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Conserved domains on  [gi|153792284|ref|NP_778146|]
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POTE ankyrin domain family member D [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
134-368 9.95e-49

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 171.29  E-value: 9.95e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792284 134 HIRREDLDKLHRAAWWGKVPRKDLIVMLRDTDMNKRDKEKRTALHLASANGNSEVVQLLLDRRCQLNVLDNKKRTALIKA 213
Cdd:COG0666   48 ALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLA 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792284 214 IQCQEDECVLMLLEHGADRNIPDEYGNTALHYAIYNEDKLMAKALLLYGADIESKNKCGLTPLLLGVHEQKQQVVKFLIK 293
Cdd:COG0666  128 AYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLE 207

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153792284 294 KKANLNVLDRYGRTALILAVCCGSASIVNLLLEQNVDVSSQDLSGQTAREYAVSSHHHVICELLSDYKEKQMLKI 368
Cdd:COG0666  208 AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282
CCDC144C super family cl25942
CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ...
 526-582 9.15e-17

CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ankyrin repeat domain-containing protein 26-like 1 found in eukaryotes. Its function remains unknown, however, it is known to contain a coiled-coil domain which corresponds to this region. The ankyrin repeat which features in this protein is a common amino acid motif.


The actual alignment was detected with superfamily member pfam14915:

Pssm-ID: 464371 [Multi-domain]  Cd Length: 304  Bit Score: 81.19  E-value: 9.15e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 153792284  526 NSVLQEEIAMLRLELDETKHQNQLRENKILEEIESVKEKTDKLLRAMQLNEEALTKT 582
Cdd:pfam14915   1 NCMLQDEIAMLRLEIDTIKNQNQEKEKKYLEDIEILKEKNDDLQKTLKLNEETLTKT 57
EnvC super family cl34844
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 470-575 1.30e-03

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


The actual alignment was detected with superfamily member COG4942:

Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 41.29  E-value: 1.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792284 470 SDEQNDTRKQLSEEQNTgISQdeiLTNKQKQIEVAEQKMNSELSLSHKKEEDLLRENSVLQEEIAMLRLELDEtkhqNQL 549
Cdd:COG4942   19 ADAAAEAEAELEQLQQE-IAE---LEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE----LEK 90

                         90       100
                 ....*....|....*....|....*.
gi 153792284 550 RENKILEEIESVKEKTDKLLRAMQLN 575
Cdd:COG4942   91 EIAELRAELEAQKEELAELLRALYRL 116
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
134-368 9.95e-49

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 171.29  E-value: 9.95e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792284 134 HIRREDLDKLHRAAWWGKVPRKDLIVMLRDTDMNKRDKEKRTALHLASANGNSEVVQLLLDRRCQLNVLDNKKRTALIKA 213
Cdd:COG0666   48 ALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLA 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792284 214 IQCQEDECVLMLLEHGADRNIPDEYGNTALHYAIYNEDKLMAKALLLYGADIESKNKCGLTPLLLGVHEQKQQVVKFLIK 293
Cdd:COG0666  128 AYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLE 207

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153792284 294 KKANLNVLDRYGRTALILAVCCGSASIVNLLLEQNVDVSSQDLSGQTAREYAVSSHHHVICELLSDYKEKQMLKI 368
Cdd:COG0666  208 AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282
Ank_2 pfam12796
Ankyrin repeats (3 copies);
177-269 2.21e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 88.63  E-value: 2.21e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792284  177 LHLASANGNSEVVQLLLDRRCQLNVLDNKKRTALIKAIQCQEDECVLMLLEHgADRNIPDeYGNTALHYAIYNEDKLMAK 256
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 153792284  257 ALLLYGADIESKN 269
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 200-349 2.45e-20

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 94.32  E-value: 2.45e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792284 200 NVLDNKKRTALIKAIQCQEDECVL---MLLEHGADRNIPDEYGNTALHYAIYN---EDKLMAKALLLYGADIESKNKCGL 273
Cdd:PHA03095   5 ESVDIIMEAALYDYLLNASNVTVEevrRLLAAGADVNFRGEYGKTPLHLYLHYsseKVKDIVRLLLEAGADVNAPERCGF 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792284 274 TPL-LLGVHEQKQQVVKFLIKKKANLNVLDRYGRTalILAVCCGSASI----VNLLLEQNVDVSSQDLSGQTAREYAVSS 348
Cdd:PHA03095  85 TPLhLYLYNATTLDVIKLLIKAGADVNAKDKVGRT--PLHVYLSGFNInpkvIRLLLRKGADVNALDLYGMTPLAVLLKS 162


                 .
gi 153792284 349 H 349
Cdd:PHA03095 163 R 163
CCDC144C pfam14915
CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ...
 526-582 9.15e-17

CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ankyrin repeat domain-containing protein 26-like 1 found in eukaryotes. Its function remains unknown, however, it is known to contain a coiled-coil domain which corresponds to this region. The ankyrin repeat which features in this protein is a common amino acid motif.


Pssm-ID: 464371 [Multi-domain]  Cd Length: 304  Bit Score: 81.19  E-value: 9.15e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 153792284  526 NSVLQEEIAMLRLELDETKHQNQLRENKILEEIESVKEKTDKLLRAMQLNEEALTKT 582
Cdd:pfam14915   1 NCMLQDEIAMLRLEIDTIKNQNQEKEKKYLEDIEILKEKNDDLQKTLKLNEETLTKT 57
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 163-340 4.09e-10

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 62.34  E-value: 4.09e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792284 163 DTDMNKRDKEKRTALHLASANGNSEVVQLLLdrrcqlnvldnkkrtalikaiqcqedECVLMLLehgadrNIP---DEY- 238
Cdd:cd22192   41 SCDLFQRGALGETALHVAALYDNLEAAVVLM--------------------------EAAPELV------NEPmtsDLYq 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792284 239 GNTALHYAIYNEDKLMAKALLLYGADIESKNKCGLtplllgvheqkqqvvkFLIKKKANLNVldrYGRTALILAVCCGSA 318
Cdd:cd22192   89 GETALHIAVVNQNLNLVRELIARGADVVSPRATGT----------------FFRPGPKNLIY---YGEHPLSFAACVGNE 149

                        170       180
                 ....*....|....*....|..
gi 153792284 319 SIVNLLLEQNVDVSSQDLSGQT 340
Cdd:cd22192  150 EIVRLLIEHGADIRAQDSLGNT 171
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 174-362 1.36e-08

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 57.78  E-value: 1.36e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792284  174 RTAL-HLASANGNSEVVQLLLDRRCQLNVLDNKKRTALIKAIQCQEDECVLMLLEHGADRNIP-------DEY--GNTAL 243
Cdd:TIGR00870  53 RSALfVAAIENENLELTELLLNLSCRGAVGDTLLHAISLEYVDAVEAILLHLLAAFRKSGPLElandqytSEFtpGITAL 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792284  244 HYAIYNEDKLMAKALLLYGADIESKNKCgltplllgvheqkqqvVKFLIKKKANLNvldRYGRTALILAVCCGSASIVNL 323
Cdd:TIGR00870 133 HLAAHRQNYEIVKLLLERGASVPARACG----------------DFFVKSQGVDSF---YHGESPLNAAACLGSPSIVAL 193

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 153792284  324 LLEQNVDVSSQDLSGQTAREYAVsshhhVICELLSDYKE 362
Cdd:TIGR00870 194 LSEDPADILTADSLGNTLLHLLV-----MENEFKAEYEE 227
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 238-266 4.52e-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: 37.57  E-value: 4.52e-04
                           10        20
                   ....*....|....*....|....*....
gi 153792284   238 YGNTALHYAIYNEDKLMAKALLLYGADIE 266
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 489-584 8.03e-04

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.12  E-value: 8.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792284 489 SQDEILTNKQKQIEVAEQKMNSELSLSHKKEEDLLRENSVLQEEIAMLRLELDETkhQNQLRENKilEEIESVKEKTDKL 568
Cdd:COG3883   16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKL--QAEIAEAE--AEIEERREELGER 91

                         90
                 ....*....|....*.
gi 153792284 569 LRAMQLNEEALTKTNI 584
Cdd:COG3883   92 ARALYRSGGSVSYLDV 107
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 470-575 1.30e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 41.29  E-value: 1.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792284 470 SDEQNDTRKQLSEEQNTgISQdeiLTNKQKQIEVAEQKMNSELSLSHKKEEDLLRENSVLQEEIAMLRLELDEtkhqNQL 549
Cdd:COG4942   19 ADAAAEAEAELEQLQQE-IAE---LEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE----LEK 90

                         90       100
                 ....*....|....*....|....*.
gi 153792284 550 RENKILEEIESVKEKTDKLLRAMQLN 575
Cdd:COG4942   91 EIAELRAELEAQKEELAELLRALYRL 116
PRK00106 PRK00106
ribonuclease Y;
454-573 3.34e-03

ribonuclease Y;


Pssm-ID: 178867 [Multi-domain]  Cd Length: 535  Bit Score: 40.24  E-value: 3.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792284 454 KPENQQFPDTENEEYHSDEQ--NDTRKQLSEEQNTGISQDEILTNKQKQIEVAEQKMNSE-----------LSLSHKKEE 520
Cdd:PRK00106  78 KEEARKYREEIEQEFKSERQelKQIESRLTERATSLDRKDENLSSKEKTLESKEQSLTDKskhidereeqvEKLEEQKKA 157

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 153792284 521 DLLRENSVLQEEIAMLRLELDETKHQNQLrENKILEEIESVKEKTDK-----LLRAMQ 573
Cdd:PRK00106 158 ELERVAALSQAEAREIILAETENKLTHEI-ATRIREAEREVKDRSDKmakdlLAQAMQ 214
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 470-583 3.92e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 40.00  E-value: 3.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792284  470 SDEQNDTRKQLSEEQNTGISQDEILTNKQKQIevaeQKMNSELS-LSHKKEEDLLREnsvLQEEIAMLRLELDETkhQNQ 548
Cdd:TIGR04523 259 KDEQNKIKKQLSEKQKELEQNNKKIKELEKQL----NQLKSEISdLNNQKEQDWNKE---LKSELKNQEKKLEEI--QNQ 329

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 153792284  549 LREN-----KILEEIESV-KEKTDKLLRAMQLNEEALTKTN 583
Cdd:TIGR04523 330 ISQNnkiisQLNEQISQLkKELTNSESENSEKQRELEEKQN 370
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
134-368 9.95e-49

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 171.29  E-value: 9.95e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792284 134 HIRREDLDKLHRAAWWGKVPRKDLIVMLRDTDMNKRDKEKRTALHLASANGNSEVVQLLLDRRCQLNVLDNKKRTALIKA 213
Cdd:COG0666   48 ALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLA 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792284 214 IQCQEDECVLMLLEHGADRNIPDEYGNTALHYAIYNEDKLMAKALLLYGADIESKNKCGLTPLLLGVHEQKQQVVKFLIK 293
Cdd:COG0666  128 AYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLE 207

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153792284 294 KKANLNVLDRYGRTALILAVCCGSASIVNLLLEQNVDVSSQDLSGQTAREYAVSSHHHVICELLSDYKEKQMLKI 368
Cdd:COG0666  208 AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
135-391 8.20e-48

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 168.59  E-value: 8.20e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792284 135 IRREDLDKLHRAAWWGKVPRKDLIVMLRDTDMNKRDKEKRTALHLASANGNSEVVQLLLDRRCQLNVLDNKKRTALIKAI 214
Cdd:COG0666   16 LLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAA 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792284 215 QCQEDECVLMLLEHGADRNIPDEYGNTALHYAIYNEDKLMAKALLLYGADIESKNKCGLTPLLLGVHEQKQQVVKFLIKK 294
Cdd:COG0666   96 RNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEA 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792284 295 KANLNVLDRYGRTALILAVCCGSASIVNLLLEQNVDVSSQDLSGQTAREYAVSSHHHVICELLSDYKEKQMLKISSENSN 374
Cdd:COG0666  176 GADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTA 255

                        250
                 ....*....|....*..
gi 153792284 375 PEQDLKLTSEEESQRLK 391
Cdd:COG0666  256 LLLAAAAGAALIVKLLL 272
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
143-341 1.42e-41

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 151.65  E-value: 1.42e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792284 143 LHRAAWWGkvpRKDLIVML--RDTDMNKRDKEKRTALHLASANGNSEVVQLLLDRRCQLNVLDNKKRTALIKAIQCQEDE 220
Cdd:COG0666   91 LHAAARNG---DLEIVKLLleAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLE 167

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792284 221 CVLMLLEHGADRNIPDEYGNTALHYAIYNEDKLMAKALLLYGADIESKNKCGLTPLLLGVHEQKQQVVKFLIKKKANLNV 300
Cdd:COG0666  168 IVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNA 247

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 153792284 301 LDRYGRTALILAVCCGSASIVNLLLEQNVDVSSQDLSGQTA 341
Cdd:COG0666  248 KDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
157-357 4.58e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 136.62  E-value: 4.58e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792284 157 LIVMLRDTDMNKRDKEKRTALHLASANGNSEVVQLLLDRRCQLNVLDNKKRTALIKAIQCQEDECVLMLLEHGADRNIPD 236
Cdd:COG0666    5 LLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKD 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792284 237 EYGNTALHYAIYNEDKLMAKALLLYGADIESKNKCGLTPLLLGVHEQKQQVVKFLIKKKANLNVLDRYGRTALILAVCCG 316
Cdd:COG0666   85 DGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANG 164

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 153792284 317 SASIVNLLLEQNVDVSSQDLSGQTAREYAVSSHHHVICELL 357
Cdd:COG0666  165 NLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLL 205
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
143-309 7.91e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 127.38  E-value: 7.91e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792284 143 LHRAAWWGKVprkDLIVML--RDTDMNKRDKEKRTALHLASANGNSEVVQLLLDRRCQLNVLDNKKRTALIKAIQCQEDE 220
Cdd:COG0666  124 LHLAAYNGNL---EIVKLLleAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLE 200

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792284 221 CVLMLLEHGADRNIPDEYGNTALHYAIYNEDKLMAKALLLYGADIESKNKCGLTPLLLGVHEQKQQVVKFLIKKKANLNV 300
Cdd:COG0666  201 IVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAA 280


                 ....*....
gi 153792284 301 LDRYGRTAL 309
Cdd:COG0666  281 ALLDLLTLL 289
Ank_2 pfam12796
Ankyrin repeats (3 copies);
177-269 2.21e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 88.63  E-value: 2.21e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792284  177 LHLASANGNSEVVQLLLDRRCQLNVLDNKKRTALIKAIQCQEDECVLMLLEHgADRNIPDeYGNTALHYAIYNEDKLMAK 256
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 153792284  257 ALLLYGADIESKN 269
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 200-349 2.45e-20

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 94.32  E-value: 2.45e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792284 200 NVLDNKKRTALIKAIQCQEDECVL---MLLEHGADRNIPDEYGNTALHYAIYN---EDKLMAKALLLYGADIESKNKCGL 273
Cdd:PHA03095   5 ESVDIIMEAALYDYLLNASNVTVEevrRLLAAGADVNFRGEYGKTPLHLYLHYsseKVKDIVRLLLEAGADVNAPERCGF 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792284 274 TPL-LLGVHEQKQQVVKFLIKKKANLNVLDRYGRTalILAVCCGSASI----VNLLLEQNVDVSSQDLSGQTAREYAVSS 348
Cdd:PHA03095  85 TPLhLYLYNATTLDVIKLLIKAGADVNAKDKVGRT--PLHVYLSGFNInpkvIRLLLRKGADVNALDLYGMTPLAVLLKS 162


                 .
gi 153792284 349 H 349
Cdd:PHA03095 163 R 163
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 154-332 2.04e-18

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 87.80  E-value: 2.04e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792284 154 RKDLIVMLRDT--DMNKRDKEKRTALHLAS-----ANGNSEVVQLLLDRRCQLNVLDNKKRTALIKAIQC--QEDECVLM 224
Cdd:PHA03100  47 NIDVVKILLDNgaDINSSTKNNSTPLHYLSnikynLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEY 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792284 225 LLEHGADRNIPDEYGNTALH-YAIYNEDKL-MAKALLL----------------YGADIESKNKCGLTPLLLGVHEQKQQ 286
Cdd:PHA03100 127 LLDNGANVNIKNSDGENLLHlYLESNKIDLkILKLLIDkgvdinaknrvnyllsYGVPINIKDVYGFTPLHYAVYNNNPE 206

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 153792284 287 VVKFLIKKKANLNVLDRYGRTALILAVCCGSASIVNLLLEQNVDVS 332
Cdd:PHA03100 207 FVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252
Ank_2 pfam12796
Ankyrin repeats (3 copies);
243-335 2.12e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.16  E-value: 2.12e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792284  243 LHYAIYNEDKLMAKALLLYGADIESKNKCGLTPLLLGVHEQKQQVVKFLIkKKANLNVLDrYGRTALILAVCCGSASIVN 322
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 153792284  323 LLLEQNVDVSSQD 335
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 218-334 4.02e-18

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 87.24  E-value: 4.02e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792284 218 EDECVLMLLEHGADRNIPDEY-GNTALHYAIYNEDKLMAKALLLYGADIESKNKCGLTPLLLGVHEQKQQVVKFLIKKKA 296
Cdd:PHA02878 146 EAEITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGA 225

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 153792284 297 NLNVLDRYGRTALILAVC-CGSASIVNLLLEQNVDVSSQ 334
Cdd:PHA02878 226 STDARDKCGNTPLHISVGyCKDYDILKLLLEHGVDVNAK 264
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 155-359 4.95e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 86.94  E-value: 4.95e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792284 155 KDLIVMLRDT--DMNKRDKEKRTALHLASANGNSEVVQLLLDRRCQLNVLDNKKRTALIKAIQCQEDECVLMLLEHGADR 232
Cdd:PHA02874 104 KDMIKTILDCgiDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYA 183

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792284 233 NIPDEYGNTALHYAIYNEDKLMAKALLLYGADIESKNKCGLTPLLLGVHEQKqQVVKFLIkKKANLNVLDRYGRTALILA 312
Cdd:PHA02874 184 NVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIELLI-NNASINDQDIDGSTPLHHA 261

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 153792284 313 V---CcgSASIVNLLLEQNVDVSSQDLSGQTAREYAVS--SHHHVICELLSD 359
Cdd:PHA02874 262 InppC--DIDIIDILLYHKADISIKDNKGENPIDTAFKyiNKDPVIKDIIAN 311
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 163-346 4.43e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 83.56  E-value: 4.43e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792284 163 DTDMNKRDKEKRTALHLASANGNSEVVQLLLDRRCQLNVLDNKKRTAL-----IKAIQCQEDECVLMLLEHGADRNIPDE 237
Cdd:PHA03100  25 DDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLhylsnIKYNLTDVKEIVKLLLEYGANVNAPDN 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792284 238 YGNTALHYAIYN--EDKLMAKALLLYGADIESKNKCGLTPL--LLGVHEQKQQVVKFLIKKKANLNVLDRygrtalilav 313
Cdd:PHA03100 105 NGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLhlYLESNKIDLKILKLLIDKGVDINAKNR---------- 174

                        170       180       190
                 ....*....|....*....|....*....|...
gi 153792284 314 ccgsasiVNLLLEQNVDVSSQDLSGQTAREYAV 346
Cdd:PHA03100 175 -------VNYLLSYGVPINIKDVYGFTPLHYAV 200
CCDC144C pfam14915
CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ...
 526-582 9.15e-17

CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ankyrin repeat domain-containing protein 26-like 1 found in eukaryotes. Its function remains unknown, however, it is known to contain a coiled-coil domain which corresponds to this region. The ankyrin repeat which features in this protein is a common amino acid motif.


Pssm-ID: 464371 [Multi-domain]  Cd Length: 304  Bit Score: 81.19  E-value: 9.15e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 153792284  526 NSVLQEEIAMLRLELDETKHQNQLRENKILEEIESVKEKTDKLLRAMQLNEEALTKT 582
Cdd:pfam14915   1 NCMLQDEIAMLRLEIDTIKNQNQEKEKKYLEDIEILKEKNDDLQKTLKLNEETLTKT 57
Ank_2 pfam12796
Ankyrin repeats (3 copies);
143-236 1.95e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 74.77  E-value: 1.95e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792284  143 LHRAAWWGKVprkDLIVML--RDTDMNKRDKEKRTALHLASANGNSEVVQLLLDrRCQLNVlDNKKRTALIKAIQCQEDE 220
Cdd:pfam12796   1 LHLAAKNGNL---ELVKLLleNGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNL-KDNGRTALHYAARSGHLE 75

                          90
                  ....*....|....*.
gi 153792284  221 CVLMLLEHGADRNIPD 236
Cdd:pfam12796  76 IVKLLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 165-357 4.64e-16

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 80.84  E-value: 4.64e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792284 165 DMNKRDKEKRTALHLASANGNS---EVVQLLLDRRCQLNVLDNKKRTALIKAIQCQEDECVL-MLLEHGADRNIPDEYGN 240
Cdd:PHA03095  39 DVNFRGEYGKTPLHLYLHYSSEkvkDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDVIkLLIKAGADVNAKDKVGR 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792284 241 TALHyaIY----NEDKLMAKALLLYGADIESKNKCGLTPL--LLGVHEQKQQVVKFLIKKKANLNVLDRYGRTAL----- 309
Cdd:PHA03095 119 TPLH--VYlsgfNINPKVIRLLLRKGADVNALDLYGMTPLavLLKSRNANVELLRLLIDAGADVYAVDDRFRSLLhhhlq 196

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792284 310 ------------ILAVCCGSA--------------------SIVNLLLEQNVDVSSQDLSGQTAREYAVSSHHHVICELL 357
Cdd:PHA03095 197 sfkprarivrelIRAGCDPAAtdmlgntplhsmatgssckrSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRL 276
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 158-304 6.82e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 80.09  E-value: 6.82e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792284 158 IVMLRDTDMNKRDKEKRTALHLASAN--GNSEVVQLLLDRRCQLNVLDNKKRTALIKAIQCQEDEC-------------- 221
Cdd:PHA03100  91 LLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLkilkllidkgvdin 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792284 222 ----VLMLLEHGADRNIPDEYGNTALHYAIYNEDKLMAKALLLYGADIESKNKCGLTPLLLGVHEQKQQVVKFLIKKKAN 297
Cdd:PHA03100 171 aknrVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPS 250


                 ....*..
gi 153792284 298 LNVLDRY 304
Cdd:PHA03100 251 IKTIIET 257
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 158-357 6.63e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 76.93  E-value: 6.63e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792284 158 IVMLRDTDMNKRDKEKRTALHLASANGNSEVVQLLLDRRCQLNVLDNKKRTALIKAIQ---------------------- 215
Cdd:PHA02874  20 IIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKigahdiikllidngvdtsilpi 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792284 216 -CQEDECVLMLLEHGADRNIPDEYGNTALHYAIYNEDKLMAKALLLYGADIESKNKCGLTPLLLGVHEQKQQVVKFLIKK 294
Cdd:PHA02874 100 pCIEKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEK 179

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 153792284 295 KANLNVLDRYGRTALILAVCCGSASIVNLLLEQNVDVSSQDLSGQTAREYAVSSHHHVIcELL 357
Cdd:PHA02874 180 GAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAI-ELL 241
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 165-360 2.66e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 75.87  E-value: 2.66e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792284 165 DMNKRDKEKRTALHLASANGNSEVVQLLLDRRCQLNVLD-----------------------------NKKRTALIKAIQ 215
Cdd:PHA02876 170 DVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIAlddlsvlecavdsknidtikaiidnrsniNKNDLSLLKAIR 249

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792284 216 CQEDECVLMLLEHGADRNIPDEYGNTALHYAIYNE--DKLMAKaLLLYGADIESKNKCGLTPL-LLGVHEQKQQVVKFLI 292
Cdd:PHA02876 250 NEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPslSRLVPK-LLERGADVNAKNIKGETPLyLMAKNGYDTENIRTLI 328

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 153792284 293 KKKANLNVLDRYGRTALILAVCCG-SASIVNLLLEQNVDVSSQDLSGQTAREYAVSSHHHVICELLSDY 360
Cdd:PHA02876 329 MLGADVNAADRLYITPLHQASTLDrNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDY 397
PHA03095 PHA03095
ankyrin-like protein; Provisional
 165-328 3.48e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 75.06  E-value: 3.48e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792284 165 DMNKRDKEKRTALH--LASANGNSEVVQLLLDRRCQLNVLDNKKRTAL-IKAIQCQEDECVL-MLLEHGADRNIPDEYGN 240
Cdd:PHA03095 144 DVNALDLYGMTPLAvlLKSRNANVELLRLLIDAGADVYAVDDRFRSLLhHHLQSFKPRARIVrELIRAGCDPAATDMLGN 223

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792284 241 TALHY-AIYNEDK--LMAKaLLLYGADIESKNKCGLTPLLLGVHEQKQQVVKFLIKKKANLNVLDRYGRTALILAVCCGS 317
Cdd:PHA03095 224 TPLHSmATGSSCKrsLVLP-LLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNN 302

                        170
                 ....*....|.
gi 153792284 318 ASIVNLLLEQN 328
Cdd:PHA03095 303 GRAVRAALAKN 313
PHA03095 PHA03095
ankyrin-like protein; Provisional
 165-353 1.92e-13

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 72.75  E-value: 1.92e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792284 165 DMNKRDKEKRTALH--LASANGNSEVVQLLLDRRCQLNVLDNKKRT---ALIKAIQCqEDECVLMLLEHGADRNIPDEYG 239
Cdd:PHA03095 109 DVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTplaVLLKSRNA-NVELLRLLIDAGADVYAVDDRF 187

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792284 240 NTALHY-AIY---NEDKLmaKALLLYGADIESKNKCGLTPL--LLGVHEQKQQVVKFLIKKKANLNVLDRYGRTALILAV 313
Cdd:PHA03095 188 RSLLHHhLQSfkpRARIV--RELIRAGCDPAATDMLGNTPLhsMATGSSCKRSLVLPLLIAGISINARNRYGQTPLHYAA 265

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 153792284 314 CCGSASIVNLLLEQNVDVSSQDLSGQTAREYAVSSHHHVI 353
Cdd:PHA03095 266 VFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRA 305
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 185-346 8.90e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 70.38  E-value: 8.90e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792284 185 NSEVVQLLLDRRCQLNVLDNKKRTALIKAIQCQEDECVLMLLEHGADRNIPDEYGNTALHYAIYNEDKLMAKALLLYGAD 264
Cdd:PHA02874 103 EKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAY 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792284 265 IESKNKCGLTPLLLGVHEQKQQVVKFLIKKKANLNVLDRYGRTALILAVcCGSASIVNLLLeQNVDVSSQDLSGQTAREY 344
Cdd:PHA02874 183 ANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAI-IHNRSAIELLI-NNASINDQDIDGSTPLHH 260


                 ..
gi 153792284 345 AV 346
Cdd:PHA02874 261 AI 262
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
222-357 3.25e-12

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 67.29  E-value: 3.25e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792284 222 VLMLLEHGADRNIPDEYGNTALHYAIYNEDKLMAKALLLYGADIESKNKCGLTPLLLGVHEQKQQVVKFLIKKKANLNVL 301
Cdd:COG0666    4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 153792284 302 DRYGRTALILAVCCGSASIVNLLLEQNVDVSSQDLSGQTAREYAVSSHHHVICELL 357
Cdd:COG0666   84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLL 139
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 143-301 7.10e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 67.71  E-value: 7.10e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792284 143 LHRAAWWGKVPRKDLIVMLRDTDMNKRDKEKRTALHLASANGNSEVVQLLLDRRCQLNVLDNKKRTALIKAIQCQEDECV 222
Cdd:PHA02875  72 LHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGI 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792284 223 LMLLEHGADRNIPDEYGNTALHYAIYNEDKLMAKALLLYGADIE--SKNKCgLTPLLLGVHEQKQQVVKFLIKKKANLNV 300
Cdd:PHA02875 152 ELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDyfGKNGC-VAALCYAIENNKIDIVRLFIKRGADCNI 230


                 .
gi 153792284 301 L 301
Cdd:PHA02875 231 M 231
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 174-330 7.97e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 67.32  E-value: 7.97e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792284 174 RTALHLASANGNSEVVQLLLDRRCQLN-VLDNKKRTALIKAIQCQEDECVLMLLEHGADRNIPDEYGNTALHYAIYNEDK 252
Cdd:PHA02875  69 ESELHDAVEEGDVKAVEELLDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDI 148

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 153792284 253 LMAKALLLYGADIESKNKCGLTPLLLGVHEQKQQVVKFLIKKKANLNVLDRYGR-TALILAVCCGSASIVNLLLEQNVD 330
Cdd:PHA02875 149 KGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGAD 227
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 180-343 1.51e-11

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 67.20  E-value: 1.51e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792284 180 ASANGNSEVVQLLLDRRCQLNVLDNKKRTAL-IKAIQCQEDeCVLMLLEHGADRNIPDEYGNTAL-------HYAIYNed 251
Cdd:PLN03192 532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLhIAASKGYED-CVLVLLKHACNVHIRDANGNTALwnaisakHHKIFR-- 608

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792284 252 klmakalLLYGADIESKNKCGLTPLLLGVHEQKQQVVKFLIKKKANLNVLDRYGRTALILAVCCGSASIVNLLLEQNVDV 331
Cdd:PLN03192 609 -------ILYHFASISDPHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681

                        170
                 ....*....|....*.
gi 153792284 332 SS----QDLSGQTARE 343
Cdd:PLN03192 682 DKantdDDFSPTELRE 697
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 143-360 1.58e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 67.01  E-value: 1.58e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792284 143 LHRAAWWGKVPRKDLIVMLRDTDMNKRDKEKRTALHLASANG-NSEVVQLLLDRRCQLNVLDNKKRTALIKAIQCQED-E 220
Cdd:PHA02876 277 LHHASQAPSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAADRLYITPLHQASTLDRNkD 356

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792284 221 CVLMLLEHGADRNIPDEYGNTALHYAIYNEDKLMAKALLLYGADIESKNK----------CGLTPLLlgvheqkqqVVKF 290
Cdd:PHA02876 357 IVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQkigtalhfalCGTNPYM---------SVKT 427

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153792284 291 LIKKKANLNVLDRYGRTALILAvCCGSA--SIVNLLLEQNVDVSSQDLSGQTAREYAVSshHHVICELLSDY 360
Cdd:PHA02876 428 LIDRGANVNSKNKDLSTPLHYA-CKKNCklDVIEMLLDNGADVNAINIQNQYPLLIALE--YHGIVNILLHY 496
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 165-280 1.95e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 66.44  E-value: 1.95e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792284 165 DMNKRDKEK-RTALHLASANGNSEVVQLLLDRRCQLNVLDNKKRTALIKAIQCQEDECVLMLLEHGADRNIPDEYGNTAL 243
Cdd:PHA02878 159 DINMKDRHKgNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPL 238

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153792284 244 HYA-----------------------------------IYNEDKLmaKALLLYGADIESKNKCGLTPLLLGV 280
Cdd:PHA02878 239 HISvgyckdydilklllehgvdvnaksyilgltalhssIKSERKL--KLLLEYGADINSLNSYKLTPLSSAV 308
Ank_2 pfam12796
Ankyrin repeats (3 copies);
287-367 4.56e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 59.36  E-value: 4.56e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792284  287 VVKFLIKKKANLNVLDRYGRTALILAVCCGSASIVNLLLEqNVDVSSQDlSGQTAREYAVSSHHHVICELLSDYKEKQML 366
Cdd:pfam12796  12 LVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVKLLLEKGADINV 89


                  .
gi 153792284  367 K 367
Cdd:pfam12796  90 K 90
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 156-298 9.48e-11

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 64.89  E-value: 9.48e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792284 156 DLIVMLRDTDMNkrDKEKRTALHLASANGNSEVVQLLLDRRCQLNVLDNKKRTALIKAIQCQEDEcVLMLLEHGADRNIP 235
Cdd:PLN03192 543 ELLKAKLDPDIG--DSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHK-IFRILYHFASISDP 619

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 153792284 236 DEYGNTaLHYAIYNEDKLMAKALLLYGADIESKNKCGLTPLLLGVHEQKQQVVKFLIKKKANL 298
Cdd:PLN03192 620 HAAGDL-LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 163-340 4.09e-10

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 62.34  E-value: 4.09e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792284 163 DTDMNKRDKEKRTALHLASANGNSEVVQLLLdrrcqlnvldnkkrtalikaiqcqedECVLMLLehgadrNIP---DEY- 238
Cdd:cd22192   41 SCDLFQRGALGETALHVAALYDNLEAAVVLM--------------------------EAAPELV------NEPmtsDLYq 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792284 239 GNTALHYAIYNEDKLMAKALLLYGADIESKNKCGLtplllgvheqkqqvvkFLIKKKANLNVldrYGRTALILAVCCGSA 318
Cdd:cd22192   89 GETALHIAVVNQNLNLVRELIARGADVVSPRATGT----------------FFRPGPKNLIY---YGEHPLSFAACVGNE 149

                        170       180
                 ....*....|....*....|..
gi 153792284 319 SIVNLLLEQNVDVSSQDLSGQT 340
Cdd:cd22192  150 EIVRLLIEHGADIRAQDSLGNT 171
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 175-331 7.07e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 61.16  E-value: 7.07e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792284 175 TALHLASANGNSEVVQLLLDRRCQLNVLDNKKRTALIKAIQCQEDECVLMLLEHGADRN-IPDEYGNTALHYAIYNEDKL 253
Cdd:PHA02875  37 SPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADdVFYKDGMTPLHLATILKKLD 116

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 153792284 254 MAKALLLYGADIESKNKCGLTPLLLGVHEQKQQVVKFLIKKKANLNVLDRYGRTALILAVCCGSASIVNLLLEQNVDV 331
Cdd:PHA02875 117 IMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANI 194
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 174-359 3.70e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 58.85  E-value: 3.70e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792284 174 RTALHLASANGNSEVVQLLLDRRCQLNVLDNKKRTALIKAIQCQEDECVLMLLEHGA--DRNIPDEygNTALHYAIYNED 251
Cdd:PHA02875   3 QVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAipDVKYPDI--ESELHDAVEEGD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792284 252 KLMAKALLLYGADIESK-NKCGLTPLLLGVHEQKQQVVKFLIKKKANLNVLDRYGRTALILAVCCGSASIVNLLLEQNVD 330
Cdd:PHA02875  81 VKAVEELLDLGKFADDVfYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKAC 160

                        170       180
                 ....*....|....*....|....*....
gi 153792284 331 VSSQDLSGQTAREYAVSSHHHVICELLSD 359
Cdd:PHA02875 161 LDIEDCCGCTPLIIAMAKGDIAICKMLLD 189
PHA03095 PHA03095
ankyrin-like protein; Provisional
 165-303 1.09e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 57.73  E-value: 1.09e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792284 165 DMNKRDKEKRTALH--LASANGNSEVVQLLLDRRCQLNVLDNKKRTAL-IKAIQCQ-EDECVLMLLEHGADRNIPDEYGN 240
Cdd:PHA03095 179 DVYAVDDRFRSLLHhhLQSFKPRARIVRELIRAGCDPAATDMLGNTPLhSMATGSScKRSLVLPLLIAGISINARNRYGQ 258

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 153792284 241 TALHYA-IYNEDKLMAKaLLLYGADIESKNKCGLTPLLLGVHEQKQQVVKFLIKKKANLNVLDR 303
Cdd:PHA03095 259 TPLHYAaVFNNPRACRR-LIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVAA 321
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 174-362 1.36e-08

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 57.78  E-value: 1.36e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792284  174 RTAL-HLASANGNSEVVQLLLDRRCQLNVLDNKKRTALIKAIQCQEDECVLMLLEHGADRNIP-------DEY--GNTAL 243
Cdd:TIGR00870  53 RSALfVAAIENENLELTELLLNLSCRGAVGDTLLHAISLEYVDAVEAILLHLLAAFRKSGPLElandqytSEFtpGITAL 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792284  244 HYAIYNEDKLMAKALLLYGADIESKNKCgltplllgvheqkqqvVKFLIKKKANLNvldRYGRTALILAVCCGSASIVNL 323
Cdd:TIGR00870 133 HLAAHRQNYEIVKLLLERGASVPARACG----------------DFFVKSQGVDSF---YHGESPLNAAACLGSPSIVAL 193

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 153792284  324 LLEQNVDVSSQDLSGQTAREYAVsshhhVICELLSDYKE 362
Cdd:TIGR00870 194 LSEDPADILTADSLGNTLLHLLV-----MENEFKAEYEE 227
Ank_5 pfam13857
Ankyrin repeats (many copies);
192-246 1.40e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 51.19  E-value: 1.40e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 153792284  192 LLDRR-CQLNVLDNKKRTALIKAIQCQEDECVLMLLEHGADRNIPDEYGNTALHYA 246
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
207-259 4.59e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.58  E-value: 4.59e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 153792284  207 RTALIKAIQCQEDECVLMLLEHGADRNIPDEYGNTALHYAIYNEDKLMAKALL 259
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 217-340 5.34e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 55.84  E-value: 5.34e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792284 217 QEDECVL--MLLEHGADRNIPDEYGNTALHYAIYNEDKLMAKALLLYGADIESKNKCGLTPLLLGVHEQKQQVVKFLIKK 294
Cdd:PHA02876 154 QQDELLIaeMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDN 233

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 153792284 295 KANL-----------------------------NVLDRYGRTALILAVCCGSAS-IVNLLLEQNVDVSSQDLSGQT 340
Cdd:PHA02876 234 RSNInkndlsllkairnedletslllydagfsvNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGET 309
Ank_5 pfam13857
Ankyrin repeats (many copies);
225-276 2.60e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 47.73  E-value: 2.60e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 153792284  225 LLEHG-ADRNIPDEYGNTALHYAIYNEDKLMAKALLLYGADIESKNKCGLTPL 276
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
Ank_5 pfam13857
Ankyrin repeats (many copies);
165-213 3.42e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 47.34  E-value: 3.42e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 153792284  165 DMNKRDKEKRTALHLASANGNSEVVQLLLDRRCQLNVLDNKKRTALIKA 213
Cdd:pfam13857   8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 175-295 4.65e-07

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 52.71  E-value: 4.65e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792284 175 TALHLASANGNSEVVQLLLDRRCQLN------VLDNKKRTALI---------KAIQCQEdECVLMLLEHGADRNIPDEYG 239
Cdd:cd22192   91 TALHIAVVNQNLNLVRELIARGADVVspratgTFFRPGPKNLIyygehplsfAACVGNE-EIVRLLIEHGADIRAQDSLG 169

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 153792284 240 NTALHYAIYNEDKLMAKAL--LLYGADIES--------KNKCGLTPLLLGVHEQKQQVVKFLIKKK 295
Cdd:cd22192  170 NTVLHILVLQPNKTFACQMydLILSYDKEDdlqpldlvPNNQGLTPFKLAAKEGNIVMFQHLVQKR 235
Ank_4 pfam13637
Ankyrin repeats (many copies);
143-193 7.73e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.11  E-value: 7.73e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 153792284  143 LHRAAWWGKVprkDLIVMLRDT--DMNKRDKEKRTALHLASANGNSEVVQLLL 193
Cdd:pfam13637   5 LHAAAASGHL---ELLRLLLEKgaDINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
239-292 8.04e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.11  E-value: 8.04e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 153792284  239 GNTALHYAIYNEDKLMAKALLLYGADIESKNKCGLTPLLLGVHEQKQQVVKFLI 292
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
296-345 9.22e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.19  E-value: 9.22e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 153792284  296 ANLNVLDRYGRTALILAVCCGSASIVNLLLEQNVDVSSQDLSGQTAREYA 345
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02798 PHA02798
ankyrin-like protein; Provisional
 157-330 1.18e-06

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 51.37  E-value: 1.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792284 157 LIVMLRDTDMNKRDKEKRTALHLASANG---NSEVVQLLLDRRCQLNVLDNKKRTALIKAIQ--CQED-ECVLMLLEHGA 230
Cdd:PHA02798  93 KILIENGADINKKNSDGETPLYCLLSNGyinNLEILLFMIENGADTTLLDKDGFTMLQVYLQsnHHIDiEIIKLLLEKGV 172

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792284 231 DRN-IPDEYGNTALH-YAIYN---------------------EDKLMAKALLLY---------------------GADIE 266
Cdd:PHA02798 173 DINtHNNKEKYDTLHcYFKYNidridadilklfvdngfiinkENKSHKKKFMEYlnsllydnkrfkknildfifsYIDIN 252

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 153792284 267 SKNKCGLTPLLLGVHEQKQQVVKFLIKKKANLNVLDRYGRTALILAVCCGSASIVNLLLEQNVD 330
Cdd:PHA02798 253 QVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFENESKFIFNSILNKKPN 316
Ank_4 pfam13637
Ankyrin repeats (many copies);
272-325 1.37e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.34  E-value: 1.37e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 153792284  272 GLTPLLLGVHEQKQQVVKFLIKKKANLNVLDRYGRTALILAVCCGSASIVNLLL 325
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_2 pfam12796
Ankyrin repeats (3 copies);
309-365 2.11e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 46.26  E-value: 2.11e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 153792284  309 LILAVCCGSASIVNLLLEQNVDVSSQDLSGQTAREYAVSSHHHVICELLSDYKEKQM 365
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL 57
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 207-340 6.57e-06

Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 49.11  E-value: 6.57e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792284 207 RTALIKAI---QCQEDECVLMLLEHGADRNIP---------DEY--GNTALHYAIYNEDKLMAKALLLYGADIESKnKCG 272
Cdd:cd21882   27 KTCLHKAAlnlNDGVNEAIMLLLEAAPDSGNPkelvnapctDEFyqGQTALHIAIENRNLNLVRLLVENGADVSAR-ATG 105

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153792284 273 ltplllgvheqkqqvvKFLIKKKANLNVldrYGRTALILAVCCGSASIVNLLLE---QNVDVSSQDLSGQT 340
Cdd:cd21882  106 ----------------RFFRKSPGNLFY---FGELPLSLAACTNQEEIVRLLLEngaQPAALEAQDSLGNT 157
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 172-295 9.45e-06

Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 48.72  E-value: 9.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792284 172 EKRTALHLASANGNSEVVQLLLDRRCQLNVLDNK---KRTA----------LIKAIQCQEDECVLMLLEHGAD-RNIP-- 235
Cdd:cd21882   72 QGQTALHIAIENRNLNLVRLLVENGADVSARATGrffRKSPgnlfyfgelpLSLAACTNQEEIVRLLLENGAQpAALEaq 151

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 153792284 236 DEYGNTALHYAIYNEDKL---------MAKALLLYGADI-------ESKNKCGLTPLLLGVHEQKQQVVKFLIKKK 295
Cdd:cd21882  152 DSLGNTVLHALVLQADNTpensafvcqMYNLLLSYGAHLdptqqleEIPNHQGLTPLKLAAVEGKIVMFQHILQRE 227
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 192-361 1.14e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 48.12  E-value: 1.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792284 192 LLDRRCQLNVLDNKKRTALIKAIQCQEDECVLMLLEHGADRNIPDEYGNTALHY-----AIYNEDKLMAKALLLYGADIE 266
Cdd:PHA03100  21 IIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYlsnikYNLTDVKEIVKLLLEYGANVN 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792284 267 SKNKCGLTPLLlgvheqkqqvvkFLIKKKANlnvldrygrtalilavccgSASIVNLLLEQNVDVSSQDLSGQTAREYAV 346
Cdd:PHA03100 101 APDNNGITPLL------------YAISKKSN-------------------SYSIVEYLLDNGANVNIKNSDGENLLHLYL 149

                        170
                 ....*....|....*..
gi 153792284 347 SSHHHV--ICELLSDYK 361
Cdd:PHA03100 150 ESNKIDlkILKLLIDKG 166
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 207-340 2.11e-05

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are thermo-sensing channels that function directly in temperature-sensing and nociception; they share substantial structural and functional properties. Transient Receptor Potential (TRP) ion channels activated by temperature (thermo TRPs) are important molecular players in acute, inflammatory, and chronic pain states. So far, 11 TRP channels in mammalian cells have been identified as thermosensitive TRP (thermo-TRP) channels. TRPV1-4 channels are activated by different heat temperatures, for example, TRPV1 and TRPV2 are activated by high temperatures (>43C and >55C, respectively). TRPV1-4 belong to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 47.48  E-value: 2.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792284 207 RTALIKA---IQCQEDECVLMLLEHGADRNIPDEY-----------GNTALHYAIYNEDKLMAKALLLYGADIESKnKCG 272
Cdd:cd22193   30 KTCLMKAllnLNPGTNDTIRILLDIAEKTDNLKRFinaeytdeyyeGQTALHIAIERRQGDIVALLVENGADVHAH-AKG 108

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153792284 273 ltplllgvheqkqqvvKFLIKKKANLNVLdrYGRTALILAVCCGSASIVNLLLE---QNVDVSSQDLSGQT 340
Cdd:cd22193  109 ----------------RFFQPKYQGEGFY--FGELPLSLAACTNQPDIVQYLLEnehQPADIEAQDSRGNT 161
PHA02946 PHA02946
ankyin-like protein; Provisional
 185-354 2.58e-05

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 46.97  E-value: 2.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792284 185 NSEVVQLLLDRRCQLNVLDNKKRTALIKAIQCQEDECVLMLLEHGADRNIPDEYGNTALHYAIYNEDKLMAKALLL--YG 262
Cdd:PHA02946  51 DERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEVIERINLLvqYG 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792284 263 ADI-ESKNKCGLTPlLLGVHEQKQQVVKFLIKKKANLNVLDRYGRTALILAVCCGS--ASIVNLLLEQNVDVSSQDLSGQ 339
Cdd:PHA02946 131 AKInNSVDEEGCGP-LLACTDPSERVFKKIMSIGFEARIVDKFGKNHIHRHLMSDNpkASTISWMMKLGISPSKPDHDGN 209

                        170
                 ....*....|....*
gi 153792284 340 TAReyavsshhHVIC 354
Cdd:PHA02946 210 TPL--------HIVC 216
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 238-270 4.37e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 40.74  E-value: 4.37e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 153792284  238 YGNTALHYAIYNEDKL-MAKALLLYGADIESKNK 270
Cdd:pfam00023   1 DGNTPLHLAAGRRGNLeIVKLLLSKGADVNARDK 34
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 224-293 1.10e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 45.27  E-value: 1.10e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792284 224 MLLEHGADRNIPDEYGNTALHYAIYNEDKLMAKALLLYGADIESKNKCGLTPLLLGVHEQKQQVVKFLIK 293
Cdd:PTZ00322 100 ILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 165-238 1.71e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.50  E-value: 1.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792284 165 DMNKRDKEKRTALHLASANGNSEVVQLLLDRRCQLNVLDNKKRTALIKAIQCQEDECVLMLLEH------GADRNIPDEY 238
Cdd:PTZ00322 107 DPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHsqchfeLGANAKPDSF 186
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 174-204 3.65e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 38.04  E-value: 3.65e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 153792284  174 RTALHLASA-NGNSEVVQLLLDRRCQLNVLDN 204
Cdd:pfam00023   3 NTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 238-265 3.90e-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: 38.01  E-value: 3.90e-04
                          10        20
                  ....*....|....*....|....*...
gi 153792284  238 YGNTALHYAIYNEDKLMAKALLLYGADI 265
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADI 28
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 288-360 4.10e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 43.35  E-value: 4.10e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 153792284 288 VKFLIKKKANLNVLDRYGRTALILAVCCGSASIVNLLLEQNVDVSSQDLSGQTAREYAVSSHHHVICELLSDY 360
Cdd:PTZ00322  98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 280-350 4.34e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 43.13  E-value: 4.34e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153792284 280 VHEQKQQVVKFLIKKKANLNVLDRYGRTALILAVCCGSASIVNLLLEQNVDVSSQDLSGQTAREYAVSSHH 350
Cdd:PHA02876 153 IQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKN 223
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 238-266 4.52e-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: 37.57  E-value: 4.52e-04
                           10        20
                   ....*....|....*....|....*....
gi 153792284   238 YGNTALHYAIYNEDKLMAKALLLYGADIE 266
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 251-338 7.42e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 42.58  E-value: 7.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792284 251 DKLMAKALLLYGADIESKNKCGLTPLLLGVHEQKQQVVKFLIKKKANLNVLDRYGRTALILAVCCGSASIVNLLLEQNVD 330
Cdd:PTZ00322  94 DAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQC 173


                 ....*...
gi 153792284 331 VSSQDLSG 338
Cdd:PTZ00322 174 HFELGANA 181
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 489-584 8.03e-04

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.12  E-value: 8.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792284 489 SQDEILTNKQKQIEVAEQKMNSELSLSHKKEEDLLRENSVLQEEIAMLRLELDETkhQNQLRENKilEEIESVKEKTDKL 568
Cdd:COG3883   16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKL--QAEIAEAE--AEIEERREELGER 91

                         90
                 ....*....|....*.
gi 153792284 569 LRAMQLNEEALTKTNI 584
Cdd:COG3883   92 ARALYRSGGSVSYLDV 107
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 470-575 1.30e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 41.29  E-value: 1.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792284 470 SDEQNDTRKQLSEEQNTgISQdeiLTNKQKQIEVAEQKMNSELSLSHKKEEDLLRENSVLQEEIAMLRLELDEtkhqNQL 549
Cdd:COG4942   19 ADAAAEAEAELEQLQQE-IAE---LEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE----LEK 90

                         90       100
                 ....*....|....*....|....*.
gi 153792284 550 RENKILEEIESVKEKTDKLLRAMQLN 575
Cdd:COG4942   91 EIAELRAELEAQKEELAELLRALYRL 116
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 174-201 1.31e-03

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 36.47  E-value: 1.31e-03
                          10        20
                  ....*....|....*....|....*...
gi 153792284  174 RTALHLASANGNSEVVQLLLDRRCQLNV 201
Cdd:pfam13606   3 NTPLHLAARNGRLEIVKLLLENGADINA 30
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 342-579 1.51e-03

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 41.65  E-value: 1.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792284  342 REYAVSSHHhvicELLSDYKEKQMLKISSENSNPEQD--------LKLTSEEESQRLKVSENSQPEKMSQEPEINKDCDR 413
Cdd:pfam17380 331 RQAAIYAEQ----ERMAMERERELERIRQEERKRELErirqeeiaMEISRMRELERLQMERQQKNERVRQELEAARKVKI 406

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792284  414 EVEEEIKKHGSNPVGLPENLTNGASAGNGDDGLIPQRRSRKPENQQFPDTEN----EEYHSDEQNDTRK----------- 478
Cdd:pfam17380 407 LEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERqqqvERLRQQEEERKRKklelekekrdr 486

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792284  479 QLSEEQNTGISQDEILTNKQKQIEVAEQKmnselSLSHKKEEDllRENSVLQEEiaMLRLELDETKHQNQLRENK-ILEE 557
Cdd:pfam17380 487 KRAEEQRRKILEKELEERKQAMIEEERKR-----KLLEKEMEE--RQKAIYEEE--RRREAEEERRKQQEMEERRrIQEQ 557

                         250       260
                  ....*....|....*....|..
gi 153792284  558 IESVKEKTDKlLRAMQLNEEAL 579
Cdd:pfam17380 558 MRKATEERSR-LEAMEREREMM 578
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 291-357 1.76e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 41.39  E-value: 1.76e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 153792284 291 LIKKKANLNVLDRYGRTALILAVCCGSASIVNLLLEQNVDVSSQDLSGQTAREYAVSSHHHVICELL 357
Cdd:PLN03192 544 LLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRIL 610
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 172-201 1.77e-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: 36.03  E-value: 1.77e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 153792284   172 EKRTALHLASANGNSEVVQLLLDRRCQLNV 201
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02791 PHA02791
ankyrin-like protein; Provisional
 155-247 1.78e-03

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 40.80  E-value: 1.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792284 155 KDLIVMLRDTDMNKRDKEKRTALHLASANGNSEVVQLLLDRRCQLNVLDNKkrTALIKAIQCQEDECVLMLLEHGADRNI 234
Cdd:PHA02791  12 KQLKSFLSSKDAFKADVHGHSALYYAIADNNVRLVCTLLNAGALKNLLENE--FPLHQAATLEDTKIVKILLFSGMDDSQ 89

                         90
                 ....*....|...
gi 153792284 235 PDEYGNTALHYAI 247
Cdd:PHA02791  90 FDDKGNTALYYAV 102
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 165-340 2.10e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely related to TRPV1, sharing high sequence identity (>50%), but TRPV2 shows a higher temperature threshold and sensitivity for activation than TRPV1. TRPV2 can be stimulated by ligands or lipids, and is involved in osmosensation and mechanosensation. TRPV2 is expressed in both neuronal and non-neuronal tissues, and it has been implicated in diverse physiological and pathophysiological processes, including cardiac-structure maintenance, innate immunity, and cancer. TRPV2 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411981 [Multi-domain]  Cd Length: 640  Bit Score: 40.99  E-value: 2.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792284 165 DMNKRDKEKrtaLHLASANGNSEVVQLLLD--RRCQLNVLDNK------KRTALIKAIQCQED---ECVLMLLEHGADRN 233
Cdd:cd22197    1 DPNRFDRDR---LFSVVSRGNPEELAGLLEylRRTSKYLTDSEytegstGKTCLMKAVLNLQDgvnACIMPLLEIDKDSG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792284 234 IP---------DEY--GNTALHYAIYNEDKLMAKALLLYGADIESKNKcgltplllGVHEQKQQVVKFLikkkanlnvld 302
Cdd:cd22197   78 NPkplvnaqctDEYyrGHSALHIAIEKRSLQCVKLLVENGADVHARAC--------GRFFQKKQGTCFY----------- 138

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 153792284 303 rYGRTALILAVCCGSASIVNLLLEQNVDVSS---QDLSGQT 340
Cdd:cd22197  139 -FGELPLSLAACTKQWDVVNYLLENPHQPASlqaQDSLGNT 178
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 304-335 2.36e-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: 35.73  E-value: 2.36e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 153792284  304 YGRTALILAVC-CGSASIVNLLLEQNVDVSSQD 335
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 164-340 2.60e-03

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 40.90  E-value: 2.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792284 164 TDMNKRDKEKRtaLHLASANGNSEVVQLL-----LDRRC-----------QLNVLDNKKrTALIKA---IQCQEDECVLM 224
Cdd:cd22194   39 AKEEQRDKKKR--LKKVSEAAVEELGELLkelkdLSRRRrktdvpdflmhKLTASDTGK-TCLMKAllnINENTKEIVRI 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792284 225 LLEHGADRNIPD-----EY------GNTALHYAIYNEDKLMAKALLLYGADIESKNKcgltplllGVHEQ-KQQVVKFLi 292
Cdd:cd22194  116 LLAFAEENGILDrfinaEYteeayeGQTALNIAIERRQGDIVKLLIAKGADVNAHAK--------GVFFNpKYKHEGFY- 186

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 153792284 293 kkkanlnvldrYGRTALILAVCCGSASIVNLLLEQ-NVDVSSQDLSGQT 340
Cdd:cd22194  187 -----------FGETPLALAACTNQPEIVQLLMEKeSTDITSQDSRGNT 224
PHA02798 PHA02798
ankyrin-like protein; Provisional
 178-309 2.64e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 40.59  E-value: 2.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792284 178 HLASANGNSEVVQLLLDRRCQLNVLDNKKRTALIKAIQCQED-----ECVLMLLEHGADRNIPDEYGNTALhYAIYNEDK 252
Cdd:PHA02798  43 YLQRDSPSTDIVKLFINLGANVNGLDNEYSTPLCTILSNIKDykhmlDIVKILIENGADINKKNSDGETPL-YCLLSNGY 121

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153792284 253 LMAKALLLY----GADIESKNKCGLTPLLLGV---HEQKQQVVKFLIKKKANLNVL-DRYGRTAL 309
Cdd:PHA02798 122 INNLEILLFmienGADTTLLDKDGFTMLQVYLqsnHHIDIEIIKLLLEKGVDINTHnNKEKYDTL 186
PRK00106 PRK00106
ribonuclease Y;
454-573 3.34e-03

ribonuclease Y;


Pssm-ID: 178867 [Multi-domain]  Cd Length: 535  Bit Score: 40.24  E-value: 3.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792284 454 KPENQQFPDTENEEYHSDEQ--NDTRKQLSEEQNTGISQDEILTNKQKQIEVAEQKMNSE-----------LSLSHKKEE 520
Cdd:PRK00106  78 KEEARKYREEIEQEFKSERQelKQIESRLTERATSLDRKDENLSSKEKTLESKEQSLTDKskhidereeqvEKLEEQKKA 157

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 153792284 521 DLLRENSVLQEEIAMLRLELDETKHQNQLrENKILEEIESVKEKTDK-----LLRAMQ 573
Cdd:PRK00106 158 ELERVAALSQAEAREIILAETENKLTHEI-ATRIREAEREVKDRSDKmakdlLAQAMQ 214
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 470-583 3.92e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 40.00  E-value: 3.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792284  470 SDEQNDTRKQLSEEQNTGISQDEILTNKQKQIevaeQKMNSELS-LSHKKEEDLLREnsvLQEEIAMLRLELDETkhQNQ 548
Cdd:TIGR04523 259 KDEQNKIKKQLSEKQKELEQNNKKIKELEKQL----NQLKSEISdLNNQKEQDWNKE---LKSELKNQEKKLEEI--QNQ 329

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 153792284  549 LREN-----KILEEIESV-KEKTDKLLRAMQLNEEALTKTN 583
Cdd:TIGR04523 330 ISQNnkiisQLNEQISQLkKELTNSESENSEKQRELEEKQN 370
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 222-276 5.21e-03

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 39.90  E-value: 5.21e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 153792284 222 VLMLLEHGADRNIPDEYGNTALHY-------------AIYNEDKL-MAKALLLYGADIESKNKCGLTPL 276
Cdd:PHA02716 335 IKLLHEYGNDLNEPDNIGNTVLHTylsmlsvvnildpETDNDIRLdVIQCLISLGADITAVNCLGYTPL 403
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 188-278 8.75e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 38.43  E-value: 8.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792284 188 VVQLLLDRRCQLNVLDNKKRTALIKAIQCQEDECVLMLLEHGADRNIPDEYGN-TALHYAIYNEDKLMAKALLLYGADIE 266
Cdd:PHA02884  52 ILKLGADPEAPFPLSENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKiTPLYISVLHGCLKCLEILLSYGADIN 131

                         90
                 ....*....|..
gi 153792284 267 SKNKCGLTPLLL 278
Cdd:PHA02884 132 IQTNDMVTPIEL 143
 
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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