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Conserved domains on  [gi|78706564|ref|NP_001027085|]
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anorexia, isoform B [Drosophila melanogaster]

Protein Classification

acyl-CoA-binding domain-containing protein( domain architecture ID 12470595)

acyl-CoA-binding domain-containing protein (ACBP) with ankyrin repeats is mainly involved in acyl-CoA ester binding and trafficking in eukaryotic cells

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ACBP pfam00887
Acyl CoA binding protein;
10-85 7.44e-27

Acyl CoA binding protein;


:

Pssm-ID: 459982  Cd Length: 76  Bit Score: 98.82  E-value: 7.44e-27
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 78706564    10 DELFHLATEHVAKQSNSIGSADLLIFYGYYKQATNGPCKEQSPGLLQLQAKSKWQAWRNLGTMSQSAARQAYVQKL 85
Cdd:pfam00887   1 EEKFEAAAEFVKKLKSKPSNEEKLELYGLYKQATVGDCNTPRPGMFDFKGKAKWDAWKKLGGMSKEEAMAKYVELV 76
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
121-231 5.43e-21

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 89.24  E-value: 5.43e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706564 121 LFDHVKENNLDRLRELL-QPSDLVKLDEHGMALIHWATDRNAVEIIQFLVRSGASVNQRDAEQQTPLHYAASCGHLEALQ 199
Cdd:COG0666  91 LHAAARNGDLEIVKLLLeAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170

                        90       100       110
                ....*....|....*....|....*....|....*
gi 78706564 200 CLLELHASLELRDSDGQTCYDVA---DDEQICQVL 231
Cdd:COG0666 171 LLLEAGADVNARDNDGETPLHLAaenGHLEIVKLL 205
 
Name Accession Description Interval E-value
ACBP pfam00887
Acyl CoA binding protein;
10-85 7.44e-27

Acyl CoA binding protein;


Pssm-ID: 459982  Cd Length: 76  Bit Score: 98.82  E-value: 7.44e-27
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 78706564    10 DELFHLATEHVAKQSNSIGSADLLIFYGYYKQATNGPCKEQSPGLLQLQAKSKWQAWRNLGTMSQSAARQAYVQKL 85
Cdd:pfam00887   1 EEKFEAAAEFVKKLKSKPSNEEKLELYGLYKQATVGDCNTPRPGMFDFKGKAKWDAWKKLGGMSKEEAMAKYVELV 76
ACBP cd00435
Acyl CoA binding protein (ACBP) binds thiol esters of long fatty acids and coenzyme A in a ...
 9-92 3.51e-21

Acyl CoA binding protein (ACBP) binds thiol esters of long fatty acids and coenzyme A in a one-to-one binding mode with high specificity and affinity. Acyl-CoAs are important intermediates in fatty lipid synthesis and fatty acid degradation and play a role in regulation of intermediary metabolism and gene regulation. The suggested role of ACBP is to act as a intracellular acyl-CoA transporter and pool former. ACBPs are present in a large group of eukaryotic species and several tissue-specific isoforms have been detected.


Pssm-ID: 238248  Cd Length: 85  Bit Score: 84.30  E-value: 3.51e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706564   9 VDELFHLATEHVAKQSNSIGSADLLIFYGYYKQATNGPCKEQSPGLLQLQAKSKWQAWRNLGTMSQSAARQAYVQKLQEL 88
Cdd:cd00435   1 LQEEFEAAAEKVKKLKTKPSNEEKLQLYSLYKQATVGDCNTERPGMFDLKGRAKWDAWNSLKGMSKEDAMKAYIAKVEEL 80


                ....
gi 78706564  89 QPNW 92
Cdd:cd00435  81 IAKY 84
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
121-231 5.43e-21

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 89.24  E-value: 5.43e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706564 121 LFDHVKENNLDRLRELL-QPSDLVKLDEHGMALIHWATDRNAVEIIQFLVRSGASVNQRDAEQQTPLHYAASCGHLEALQ 199
Cdd:COG0666  91 LHAAARNGDLEIVKLLLeAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170

                        90       100       110
                ....*....|....*....|....*....|....*
gi 78706564 200 CLLELHASLELRDSDGQTCYDVA---DDEQICQVL 231
Cdd:COG0666 171 LLLEAGADVNARDNDGETPLHLAaenGHLEIVKLL 205
Ank_2 pfam12796
Ankyrin repeats (3 copies);
121-212 2.99e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 60.90  E-value: 2.99e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706564   121 LFDHVKENNLDRLRELLQ-PSDLVKLDEHGMALIHWATDRNAVEIIQFLVrSGASVNQRDaEQQTPLHYAASCGHLEALQ 199
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLEnGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 78706564   200 CLLELHASLELRD 212
Cdd:pfam12796  79 LLLEKGADINVKD 91
ACB COG4281
Acyl-CoA-binding protein [Lipid transport and metabolism];
1-88 1.15e-11

Acyl-CoA-binding protein [Lipid transport and metabolism];


Pssm-ID: 443422  Cd Length: 87  Bit Score: 59.09  E-value: 1.15e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706564   1 MSDSDTDtvdelFHLATEHVAKQSNSIGSADLLIFYGYYKQATNGPCKEQSPGLLQLQAKSKWQAWRNLGTMSQSAARQA 80
Cdd:COG4281   1 MSDLQAA-----FEAAVARVKTLTERPDNDTLLKLYALYKQATEGDVTGKRPGMTDFVGRAKYDAWAQLKGMSKDEAMQQ 75


                ....*...
gi 78706564  81 YVQKLQEL 88
Cdd:COG4281  76 YIDLVNSL 83
PTZ00458 PTZ00458
acyl CoA binding protein; Provisional
 33-92 3.02e-11

acyl CoA binding protein; Provisional


Pssm-ID: 185637  Cd Length: 90  Bit Score: 58.29  E-value: 3.02e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706564   33 LIFYGYYKQATNGPCKEQSPGLLQLQAKSKWQAWRNLGTMSQSAARQAYVQKLQELQPNW 92
Cdd:PTZ00458  27 LDLYKYYKQSTVGNCNIKEPSMFKYQDRKKYEAWKSIENLNREDAKKRYVEIVTELFPNW 86
PHA03095 PHA03095
ankyrin-like protein; Provisional
 120-218 9.52e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 55.03  E-value: 9.52e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706564  120 TLFDHVKENNLDR---LRELLQPS-DLVKLDEHGMALIHWAT--DRNAVEIIQFLVRSGASVNQRDAEQQTPLHYAASCG 193
Cdd:PHA03095 189 SLLHHHLQSFKPRariVRELIRAGcDPAATDMLGNTPLHSMAtgSSCKRSLVLPLLIAGISINARNRYGQTPLHYAAVFN 268

                         90       100
                 ....*....|....*....|....*
gi 78706564  194 HLEALQCLLELHASLELRDSDGQTC 218
Cdd:PHA03095 269 NPRACRRLIALGADINAVSSDGNTP 293
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 184-210 5.44e-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: 36.41  E-value: 5.44e-04
                           10        20
                   ....*....|....*....|....*..
gi 78706564    184 TPLHYAASCGHLEALQCLLELHASLEL 210
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
ACBP pfam00887
Acyl CoA binding protein;
10-85 7.44e-27

Acyl CoA binding protein;


Pssm-ID: 459982  Cd Length: 76  Bit Score: 98.82  E-value: 7.44e-27
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 78706564    10 DELFHLATEHVAKQSNSIGSADLLIFYGYYKQATNGPCKEQSPGLLQLQAKSKWQAWRNLGTMSQSAARQAYVQKL 85
Cdd:pfam00887   1 EEKFEAAAEFVKKLKSKPSNEEKLELYGLYKQATVGDCNTPRPGMFDFKGKAKWDAWKKLGGMSKEEAMAKYVELV 76
ACBP cd00435
Acyl CoA binding protein (ACBP) binds thiol esters of long fatty acids and coenzyme A in a ...
 9-92 3.51e-21

Acyl CoA binding protein (ACBP) binds thiol esters of long fatty acids and coenzyme A in a one-to-one binding mode with high specificity and affinity. Acyl-CoAs are important intermediates in fatty lipid synthesis and fatty acid degradation and play a role in regulation of intermediary metabolism and gene regulation. The suggested role of ACBP is to act as a intracellular acyl-CoA transporter and pool former. ACBPs are present in a large group of eukaryotic species and several tissue-specific isoforms have been detected.


Pssm-ID: 238248  Cd Length: 85  Bit Score: 84.30  E-value: 3.51e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706564   9 VDELFHLATEHVAKQSNSIGSADLLIFYGYYKQATNGPCKEQSPGLLQLQAKSKWQAWRNLGTMSQSAARQAYVQKLQEL 88
Cdd:cd00435   1 LQEEFEAAAEKVKKLKTKPSNEEKLQLYSLYKQATVGDCNTERPGMFDLKGRAKWDAWNSLKGMSKEDAMKAYIAKVEEL 80


                ....
gi 78706564  89 QPNW 92
Cdd:cd00435  81 IAKY 84
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
121-231 5.43e-21

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 89.24  E-value: 5.43e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706564 121 LFDHVKENNLDRLRELL-QPSDLVKLDEHGMALIHWATDRNAVEIIQFLVRSGASVNQRDAEQQTPLHYAASCGHLEALQ 199
Cdd:COG0666  91 LHAAARNGDLEIVKLLLeAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170

                        90       100       110
                ....*....|....*....|....*....|....*
gi 78706564 200 CLLELHASLELRDSDGQTCYDVA---DDEQICQVL 231
Cdd:COG0666 171 LLLEAGADVNARDNDGETPLHLAaenGHLEIVKLL 205
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
125-222 1.32e-18

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 82.69  E-value: 1.32e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706564 125 VKENNLDRLRELLQP-SDLVKLDEHGMALIHWATDRNAVEIIQFLVRSGASVNQRDAEQQTPLHYAASCGHLEALQCLLE 203
Cdd:COG0666 128 AYNGNLEIVKLLLEAgADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLE 207

                        90
                ....*....|....*....
gi 78706564 204 LHASLELRDSDGQTCYDVA 222
Cdd:COG0666 208 AGADVNAKDNDGKTALDLA 226
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
128-217 6.42e-16

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 75.38  E-value: 6.42e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706564 128 NNLDRLRELLQPSDLVKLDEHGMALIHWATDRNAVEIIQFLVRSGASVNQRDAEQQTPLHYAASCGHLEALQCLLELHAS 207
Cdd:COG0666  66 DLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGAD 145

                        90
                ....*....|
gi 78706564 208 LELRDSDGQT 217
Cdd:COG0666 146 VNAQDNDGNT 155
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
125-239 1.36e-12

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 65.75  E-value: 1.36e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706564 125 VKENNLDRLRELLQ-PSDLVKLDEHGMALIHWATDRNAVEIIQFLVRSGASVNQRDAEQQTPLHYAASCGHLEALQCLLE 203
Cdd:COG0666 161 AANGNLEIVKLLLEaGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 78706564 204 LHASLELRDSDGQTCYDVADDEQICQVLQTERERLA 239
Cdd:COG0666 241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALL 276
Ank_2 pfam12796
Ankyrin repeats (3 copies);
121-212 2.99e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 60.90  E-value: 2.99e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706564   121 LFDHVKENNLDRLRELLQ-PSDLVKLDEHGMALIHWATDRNAVEIIQFLVrSGASVNQRDaEQQTPLHYAASCGHLEALQ 199
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLEnGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 78706564   200 CLLELHASLELRD 212
Cdd:pfam12796  79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
153-217 5.48e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 60.13  E-value: 5.48e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 78706564   153 IHWATDRNAVEIIQFLVRSGASVNQRDAEQQTPLHYAASCGHLEALQCLLElHASLELRDsDGQT 217
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRT 63
ACB COG4281
Acyl-CoA-binding protein [Lipid transport and metabolism];
1-88 1.15e-11

Acyl-CoA-binding protein [Lipid transport and metabolism];


Pssm-ID: 443422  Cd Length: 87  Bit Score: 59.09  E-value: 1.15e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706564   1 MSDSDTDtvdelFHLATEHVAKQSNSIGSADLLIFYGYYKQATNGPCKEQSPGLLQLQAKSKWQAWRNLGTMSQSAARQA 80
Cdd:COG4281   1 MSDLQAA-----FEAAVARVKTLTERPDNDTLLKLYALYKQATEGDVTGKRPGMTDFVGRAKYDAWAQLKGMSKDEAMQQ 75


                ....*...
gi 78706564  81 YVQKLQEL 88
Cdd:COG4281  76 YIDLVNSL 83
PTZ00458 PTZ00458
acyl CoA binding protein; Provisional
 33-92 3.02e-11

acyl CoA binding protein; Provisional


Pssm-ID: 185637  Cd Length: 90  Bit Score: 58.29  E-value: 3.02e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706564   33 LIFYGYYKQATNGPCKEQSPGLLQLQAKSKWQAWRNLGTMSQSAARQAYVQKLQELQPNW 92
Cdd:PTZ00458  27 LDLYKYYKQSTVGNCNIKEPSMFKYQDRKKYEAWKSIENLNREDAKKRYVEIVTELFPNW 86
Ank_4 pfam13637
Ankyrin repeats (many copies);
149-202 5.62e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.43  E-value: 5.62e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 78706564   149 GMALIHWATDRNAVEIIQFLVRSGASVNQRDAEQQTPLHYAASCGHLEALQCLL 202
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
 120-218 9.52e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 55.03  E-value: 9.52e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706564  120 TLFDHVKENNLDR---LRELLQPS-DLVKLDEHGMALIHWAT--DRNAVEIIQFLVRSGASVNQRDAEQQTPLHYAASCG 193
Cdd:PHA03095 189 SLLHHHLQSFKPRariVRELIRAGcDPAATDMLGNTPLHSMAtgSSCKRSLVLPLLIAGISINARNRYGQTPLHYAAVFN 268

                         90       100
                 ....*....|....*....|....*
gi 78706564  194 HLEALQCLLELHASLELRDSDGQTC 218
Cdd:PHA03095 269 NPRACRRLIALGADINAVSSDGNTP 293
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 152-232 1.80e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 54.52  E-value: 1.80e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706564  152 LIHWATDRNAVEIiQFLVRSGASVNQRDAEQQTPLHYAASCGHLEALQCLLELHASLELRDSDGQTCYDVADDEQICQVL 231
Cdd:PTZ00322  86 LCQLAASGDAVGA-RILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVV 164


                 .
gi 78706564  232 Q 232
Cdd:PTZ00322 165 Q 165
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
126-222 3.22e-08

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 53.03  E-value: 3.22e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706564 126 KENNLDRLRELLQPSDLVKLDEHGMALIHWATDRNAVEIIQFLVRSGASVNQRDAEQQTPLHYAASCGHLEALQCLLELH 205
Cdd:COG0666  31 LLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAG 110

                        90
                ....*....|....*..
gi 78706564 206 ASLELRDSDGQTCYDVA 222
Cdd:COG0666 111 ADVNARDKDGETPLHLA 127
Ank_5 pfam13857
Ankyrin repeats (many copies);
173-222 8.64e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 47.73  E-value: 8.64e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 78706564   173 ASVNQRDAEQQTPLHYAASCGHLEALQCLLELHASLELRDSDGQTCYDVA 222
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 116-203 9.44e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 51.89  E-value: 9.44e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706564  116 DSEKTLFDH--VKENNLDRLRELLQ-PSDLVKLDEHGMALIHWATDRNAVEIIQFLVRSGASVNQRDAEQQTPLHYAASC 192
Cdd:PHA02874 121 DAELKTFLHyaIKKGDLESIKMLFEyGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEY 200

                         90
                 ....*....|.
gi 78706564  193 GHLEALQCLLE 203
Cdd:PHA02874 201 GDYACIKLLID 211
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 116-231 1.31e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 48.45  E-value: 1.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706564  116 DSEKTLFDHVKENNLDRLRELLQPSDLVK--LDEHGMALIHWATDRNAVEIIQFLVRSGASVNQRDAEQQTPLHYAASCG 193
Cdd:PHA02875  67 DIESELHDAVEEGDVKAVEELLDLGKFADdvFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMG 146

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 78706564  194 HLEALQCLLELHASLELRDSDGQT--CYDVA-DDEQICQVL 231
Cdd:PHA02875 147 DIKGIELLIDHKACLDIEDCCGCTplIIAMAkGDIAICKML 187
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 163-221 9.88e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 46.11  E-value: 9.88e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 78706564  163 EIIQFLVRSGASVNQRDAEQQTPLHYAASCGHLEALQCLLELHASLELRDSDGqtCYDV 221
Cdd:PHA02874 105 DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNG--CYPI 161
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 119-209 1.35e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 45.43  E-value: 1.35e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706564  119 KTLFDH-VKENNLDRLRELLQ---PSDLVklDEHGMALIHWATDRNAVEIIQFLVRSGASVNQRDAEQQTPLHYAASCGH 194
Cdd:PHA03100 160 KLLIDKgVDINAKNRVNYLLSygvPINIK--DVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNN 237

                         90
                 ....*....|....*
gi 78706564  195 LEALQCLLELHASLE 209
Cdd:PHA03100 238 KEIFKLLLNNGPSIK 252
Ank_5 pfam13857
Ankyrin repeats (many copies);
139-189 3.34e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.41  E-value: 3.34e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 78706564   139 PSDLVKLDEHGMALIHWATDRNAVEIIQFLVRSGASVNQRDAEQQTPLHYA 189
Cdd:pfam13857   6 PIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 140-217 5.81e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 43.72  E-value: 5.81e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 78706564  140 SDLVKLDEH-GMALIHWATDRNAVEIIQFLVRSGASVNQRDAEQQTPLHYAASCGHLEALQCLLELHASLELRDSDGQT 217
Cdd:PHA02878 158 ADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNT 236
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 149-218 1.58e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 42.34  E-value: 1.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706564  149 GMALIHWATDRNAV--EIIQFLVRSGASVNQ----------------RDAEQQTPLHYAASCGHLEALQCLLELHASLEL 210
Cdd:PHA03100 141 GENLLHLYLESNKIdlKILKLLIDKGVDINAknrvnyllsygvpiniKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNL 220


                 ....*...
gi 78706564  211 RDSDGQTC 218
Cdd:PHA03100 221 VNKYGDTP 228
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 150-226 1.96e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 42.36  E-value: 1.96e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 78706564  150 MALIHWATDRNAVEIIQFLVRSGASVNQRDAEQQTPLHYAASCGHLEALQCLLELHASLELRDSDGQTCYDVADDEQ 226
Cdd:PHA02876 146 MKLIKERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSK 222
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 183-208 3.86e-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.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 36.85  E-value: 3.86e-04
                          10        20
                  ....*....|....*....|....*.
gi 78706564   183 QTPLHYAASCGHLEALQCLLELHASL 208
Cdd:pfam13606   3 NTPLHLAARNGRLEIVKLLLENGADI 28
PHA03095 PHA03095
ankyrin-like protein; Provisional
 160-221 4.92e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 40.78  E-value: 4.92e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 78706564  160 NAVEIIQFLVRSGASVNQRDAEQQTPLH-YAAS-CGHLEALQCLLELHASLELRDSDGQTCYDV 221
Cdd:PHA03095  95 TTLDVIKLLIKAGADVNAKDKVGRTPLHvYLSGfNINPKVIRLLLRKGADVNALDLYGMTPLAV 158
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 184-210 5.44e-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: 36.41  E-value: 5.44e-04
                           10        20
                   ....*....|....*....|....*..
gi 78706564    184 TPLHYAASCGHLEALQCLLELHASLEL 210
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADINA 30
PHA03095 PHA03095
ankyrin-like protein; Provisional
 158-219 6.40e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 40.39  E-value: 6.40e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 78706564  158 DRNAVEIIQFLVRSGASVNQRDAEQQTPLHYAASCGH---LEALQCLLELHASLELRDSDGQT---CY 219
Cdd:PHA03095  23 SNVTVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTplhLY 90
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 152-217 6.81e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 40.33  E-value: 6.81e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 78706564  152 LIHWATDRNAVEIIQFLVRSGASVNQRDAEQQTPLHYAASCGHLEALQCLLELHASLELRDSDGQT 217
Cdd:PHA02874 127 FLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGES 192
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 183-212 7.00e-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: 36.11  E-value: 7.00e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 78706564   183 QTPLHYAA-SCGHLEALQCLLELHASLELRD 212
Cdd:pfam00023   3 NTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 116-213 9.44e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 39.86  E-value: 9.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706564  116 DSEKTLFDHVKENNLDRLRELL-----QPSDLVKLDEHGMaliHWATDRNAVEIIQFLVRSGASVNQRDAEQQTPLHYAA 190
Cdd:PHA02878 166 HKGNTALHYATENKDQRLTELLlsygaNVNIPDKTNNSPL---HHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISV 242

                         90       100
                 ....*....|....*....|....
gi 78706564  191 S-CGHLEALQCLLELHASLELRDS 213
Cdd:PHA02878 243 GyCKDYDILKLLLEHGVDVNAKSY 266
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 111-215 1.99e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 38.88  E-value: 1.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706564  111 EDQRLDSEKTLFDH---VKENNLDRLrellQPSDLVKLDEHgmalihwaTDRNAVEIIQFLVRSGASVNQRDAEQQTPLH 187
Cdd:PHA03100  44 EARNIDVVKILLDNgadINSSTKNNS----TPLHYLSNIKY--------NLTDVKEIVKLLLEYGANVNAPDNNGITPLL 111

                         90       100       110
                 ....*....|....*....|....*....|
gi 78706564  188 YAASC--GHLEALQCLLELHASLELRDSDG 215
Cdd:PHA03100 112 YAISKksNSYSIVEYLLDNGANVNIKNSDG 141
Ank_4 pfam13637
Ankyrin repeats (many copies);
184-231 2.91e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 34.94  E-value: 2.91e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 78706564   184 TPLHYAASCGHLEALQCLLELHASLELRDSDGQTCYDVA---DDEQICQVL 231
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAasnGNVEVLKLL 53
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 168-217 3.45e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 38.31  E-value: 3.45e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 78706564  168 LVRSGASVNQRDAEQQTPLHYAASCGHLEALQCLLELHASLELRDSDGQT 217
Cdd:PLN03192 544 LLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNT 593
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 153-209 4.43e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 38.12  E-value: 4.43e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 78706564  153 IHWAT--DRNAvEIIQFLVRSGASVNQRDAEQQTPLHYAASCGHLEALQCLLELHASLE 209
Cdd:PHA02876 345 LHQAStlDRNK-DIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIE 402
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 151-222 7.70e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 37.25  E-value: 7.70e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 78706564  151 ALIHwatDRNAVEiiqfLVRSGASVNQRDAEQQTPLHYAAS--CGhLEALQCLLELHASLELRDSDGQTCYDVA 222
Cdd:PHA02874 230 AIIH---NRSAIE----LLINNASINDQDIDGSTPLHHAINppCD-IDIIDILLYHKADISIKDNKGENPIDTA 295
PHA02795 PHA02795
ankyrin-like protein; Provisional
 141-224 8.48e-03

ankyrin-like protein; Provisional


Pssm-ID: 165157 [Multi-domain]  Cd Length: 437  Bit Score: 36.90  E-value: 8.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706564  141 DLVKLDEHGMALIhwATDRNAVEIIQFLVRSGASVNQRDAEQQTPLHYAASCGHLEALQCLLELHASLELRDSDGQTCYD 220
Cdd:PHA02795 182 DLYKIIQYTRGFL--VDEPTVLEIYKLCIPYIEDINQLDAGGRTLLYRAIYAGYIDLVSWLLENGANVNAVMSNGYTCLD 259


                 ....
gi 78706564  221 VADD 224
Cdd:PHA02795 260 VAVD 263
 
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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