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Conserved domains on  [gi|1958681282|ref|XP_038949682|]
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ankyrin repeat domain-containing protein 26-like isoform X3 [Rattus norvegicus]

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];
25-180 1.51e-43

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 160.12  E-value: 1.51e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282   25 LHRAASVGAVATVERFLTFRLNgVNDTDKRNRTALHYACAHGHLGVVTLLIERNCNVNARDDDKCTPLIKASQHQREDCV 104
Cdd:COG0666     91 LHAAARNGDLEIVKLLLEAGAD-VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIV 169

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958681282  105 AVLLQHGADPNAVDALGNTALHYAVHSENASIASQLLEHSANIEARTKEGFTPLSLAVQQNRGPIVELLIEKGANK 180
Cdd:COG0666    170 KLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADL 245
DUF3496 super family cl13439
Domain of unknown function (DUF3496); This presumed domain is functionally uncharacterized. ...
 884-984 9.31e-21

Domain of unknown function (DUF3496); This presumed domain is functionally uncharacterized. This domain is found in eukaryotes. This domain is about 110 amino acids in length.


The actual alignment was detected with superfamily member pfam12001:

Pssm-ID: 463425 [Multi-domain]  Cd Length: 109  Bit Score: 88.18  E-value: 9.31e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282  884 MSQIILRVKSLESRLPEIK-SHVDSTRREMEKHKQLYVEENKSRKSLFNTLSKTVEKLEVSRAKLMQLNQQKMTMETILS 962
Cdd:pfam12001    1 RSQMELRIKDLESELSKMKtSQEDSNKIELEKYKQLYLEELKVRKSLSNKLNKTNERLAEVSTKLLVEKQQNRSLLSTLT 80

                           90       100
                   ....*....|....*....|..
gi 1958681282  963 SLPAQQSPLVAKFNPAVGHNPS 984
Cdd:pfam12001   81 TRPVLESPCVGNLNNSLVLNRN 102
SCP-1 super family cl30946
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 642-958 1.26e-04

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


The actual alignment was detected with superfamily member pfam05483:

Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 46.25  E-value: 1.26e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282  642 EVGQHEMSLGNLNMNLKALHDSVTQLQE-AQLQDDPQREgvlSSARMAHLLWKLEVDCLKLEDSVKNQAEEIEELETQLL 720
Cdd:pfam05483  248 QITEKENKMKDLTFLLEESRDKANQLEEkTKLQDENLKE---LIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATK 324

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282  721 TV-ELTGDRKKERDEVT--RSTQSL--------ACALEH----EVEKIE-----------ELEKTLHGFMEVMKIAGKKL 774
Cdd:pfam05483  325 TIcQLTEEKEAQMEELNkaKAAHSFvvtefeatTCSLEEllrtEQQRLEknedqlkiitmELQKKSSELEEMTKFKNNKE 404

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282  775 DECENRELYFYEDMR----NRTFETL-------QHEINYLKDTWEpiqcKYLHqDINIQLT-----EQELLK----IKSE 834
Cdd:pfam05483  405 VELEELKKILAEDEKlldeKKQFEKIaeelkgkEQELIFLLQARE----KEIH-DLEIQLTaiktsEEHYLKevedLKTE 479

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282  835 QENyEHLHQTQ--GNVEKEVLTLRGLVQESVTQAEEEKKlEKARENNNDSRMSQIILRVKSLESRLPEIKSHVDSTRREM 912
Cdd:pfam05483  480 LEK-EKLKNIEltAHCDKLLLENKELTQEASDMTLELKK-HQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEF 557

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*..
gi 1958681282  913 -EKHKQLYVEENKSRKSLFNTLSKTVEKLEVSRAKLMQLNQQKMTME 958
Cdd:pfam05483  558 iQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIE 604
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
25-180 1.51e-43

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 160.12  E-value: 1.51e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282   25 LHRAASVGAVATVERFLTFRLNgVNDTDKRNRTALHYACAHGHLGVVTLLIERNCNVNARDDDKCTPLIKASQHQREDCV 104
Cdd:COG0666     91 LHAAARNGDLEIVKLLLEAGAD-VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIV 169

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958681282  105 AVLLQHGADPNAVDALGNTALHYAVHSENASIASQLLEHSANIEARTKEGFTPLSLAVQQNRGPIVELLIEKGANK 180
Cdd:COG0666    170 KLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADL 245
DUF3496 pfam12001
Domain of unknown function (DUF3496); This presumed domain is functionally uncharacterized. ...
 884-984 9.31e-21

Domain of unknown function (DUF3496); This presumed domain is functionally uncharacterized. This domain is found in eukaryotes. This domain is about 110 amino acids in length.


Pssm-ID: 463425 [Multi-domain]  Cd Length: 109  Bit Score: 88.18  E-value: 9.31e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282  884 MSQIILRVKSLESRLPEIK-SHVDSTRREMEKHKQLYVEENKSRKSLFNTLSKTVEKLEVSRAKLMQLNQQKMTMETILS 962
Cdd:pfam12001    1 RSQMELRIKDLESELSKMKtSQEDSNKIELEKYKQLYLEELKVRKSLSNKLNKTNERLAEVSTKLLVEKQQNRSLLSTLT 80

                           90       100
                   ....*....|....*....|..
gi 1958681282  963 SLPAQQSPLVAKFNPAVGHNPS 984
Cdd:pfam12001   81 TRPVLESPCVGNLNNSLVLNRN 102
Ank_2 pfam12796
Ankyrin repeats (3 copies);
59-150 1.57e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 87.09  E-value: 1.57e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282   59 LHYACAHGHLGVVTLLIERNCNVNARDDDKCTPLIKASQHQREDCVAVLLQHgADPNAVDAlGNTALHYAVHSENASIAS 138
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78

                           90
                   ....*....|..
gi 1958681282  139 QLLEHSANIEAR 150
Cdd:pfam12796   79 LLLEKGADINVK 90
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 48-174 2.66e-19

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 91.95  E-value: 2.66e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282   48 VNDTDKRNRTALHYACAHGHLGVVTLLIERNCNVNARDDDKCTPLIKASQHQREDCVAVLLQHGADPNAVDALGNTALHY 127
Cdd:PHA02874   117 VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHN 196

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1958681282  128 AVHSENASIASQLLEHSANIEARTKEGFTPLSLAVQQNRGpIVELLI 174
Cdd:PHA02874   197 AAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRS-AIELLI 242
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 57-176 2.36e-09

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: 61.18  E-value: 2.36e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282   57 TALHYACAHGHLGVVTLLIERNCNV-NAR---------DDDKCT----PLIKASQHQREDCVAVLLQHGADPNAVDALGN 122
Cdd:cd22192     91 TALHIAVVNQNLNLVRELIARGADVvSPRatgtffrpgPKNLIYygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGN 170

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958681282  123 TALHYAVHSENASIASQLLEHSANIEA----------RTKEGFTPLSLAVQQNRGPIVELLIEK 176
Cdd:cd22192    171 TVLHILVLQPNKTFACQMYDLILSYDKeddlqpldlvPNNQGLTPFKLAAKEGNIVMFQHLVQK 234
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 48-182 1.32e-07

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: 55.86  E-value: 1.32e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282   48 VNDTDK----RNRTALHYACAHGHLGVVTLLIERNCNVNAR-DDDKC-----TPLIKASQHQ--------REDCVAVLLQ 109
Cdd:TIGR00870  117 ANDQYTseftPGITALHLAAHRQNYEIVKLLLERGASVPARaCGDFFvksqgVDSFYHGESPlnaaaclgSPSIVALLSE 196

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282  110 HGADPNAVDALGNTALHYAV-----HSENASIASQ----------LLEHSANIEA-RTKEGFTPLSLAVQQNRGPIVELL 173
Cdd:TIGR00870  197 DPADILTADSLGNTLLHLLVmenefKAEYEELSCQmynfalslldKLRDSKELEViLNHQGLTPLKLAAKEGRIVLFRLK 276

                          170
                   ....*....|.
gi 1958681282  174 --IEKGANKHT 182
Cdd:TIGR00870  277 laIKYKQKKFV 287
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 54-83 3.70e-05

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: 41.42  E-value: 3.70e-05
                            10        20        30
                    ....*....|....*....|....*....|
gi 1958681282    54 RNRTALHYACAHGHLGVVTLLIERNCNVNA 83
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 642-958 1.26e-04

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 46.25  E-value: 1.26e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282  642 EVGQHEMSLGNLNMNLKALHDSVTQLQE-AQLQDDPQREgvlSSARMAHLLWKLEVDCLKLEDSVKNQAEEIEELETQLL 720
Cdd:pfam05483  248 QITEKENKMKDLTFLLEESRDKANQLEEkTKLQDENLKE---LIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATK 324

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282  721 TV-ELTGDRKKERDEVT--RSTQSL--------ACALEH----EVEKIE-----------ELEKTLHGFMEVMKIAGKKL 774
Cdd:pfam05483  325 TIcQLTEEKEAQMEELNkaKAAHSFvvtefeatTCSLEEllrtEQQRLEknedqlkiitmELQKKSSELEEMTKFKNNKE 404

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282  775 DECENRELYFYEDMR----NRTFETL-------QHEINYLKDTWEpiqcKYLHqDINIQLT-----EQELLK----IKSE 834
Cdd:pfam05483  405 VELEELKKILAEDEKlldeKKQFEKIaeelkgkEQELIFLLQARE----KEIH-DLEIQLTaiktsEEHYLKevedLKTE 479

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282  835 QENyEHLHQTQ--GNVEKEVLTLRGLVQESVTQAEEEKKlEKARENNNDSRMSQIILRVKSLESRLPEIKSHVDSTRREM 912
Cdd:pfam05483  480 LEK-EKLKNIEltAHCDKLLLENKELTQEASDMTLELKK-HQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEF 557

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*..
gi 1958681282  913 -EKHKQLYVEENKSRKSLFNTLSKTVEKLEVSRAKLMQLNQQKMTME 958
Cdd:pfam05483  558 iQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIE 604
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 647-877 9.82e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.12  E-value: 9.82e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282  647 EMSLGNLNMNLKALHDSVTQLqEAQLQDDPQREGVL--SSARMAHLLWKLEVDCLKLEDSVKNQAEEIEELETQLLTV-E 723
Cdd:TIGR02168  301 EQQKQILRERLANLERQLEEL-EAQLEELESKLDELaeELAELEEKLEELKEELESLEAELEELEAELEELESRLEELeE 379

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282  724 LTGDRKKERDEVTRSTQSLACALEHEVEKIEELEKTLHGFMEVMKIAGKKLDECENRELYFYEDMRNRTFETLQHEINYL 803
Cdd:TIGR02168  380 QLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERL 459

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282  804 KDTWEPIQCKYLHQDINIQLTEQELLKIKSE-------QENYEHLHQTQGNVEKEVLTLRGLVQESVTQAEEEKKLEKAR 876
Cdd:TIGR02168  460 EEALEELREELEEAEQALDAAERELAQLQARldslerlQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAI 539


                   .
gi 1958681282  877 E 877
Cdd:TIGR02168  540 E 540
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
540-947 1.05e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.13  E-value: 1.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282  540 RLLEIKNSYGDVLRrEIKKMETKhggVRKELSKITEVLSQPERQETEWGELCNLRSSLKQNENIINDGCFDGKMKTELRG 619
Cdd:PRK03918   297 KLSEFYEEYLDELR-EIEKRLSR---LEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKE 372

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282  620 RERQYHEEFGRSPLYHQCNE-----------EFEVGQHEMSLGNLNMNLKALHDSVTQLQEAQLQ--------DDPQREG 680
Cdd:PRK03918   373 ELERLKKRLTGLTPEKLEKEleelekakeeiEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgrelTEEHRKE 452

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282  681 VLSS------------ARMAHLLWKLEVDCLKLEDSVKNQ---------AEEIEELETQLLTVELTGDRKKERD-----E 734
Cdd:PRK03918   453 LLEEytaelkriekelKEIEEKERKLRKELRELEKVLKKEseliklkelAEQLKELEEKLKKYNLEELEKKAEEyeklkE 532

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282  735 VTRSTQSLACALEHEVEKIEELEKTLHGFMEVMKIAGKKLDECENR--ELYFyedmrnRTFETLQHEINYLkdtwEPIQC 812
Cdd:PRK03918   533 KLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKEleELGF------ESVEELEERLKEL----EPFYN 602

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282  813 KYLHQDINIQLTEQELLKIKSEQENYEHLHQTQGNVEKEVLTLRGLVQE---SVTQAEEEKKLEKARENnnDSRMSQIIL 889
Cdd:PRK03918   603 EYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEElekKYSEEEYEELREEYLEL--SRELAGLRA 680

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958681282  890 RVKSLESRLPEIKSHVDSTRREMEKHKQlYVEENKSrkslfntLSKTVEKLEVSRAKL 947
Cdd:PRK03918   681 ELEELEKRREEIKKTLEKLKEELEEREK-AKKELEK-------LEKALERVEELREKV 730
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 700-950 4.29e-03

Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 41.10  E-value: 4.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282  700 KLEDSVKNQAEEIEELETQLLTVELTGDRKKERDEVTRSTQSLACALEHEVEKIEELEKTLHGFMEVMKIAGKKLDECEN 779
Cdd:COG5185    279 RLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEA 358

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282  780 RELYFYEDMRNRTFETLQHEINYLKDTWEPIQCKYLHQDINIQlteqellkiKSEQENYEHLHQTQGNVEKEVLTLRGLV 859
Cdd:COG5185    359 IKEEIENIVGEVELSKSSEELDSFKDTIESTKESLDEIPQNQR---------GYAQEILATLEDTLKAADRQIEELQRQI 429

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282  860 QESVTQAEEEKKLEKARENNNDSRMSQIILRVKS-LESRLPEIKSHVDSTRRE-MEKHKQLYVEENKSRKSLFNTLSKTV 937
Cdd:COG5185    430 EQATSSNEEVSKLLNELISELNKVMREADEESQSrLEEAYDEINRSVRSKKEDlNEELTQIESRVSTLKATLEKLRAKLE 509

                          250
                   ....*....|...
gi 1958681282  938 EKLEVSRAKLMQL 950
Cdd:COG5185    510 RQLEGVRSKLDQV 522
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
25-180 1.51e-43

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 160.12  E-value: 1.51e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282   25 LHRAASVGAVATVERFLTFRLNgVNDTDKRNRTALHYACAHGHLGVVTLLIERNCNVNARDDDKCTPLIKASQHQREDCV 104
Cdd:COG0666     91 LHAAARNGDLEIVKLLLEAGAD-VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIV 169

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958681282  105 AVLLQHGADPNAVDALGNTALHYAVHSENASIASQLLEHSANIEARTKEGFTPLSLAVQQNRGPIVELLIEKGANK 180
Cdd:COG0666    170 KLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADL 245
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
25-182 6.89e-42

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 155.50  E-value: 6.89e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282   25 LHRAASVGAVATVERFLTFRLNGVNDTDKRNRTALHYACAHGHLGVVTLLIERNCNVNARDDDKCTPLIKASQHQREDCV 104
Cdd:COG0666     57 LLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIV 136

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958681282  105 AVLLQHGADPNAVDALGNTALHYAVHSENASIASQLLEHSANIEARTKEGFTPLSLAVQQNRGPIVELLIEKGANKHT 182
Cdd:COG0666    137 KLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNA 214
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
25-182 8.08e-37

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 140.86  E-value: 8.08e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282   25 LHRAASVGAVATVERFLTfrlNG--VNDTDKRNRTALHYACAHGHLGVVTLLIERNCNVNARDDDKCTPLIKASQHQRED 102
Cdd:COG0666    124 LHLAAYNGNLEIVKLLLE---AGadVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLE 200

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282  103 CVAVLLQHGADPNAVDALGNTALHYAVHSENASIASQLLEHSANIEARTKEGFTPLSLAVQQNRGPIVELLIEKGANKHT 182
Cdd:COG0666    201 IVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAA 280
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
25-179 2.51e-31

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 124.68  E-value: 2.51e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282   25 LHRAASVGAVATVERFLTFRLNGVNDTDKRNRTALHYACAHGHLGVVTLLIERNCNVNARDDDKCTPLIKASQHQREDCV 104
Cdd:COG0666     24 LLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIV 103

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958681282  105 AVLLQHGADPNAVDALGNTALHYAVHSENASIASQLLEHSANIEARTKEGFTPLSLAVQQNRGPIVELLIEKGAN 179
Cdd:COG0666    104 KLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGAD 178
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
25-158 2.42e-21

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 95.41  E-value: 2.42e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282   25 LHRAASVGAVATVERFLTFRLNgVNDTDKRNRTALHYACAHGHLGVVTLLIERNCNVNARDDDKCTPLIKASQHQREDCV 104
Cdd:COG0666    157 LHLAAANGNLEIVKLLLEAGAD-VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIV 235

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1958681282  105 AVLLQHGADPNAVDALGNTALHYAVHSENASIASQLLEHSANIEARTKEGFTPL 158
Cdd:COG0666    236 KLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
DUF3496 pfam12001
Domain of unknown function (DUF3496); This presumed domain is functionally uncharacterized. ...
 884-984 9.31e-21

Domain of unknown function (DUF3496); This presumed domain is functionally uncharacterized. This domain is found in eukaryotes. This domain is about 110 amino acids in length.


Pssm-ID: 463425 [Multi-domain]  Cd Length: 109  Bit Score: 88.18  E-value: 9.31e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282  884 MSQIILRVKSLESRLPEIK-SHVDSTRREMEKHKQLYVEENKSRKSLFNTLSKTVEKLEVSRAKLMQLNQQKMTMETILS 962
Cdd:pfam12001    1 RSQMELRIKDLESELSKMKtSQEDSNKIELEKYKQLYLEELKVRKSLSNKLNKTNERLAEVSTKLLVEKQQNRSLLSTLT 80

                           90       100
                   ....*....|....*....|..
gi 1958681282  963 SLPAQQSPLVAKFNPAVGHNPS 984
Cdd:pfam12001   81 TRPVLESPCVGNLNNSLVLNRN 102
Ank_2 pfam12796
Ankyrin repeats (3 copies);
59-150 1.57e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 87.09  E-value: 1.57e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282   59 LHYACAHGHLGVVTLLIERNCNVNARDDDKCTPLIKASQHQREDCVAVLLQHgADPNAVDAlGNTALHYAVHSENASIAS 138
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78

                           90
                   ....*....|..
gi 1958681282  139 QLLEHSANIEAR 150
Cdd:pfam12796   79 LLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
25-118 2.71e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 86.32  E-value: 2.71e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282   25 LHRAASVGAVATVERFLTFRlNGVNDTDKRNRTALHYACAHGHLGVVTLLIErNCNVNARDDDKcTPLIKASQHQREDCV 104
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENG-ADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDNGR-TALHYAARSGHLEIV 77

                           90
                   ....*....|....
gi 1958681282  105 AVLLQHGADPNAVD 118
Cdd:pfam12796   78 KLLLEKGADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 48-174 2.66e-19

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 91.95  E-value: 2.66e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282   48 VNDTDKRNRTALHYACAHGHLGVVTLLIERNCNVNARDDDKCTPLIKASQHQREDCVAVLLQHGADPNAVDALGNTALHY 127
Cdd:PHA02874   117 VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHN 196

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1958681282  128 AVHSENASIASQLLEHSANIEARTKEGFTPLSLAVQQNRGpIVELLI 174
Cdd:PHA02874   197 AAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRS-AIELLI 242
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
45-179 5.90e-19

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 88.47  E-value: 5.90e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282   45 LNGVNDTDKRNRTALHYACAHGHLGVVTLLIERNCNVNARDDDKCTPLIKASQHQREDCVAVLLQHGADPNAVDALGNTA 124
Cdd:COG0666     11 LLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTL 90

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1958681282  125 LHYAVHSENASIASQLLEHSANIEARTKEGFTPLSLAVQQNRGPIVELLIEKGAN 179
Cdd:COG0666     91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGAD 145
Ank_2 pfam12796
Ankyrin repeats (3 copies);
92-182 1.56e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 81.32  E-value: 1.56e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282   92 LIKASQHQREDCVAVLLQHGADPNAVDALGNTALHYAVHSENASIASQLLEHsANIEARTkEGFTPLSLAVQQNRGPIVE 171
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|.
gi 1958681282  172 LLIEKGANKHT 182
Cdd:pfam12796   79 LLLEKGADINV 89
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 25-179 7.48e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 84.33  E-value: 7.48e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282   25 LHRAAS--VGAVATVERFLTFRLNgVNDTDKRNRTALHYA--CAHGHLGVVTLLIERNCNVNARDDDKCtplikasqhqr 100
Cdd:PHA03100   110 LLYAISkkSNSYSIVEYLLDNGAN-VNIKNSDGENLLHLYleSNKIDLKILKLLIDKGVDINAKNRVNY----------- 177

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958681282  101 edcvavLLQHGADPNAVDALGNTALHYAVHSENASIASQLLEHSANIEARTKEGFTPLSLAVQQNRGPIVELLIEKGAN 179
Cdd:PHA03100   178 ------LLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPS 250
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 50-183 3.82e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 79.54  E-value: 3.82e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282   50 DTDKRNR----TALHYACAHGHLGVVTLLIERNCNVNARDDDKCTPLIKASQHQREDCVAVLLQHGADPNAVDALGNTAL 125
Cdd:PHA02878   159 DINMKDRhkgnTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPL 238

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282  126 HYAVHS-ENASIASQLLEHSANIEAR-TKEGFTPLSLAVQQNRgpIVELLIEKGANKHTV 183
Cdd:PHA02878   239 HISVGYcKDYDILKLLLEHGVDVNAKsYILGLTALHSSIKSER--KLKLLLEYGADINSL 296
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 47-179 5.66e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 78.55  E-value: 5.66e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282   47 GVNDTDKRNRTALHYACAHGHLGVVTLLIERNCNVNARDDDKCTPLIKASQ------HQREdCVAVLLQHGADPNAVDAL 120
Cdd:PHA03100    27 LNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNikynltDVKE-IVKLLLEYGANVNAPDNN 105

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958681282  121 GNTALHYAV--HSENASIASQLLEHSANIEARTKEGFTPLSLAVQQNRG--PIVELLIEKGAN 179
Cdd:PHA03100   106 GITPLLYAIskKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVD 168
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 48-183 3.97e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 75.86  E-value: 3.97e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282   48 VNDTDKRNRTALHYACAHGH-----LGVVTLLIERNCNVNARDDDKCTPLIKASQHQRED--CVAVLLQHGADPNAVDAL 120
Cdd:PHA03100    61 INSSTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGANVNAPDNNGITPLLYAISKKSNSysIVEYLLDNGANVNIKNSD 140

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282  121 GNTALHYAVHS--ENASIASQLLEHSANIEARTK----------------EGFTPLSLAVQQNRGPIVELLIEKGANKHT 182
Cdd:PHA03100   141 GENLLHLYLESnkIDLKILKLLIDKGVDINAKNRvnyllsygvpinikdvYGFTPLHYAVYNNNPEFVKYLLDLGANPNL 220


                   .
gi 1958681282  183 V 183
Cdd:PHA03100   221 V 221
PHA03095 PHA03095
ankyrin-like protein; Provisional
 30-183 2.06e-13

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 73.91  E-value: 2.06e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282   30 SVGAVATVERFLTFRLNGVNDTDKRNRTALHYAC--AHGHLGVVTLLIERNCNVNARDDDKCTPLIKASQHQ--REDCVA 105
Cdd:PHA03095   162 SRNANVELLRLLIDAGADVYAVDDRFRSLLHHHLqsFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSscKRSLVL 241

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958681282  106 VLLQHGADPNAVDALGNTALHYAVHSENASIASQLLEHSANIEARTKEGFTPLSLAVQQNRGPIVELLIEKGANKHTV 183
Cdd:PHA03095   242 PLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETV 319
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 24-191 4.39e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 72.33  E-value: 4.39e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282   24 QLHRAASVGAVATVERFLTFRLNGVNDTDKRNRTALHYACAHGHLGVVTLLIERNCNVNARDDDKCTPLIKASQHQREDC 103
Cdd:PHA02875    71 ELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKG 150

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282  104 VAVLLQHGADPNAVDALGNTALHYAVHSENASIASQLLEHSANIEARTKEG-FTPLSLAVQQNRGPIVELLIEKGANKHT 182
Cdd:PHA02875   151 IELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGADCNI 230


                   ....*....
gi 1958681282  183 VFRLDRSSC 191
Cdd:PHA02875   231 MFMIEGEEC 239
PHA03095 PHA03095
ankyrin-like protein; Provisional
 68-179 7.91e-12

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 68.90  E-value: 7.91e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282   68 LGVVTLLIERNCNVNARDDDKCTPL---IKASQHQREDCVAVLLQHGADPNAVDALGNTALH-YAVHSENASIASQLLEH 143
Cdd:PHA03095    27 VEEVRRLLAAGADVNFRGEYGKTPLhlyLHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHlYLYNATTLDVIKLLIKA 106

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1958681282  144 SANIEARTKEGFTPLS--LAVQQNRGPIVELLIEKGAN 179
Cdd:PHA03095   107 GADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGAD 144
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 39-164 8.86e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 68.75  E-value: 8.86e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282   39 RFLTFRLNGVNDTDKRNRTALHYACAHGHLGVVTLLIERNCNVNARDDDKCTPL-IKASQHQREDCVAVLLQHGADPNAV 117
Cdd:PHA02878   185 ELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLhISVGYCKDYDILKLLLEHGVDVNAK 264

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1958681282  118 DA-LGNTALHYAVHSENasIASQLLEHSANIEARTKEGFTPLSLAVQQ 164
Cdd:PHA02878   265 SYiLGLTALHSSIKSER--KLKLLLEYGADINSLNSYKLTPLSSAVKQ 310
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 39-183 6.33e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 66.63  E-value: 6.33e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282   39 RFLTFRLNGVNDTDKRNRTALHYACA-HGHLGVVTLLIERNCNVNARDDDKCTPLIKASQHQREDCVAVLLQHGADPNAV 117
Cdd:PHA02876   325 RTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEAL 404

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958681282  118 DALGNTALHYAVHSENASIASQ-LLEHSANIEARTKEGFTPLSLAVQQNRGP-IVELLIEKGANKHTV 183
Cdd:PHA02876   405 SQKIGTALHFALCGTNPYMSVKtLIDRGANVNSKNKDLSTPLHYACKKNCKLdVIEMLLDNGADVNAI 472
Ank_4 pfam13637
Ankyrin repeats (many copies);
90-141 1.49e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 57.28  E-value: 1.49e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1958681282   90 TPLIKASQHQREDCVAVLLQHGADPNAVDALGNTALHYAVHSENASIASQLL 141
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 25-179 2.37e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 64.70  E-value: 2.37e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282   25 LHRAASVGAVATVERFLTFRLNGVNDTDKRNRTALHYACAHGH-LGVVTLLIERNCNVNARDDDKCTPLIKASQHQR-ED 102
Cdd:PHA02876   277 LHHASQAPSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTLDRnKD 356

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958681282  103 CVAVLLQHGADPNAVDALGNTALHYAVHSENASIASQLLEHSANIEARTKEGFTPLSLAV-QQNRGPIVELLIEKGAN 179
Cdd:PHA02876   357 IVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALcGTNPYMSVKTLIDRGAN 434
Ank_4 pfam13637
Ankyrin repeats (many copies);
55-108 2.76e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 56.51  E-value: 2.76e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1958681282   55 NRTALHYACAHGHLGVVTLLIERNCNVNARDDDKCTPLIKASQHQREDCVAVLL 108
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 28-179 9.25e-10

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 62.96  E-value: 9.25e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282   28 AASVGAVATVERFLTFRLNGvNDTDKRNRTALHYACAHGHLGVVTLLIERNCNVNARDDDKCTPLIKA--SQHQREDCVA 105
Cdd:PLN03192   532 VASTGNAALLEELLKAKLDP-DIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAisAKHHKIFRIL 610

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958681282  106 VLLQHGADPNAvdalGNTALHYAVHSENASIASQLLEHSANIEARTKEGFTPLSLAVQQNRGPIVELLIEKGAN 179
Cdd:PLN03192   611 YHFASISDPHA----AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGAD 680
PHA02798 PHA02798
ankyrin-like protein; Provisional
 68-193 9.92e-10

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 62.16  E-value: 9.92e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282   68 LGVVTLLIERNCNVNARDDDKCTPL------IKASQHQReDCVAVLLQHGADPNAVDALGNTALHYAVHS---ENASIAS 138
Cdd:PHA02798    51 TDIVKLFINLGANVNGLDNEYSTPLctilsnIKDYKHML-DIVKILIENGADINKKNSDGETPLYCLLSNgyiNNLEILL 129

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958681282  139 QLLEHSANIEARTKEGFTPLSLAVQQNRG---PIVELLIEKGANKHTV---FRLDRSSCRF 193
Cdd:PHA02798   130 FMIENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEKGVDINTHnnkEKYDTLHCYF 190
PHA03095 PHA03095
ankyrin-like protein; Provisional
 48-158 1.03e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 61.96  E-value: 1.03e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282   48 VNDTDKRNRTALH-YACAHGHLGVVTLLIERNCNVNARDDDKCTPLIK--ASQHQREDCVAVLLQHGADPNAVDALGNTA 124
Cdd:PHA03095    76 VNAPERCGFTPLHlYLYNATTLDVIKLLIKAGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTP 155

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1958681282  125 LHYAVHSENASIA--SQLLEHSANIEARTKEGFTPL 158
Cdd:PHA03095   156 LAVLLKSRNANVEllRLLIDAGADVYAVDDRFRSLL 191
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 57-176 2.36e-09

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: 61.18  E-value: 2.36e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282   57 TALHYACAHGHLGVVTLLIERNCNV-NAR---------DDDKCT----PLIKASQHQREDCVAVLLQHGADPNAVDALGN 122
Cdd:cd22192     91 TALHIAVVNQNLNLVRELIARGADVvSPRatgtffrpgPKNLIYygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGN 170

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958681282  123 TALHYAVHSENASIASQLLEHSANIEA----------RTKEGFTPLSLAVQQNRGPIVELLIEK 176
Cdd:cd22192    171 TVLHILVLQPNKTFACQMYDLILSYDKeddlqpldlvPNNQGLTPFKLAAKEGNIVMFQHLVQK 234
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 104-173 2.89e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 61.07  E-value: 2.89e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282  104 VAVLLQHGADPNAVDALGNTALHYAVHSENASIASQLLEHSANIEARTKEGFTPLSLAVQQNRGPIVELL 173
Cdd:PTZ00322    98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
PHA03095 PHA03095
ankyrin-like protein; Provisional
 100-179 7.87e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 59.27  E-value: 7.87e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282  100 REDCVAVLLQHGADPNAVDALGNTALHYAVHSEN---ASIASQLLEHSANIEARTKEGFTPLSLAVQ-QNRGPIVELLIE 175
Cdd:PHA03095    26 TVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYnATTLDVIKLLIK 105


                   ....
gi 1958681282  176 KGAN 179
Cdd:PHA03095   106 AGAD 109
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 74-179 1.07e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 58.52  E-value: 1.07e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282   74 LIERNCNVNARDDDKCTPLIKASQHQREDCVAVLLQHGADPNAVDALGNTALHY-----AVHSENASIASQLLEHSANIE 148
Cdd:PHA03100    21 IIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYlsnikYNLTDVKEIVKLLLEYGANVN 100

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1958681282  149 ARTKEGFTPLSLAVQQNRG--PIVELLIEKGAN 179
Cdd:PHA03100   101 APDNNGITPLLYAISKKSNsySIVEYLLDNGAN 133
PHA03095 PHA03095
ankyrin-like protein; Provisional
 26-149 1.14e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 58.88  E-value: 1.14e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282   26 HRAASVGAVATVERFLTFRLNGVNDTDKRNRTALHYACAHGHL--GVVTLLIERNCNVNARDDDKCTPLIKASQHQREDC 103
Cdd:PHA03095   193 HHLQSFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCkrSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRA 272

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1958681282  104 VAVLLQHGADPNAVDALGNTALHYAVHSENASIASQLLEHSANIEA 149
Cdd:PHA03095   273 CRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAET 318
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 56-185 1.67e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 58.08  E-value: 1.67e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282   56 RTALHYACAHGHLGVVTLLIERNCNVN-ARDDDKCTPLIKASQHQREDCVAVLLQHGADPNAVDALGNTALHYAVHSENA 134
Cdd:PHA02875    69 ESELHDAVEEGDVKAVEELLDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDI 148

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1958681282  135 SIASQLLEHSANIEARTKEGFTPLSLAVQQNRGPIVELLIEKGANKHTVFR 185
Cdd:PHA02875   149 KGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGK 199
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 32-178 2.54e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 57.67  E-value: 2.54e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282   32 GAVATVERFLTFRLNGVNDTDKRNRTALHYACAHGHLGVVTLLIERNCNVNARDDDKCTPLIKASQHQREDCVAVLLQHG 111
Cdd:PHA02874    12 GDIEAIEKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNG 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282  112 ADP-----------------------NAVDALGNTALHYAVHSENASIASQLLEHSANIEARTKEGFTPLSLAVQQNRGP 168
Cdd:PHA02874    92 VDTsilpipciekdmiktildcgidvNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFD 171

                          170
                   ....*....|
gi 1958681282  169 IVELLIEKGA 178
Cdd:PHA02874   172 IIKLLLEKGA 181
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 37-119 2.75e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 57.37  E-value: 2.75e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282   37 VERFLTFRLNgVNDTDKRNRTALHYACAHGHLGVVTLLIERNCNVNARDDDKCTPLIKASQHQREDCVAVLLQHGADPNA 116
Cdd:PHA03100   175 VNYLLSYGVP-INIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253


                   ...
gi 1958681282  117 VDA 119
Cdd:PHA03100   254 IIE 256
Ank_5 pfam13857
Ankyrin repeats (many copies);
41-95 4.03e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 50.42  E-value: 4.03e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1958681282   41 LTFRLNGVNDTDKRNRTALHYACAHGHLGVVTLLIERNCNVNARDDDKCTPLIKA 95
Cdd:pfam13857    2 LEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
68-179 6.91e-08

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 55.35  E-value: 6.91e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282   68 LGVVTLLIERNCNVNARDDDKCTPLIKASQHQREDCVAVLLQHGADPNAVDALGNTALHYAVHSENASIASQLLEHSANI 147
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1958681282  148 EARTKEGFTPLSLAVQQNRGPIVELLIEKGAN 179
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGAD 112
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 21-121 7.46e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.45  E-value: 7.46e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282   21 AVGQLHRAASVGAVATveRFLtfrLNGVNDTDKRN---RTALHYACAHGHLGVVTLLIERNCNVNARDDDKCTPLIKASQ 97
Cdd:PTZ00322    83 TVELCQLAASGDAVGA--RIL---LTGGADPNCRDydgRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEE 157

                           90       100
                   ....*....|....*....|....
gi 1958681282   98 HQREDCVAVLLQHGADPNAVDALG 121
Cdd:PTZ00322   158 NGFREVVQLLSRHSQCHFELGANA 181
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 48-190 9.12e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 55.74  E-value: 9.12e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282   48 VNDTDKRNRTALHYACAHGHLGVVTLLIERNCNVNARDDDKCTPLIKASQHQREdcVAVLLQHGADPNAVDALGNTALHY 127
Cdd:PHA02874   183 ANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRS--AIELLINNASINDQDIDGSTPLHH 260

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958681282  128 AVHSE-NASIASQLLEHSANIEARTKEGFTPLSLAVQQ-NRGPIVELLIEKGANKHTVFRLDRSS 190
Cdd:PHA02874   261 AINPPcDIDIIDILLYHKADISIKDNKGENPIDTAFKYiNKDPVIKDIIANAVLIKEADKLKDSD 325
Ank_5 pfam13857
Ankyrin repeats (many copies);
73-128 9.56e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 49.65  E-value: 9.56e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958681282   73 LLIERNCNVNARDDDKCTPLIKASQHQREDCVAVLLQHGADPNAVDALGNTALHYA 128
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 48-182 1.32e-07

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: 55.86  E-value: 1.32e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282   48 VNDTDK----RNRTALHYACAHGHLGVVTLLIERNCNVNAR-DDDKC-----TPLIKASQHQ--------REDCVAVLLQ 109
Cdd:TIGR00870  117 ANDQYTseftPGITALHLAAHRQNYEIVKLLLERGASVPARaCGDFFvksqgVDSFYHGESPlnaaaclgSPSIVALLSE 196

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282  110 HGADPNAVDALGNTALHYAV-----HSENASIASQ----------LLEHSANIEA-RTKEGFTPLSLAVQQNRGPIVELL 173
Cdd:TIGR00870  197 DPADILTADSLGNTLLHLLVmenefKAEYEELSCQmynfalslldKLRDSKELEViLNHQGLTPLKLAAKEGRIVLFRLK 276

                          170
                   ....*....|.
gi 1958681282  174 --IEKGANKHT 182
Cdd:TIGR00870  277 laIKYKQKKFV 287
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 56-176 1.32e-07

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: 55.66  E-value: 1.32e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282   56 RTALHYACAHGHLGVVTLLIERNCNVNAR------DDDKCT-------PLIKASQHQREDCVAVLLQHGADPNAV---DA 119
Cdd:cd21882     74 QTALHIAIENRNLNLVRLLVENGADVSARatgrffRKSPGNlfyfgelPLSLAACTNQEEIVRLLLENGAQPAALeaqDS 153

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958681282  120 LGNTALHYAV-----HSENASIASQL----------LEHSANIEART-KEGFTPLSLAVQQNRGPIVELLIEK 176
Cdd:cd21882    154 LGNTVLHALVlqadnTPENSAFVCQMynlllsygahLDPTQQLEEIPnHQGLTPLKLAAVEGKIVMFQHILQR 226
Ank_4 pfam13637
Ankyrin repeats (many copies);
25-75 4.07e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 47.65  E-value: 4.07e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1958681282   25 LHRAASVGAVATVERFLTFRLNgVNDTDKRNRTALHYACAHGHLGVVTLLI 75
Cdd:pfam13637    5 LHAAAASGHLELLRLLLEKGAD-INAVDGNGETALHFAASNGNVEVLKLLL 54
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 56-86 1.40e-06

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: 45.74  E-value: 1.40e-06
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1958681282   56 RTALHYACAH-GHLGVVTLLIERNCNVNARDD 86
Cdd:pfam00023    3 NTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 54-176 2.37e-06

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: 51.68  E-value: 2.37e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282   54 RNRTALHYACAHGHLGVVTLLIERNCNVNAR---------DDDKC-----TPLIKASQHQREDCVAVLLQHGADPNAV-D 118
Cdd:cd22194    140 EGQTALNIAIERRQGDIVKLLIAKGADVNAHakgvffnpkYKHEGfyfgeTPLALAACTNQPEIVQLLMEKESTDITSqD 219

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282  119 ALGNTALHYAV------HSENASIA---SQLLEHSA--NIEA-RTKEGFTPLSLAVQQNRGPIVELLIEK 176
Cdd:cd22194    220 SRGNTVLHALVtvaedsKTQNDFVKrmyDMILLKSEnkNLETiRNNEGLTPLQLAAKMGKAEILKYILSR 289
Ank_4 pfam13637
Ankyrin repeats (many copies);
121-174 4.68e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.57  E-value: 4.68e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1958681282  121 GNTALHYAVHSENASIASQLLEHSANIEARTKEGFTPLSLAVQQNRGPIVELLI 174
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 71-152 1.08e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.51  E-value: 1.08e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282   71 VTLLIERNCNVNARDDDKCTPLIKASQHQREDCVAVLLQHGADPNAVDALGNTALHYAVHSENASIASQLLEHSA---NI 147
Cdd:PTZ00322    98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQchfEL 177


                   ....*
gi 1958681282  148 EARTK 152
Cdd:PTZ00322   178 GANAK 182
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 59-178 1.09e-05

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 46.41  E-value: 1.09e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282   59 LHYACAHGhlGVVTLLIERNCNVNA---------RDDDKCTPLIkASQHQ---REDCVaVLLQHGADPNAVDAL-GNTAL 125
Cdd:PHA02736    21 LHYLCRNG--GVTDLLAFKNAISDEnrylvleynRHGKQCVHIV-SNPDKadpQEKLK-LLMEWGADINGKERVfGNTPL 96

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1958681282  126 HYAVHSENASIASQLLEH-SANIEARTKEGFTPLSLAVQQNRGPIVELLIEKGA 178
Cdd:PHA02736    97 HIAVYTQNYELATWLCNQpGVNMEILNYAFKTPYYVACERHDAKMMNILRAKGA 150
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 48-186 1.19e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 49.29  E-value: 1.19e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282   48 VNDTDKRNRTALHYACAHGHLGVVTLLIERNCNVNARDDDKCT-----------------------------PLIKASQH 98
Cdd:PHA02876   171 VNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSvlecavdsknidtikaiidnrsninkndlSLLKAIRN 250

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282   99 QREDCVAVLLQHGADPNAVDALGNTALHYAVHSENAS-IASQLLEHSANIEARTKEGFTPLSLAVQQNRGPI-VELLIEK 176
Cdd:PHA02876   251 EDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYLMAKNGYDTEnIRTLIML 330

                          170
                   ....*....|
gi 1958681282  177 GANKHTVFRL 186
Cdd:PHA02876   331 GADVNAADRL 340
PHA02946 PHA02946
ankyin-like protein; Provisional
 60-158 1.20e-05

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 48.90  E-value: 1.20e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282   60 HYACAHGHLGV-------VTLLIERNCNVNARDDDKCTPLIKASQHQREDCVAVLLQHGADPNAVDALGNTALHYAVHSE 132
Cdd:PHA02946    37 NYHILHAYCGIkglderfVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTD 116

                           90       100
                   ....*....|....*....|....*....
gi 1958681282  133 NASIA--SQLLEHSANIEART-KEGFTPL 158
Cdd:PHA02946   117 DEVIEriNLLVQYGAKINNSVdEEGCGPL 145
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 19-141 1.46e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 48.91  E-value: 1.46e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282   19 YCAVGQLHRAASVGAVATVERFLTFRLNgVNDTDKRNRTALHYA-CAHGHLGVVTLLIERNCNVNARDDDKCTPLIKASQ 97
Cdd:PHA02876   373 YCDKTPIHYAAVRNNVVIINTLLDYGAD-IEALSQKIGTALHFAlCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACK 451

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958681282   98 HQ-REDCVAVLLQHGADPNAVD---------ALG-----NTALHYAVHSENASIASQLL 141
Cdd:PHA02876   452 KNcKLDVIEMLLDNGADVNAINiqnqyplliALEyhgivNILLHYGAELRDSRVLHKSL 510
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 54-166 2.50e-05

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: 48.31  E-value: 2.50e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282   54 RNRTALHYACAHGHLGVVTLLIERNCNVNAR--------DDDKC-----TPLIKASQHQREDCVAVLLQHGADP---NAV 117
Cdd:cd22197     93 RGHSALHIAIEKRSLQCVKLLVENGADVHARacgrffqkKQGTCfyfgeLPLSLAACTKQWDVVNYLLENPHQPaslQAQ 172

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958681282  118 DALGNTALHYAV-----HSENASIASQ----LLEHSANI-------EARTKEGFTPLSLAVQQNR 166
Cdd:cd22197    173 DSLGNTVLHALVmiadnSPENSALVIKmydgLLQAGARLcptvqleEISNHEGLTPLKLAAKEGK 237
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 50-161 3.17e-05

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 (TRPV1), a capsaicin (vanilloid) receptor, is the founding member of the vanilloid TRP subfamily (TRPV). In humans, it is expressed in the brain, kidney, pancreas, testis, uterus, spleen, stomach, small intestine, lung and liver. TRPV1 has been implicated to have function in thermo-sensation (heat), autonomic thermoregulation, nociception, food intake regulation, and multiple functions in the gastrointestinal (GI) tract. The receptor has also been involved in growth cone guidance, long-term depression, endocannabinoid signaling and osmosensing in the central nervous system. TRPV1 is up regulated in several human pathological conditions including vulvodynia, GI inflammation, Crohn's disease and ulcerative colitis. TRPV1 knock-out mice exhibit impaired sensation to thermal-mechanical acute pain. 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: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 47.88  E-value: 3.17e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282   50 DTDKRNRTALHYACAHGHLGVVTLLIERNCNVNARDDDKC--------------TPLIKASQHQREDCVAVLLQH---GA 112
Cdd:cd22196     89 DSYYKGQTALHIAIERRNMHLVELLVQNGADVHARASGEFfkkkkggpgfyfgeLPLSLAACTNQLDIVKFLLENphsPA 168

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958681282  113 DPNAVDALGNTALHYAVH-----SENASIASQL----------LEHSANIEART-KEGFTPLSLA 161
Cdd:cd22196    169 DISARDSMGNTVLHALVEvadntPENTKFVTKMyneililgakIRPLLKLEEITnKKGLTPLKLA 233
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 54-83 3.70e-05

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: 41.42  E-value: 3.70e-05
                            10        20        30
                    ....*....|....*....|....*....|
gi 1958681282    54 RNRTALHYACAHGHLGVVTLLIERNCNVNA 83
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 70-179 4.17e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 47.27  E-value: 4.17e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282   70 VVTLLIERNCNVNARDDDKCTPLIKASQHQREDCVAVLLQHGADPNAVDALGNTALHYAVHSENASIASQLLEHSANIEA 149
Cdd:PHA02874   106 MIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANV 185

                           90       100       110
                   ....*....|....*....|....*....|
gi 1958681282  150 RTKEGFTPLSLAVQQNRGPIVELLIEKGAN 179
Cdd:PHA02874   186 KDNNGESPLHNAAEYGDYACIKLLIDHGNH 215
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 90-194 4.32e-05

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: 47.31  E-value: 4.32e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282   90 TPLIKASQHQREDCVAVLL-QHGADPNAVDALGNTALHYAVHSENASIASQLLEHSANI--EARTKE---GFTPLSLAVQ 163
Cdd:cd22192     19 SPLLLAAKENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELvnEPMTSDlyqGETALHIAVV 98

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1958681282  164 QNRGPIVELLIEKGAN------KHTVFRLDRSS-CRFG 194
Cdd:cd22192     99 NQNLNLVRELIARGADvvspraTGTFFRPGPKNlIYYG 136
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 25-179 7.09e-05

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: 46.93  E-value: 7.09e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282   25 LHRAASVGAVATVERFLTFrlngvNDTDKRNR-----TALHYACAHGHLGVVTLLIErncnvNARDddkctpLIKasqhq 99
Cdd:cd22192     21 LLLAAKENDVQAIKKLLKC-----PSCDLFQRgalgeTALHVAALYDNLEAAVVLME-----AAPE------LVN----- 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282  100 rEDCVAVLLQhgadpnavdalGNTALHYAVHSENASIASQLLEHSAN-IEAR-TKEGFT------------PLSLAVQQN 165
Cdd:cd22192     80 -EPMTSDLYQ-----------GETALHIAVVNQNLNLVRELIARGADvVSPRaTGTFFRpgpknliyygehPLSFAACVG 147

                          170
                   ....*....|....
gi 1958681282  166 RGPIVELLIEKGAN 179
Cdd:cd22192    148 NEEIVRLLIEHGAD 161
Ank_5 pfam13857
Ankyrin repeats (many copies);
107-161 7.13e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.56  E-value: 7.13e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958681282  107 LLQHG-ADPNAVDALGNTALHYAVHSENASIASQLLEHSANIEARTKEGFTPLSLA 161
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 121-152 8.30e-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: 8.30e-05
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1958681282  121 GNTALHYAV-HSENASIASQLLEHSANIEARTK 152
Cdd:pfam00023    2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 54-83 8.62e-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.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 40.32  E-value: 8.62e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 1958681282   54 RNRTALHYACAHGHLGVVTLLIERNCNVNA 83
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 68-147 9.38e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 46.60  E-value: 9.38e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282   68 LGVVTLLIERNCNVNARDDDKCTPLIKASQHQREDCVAVLLQHGADPNAVDALGNTALHYAVHSENASIASQLLEHSANI 147
Cdd:PHA02876   158 LLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNI 237
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 92-179 1.04e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 46.21  E-value: 1.04e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282   92 LIKASQHQREDCVA-VLLQHGADPNAVDALGNTALHYAVHSENASIASQLLEHSANIEARTKEGFTPLSLAVQQNRGPIV 170
Cdd:PHA02876   148 LIKERIQQDELLIAeMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTI 227


                   ....*....
gi 1958681282  171 ELLIEKGAN 179
Cdd:PHA02876   228 KAIIDNRSN 236
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 642-958 1.26e-04

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 46.25  E-value: 1.26e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282  642 EVGQHEMSLGNLNMNLKALHDSVTQLQE-AQLQDDPQREgvlSSARMAHLLWKLEVDCLKLEDSVKNQAEEIEELETQLL 720
Cdd:pfam05483  248 QITEKENKMKDLTFLLEESRDKANQLEEkTKLQDENLKE---LIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATK 324

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282  721 TV-ELTGDRKKERDEVT--RSTQSL--------ACALEH----EVEKIE-----------ELEKTLHGFMEVMKIAGKKL 774
Cdd:pfam05483  325 TIcQLTEEKEAQMEELNkaKAAHSFvvtefeatTCSLEEllrtEQQRLEknedqlkiitmELQKKSSELEEMTKFKNNKE 404

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282  775 DECENRELYFYEDMR----NRTFETL-------QHEINYLKDTWEpiqcKYLHqDINIQLT-----EQELLK----IKSE 834
Cdd:pfam05483  405 VELEELKKILAEDEKlldeKKQFEKIaeelkgkEQELIFLLQARE----KEIH-DLEIQLTaiktsEEHYLKevedLKTE 479

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282  835 QENyEHLHQTQ--GNVEKEVLTLRGLVQESVTQAEEEKKlEKARENNNDSRMSQIILRVKSLESRLPEIKSHVDSTRREM 912
Cdd:pfam05483  480 LEK-EKLKNIEltAHCDKLLLENKELTQEASDMTLELKK-HQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEF 557

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*..
gi 1958681282  913 -EKHKQLYVEENKSRKSLFNTLSKTVEKLEVSRAKLMQLNQQKMTME 958
Cdd:pfam05483  558 iQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIE 604
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 56-179 1.59e-04

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: 45.64  E-value: 1.59e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282   56 RTALHYACAHGHLGV---VTLLIERncnvnARDDDKCTPLIKASqhqredCVAVLLQhgadpnavdalGNTALHYAVHSE 132
Cdd:cd21882     27 KTCLHKAALNLNDGVneaIMLLLEA-----APDSGNPKELVNAP------CTDEFYQ-----------GQTALHIAIENR 84

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282  133 NASIASQLLEHSANIEARTKEGF-------------TPLSLAVQQNRGPIVELLIEKGAN 179
Cdd:cd21882     85 NLNLVRLLVENGADVSARATGRFfrkspgnlfyfgeLPLSLAACTNQEEIVRLLLENGAQ 144
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 54-208 2.61e-04

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: 44.79  E-value: 2.61e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282   54 RNRTALHYACAHGHLGVVTLLIERNCNVNAR---------DDDKC-----TPLIKASQHQREDCVAVLLQHG---ADPNA 116
Cdd:cd22193     75 EGQTALHIAIERRQGDIVALLVENGADVHAHakgrffqpkYQGEGfyfgeLPLSLAACTNQPDIVQYLLENEhqpADIEA 154

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282  117 VDALGNTALHYAVH-SENA--------SIASQLLEHSANI-------EARTKEGFTPLSLAVQQNRGPIVELLIEKGANK 180
Cdd:cd22193    155 QDSRGNTVLHALVTvADNTkentkfvtRMYDMILIRGAKLcptveleEIRNNDGLTPLQLAAKMGKIEILKYILQREIKE 234

                          170       180       190
                   ....*....|....*....|....*....|
gi 1958681282  181 HTVFRLDR--SSCRFGPDGSSRkKDDSNVD 208
Cdd:cd22193    235 PELRHLSRkfTDWAYGPVSSSL-YDLSNVD 263
PHA02798 PHA02798
ankyrin-like protein; Provisional
 80-147 2.75e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 44.83  E-value: 2.75e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958681282   80 NVNARDDDKCTPLIKASQHQREDCVAVLLQHGADPNAVDALGNTALHYAVHSENASIASQLLEHSANI 147
Cdd:PHA02798   250 DINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFENESKFIFNSILNKKPNK 317
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 121-179 3.48e-04

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: 44.75  E-value: 3.48e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958681282  121 GNTALHYAVHSENASIASQLLEHSANIEARTK----------EGF----TPLSLAVQQNRGPIVELLIEKGAN 179
Cdd:cd22194    141 GQTALNIAIERRQGDIVKLLIAKGADVNAHAKgvffnpkykhEGFyfgeTPLALAACTNQPEIVQLLMEKEST 213
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 121-149 6.20e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.95  E-value: 6.20e-04
                            10        20
                    ....*....|....*....|....*....
gi 1958681282   121 GNTALHYAVHSENASIASQLLEHSANIEA 149
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 647-877 9.82e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.12  E-value: 9.82e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282  647 EMSLGNLNMNLKALHDSVTQLqEAQLQDDPQREGVL--SSARMAHLLWKLEVDCLKLEDSVKNQAEEIEELETQLLTV-E 723
Cdd:TIGR02168  301 EQQKQILRERLANLERQLEEL-EAQLEELESKLDELaeELAELEEKLEELKEELESLEAELEELEAELEELESRLEELeE 379

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282  724 LTGDRKKERDEVTRSTQSLACALEHEVEKIEELEKTLHGFMEVMKIAGKKLDECENRELYFYEDMRNRTFETLQHEINYL 803
Cdd:TIGR02168  380 QLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERL 459

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282  804 KDTWEPIQCKYLHQDINIQLTEQELLKIKSE-------QENYEHLHQTQGNVEKEVLTLRGLVQESVTQAEEEKKLEKAR 876
Cdd:TIGR02168  460 EEALEELREELEEAEQALDAAERELAQLQARldslerlQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAI 539


                   .
gi 1958681282  877 E 877
Cdd:TIGR02168  540 E 540
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 55-178 1.04e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 42.67  E-value: 1.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282   55 NRTALHYACAHGHLGVVTLLIERNCNVNARDDDKCTPLIKASQHQREDCVAVLLQHGADPN------------------- 115
Cdd:PHA02875     2 DQVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDvkypdieselhdaveegdv 81

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958681282  116 -AVDAL--------------GNTALHYAVHSENASIASQLLEHSANIEARTKEGFTPLSLAVQQNRGPIVELLIEKGA 178
Cdd:PHA02875    82 kAVEELldlgkfaddvfykdGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKA 159
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
540-947 1.05e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.13  E-value: 1.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282  540 RLLEIKNSYGDVLRrEIKKMETKhggVRKELSKITEVLSQPERQETEWGELCNLRSSLKQNENIINDGCFDGKMKTELRG 619
Cdd:PRK03918   297 KLSEFYEEYLDELR-EIEKRLSR---LEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKE 372

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282  620 RERQYHEEFGRSPLYHQCNE-----------EFEVGQHEMSLGNLNMNLKALHDSVTQLQEAQLQ--------DDPQREG 680
Cdd:PRK03918   373 ELERLKKRLTGLTPEKLEKEleelekakeeiEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgrelTEEHRKE 452

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282  681 VLSS------------ARMAHLLWKLEVDCLKLEDSVKNQ---------AEEIEELETQLLTVELTGDRKKERD-----E 734
Cdd:PRK03918   453 LLEEytaelkriekelKEIEEKERKLRKELRELEKVLKKEseliklkelAEQLKELEEKLKKYNLEELEKKAEEyeklkE 532

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282  735 VTRSTQSLACALEHEVEKIEELEKTLHGFMEVMKIAGKKLDECENR--ELYFyedmrnRTFETLQHEINYLkdtwEPIQC 812
Cdd:PRK03918   533 KLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKEleELGF------ESVEELEERLKEL----EPFYN 602

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282  813 KYLHQDINIQLTEQELLKIKSEQENYEHLHQTQGNVEKEVLTLRGLVQE---SVTQAEEEKKLEKARENnnDSRMSQIIL 889
Cdd:PRK03918   603 EYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEElekKYSEEEYEELREEYLEL--SRELAGLRA 680

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958681282  890 RVKSLESRLPEIKSHVDSTRREMEKHKQlYVEENKSrkslfntLSKTVEKLEVSRAKL 947
Cdd:PRK03918   681 ELEELEKRREEIKKTLEKLKEELEEREK-AKKELEK-------LEKALERVEELREKV 730
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 87-118 1.20e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 37.27  E-value: 1.20e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1958681282   87 DKCTPLIKAS-QHQREDCVAVLLQHGADPNAVD 118
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 90-187 1.53e-03

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: 42.48  E-value: 1.53e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282   90 TPLIKAS---QHQREDCVAVLLQHGADPNAVDAL-----------GNTALHYAVHSENASIASQLLEHSANIEARTK--- 152
Cdd:cd22193     31 TCLMKALlnlNPGTNDTIRILLDIAEKTDNLKRFinaeytdeyyeGQTALHIAIERRQGDIVALLVENGADVHAHAKgrf 110

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1958681282  153 -------EGF----TPLSLAVQQNRGPIVELLIEKGANKHTVFRLD 187
Cdd:cd22193    111 fqpkyqgEGFyfgeLPLSLAACTNQPDIVQYLLENEHQPADIEAQD 156
PHA02917 PHA02917
ankyrin-like protein; Provisional
 104-173 1.86e-03

ankyrin-like protein; Provisional


Pssm-ID: 165231 [Multi-domain]  Cd Length: 661  Bit Score: 42.29  E-value: 1.86e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282  104 VAVLLQHGADPNAVDALGNTALHYAVHSENASIASQLLEHSANIEARTKEGFTPLSLAVQQNRGpiVELL 173
Cdd:PHA02917   435 INICLPYLKDINMIDKRGETLLHKAVRYNKQSLVSLLLESGSDVNIRSNNGYTCIAIAINESRN--IELL 502
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 87-116 2.48e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.41  E-value: 2.48e-03
                            10        20        30
                    ....*....|....*....|....*....|
gi 1958681282    87 DKCTPLIKASQHQREDCVAVLLQHGADPNA 116
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 652-949 4.18e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.20  E-value: 4.18e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282  652 NLNMNLKALHDSVTQLQE--AQLQDDPQREGVLSSARMAHLLwKLEVDCLKLEDSVKNQAEEIEELETQLltVELTGDRK 729
Cdd:TIGR02168  695 ELEKALAELRKELEELEEelEQLRKELEELSRQISALRKDLA-RLEAEVEQLEERIAQLSKELTELEAEI--EELEERLE 771

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282  730 KERDEvtrstqslacALEHEvEKIEELEKTLHGFMEVMKIAGKKLDECENR---------ELYFYEDMRNRTFETLQHEI 800
Cdd:TIGR02168  772 EAEEE----------LAEAE-AEIEELEAQIEQLKEELKALREALDELRAEltllneeaaNLRERLESLERRIAATERRL 840

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282  801 NYLKDTWEPIQ------------CKYLHQDINIQLteQELLKIKSEQENYEHLHQTQ-GNVEKEVLTLRGLVQESvtqae 867
Cdd:TIGR02168  841 EDLEEQIEELSedieslaaeieeLEELIEELESEL--EALLNERASLEEALALLRSElEELSEELRELESKRSEL----- 913

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282  868 eEKKLEKARENNNDSRMSQIILRVK--SLESRLPE---------------IKSHVDSTRREMEKHKQ----------LYV 920
Cdd:TIGR02168  914 -RRELEELREKLAQLELRLEGLEVRidNLQERLSEeysltleeaealenkIEDDEEEARRRLKRLENkikelgpvnlAAI 992

                          330       340
                   ....*....|....*....|....*....
gi 1958681282  921 EENKSRKSLFNTLSKTVEKLEVSRAKLMQ 949
Cdd:TIGR02168  993 EEYEELKERYDFLTAQKEDLTEAKETLEE 1021
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 700-950 4.29e-03

Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 41.10  E-value: 4.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282  700 KLEDSVKNQAEEIEELETQLLTVELTGDRKKERDEVTRSTQSLACALEHEVEKIEELEKTLHGFMEVMKIAGKKLDECEN 779
Cdd:COG5185    279 RLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEA 358

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282  780 RELYFYEDMRNRTFETLQHEINYLKDTWEPIQCKYLHQDINIQlteqellkiKSEQENYEHLHQTQGNVEKEVLTLRGLV 859
Cdd:COG5185    359 IKEEIENIVGEVELSKSSEELDSFKDTIESTKESLDEIPQNQR---------GYAQEILATLEDTLKAADRQIEELQRQI 429

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282  860 QESVTQAEEEKKLEKARENNNDSRMSQIILRVKS-LESRLPEIKSHVDSTRRE-MEKHKQLYVEENKSRKSLFNTLSKTV 937
Cdd:COG5185    430 EQATSSNEEVSKLLNELISELNKVMREADEESQSrLEEAYDEINRSVRSKKEDlNEELTQIESRVSTLKATLEKLRAKLE 509

                          250
                   ....*....|...
gi 1958681282  938 EKLEVSRAKLMQL 950
Cdd:COG5185    510 RQLEGVRSKLDQV 522
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 121-175 4.35e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 (TRPV1), a capsaicin (vanilloid) receptor, is the founding member of the vanilloid TRP subfamily (TRPV). In humans, it is expressed in the brain, kidney, pancreas, testis, uterus, spleen, stomach, small intestine, lung and liver. TRPV1 has been implicated to have function in thermo-sensation (heat), autonomic thermoregulation, nociception, food intake regulation, and multiple functions in the gastrointestinal (GI) tract. The receptor has also been involved in growth cone guidance, long-term depression, endocannabinoid signaling and osmosensing in the central nervous system. TRPV1 is up regulated in several human pathological conditions including vulvodynia, GI inflammation, Crohn's disease and ulcerative colitis. TRPV1 knock-out mice exhibit impaired sensation to thermal-mechanical acute pain. 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: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 40.94  E-value: 4.35e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958681282  121 GNTALHYAVHSENASIASQLLEHSANIEART----------KEGF----TPLSLAVQQNRGPIVELLIE 175
Cdd:cd22196     94 GQTALHIAIERRNMHLVELLVQNGADVHARAsgeffkkkkgGPGFyfgeLPLSLAACTNQLDIVKFLLE 162
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 121-149 5.45e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 35.31  E-value: 5.45e-03
                           10        20
                   ....*....|....*....|....*....
gi 1958681282  121 GNTALHYAVHSENASIASQLLEHSANIEA 149
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02791 PHA02791
ankyrin-like protein; Provisional
 52-176 6.82e-03

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 39.64  E-value: 6.82e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282   52 DKRNRTALHYACAHGHLGVVTLLIERNCNVNARDDDkcTPLIKASQHQREDCVAVLLQHGADPNAVDALGNTALHYAVHS 131
Cdd:PHA02791    27 DVHGHSALYYAIADNNVRLVCTLLNAGALKNLLENE--FPLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVDS 104

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1958681282  132 ENASIASQLLEHSANIEARTKEGF-TPLSLAVQQNRGPIVELLIEK 176
Cdd:PHA02791   105 GNMQTVKLFVKKNWRLMFYGKTGWkTSFYHAVMLNDVSIVSYFLSE 150
PHA02792 PHA02792
ankyrin-like protein; Provisional
 75-172 7.04e-03

ankyrin-like protein; Provisional


Pssm-ID: 165155 [Multi-domain]  Cd Length: 631  Bit Score: 40.32  E-value: 7.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282   75 IERNCNVNARDDDKC---TPLIKASQHQREDCVAVLL---QHGADPNAVDALGNTALHYAVHSENASIASQLLEHSANIE 148
Cdd:PHA02792   358 ILKNGNVVVEDDDNIiniMPLFPTLSIHESDVLSILKlckPYIDDINKIDKHGRSILYYCIESHSVSLVEWLIDNGADIN 437

                           90       100
                   ....*....|....*....|....
gi 1958681282  149 ARTKEGFTPLSLAVQQNRGPIVEL 172
Cdd:PHA02792   438 ITTKYGSTCIGICVILAHACIPEI 461
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 541-894 7.50e-03

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 40.42  E-value: 7.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282  541 LLEIKNSYGDVLRREIKKMETKHGGVRKELSKITEVLSQPERQetewgeLCNLRSSLKQNENIINDGCFDGKMKTELRGR 620
Cdd:TIGR00606  731 LAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETL------LGTIMPEEESAKVCLTDVTIMERFQMELKDV 804

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282  621 ERQYHEEFGRSP------LYHQCNEEFEVGQHEMS--LGNLNMNLKALHDSVTQLQEAQLQDDPQREGVLSSARMAHLLW 692
Cdd:TIGR00606  805 ERKIAQQAAKLQgsdldrTVQQVNQEKQEKQHELDtvVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQ 884

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282  693 KLEVDCLKLEDSVKNQAEEIEELETQLLTVELT-GDRKKERDEVTRSTQSLACALEHEVEKIEELEKTLHGFMEVM---- 767
Cdd:TIGR00606  885 QFEEQLVELSTEVQSLIREIKDAKEQDSPLETFlEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIenki 964

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681282  768 -------------KIAG--KKLDECENRELYFYEDMR--NRTFETLQHEINYLKDTW-------EPIQCKYLHQDINIQL 823
Cdd:TIGR00606  965 qdgkddylkqketELNTvnAQLEECEKHQEKINEDMRlmRQDIDTQKIQERWLQDNLtlrkrenELKEVEEELKQHLKEM 1044

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958681282  824 TEQELLKIKSEQENYEHLHQTQGNVEKEVLTLRGLVQESVTQAEEEKKLEKARENNNDSRMSQIILRVKSL 894
Cdd:TIGR00606 1045 GQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQFRDAEEKYREMMIVMRTTEL 1115
Ank_5 pfam13857
Ankyrin repeats (many copies);
140-179 9.60e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.40  E-value: 9.60e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1958681282  140 LLEH-SANIEARTKEGFTPLSLAVQQNRGPIVELLIEKGAN 179
Cdd:pfam13857    1 LLEHgPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVD 41
 
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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