240 RNSPLHCAVLAGNVDSVHILLEAGASVDMQNDNGHTAIDLA 280
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFA 41
Ank_5 pfam13857
Ankyrin repeats (many copies);
225-280 3.14e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.95  E-value: 3.14e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 359338997  225 LIKC-NASVNAVDKvNRNSPLHCAVLAGNVDSVHILLEAGASVDMQNDNGHTAIDLA 280
Cdd:pfam13857   1 LLEHgPIDLNRLDG-EGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 84-164 3.21e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 46.58  E-value: 3.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359338997  84 ALERCKELVEAGYDVRQPDKENVTLLHWAAINNRADIVKYYISKGAVIDqLGGDLNSTPLHWAIRQGHLSMVIQLMRYGA 163
Cdd:PHA03100 171 AKNRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPN-LVNKYGDTPLHIAILNNNKEIFKLLLNNGP 249


                 .
gi 359338997 164 D 164
Cdd:PHA03100 250 S 250
Ank_4 pfam13637
Ankyrin repeats (many copies);
139-191 6.12e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.11  E-value: 6.12e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 359338997  139 NSTPLHWAIRQGHLSMVIQLMRYGADPSLADGEGYRGLHLAVLFQNMPIAAYL 191
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 85-184 6.85e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 45.81  E-value: 6.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359338997  85 LERCKELVEAGYDVrqpdkenvtllhwaainNRADIVKYYISKGAVIDQLggDLN-STPLHWAIRQGHLSMVIQLMRYGA 163
Cdd:PHA03100 156 LKILKLLIDKGVDI-----------------NAKNRVNYLLSYGVPINIK--DVYgFTPLHYAVYNNNPEFVKYLLDLGA 216

                         90       100
                 ....*....|....*....|.
gi 359338997 164 DPSLADGEGYRGLHLAVLFQN 184
Cdd:PHA03100 217 NPNLVNKYGDTPLHIAILNNN 237
Ank_5 pfam13857
Ankyrin repeats (many copies);
124-179 9.25e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.41  E-value: 9.25e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 359338997  124 YISKGAVIDQLGGDLNSTPLHWAIRQGHLSMVIQLMRYGADPSLADGEGYRGLHLA 179
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 135-180 1.34e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.89  E-value: 1.34e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 359338997 135 GGDLNS------TPLHWAIRQGHLSMVIQLMRYGADPSLADGEGYRGLHLAV 180
Cdd:PTZ00322 105 GADPNCrdydgrTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAE 156
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 81-266 2.09e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 44.28  E-value: 2.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359338997  81 QFGALERCKE----LVEAGYDVRQPDKENVTLLHWAAINNRADIVKYYISKGAVIDQLGGDLnSTPLHWAIrqghlsmvi 156
Cdd:PHA02876 347 QASTLDRNKDivitLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKI-GTALHFAL--------- 416

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359338997 157 qlmrYGADPSLAdgegyrglhlavlfqnmpiAAYLMAKGQEVDLPDLNGQTPLMLAAQKIIGPEPTNFLIKCNASVNAVD 236
Cdd:PHA02876 417 ----CGTNPYMS-------------------VKTLIDRGANVNSKNKDLSTPLHYACKKNCKLDVIEMLLDNGADVNAIN 473

                        170       180       190
                 ....*....|....*....|....*....|
gi 359338997 237 KVNRnSPLHCAVlaGNVDSVHILLEAGASV 266
Cdd:PHA02876 474 IQNQ-YPLLIAL--EYHGIVNILLHYGAEL 500
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 239-271 3.99e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 38.04  E-value: 3.99e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 359338997  239 NRNSPLHCAVL-AGNVDSVHILLEAGASVDMQND 271
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 141-167 4.13e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.95  E-value: 4.13e-04
                           10        20
                   ....*....|....*....|....*..
gi 359338997   141 TPLHWAIRQGHLSMVIQLMRYGADPSL 167
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 239-268 4.34e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.95  E-value: 4.34e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 359338997   239 NRNSPLHCAVLAGNVDSVHILLEAGASVDM 268
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_2 pfam12796
Ankyrin repeats (3 copies);
244-277 8.16e-04

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 38.94  E-value: 8.16e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 359338997  244 LHCAVLAGNVDSVHILLEAGASVDMQNDNGHTAI 277
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTAL 34
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 141-169 2.08e-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: 36.11  E-value: 2.08e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 359338997  141 TPLHWAI-RQGHLSMVIQLMRYGADPSLAD 169
Cdd:pfam00023   4 TPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
PHA02798 PHA02798
ankyrin-like protein; Provisional
 84-285 2.80e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 40.59  E-value: 2.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359338997  84 ALERCKELVEAGYDVRQPDKENVT----LLHWAAINNRaDIVKYYISKGAVIDQLGGDlNSTPLHWAIRQGH---LSMVI 156
Cdd:PHA02798  88 MLDIVKILIENGADINKKNSDGETplycLLSNGYINNL-EILLFMIENGADTTLLDKD-GFTMLQVYLQSNHhidIEIIK 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359338997 157 QLMRYGAD-PSLADGEGYRGLHLAVLFQ----NMPIAAYLMAKGQEVDLPDLNGQTPLM------LAAQKIIGPEPTNFL 225
Cdd:PHA02798 166 LLLEKGVDiNTHNNKEKYDTLHCYFKYNidriDADILKLFVDNGFIINKENKSHKKKFMeylnslLYDNKRFKKNILDFI 245

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 359338997 226 IKcNASVNAVDKVNRNsPLHCAVLAGNVDSVHILLEAGASVDMQNDNGHTAIDLAQQVHS 285
Cdd:PHA02798 246 FS-YIDINQVDELGFN-PLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFENES 303
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 109-280 4.25e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 40.25  E-value: 4.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359338997 109 LHWAAINNRADIVKYYISKGAVIDQLGGDlNSTPLHWAIRQGHLSMVIQLMRYGADPSLadGEGYRGLHLAVLFQNMPIA 188
Cdd:PHA02878  41 LHQAVEARNLDVVKSLLTRGHNVNQPDHR-DLTPLHIICKEPNKLGMKEMIRSINKCSV--FYTLVAIKDAFNNRNVEIF 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359338997 189 AYLMA----KGQEVDLPDLNgqtplMLAAQKIIGPEPTNFLIKCNASVNAVDKVNR------------------------ 240
Cdd:PHA02878 118 KIILTnrykNIQTIDLVYID-----KKSKDDIIEAEITKLLLSYGADINMKDRHKGntalhyatenkdqrltelllsyga 192

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 359338997 241 ---------NSPLHCAVLAGNVDSVHILLEAGASVDMQNDNGHTAIDLA 280
Cdd:PHA02878 193 nvnipdktnNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHIS 241
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 141-166 5.18e-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: 34.93  E-value: 5.18e-03
                          10        20
                  ....*....|....*....|....*.
gi 359338997  141 TPLHWAIRQGHLSMVIQLMRYGADPS 166
Cdd:pfam13606   4 TPLHLAARNGRLEIVKLLLENGADIN 29
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 107-132 6.56e-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: 34.54  E-value: 6.56e-03
                          10        20
                  ....*....|....*....|....*.
gi 359338997  107 TLLHWAAINNRADIVKYYISKGAVID 132
Cdd:pfam13606   4 TPLHLAARNGRLEIVKLLLENGADIN 29
Ank_4 pfam13637
Ankyrin repeats (many copies);
76-123 6.78e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 35.33  E-value: 6.78e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 359338997   76 IIKATQFGALERCKELVEAGYDVRQPDKENVTLLHWAAINNRADIVKY 123
Cdd:pfam13637   5 LHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKL 52
Ank_5 pfam13857
Ankyrin repeats (many copies);
91-146 6.91e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.40  E-value: 6.91e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 359338997   91 LVEAGY-DVRQPDKENVTLLHWAAINNRADIVKYYISKGAVIDQLGGDlNSTPLHWA 146
Cdd:pfam13857   1 LLEHGPiDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEE-GLTALDLA 56
 
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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