NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|17554212|ref|NP_499007|]
View 

lin-12/Notch intracellular domain [Caenorhabditis elegans]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1070-1295 3.36e-38

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 145.10  E-value: 3.36e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554212 1070 EDLIVHEAKECIAAGADVNAMDCDENTPLMLAVLARRRRLVAYLMKAGADPTIYNKSERSALHQAAANRDFGMMVYMLns 1149
Cdd:COG0666   30 LLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLL-- 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554212 1150 tKLKGDIEELDRNGMTALMIVAHNegrDQVASAKLLVEKGAKVDydgaaRKDSEkykGRTALHYAAQVSNMPIVKYLVgE 1229
Cdd:COG0666  108 -EAGADVNARDKDGETPLHLAAYN---GNLEIVKLLLEAGADVN-----AQDND---GNTPLHLAAANGNLEIVKLLL-E 174

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17554212 1230 KGSNKDKQDEDGKTPIMLAAQEGRIEVVMYLIQQGASVEAVDATDHTARQLAQANNHHNIVDIFDR 1295
Cdd:COG0666  175 AGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240
NOD pfam06816
NOTCH protein; NOTCH signalling plays a fundamental role during a great number of ...
 753-807 6.35e-18

NOTCH protein; NOTCH signalling plays a fundamental role during a great number of developmental processes in multicellular animals. NOD and NODP represent a region present in many NOTCH proteins and NOTCH homologs in multiple species such as NOTCH2 and NOTCH3, LIN12, SC1 and TAN1. Role of NOD domain remains to be elucidated.


:

Pssm-ID: 462014  Cd Length: 56  Bit Score: 78.71  E-value: 6.35e-18
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 17554212    753 TNATIITNIRITVQMDPKEFQVTGGQSLMEISSALRVTVRIQRDEEG-PLVFQWNG 807
Cdd:pfam06816    1 PEKLAEGVLVIVVLMDPEELLNNSVQFLRELSTVLRTNVRFKKDENGnPMIYPWYG 56
NODP pfam07684
NOTCH protein; NOTCH signalling plays a fundamental role during a great number of ...
 842-898 2.96e-10

NOTCH protein; NOTCH signalling plays a fundamental role during a great number of developmental processes in multicellular animals. NOD and NODP represent a region present in many NOTCH proteins and NOTCH homologs in multiple species such as NOTCH2 and NOTCH3, LIN12, SC1 and TAN1. The role of the NOD and NODP domains remains to be elucidated.


:

Pssm-ID: 462229  Cd Length: 59  Bit Score: 57.28  E-value: 2.96e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554212    842 IGVVVYLEVQ-ENCDTG--KClYKDAQSVVDSISARLAKKGIDsFGIPISEALVAEPRKS 898
Cdd:pfam07684    2 IGSVVYLEIDnRKCSQSsdEC-FSTAQSAADFLAALAAKGGLD-LPYPIKEVRSEPPPPP 59
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 365-401 8.72e-10

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


:

Pssm-ID: 238011  Cd Length: 38  Bit Score: 55.34  E-value: 8.72e-10
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 17554212  365 DKNECLSENMCLNNGTCVNLPGSFRCDCARGFGGKWC 401
Cdd:cd00054    1 DIDECASGNPCQNGGTCVNTVGSYRCSCPPGYTGRNC 37
Notch pfam00066
LNR domain; The LNR (Lin-12/Notch repeat) domain is found in three tandem copies in Notch ...
 715-750 1.73e-08

LNR domain; The LNR (Lin-12/Notch repeat) domain is found in three tandem copies in Notch related proteins. The structure of the domain has been determined by NMR and was shown to contain three disulphide bonds and coordinate a calcium ion. Three repeats are also found in the PAPP-A peptidase.


:

Pssm-ID: 459658  Cd Length: 35  Bit Score: 51.37  E-value: 1.73e-08
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 17554212    715 RCPvkiREHCASRFANGICDPECNTNGCGFDGGDCD 750
Cdd:pfam00066    3 NCP---YPYCWDKFGNGVCDEECNNAECLWDGGDCS 35
NL smart00004
Domain found in Notch and Lin-12; The Notch protein is essential for the proper ...
 635-668 2.67e-08

Domain found in Notch and Lin-12; The Notch protein is essential for the proper differentiation of the Drosophila ectoderm. This protein contains 3 NL domains.


:

Pssm-ID: 197463  Cd Length: 38  Bit Score: 50.79  E-value: 2.67e-08
                            10        20        30
                    ....*....|....*....|....*....|....
gi 17554212     635 RSVCEKRKCSERANDGNCDADCNYAACKFDGGDC 668
Cdd:smart00004    5 WSRCEDAQCWDKFGDGVCDEECNNAECLWDGGDC 38
Notch pfam00066
LNR domain; The LNR (Lin-12/Notch repeat) domain is found in three tandem copies in Notch ...
 675-709 8.14e-08

LNR domain; The LNR (Lin-12/Notch repeat) domain is found in three tandem copies in Notch related proteins. The structure of the domain has been determined by NMR and was shown to contain three disulphide bonds and coordinate a calcium ion. Three repeats are also found in the PAPP-A peptidase.


:

Pssm-ID: 459658  Cd Length: 35  Bit Score: 49.45  E-value: 8.14e-08
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 17554212    675 FSKCRYgNMCADFFANGVCNQACNNEECLYDGMDC 709
Cdd:pfam00066    1 WPNCPY-PYCWDKFGNGVCDEECNNAECLWDGGDC 34
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 152-189 4.13e-06

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


:

Pssm-ID: 238011  Cd Length: 38  Bit Score: 44.94  E-value: 4.13e-06
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 17554212  152 DVNECEENkNACGNRSTCMNTLGTYICVCPQGFLPPDC 189
Cdd:cd00054    1 DIDECASG-NPCQNGGTCVNTVGSYRCSCPPGYTGRNC 37
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 545-579 1.37e-05

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


:

Pssm-ID: 238011  Cd Length: 38  Bit Score: 43.39  E-value: 1.37e-05
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 17554212  545 DLCLE-NPCSNGGVCHQHRESFSCDCPPGFYGNGCE 579
Cdd:cd00054    3 DECASgNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 293-323 7.17e-04

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


:

Pssm-ID: 238011  Cd Length: 38  Bit Score: 38.39  E-value: 7.17e-04
                         10        20        30
                 ....*....|....*....|....*....|.
gi 17554212  293 NNKCEAGSKCINGVNSYFCDCPPERTGPYCE 323
Cdd:cd00054    8 GNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 252-285 1.67e-03

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


:

Pssm-ID: 238011  Cd Length: 38  Bit Score: 37.23  E-value: 1.67e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 17554212  252 DSCAS-NPCS-HGVCISFSGGFQCICDDGYSGSYCQ 285
Cdd:cd00054    3 DECASgNPCQnGGTCVNTVGSYRCSCPPGYTGRNCE 38
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 505-541 4.70e-03

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


:

Pssm-ID: 238011  Cd Length: 38  Bit Score: 36.08  E-value: 4.70e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 17554212  505 NLCLS-DPCMNNATCIDVDAhiGYACICKQGFEGDICE 541
Cdd:cd00054    3 DECASgNPCQNGGTCVNTVG--SYRCSCPPGYTGRNCE 38
EGF_2 pfam07974
EGF-like domain; This family contains EGF domains found in a variety of extracellular proteins.
 220-245 7.47e-03

EGF-like domain; This family contains EGF domains found in a variety of extracellular proteins.


:

Pssm-ID: 400365  Cd Length: 26  Bit Score: 35.40  E-value: 7.47e-03
                           10        20
                   ....*....|....*....|....*.
gi 17554212    220 YCQNGGFCDKASSKCQCPPGYHGSTC 245
Cdd:pfam07974    1 ICSGRGTCVNQCGKCVCDSGYQGATC 26
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1070-1295 3.36e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 145.10  E-value: 3.36e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554212 1070 EDLIVHEAKECIAAGADVNAMDCDENTPLMLAVLARRRRLVAYLMKAGADPTIYNKSERSALHQAAANRDFGMMVYMLns 1149
Cdd:COG0666   30 LLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLL-- 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554212 1150 tKLKGDIEELDRNGMTALMIVAHNegrDQVASAKLLVEKGAKVDydgaaRKDSEkykGRTALHYAAQVSNMPIVKYLVgE 1229
Cdd:COG0666  108 -EAGADVNARDKDGETPLHLAAYN---GNLEIVKLLLEAGADVN-----AQDND---GNTPLHLAAANGNLEIVKLLL-E 174

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17554212 1230 KGSNKDKQDEDGKTPIMLAAQEGRIEVVMYLIQQGASVEAVDATDHTARQLAQANNHHNIVDIFDR 1295
Cdd:COG0666  175 AGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240
PHA03095 PHA03095
ankyrin-like protein; Provisional
 1052-1298 1.34e-18

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 90.85  E-value: 1.34e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554212  1052 HNRTVLHWIASNSSaEKSEDLIvheaKECIAAGADVNAMDCDENTPLMLAVL-ARRRRLVAYLMKAGADPTIYNKSERSA 1130
Cdd:PHA03095   46 YGKTPLHLYLHYSS-EKVKDIV----RLLLEAGADVNAPERCGFTPLHLYLYnATTLDVIKLLIKAGADVNAKDKVGRTP 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554212  1131 LHQAAANR--DFGMMVYMLNstkLKGDIEELDRNGMTALMIVAHNEGRDqVASAKLLVEKGAKV-----DYDGA------ 1197
Cdd:PHA03095  121 LHVYLSGFniNPKVIRLLLR---KGADVNALDLYGMTPLAVLLKSRNAN-VELLRLLIDAGADVyavddRFRSLlhhhlq 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554212  1198 -ARKDSEKYK---------------GRTALHYAAQVSNMP---IVKYLvgEKGSNKDKQDEDGKTPIMLAAQEGRIEVVM 1258
Cdd:PHA03095  197 sFKPRARIVReliragcdpaatdmlGNTPLHSMATGSSCKrslVLPLL--IAGISINARNRYGQTPLHYAAVFNNPRACR 274

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 17554212  1259 YLIQQGASVEAVDATDHTARQLAQANNHHNIVDIFDRCRP 1298
Cdd:PHA03095  275 RLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNP 314
NOD pfam06816
NOTCH protein; NOTCH signalling plays a fundamental role during a great number of ...
 753-807 6.35e-18

NOTCH protein; NOTCH signalling plays a fundamental role during a great number of developmental processes in multicellular animals. NOD and NODP represent a region present in many NOTCH proteins and NOTCH homologs in multiple species such as NOTCH2 and NOTCH3, LIN12, SC1 and TAN1. Role of NOD domain remains to be elucidated.


Pssm-ID: 462014  Cd Length: 56  Bit Score: 78.71  E-value: 6.35e-18
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 17554212    753 TNATIITNIRITVQMDPKEFQVTGGQSLMEISSALRVTVRIQRDEEG-PLVFQWNG 807
Cdd:pfam06816    1 PEKLAEGVLVIVVLMDPEELLNNSVQFLRELSTVLRTNVRFKKDENGnPMIYPWYG 56
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1167-1271 5.14e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 71.69  E-value: 5.14e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554212   1167 LMIVAHNEGRDQVasaKLLVEKGAKVDYDGAarkdsekyKGRTALHYAAQVSNMPIVKYLVGEKGSNKDkqdEDGKTPIM 1246
Cdd:pfam12796    1 LHLAAKNGNLELV---KLLLENGADANLQDK--------NGRTALHLAAKNGHLEIVKLLLEHADVNLK---DNGRTALH 66

                           90       100
                   ....*....|....*....|....*
gi 17554212   1247 LAAQEGRIEVVMYLIQQGASVEAVD 1271
Cdd:pfam12796   67 YAARSGHLEIVKLLLEKGADINVKD 91
NODP pfam07684
NOTCH protein; NOTCH signalling plays a fundamental role during a great number of ...
 842-898 2.96e-10

NOTCH protein; NOTCH signalling plays a fundamental role during a great number of developmental processes in multicellular animals. NOD and NODP represent a region present in many NOTCH proteins and NOTCH homologs in multiple species such as NOTCH2 and NOTCH3, LIN12, SC1 and TAN1. The role of the NOD and NODP domains remains to be elucidated.


Pssm-ID: 462229  Cd Length: 59  Bit Score: 57.28  E-value: 2.96e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554212    842 IGVVVYLEVQ-ENCDTG--KClYKDAQSVVDSISARLAKKGIDsFGIPISEALVAEPRKS 898
Cdd:pfam07684    2 IGSVVYLEIDnRKCSQSsdEC-FSTAQSAADFLAALAAKGGLD-LPYPIKEVRSEPPPPP 59
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 365-401 8.72e-10

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 55.34  E-value: 8.72e-10
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 17554212  365 DKNECLSENMCLNNGTCVNLPGSFRCDCARGFGGKWC 401
Cdd:cd00054    1 DIDECASGNPCQNGGTCVNTVGSYRCSCPPGYTGRNC 37
Notch pfam00066
LNR domain; The LNR (Lin-12/Notch repeat) domain is found in three tandem copies in Notch ...
 715-750 1.73e-08

LNR domain; The LNR (Lin-12/Notch repeat) domain is found in three tandem copies in Notch related proteins. The structure of the domain has been determined by NMR and was shown to contain three disulphide bonds and coordinate a calcium ion. Three repeats are also found in the PAPP-A peptidase.


Pssm-ID: 459658  Cd Length: 35  Bit Score: 51.37  E-value: 1.73e-08
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 17554212    715 RCPvkiREHCASRFANGICDPECNTNGCGFDGGDCD 750
Cdd:pfam00066    3 NCP---YPYCWDKFGNGVCDEECNNAECLWDGGDCS 35
NL smart00004
Domain found in Notch and Lin-12; The Notch protein is essential for the proper ...
 635-668 2.67e-08

Domain found in Notch and Lin-12; The Notch protein is essential for the proper differentiation of the Drosophila ectoderm. This protein contains 3 NL domains.


Pssm-ID: 197463  Cd Length: 38  Bit Score: 50.79  E-value: 2.67e-08
                            10        20        30
                    ....*....|....*....|....*....|....
gi 17554212     635 RSVCEKRKCSERANDGNCDADCNYAACKFDGGDC 668
Cdd:smart00004    5 WSRCEDAQCWDKFGDGVCDEECNNAECLWDGGDC 38
EGF_CA smart00179
Calcium-binding EGF-like domain;
365-396 2.69e-08

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 51.09  E-value: 2.69e-08
                            10        20        30
                    ....*....|....*....|....*....|..
gi 17554212     365 DKNECLSENMCLNNGTCVNLPGSFRCDCARGF 396
Cdd:smart00179    1 DIDECASGNPCQNGGTCVNTVGSYRCECPPGY 32
NL smart00004
Domain found in Notch and Lin-12; The Notch protein is essential for the proper ...
 709-749 4.81e-08

Domain found in Notch and Lin-12; The Notch protein is essential for the proper differentiation of the Drosophila ectoderm. This protein contains 3 NL domains.


Pssm-ID: 197463  Cd Length: 38  Bit Score: 50.40  E-value: 4.81e-08
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|.
gi 17554212     709 CLPAVVRCPVKireHCASRFANGICDPECNTNGCGFDGGDC 749
Cdd:smart00004    1 PQDPWSRCEDA---QCWDKFGDGVCDEECNNAECLWDGGDC 38
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 1163-1274 7.36e-08

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: 56.81  E-value: 7.36e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554212 1163 GMTALMIVAHNEGRDQVASAKLLVEKGAKVDYDGA---ARKDSEKYKGRTALHYAAQVSNMPIVKYLVGEKGSNKDKQDE 1239
Cdd:cd21882   26 GKTCLHKAALNLNDGVNEAIMLLLEAAPDSGNPKElvnAPCTDEFYQGQTALHIAIENRNLNLVRLLVENGADVSARATG 105

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 17554212 1240 D------------GKTPIMLAAQEGRIEVVMYLIQQGASVEAVDATD 1274
Cdd:cd21882  106 RffrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGAQPAALEAQD 152
Notch pfam00066
LNR domain; The LNR (Lin-12/Notch repeat) domain is found in three tandem copies in Notch ...
 675-709 8.14e-08

LNR domain; The LNR (Lin-12/Notch repeat) domain is found in three tandem copies in Notch related proteins. The structure of the domain has been determined by NMR and was shown to contain three disulphide bonds and coordinate a calcium ion. Three repeats are also found in the PAPP-A peptidase.


Pssm-ID: 459658  Cd Length: 35  Bit Score: 49.45  E-value: 8.14e-08
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 17554212    675 FSKCRYgNMCADFFANGVCNQACNNEECLYDGMDC 709
Cdd:pfam00066    1 WPNCPY-PYCWDKFGNGVCDEECNNAECLWDGGDC 34
Notch pfam00066
LNR domain; The LNR (Lin-12/Notch repeat) domain is found in three tandem copies in Notch ...
 638-669 2.23e-06

LNR domain; The LNR (Lin-12/Notch repeat) domain is found in three tandem copies in Notch related proteins. The structure of the domain has been determined by NMR and was shown to contain three disulphide bonds and coordinate a calcium ion. Three repeats are also found in the PAPP-A peptidase.


Pssm-ID: 459658  Cd Length: 35  Bit Score: 45.60  E-value: 2.23e-06
                           10        20        30
                   ....*....|....*....|....*....|..
gi 17554212    638 CEKRKCSERANDGNCDADCNYAACKFDGGDCS 669
Cdd:pfam00066    4 CPYPYCWDKFGNGVCDEECNNAECLWDGGDCS 35
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 1087-1301 3.69e-06

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: 51.62  E-value: 3.69e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554212   1087 VNAMDCDEnTPLMLAVL-ARRRRLVAYLMKAGADPTIYNKS-----ERSALHQAAANRDFGMMVYMLNSTKLKGDIEEld 1160
Cdd:TIGR00870    7 VPAEESPL-SDEEKAFLpAAERGDLASVYRDLEEPKKLNINcpdrlGRSALFVAAIENENLELTELLLNLSCRGAVGD-- 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554212   1161 rngmTALMIVAHNEGRDQVASAKLLVEKGAKVDYDGAA--RKDSEKYKGRTALHYAAQVSNMPIVKYLVgEKGSN----- 1233
Cdd:TIGR00870   84 ----TLLHAISLEYVDAVEAILLHLLAAFRKSGPLELAndQYTSEFTPGITALHLAAHRQNYEIVKLLL-ERGASvpara 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554212   1234 -----KDKQDED----GKTPIMLAAQEGRIEVVMYLIQQGASVEAVDATDHTARQLAQANNHHN-------------IVD 1291
Cdd:TIGR00870  159 cgdffVKSQGVDsfyhGESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVMENEFKaeyeelscqmynfALS 238

                          250
                   ....*....|
gi 17554212   1292 IFDRCRPERE 1301
Cdd:TIGR00870  239 LLDKLRDSKE 248
NL smart00004
Domain found in Notch and Lin-12; The Notch protein is essential for the proper ...
 673-709 3.99e-06

Domain found in Notch and Lin-12; The Notch protein is essential for the proper differentiation of the Drosophila ectoderm. This protein contains 3 NL domains.


Pssm-ID: 197463  Cd Length: 38  Bit Score: 44.62  E-value: 3.99e-06
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 17554212     673 EPFSKCRYGNmCADFFANGVCNQACNNEECLYDGMDC 709
Cdd:smart00004    3 DPWSRCEDAQ-CWDKFGDGVCDEECNNAECLWDGGDC 38
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 152-189 4.13e-06

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 44.94  E-value: 4.13e-06
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 17554212  152 DVNECEENkNACGNRSTCMNTLGTYICVCPQGFLPPDC 189
Cdd:cd00054    1 DIDECASG-NPCQNGGTCVNTVGSYRCSCPPGYTGRNC 37
EGF_CA smart00179
Calcium-binding EGF-like domain;
152-184 1.19e-05

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 43.39  E-value: 1.19e-05
                            10        20        30
                    ....*....|....*....|....*....|...
gi 17554212     152 DVNECEENkNACGNRSTCMNTLGTYICVCPQGF 184
Cdd:smart00179    1 DIDECASG-NPCQNGGTCVNTVGSYRCECPPGY 32
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 545-579 1.37e-05

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 43.39  E-value: 1.37e-05
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 17554212  545 DLCLE-NPCSNGGVCHQHRESFSCDCPPGFYGNGCE 579
Cdd:cd00054    3 DECASgNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 547-576 4.17e-05

EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.


Pssm-ID: 394967  Cd Length: 31  Bit Score: 41.60  E-value: 4.17e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 17554212    547 CLENPCSNGGVCHQHRESFSCDCPPGFYGN 576
Cdd:pfam00008    1 CAPNPCSNGGTCVDTPGGYTCICPEGYTGK 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 1240-1269 1.60e-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: 40.26  E-value: 1.60e-04
                            10        20        30
                    ....*....|....*....|....*....|
gi 17554212    1240 DGKTPIMLAAQEGRIEVVMYLIQQGASVEA 1269
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
EGF_CA pfam07645
Calcium-binding EGF domain;
152-183 3.31e-04

Calcium-binding EGF domain;


Pssm-ID: 429571  Cd Length: 32  Bit Score: 39.14  E-value: 3.31e-04
                           10        20        30
                   ....*....|....*....|....*....|..
gi 17554212    152 DVNECEENKNACGNRSTCMNTLGTYICVCPQG 183
Cdd:pfam07645    1 DVDECATGTHNCPANTVCVNTIGSFECRCPDG 32
EGF_CA smart00179
Calcium-binding EGF-like domain;
545-579 4.49e-04

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 39.15  E-value: 4.49e-04
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 17554212     545 DLCLE-NPCSNGGVCHQHRESFSCDCPPGFY-GNGCE 579
Cdd:smart00179    3 DECASgNPCQNGGTCVNTVGSYRCECPPGYTdGRNCE 39
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 293-323 7.17e-04

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 38.39  E-value: 7.17e-04
                         10        20        30
                 ....*....|....*....|....*....|.
gi 17554212  293 NNKCEAGSKCINGVNSYFCDCPPERTGPYCE 323
Cdd:cd00054    8 GNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 252-285 1.67e-03

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 37.23  E-value: 1.67e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 17554212  252 DSCAS-NPCS-HGVCISFSGGFQCICDDGYSGSYCQ 285
Cdd:cd00054    3 DECASgNPCQnGGTCVNTVGSYRCSCPPGYTGRNCE 38
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 371-399 4.35e-03

EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.


Pssm-ID: 394967  Cd Length: 31  Bit Score: 36.21  E-value: 4.35e-03
                           10        20
                   ....*....|....*....|....*....
gi 17554212    371 SENMCLNNGTCVNLPGSFRCDCARGFGGK 399
Cdd:pfam00008    2 APNPCSNGGTCVDTPGGYTCICPEGYTGK 30
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 505-541 4.70e-03

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 36.08  E-value: 4.70e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 17554212  505 NLCLS-DPCMNNATCIDVDAhiGYACICKQGFEGDICE 541
Cdd:cd00054    3 DECASgNPCQNGGTCVNTVG--SYRCSCPPGYTGRNCE 38
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 507-538 5.04e-03

EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.


Pssm-ID: 394967  Cd Length: 31  Bit Score: 35.82  E-value: 5.04e-03
                           10        20        30
                   ....*....|....*....|....*....|..
gi 17554212    507 CLSDPCMNNATCIDVDahIGYACICKQGFEGD 538
Cdd:pfam00008    1 CAPNPCSNGGTCVDTP--GGYTCICPEGYTGK 30
EGF_2 pfam07974
EGF-like domain; This family contains EGF domains found in a variety of extracellular proteins.
 220-245 7.47e-03

EGF-like domain; This family contains EGF domains found in a variety of extracellular proteins.


Pssm-ID: 400365  Cd Length: 26  Bit Score: 35.40  E-value: 7.47e-03
                           10        20
                   ....*....|....*....|....*.
gi 17554212    220 YCQNGGFCDKASSKCQCPPGYHGSTC 245
Cdd:pfam07974    1 ICSGRGTCVNQCGKCVCDSGYQGATC 26
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1070-1295 3.36e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 145.10  E-value: 3.36e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554212 1070 EDLIVHEAKECIAAGADVNAMDCDENTPLMLAVLARRRRLVAYLMKAGADPTIYNKSERSALHQAAANRDFGMMVYMLns 1149
Cdd:COG0666   30 LLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLL-- 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554212 1150 tKLKGDIEELDRNGMTALMIVAHNegrDQVASAKLLVEKGAKVDydgaaRKDSEkykGRTALHYAAQVSNMPIVKYLVgE 1229
Cdd:COG0666  108 -EAGADVNARDKDGETPLHLAAYN---GNLEIVKLLLEAGADVN-----AQDND---GNTPLHLAAANGNLEIVKLLL-E 174

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17554212 1230 KGSNKDKQDEDGKTPIMLAAQEGRIEVVMYLIQQGASVEAVDATDHTARQLAQANNHHNIVDIFDR 1295
Cdd:COG0666  175 AGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1070-1292 4.41e-37

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 142.02  E-value: 4.41e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554212 1070 EDLIVHEAKECIAAGADVNAMDCDENTPLMLAVLARRRRLVAYLMKAGADPTIYNKSERSALHQAAANRDFGMMVYMLNs 1149
Cdd:COG0666   63 LAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLE- 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554212 1150 tklKG-DIEELDRNGMTALMIVAHNegrDQVASAKLLVEKGAKVDYdgaarKDSEkykGRTALHYAAQVSNMPIVKYLVg 1228
Cdd:COG0666  142 ---AGaDVNAQDNDGNTPLHLAAAN---GNLEIVKLLLEAGADVNA-----RDND---GETPLHLAAENGHLEIVKLLL- 206

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17554212 1229 EKGSNKDKQDEDGKTPIMLAAQEGRIEVVMYLIQQGASVEAVDATDHTARQLAQANNHHNIVDI 1292
Cdd:COG0666  207 EAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKL 270
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1081-1292 4.36e-29

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 118.90  E-value: 4.36e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554212 1081 IAAGADVNAMDCDENTPLMLAVLARRRRLVAYLMKAGADPTIYNKSERSALHQAAANRDFGMMVYMLnstKLKGDIEELD 1160
Cdd:COG0666    8 LLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLL---AAGADINAKD 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554212 1161 RNGMTALMIVAHNegrDQVASAKLLVEKGAKVDYDGAarkdsekyKGRTALHYAAQVSNMPIVKYLVgEKGSNKDKQDED 1240
Cdd:COG0666   85 DGGNTLLHAAARN---GDLEIVKLLLEAGADVNARDK--------DGETPLHLAAYNGNLEIVKLLL-EAGADVNAQDND 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 17554212 1241 GKTPIMLAAQEGRIEVVMYLIQQGASVEAVDATDHTARQLAQANNHHNIVDI 1292
Cdd:COG0666  153 GNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKL 204
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1045-1277 1.85e-25

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 108.12  E-value: 1.85e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554212 1045 VNIIDpRHNRTVLHWIASNSSAEKsedlivheAKECIAAGADVNAMDCDENTPLMLAVLARRRRLVAYLMKAGADPTIYN 1124
Cdd:COG0666  113 VNARD-KDGETPLHLAAYNGNLEI--------VKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARD 183

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554212 1125 KSERSALHQAAANRDFGMmvymlnstklkgdieeldrngmtalmivahnegrdqvasAKLLVEKGAKVDydgaaRKDSEk 1204
Cdd:COG0666  184 NDGETPLHLAAENGHLEI---------------------------------------VKLLLEAGADVN-----AKDND- 218

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17554212 1205 ykGRTALHYAAQVSNMPIVKYLVgEKGSNKDKQDEDGKTPIMLAAQEGRIEVVMYLIQQGASVEAVDATDHTA 1277
Cdd:COG0666  219 --GKTALDLAAENGNLEIVKLLL-EAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
PHA03095 PHA03095
ankyrin-like protein; Provisional
 1052-1298 1.34e-18

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 90.85  E-value: 1.34e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554212  1052 HNRTVLHWIASNSSaEKSEDLIvheaKECIAAGADVNAMDCDENTPLMLAVL-ARRRRLVAYLMKAGADPTIYNKSERSA 1130
Cdd:PHA03095   46 YGKTPLHLYLHYSS-EKVKDIV----RLLLEAGADVNAPERCGFTPLHLYLYnATTLDVIKLLIKAGADVNAKDKVGRTP 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554212  1131 LHQAAANR--DFGMMVYMLNstkLKGDIEELDRNGMTALMIVAHNEGRDqVASAKLLVEKGAKV-----DYDGA------ 1197
Cdd:PHA03095  121 LHVYLSGFniNPKVIRLLLR---KGADVNALDLYGMTPLAVLLKSRNAN-VELLRLLIDAGADVyavddRFRSLlhhhlq 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554212  1198 -ARKDSEKYK---------------GRTALHYAAQVSNMP---IVKYLvgEKGSNKDKQDEDGKTPIMLAAQEGRIEVVM 1258
Cdd:PHA03095  197 sFKPRARIVReliragcdpaatdmlGNTPLHSMATGSSCKrslVLPLL--IAGISINARNRYGQTPLHYAAVFNNPRACR 274

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 17554212  1259 YLIQQGASVEAVDATDHTARQLAQANNHHNIVDIFDRCRP 1298
Cdd:PHA03095  275 RLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNP 314
NOD pfam06816
NOTCH protein; NOTCH signalling plays a fundamental role during a great number of ...
 753-807 6.35e-18

NOTCH protein; NOTCH signalling plays a fundamental role during a great number of developmental processes in multicellular animals. NOD and NODP represent a region present in many NOTCH proteins and NOTCH homologs in multiple species such as NOTCH2 and NOTCH3, LIN12, SC1 and TAN1. Role of NOD domain remains to be elucidated.


Pssm-ID: 462014  Cd Length: 56  Bit Score: 78.71  E-value: 6.35e-18
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 17554212    753 TNATIITNIRITVQMDPKEFQVTGGQSLMEISSALRVTVRIQRDEEG-PLVFQWNG 807
Cdd:pfam06816    1 PEKLAEGVLVIVVLMDPEELLNNSVQFLRELSTVLRTNVRFKKDENGnPMIYPWYG 56
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1167-1271 5.14e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 71.69  E-value: 5.14e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554212   1167 LMIVAHNEGRDQVasaKLLVEKGAKVDYDGAarkdsekyKGRTALHYAAQVSNMPIVKYLVGEKGSNKDkqdEDGKTPIM 1246
Cdd:pfam12796    1 LHLAAKNGNLELV---KLLLENGADANLQDK--------NGRTALHLAAKNGHLEIVKLLLEHADVNLK---DNGRTALH 66

                           90       100
                   ....*....|....*....|....*
gi 17554212   1247 LAAQEGRIEVVMYLIQQGASVEAVD 1271
Cdd:pfam12796   67 YAARSGHLEIVKLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1211-1292 1.41e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 67.83  E-value: 1.41e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554212   1211 LHYAAQVSNMPIVKYLVgEKGSNKDKQDEDGKTPIMLAAQEGRIEVVMYLIQQGasveAVDATDH--TARQLAQANNHHN 1288
Cdd:pfam12796    1 LHLAAKNGNLELVKLLL-ENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA----DVNLKDNgrTALHYAARSGHLE 75


                   ....
gi 17554212   1289 IVDI 1292
Cdd:pfam12796   76 IVKL 79
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 1084-1273 2.31e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 70.85  E-value: 2.31e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554212  1084 GADVNAMDCDENTPLML-----AVLARRRRLVAYLMKAGADPTIYNKSERSALHQAAANR--DFGMMVYMLNSTKlkgDI 1156
Cdd:PHA03100   58 GADINSSTKNNSTPLHYlsnikYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKKsnSYSIVEYLLDNGA---NV 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554212  1157 EELDRNGMTALMIVAHNeGRDQVASAKLLVEKGAKVDydgaaRKDSEKY-------------KGRTALHYAAQVSNMPIV 1223
Cdd:PHA03100  135 NIKNSDGENLLHLYLES-NKIDLKILKLLIDKGVDIN-----AKNRVNYllsygvpinikdvYGFTPLHYAVYNNNPEFV 208

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 17554212  1224 KYLVgEKGSNKDKQDEDGKTPIMLAAQEGRIEVVMYLIQQGASVEAVDAT 1273
Cdd:PHA03100  209 KYLL-DLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1098-1193 5.23e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 60.51  E-value: 5.23e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554212   1098 LMLAVLARRRRLVAYLMKAGADPTIYNKSERSALHQAAANRDFGMMVYMLNstklKGDIEELDrNGMTALMIVAHNegrD 1177
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE----HADVNLKD-NGRTALHYAARS---G 72

                           90
                   ....*....|....*.
gi 17554212   1178 QVASAKLLVEKGAKVD 1193
Cdd:pfam12796   73 HLEIVKLLLEKGADIN 88
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1180-1293 1.30e-10

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 64.20  E-value: 1.30e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554212 1180 ASAKLLVEKGAKVDYDGAARKDSEKYKGRTALHYAAQVSNMPIVKYLVgEKGSNKDKQDEDGKTPIMLAAQEGRIEVVMY 1259
Cdd:COG0666   27 AAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLL-AAGADINAKDDGGNTLLHAAARNGDLEIVKL 105

                         90       100       110
                 ....*....|....*....|....*....|....
gi 17554212 1260 LIQQGASVEAVDATDHTARQLAQANNHHNIVDIF 1293
Cdd:COG0666  106 LLEAGADVNARDKDGETPLHLAAYNGNLEIVKLL 139
NODP pfam07684
NOTCH protein; NOTCH signalling plays a fundamental role during a great number of ...
 842-898 2.96e-10

NOTCH protein; NOTCH signalling plays a fundamental role during a great number of developmental processes in multicellular animals. NOD and NODP represent a region present in many NOTCH proteins and NOTCH homologs in multiple species such as NOTCH2 and NOTCH3, LIN12, SC1 and TAN1. The role of the NOD and NODP domains remains to be elucidated.


Pssm-ID: 462229  Cd Length: 59  Bit Score: 57.28  E-value: 2.96e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554212    842 IGVVVYLEVQ-ENCDTG--KClYKDAQSVVDSISARLAKKGIDsFGIPISEALVAEPRKS 898
Cdd:pfam07684    2 IGSVVYLEIDnRKCSQSsdEC-FSTAQSAADFLAALAAKGGLD-LPYPIKEVRSEPPPPP 59
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 1096-1293 8.45e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 62.70  E-value: 8.45e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554212  1096 TPLMLAVLARRRRLVAYLMKAGADPTIYNKSERSALHQAAANRDFGMMVYMLNSTKLKGDIeeLDRNGMTALMIVAHNEG 1175
Cdd:PHA02875   37 SPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDV--FYKDGMTPLHLATILKK 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554212  1176 RDQVasaKLLVEKGAKVDYDGAARKdsekykgrTALHYAAQVSNMPIVKYLVGEKGSNkDKQDEDGKTPIMLAAQEGRIE 1255
Cdd:PHA02875  115 LDIM---KLLIARGADPDIPNTDKF--------SPLHLAVMMGDIKGIELLIDHKACL-DIEDCCGCTPLIIAMAKGDIA 182

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 17554212  1256 VVMYLIQQGASVEAVDAT-DHTARQLAQANNHHNIVDIF 1293
Cdd:PHA02875  183 ICKMLLDSGANIDYFGKNgCVAALCYAIENNKIDIVRLF 221
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 365-401 8.72e-10

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 55.34  E-value: 8.72e-10
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 17554212  365 DKNECLSENMCLNNGTCVNLPGSFRCDCARGFGGKWC 401
Cdd:cd00054    1 DIDECASGNPCQNGGTCVNTVGSYRCSCPPGYTGRNC 37
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1045-1164 1.01e-09

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 61.51  E-value: 1.01e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554212 1045 VNIIDpRHNRTVLHWIASNSSAEksedlIVheaKECIAAGADVNAMDCDENTPLMLAVLARRRRLVAYLMKAGADPTIYN 1124
Cdd:COG0666  179 VNARD-NDGETPLHLAAENGHLE-----IV---KLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKD 249

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 17554212 1125 KSERSALHQAAANRDFGMMVYMLNSTKLKGDIEELDRNGM 1164
Cdd:COG0666  250 KDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
Notch pfam00066
LNR domain; The LNR (Lin-12/Notch repeat) domain is found in three tandem copies in Notch ...
 715-750 1.73e-08

LNR domain; The LNR (Lin-12/Notch repeat) domain is found in three tandem copies in Notch related proteins. The structure of the domain has been determined by NMR and was shown to contain three disulphide bonds and coordinate a calcium ion. Three repeats are also found in the PAPP-A peptidase.


Pssm-ID: 459658  Cd Length: 35  Bit Score: 51.37  E-value: 1.73e-08
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 17554212    715 RCPvkiREHCASRFANGICDPECNTNGCGFDGGDCD 750
Cdd:pfam00066    3 NCP---YPYCWDKFGNGVCDEECNNAECLWDGGDCS 35
NL smart00004
Domain found in Notch and Lin-12; The Notch protein is essential for the proper ...
 635-668 2.67e-08

Domain found in Notch and Lin-12; The Notch protein is essential for the proper differentiation of the Drosophila ectoderm. This protein contains 3 NL domains.


Pssm-ID: 197463  Cd Length: 38  Bit Score: 50.79  E-value: 2.67e-08
                            10        20        30
                    ....*....|....*....|....*....|....
gi 17554212     635 RSVCEKRKCSERANDGNCDADCNYAACKFDGGDC 668
Cdd:smart00004    5 WSRCEDAQCWDKFGDGVCDEECNNAECLWDGGDC 38
EGF_CA smart00179
Calcium-binding EGF-like domain;
365-396 2.69e-08

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 51.09  E-value: 2.69e-08
                            10        20        30
                    ....*....|....*....|....*....|..
gi 17554212     365 DKNECLSENMCLNNGTCVNLPGSFRCDCARGF 396
Cdd:smart00179    1 DIDECASGNPCQNGGTCVNTVGSYRCECPPGY 32
Ank_4 pfam13637
Ankyrin repeats (many copies);
1207-1261 2.85e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.51  E-value: 2.85e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 17554212   1207 GRTALHYAAQVSNMPIVKYLVgEKGSNKDKQDEDGKTPIMLAAQEGRIEVVMYLI 1261
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLL-EKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
NL smart00004
Domain found in Notch and Lin-12; The Notch protein is essential for the proper ...
 709-749 4.81e-08

Domain found in Notch and Lin-12; The Notch protein is essential for the proper differentiation of the Drosophila ectoderm. This protein contains 3 NL domains.


Pssm-ID: 197463  Cd Length: 38  Bit Score: 50.40  E-value: 4.81e-08
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|.
gi 17554212     709 CLPAVVRCPVKireHCASRFANGICDPECNTNGCGFDGGDC 749
Cdd:smart00004    1 PQDPWSRCEDA---QCWDKFGDGVCDEECNNAECLWDGGDC 38
PHA03095 PHA03095
ankyrin-like protein; Provisional
 1051-1203 5.81e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 56.96  E-value: 5.81e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554212  1051 RHNRTVLHWIASNSSAEKS--EDLIvheakeciAAGADVNAMDCDENTPLMLAVLARRRRLVAYLMKAGADPTIYNKSER 1128
Cdd:PHA03095  220 MLGNTPLHSMATGSSCKRSlvLPLL--------IAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGN 291

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17554212  1129 SALHQAAANRDFGMMVYMLNStklKGDIEELDRngmtALMIVAHNEGRDQVASAKLLVekgAKVDYDGAARKDSE 1203
Cdd:PHA03095  292 TPLSLMVRNNNGRAVRAALAK---NPSAETVAA----TLNTASVAGGDIPSDATRLCV---AKVVLRGAFSLLPE 356
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 1163-1274 7.36e-08

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: 56.81  E-value: 7.36e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554212 1163 GMTALMIVAHNEGRDQVASAKLLVEKGAKVDYDGA---ARKDSEKYKGRTALHYAAQVSNMPIVKYLVGEKGSNKDKQDE 1239
Cdd:cd21882   26 GKTCLHKAALNLNDGVNEAIMLLLEAAPDSGNPKElvnAPCTDEFYQGQTALHIAIENRNLNLVRLLVENGADVSARATG 105

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 17554212 1240 D------------GKTPIMLAAQEGRIEVVMYLIQQGASVEAVDATD 1274
Cdd:cd21882  106 RffrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGAQPAALEAQD 152
Notch pfam00066
LNR domain; The LNR (Lin-12/Notch repeat) domain is found in three tandem copies in Notch ...
 675-709 8.14e-08

LNR domain; The LNR (Lin-12/Notch repeat) domain is found in three tandem copies in Notch related proteins. The structure of the domain has been determined by NMR and was shown to contain three disulphide bonds and coordinate a calcium ion. Three repeats are also found in the PAPP-A peptidase.


Pssm-ID: 459658  Cd Length: 35  Bit Score: 49.45  E-value: 8.14e-08
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 17554212    675 FSKCRYgNMCADFFANGVCNQACNNEECLYDGMDC 709
Cdd:pfam00066    1 WPNCPY-PYCWDKFGNGVCDEECNNAECLWDGGDC 34
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 1081-1267 1.89e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 55.84  E-value: 1.89e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554212  1081 IAAGADVNAMDCDENTPLMLA-VLARRRRLVAYLMKAGADPTIYNKSERSALHQAAANRDFGMMVYMLNstkLKGDIEEL 1159
Cdd:PHA02876  328 IMLGADVNAADRLYITPLHQAsTLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLD---YGADIEAL 404

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554212  1160 DRNGMTALMIVAHneGRDQVASAKLLVEKGAKVdydgaarkDSEKYKGRTALHYAAQVSNMPIVKYLVGEKGSNKDKQDE 1239
Cdd:PHA02876  405 SQKIGTALHFALC--GTNPYMSVKTLIDRGANV--------NSKNKDLSTPLHYACKKNCKLDVIEMLLDNGADVNAINI 474

                         170       180
                  ....*....|....*....|....*...
gi 17554212  1240 DGKTPIMLAAqeGRIEVVMYLIQQGASV 1267
Cdd:PHA02876  475 QNQYPLLIAL--EYHGIVNILLHYGAEL 500
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 1077-1271 3.70e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 54.68  E-value: 3.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554212  1077 AKECIAAGADVNAMDCDENTPLMLAVLARRRRLVAYLMKAGADPTIYNKSERSALHQAAANRDFGMMVYMLNSTklkgdi 1156
Cdd:PHA02876  161 AEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNR------ 234

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554212  1157 EELDRNGMTALMIVAHNEgrdqVASAKLLVEKGAKVDydgaarkDSEKYKgRTALHYAAQVSNMPIVKYLVGEKGSNKDK 1236
Cdd:PHA02876  235 SNINKNDLSLLKAIRNED----LETSLLLYDAGFSVN-------SIDDCK-NTPLHHASQAPSLSRLVPKLLERGADVNA 302

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 17554212  1237 QDEDGKTPIMLAAQEG-RIEVVMYLIQQGASVEAVD 1271
Cdd:PHA02876  303 KNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAAD 338
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 1067-1293 6.46e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 53.52  E-value: 6.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554212  1067 EKSEDLIVHEAKECIAAGADVNAMDCDENTPLMLAVLARRRRLVAYLMKAGADPTIYNKSERSALHQAAanrdfgmmVYM 1146
Cdd:PHA03100    8 TKSRIIKVKNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLS--------NIK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554212  1147 LNSTKLK----------GDIEELDRNGMTALMIVAHNEgRDQVASAKLLVEKGAKVDydgaarkdSEKYKGRTALHYAAQ 1216
Cdd:PHA03100   80 YNLTDVKeivkllleygANVNAPDNNGITPLLYAISKK-SNSYSIVEYLLDNGANVN--------IKNSDGENLLHLYLE 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17554212  1217 VS--NMPIVKYLVgEKGSNKDKQDedgktpimlaaqegRIEvvmYLIQQGASVEAVDATDHTARQLAQANNHHNIVDIF 1293
Cdd:PHA03100  151 SNkiDLKILKLLI-DKGVDINAKN--------------RVN---YLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYL 211
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 1113-1274 1.04e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 53.33  E-value: 1.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554212  1113 LMKAGADPTIYNKSERSALHQAAANRDFGMMVYMLnstKLKGDIEELDRNGMTALMivahnegrDQVASAKllvEKGAKV 1192
Cdd:PLN03192  544 LLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLL---KHACNVHIRDANGNTALW--------NAISAKH---HKIFRI 609

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554212  1193 DYDGAARkdSEKYKGRTALHYAAQVSNMPIVKYLVgEKGSNKDKQDEDGKTPIMLAAQEGRIEVVMYLIQQGASVEAVDA 1272
Cdd:PLN03192  610 LYHFASI--SDPHAAGDLLCTAAKRNDLTAMKELL-KQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANT 686


                  ..
gi 17554212  1273 TD 1274
Cdd:PLN03192  687 DD 688
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 1078-1276 1.12e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 52.96  E-value: 1.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554212  1078 KECIAAGADVNAMDCDENTPLMLAVLARRRRLVAYLMKAGADPTIYNksERSALHQAAANRDFGMM-VYMLNSTKLKGDI 1156
Cdd:PHA02878   54 KSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVFY--TLVAIKDAFNNRNVEIFkIILTNRYKNIQTI 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554212  1157 E-----ELDRNGMTALMIVahnegrdqvasaKLLVEKGAKVdydgaarKDSEKYKGRTALHYAAQVSNMPIVKYLVgEKG 1231
Cdd:PHA02878  132 DlvyidKKSKDDIIEAEIT------------KLLLSYGADI-------NMKDRHKGNTALHYATENKDQRLTELLL-SYG 191

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 17554212  1232 SNKDKQDEDGKTPIMLAAQEGRIEVVMYLIQQGASVEAVDATDHT 1276
Cdd:PHA02878  192 ANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNT 236
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 1081-1294 1.41e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 52.66  E-value: 1.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554212  1081 IAAGADVNAMDCDENTPLMLAVLARRRRLVAYLMKAGADPTIY-----------------------NKSERSALHQAAAN 1137
Cdd:PHA02874   55 IKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSILpipciekdmiktildcgidvnikDAELKTFLHYAIKK 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554212  1138 RDFGMMVYMLnstKLKGDIEELDRNGMTALMIVAHNEGRDQVasaKLLVEKGAKVDYDgaarkdseKYKGRTALHYAAQV 1217
Cdd:PHA02874  135 GDLESIKMLF---EYGADVNIEDDNGCYPIHIAIKHNFFDII---KLLLEKGAYANVK--------DNNGESPLHNAAEY 200

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17554212  1218 SNMPIVKYLVgEKGSNKDKQDEDGKTPIMLAAQEGRiEVVMYLIQQgASVEAVDATDHTArqLAQANNHHNIVDIFD 1294
Cdd:PHA02874  201 GDYACIKLLI-DHGNHIMNKCKNGFTPLHNAIIHNR-SAIELLINN-ASINDQDIDGSTP--LHHAINPPCDIDIID 272
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 1093-1302 1.60e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 52.30  E-value: 1.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554212  1093 DENTPLMLAVLARRRRLVAYLMKAGADPTIYNKSERSALHQAAANRDFGMMVYMLNStKLKGDIEelDRNGMTALMIVAh 1172
Cdd:PHA02875  101 DGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDH-KACLDIE--DCCGCTPLIIAM- 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554212  1173 neGRDQVASAKLLVEKGAKVDYDGaarkdseKYKGRTALHYAAQVSNMPIVKYLVgekgsnkdKQDEDGKTPIMLAAQEG 1252
Cdd:PHA02875  177 --AKGDIAICKMLLDSGANIDYFG-------KNGCVAALCYAIENNKIDIVRLFI--------KRGADCNIMFMIEGEEC 239

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17554212  1253 RIEVVMYLIQQGASVEAVDA-------TDHT---------ARQLAQANNHHNIVDIFDRCRPEREY 1302
Cdd:PHA02875  240 TILDMICNMCTNLESEAIDAliadiaiRIHKktirrdegfKNNMSTIEDKEEFKDVFEKCIIELRR 305
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 1229-1299 2.18e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.21  E-value: 2.18e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17554212  1229 EKGSNKDKQDEDGKTPIMLAAQEGRIEVVMYLIQQGASVEAVDATDHTARQLAQANNHHNIVDIFDRCRPE 1299
Cdd:PTZ00322  103 TGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQC 173
Notch pfam00066
LNR domain; The LNR (Lin-12/Notch repeat) domain is found in three tandem copies in Notch ...
 638-669 2.23e-06

LNR domain; The LNR (Lin-12/Notch repeat) domain is found in three tandem copies in Notch related proteins. The structure of the domain has been determined by NMR and was shown to contain three disulphide bonds and coordinate a calcium ion. Three repeats are also found in the PAPP-A peptidase.


Pssm-ID: 459658  Cd Length: 35  Bit Score: 45.60  E-value: 2.23e-06
                           10        20        30
                   ....*....|....*....|....*....|..
gi 17554212    638 CEKRKCSERANDGNCDADCNYAACKFDGGDCS 669
Cdd:pfam00066    4 CPYPYCWDKFGNGVCDEECNNAECLWDGGDCS 35
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 1120-1294 3.31e-06

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: 51.73  E-value: 3.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554212 1120 PTIYNkseRSALHQAAANRDF----GMMVYMLNSTKLKGDIEELD-RNGMTAL---MIVAHNEGRDQVASAKLLVEKGAK 1191
Cdd:cd22196    2 FKLYD---RRRIFDAVAKGDCkeldGLLEYLMRTKKRLTDSEFKDpETGKTCLlkaMLNLHNGQNDTISLLLDIAEKTGN 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554212 1192 V-DYDGAARKDSeKYKGRTALHYAAQVSNMPIVKYLVgEKGSN----------KDKQDED----GKTPIMLAAQEGRIEV 1256
Cdd:cd22196   79 LkEFVNAAYTDS-YYKGQTALHIAIERRNMHLVELLV-QNGADvharasgeffKKKKGGPgfyfGELPLSLAACTNQLDI 156

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 17554212 1257 VMYLIQQGASVEAVDATDhtarqlAQANN-HHNIVDIFD 1294
Cdd:cd22196  157 VKFLLENPHSPADISARD------SMGNTvLHALVEVAD 189
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 1087-1301 3.69e-06

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: 51.62  E-value: 3.69e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554212   1087 VNAMDCDEnTPLMLAVL-ARRRRLVAYLMKAGADPTIYNKS-----ERSALHQAAANRDFGMMVYMLNSTKLKGDIEEld 1160
Cdd:TIGR00870    7 VPAEESPL-SDEEKAFLpAAERGDLASVYRDLEEPKKLNINcpdrlGRSALFVAAIENENLELTELLLNLSCRGAVGD-- 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554212   1161 rngmTALMIVAHNEGRDQVASAKLLVEKGAKVDYDGAA--RKDSEKYKGRTALHYAAQVSNMPIVKYLVgEKGSN----- 1233
Cdd:TIGR00870   84 ----TLLHAISLEYVDAVEAILLHLLAAFRKSGPLELAndQYTSEFTPGITALHLAAHRQNYEIVKLLL-ERGASvpara 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554212   1234 -----KDKQDED----GKTPIMLAAQEGRIEVVMYLIQQGASVEAVDATDHTARQLAQANNHHN-------------IVD 1291
Cdd:TIGR00870  159 cgdffVKSQGVDsfyhGESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVMENEFKaeyeelscqmynfALS 238

                          250
                   ....*....|
gi 17554212   1292 IFDRCRPERE 1301
Cdd:TIGR00870  239 LLDKLRDSKE 248
NL smart00004
Domain found in Notch and Lin-12; The Notch protein is essential for the proper ...
 673-709 3.99e-06

Domain found in Notch and Lin-12; The Notch protein is essential for the proper differentiation of the Drosophila ectoderm. This protein contains 3 NL domains.


Pssm-ID: 197463  Cd Length: 38  Bit Score: 44.62  E-value: 3.99e-06
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 17554212     673 EPFSKCRYGNmCADFFANGVCNQACNNEECLYDGMDC 709
Cdd:smart00004    3 DPWSRCEDAQ-CWDKFGDGVCDEECNNAECLWDGGDC 38
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 152-189 4.13e-06

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 44.94  E-value: 4.13e-06
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 17554212  152 DVNECEENkNACGNRSTCMNTLGTYICVCPQGFLPPDC 189
Cdd:cd00054    1 DIDECASG-NPCQNGGTCVNTVGSYRCSCPPGYTGRNC 37
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1245-1293 6.42e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 45.88  E-value: 6.42e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 17554212   1245 IMLAAQEGRIEVVMYLIQQGASVEAVDATDHTARQLAQANNHHNIVDIF 1293
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLL 49
EGF_CA smart00179
Calcium-binding EGF-like domain;
152-184 1.19e-05

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 43.39  E-value: 1.19e-05
                            10        20        30
                    ....*....|....*....|....*....|...
gi 17554212     152 DVNECEENkNACGNRSTCMNTLGTYICVCPQGF 184
Cdd:smart00179    1 DIDECASG-NPCQNGGTCVNTVGSYRCECPPGY 32
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 1189-1260 1.24e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.90  E-value: 1.24e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17554212  1189 GAKVDYDGAARKDSEKYKGRTALHYAAQVSNMPIVKYLVgEKGSNKDKQDEDGKTPIMLAAQEGRIEVVMYL 1260
Cdd:PTZ00322   97 GARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLL-EFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 545-579 1.37e-05

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 43.39  E-value: 1.37e-05
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 17554212  545 DLCLE-NPCSNGGVCHQHRESFSCDCPPGFYGNGCE 579
Cdd:cd00054    3 DECASgNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 1045-1193 2.16e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 48.72  E-value: 2.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554212  1045 VNIIDPRHNRTVLHWIASNSSAEKSEDLIVHeakeciaaGADVNAMDCDENTPLMLAVLARRRRLVAYLMKAGADPTIYN 1124
Cdd:PHA02878  160 INMKDRHKGNTALHYATENKDQRLTELLLSY--------GANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARD 231

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17554212  1125 KSERSALHQAAAnrdfgmmvYMLNSTKLKGDIEE-LDRN------GMTALMIVAHNEGRdqvasAKLLVEKGAKVD 1193
Cdd:PHA02878  232 KCGNTPLHISVG--------YCKDYDILKLLLEHgVDVNaksyilGLTALHSSIKSERK-----LKLLLEYGADIN 294
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1045-1124 2.78e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 43.95  E-value: 2.78e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554212   1045 VNIIDPRhNRTVLHWIASNSSAEksedlIVheakECIAAGADVNaMDCDENTPLMLAVLARRRRLVAYLMKAGADPTIYN 1124
Cdd:pfam12796   23 ANLQDKN-GRTALHLAAKNGHLE-----IV----KLLLEHADVN-LKDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 1240-1271 3.71e-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: 41.89  E-value: 3.71e-05
                           10        20        30
                   ....*....|....*....|....*....|...
gi 17554212   1240 DGKTPIMLAA-QEGRIEVVMYLIQQGASVEAVD 1271
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 547-576 4.17e-05

EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.


Pssm-ID: 394967  Cd Length: 31  Bit Score: 41.60  E-value: 4.17e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 17554212    547 CLENPCSNGGVCHQHRESFSCDCPPGFYGN 576
Cdd:pfam00008    1 CAPNPCSNGGTCVDTPGGYTCICPEGYTGK 30
EGF cd00053
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ...
 368-399 4.34e-05

Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large number of proteins, mostly animal; the list of proteins currently known to contain one or more copies of an EGF-like pattern is large and varied; the functional significance of EGF-like domains in what appear to be unrelated proteins is not yet clear; a common feature is that these repeats are found in the extracellular domain of membrane-bound proteins or in proteins known to be secreted (exception: prostaglandin G/H synthase); the domain includes six cysteine residues which have been shown to be involved in disulfide bonds; the main structure is a two-stranded beta-sheet followed by a loop to a C-terminal short two-stranded sheet; Subdomains between the conserved cysteines vary in length; the region between the 5th and 6th cysteine contains two conserved glycines of which at least one is present in most EGF-like domains; a subset of these bind calcium.


Pssm-ID: 238010  Cd Length: 36  Bit Score: 41.69  E-value: 4.34e-05
                         10        20        30
                 ....*....|....*....|....*....|..
gi 17554212  368 ECLSENMCLNNGTCVNLPGSFRCDCARGFGGK 399
Cdd:cd00053    1 ECAASNPCSNGGTCVNTPGSYRCVCPPGYTGD 32
PHA03095 PHA03095
ankyrin-like protein; Provisional
 1183-1292 6.68e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 47.33  E-value: 6.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554212  1183 KLLVEKGAKVDYDGAArkdsekykGRTALHYAAQVSNMP---IVKYLVgEKGSNKDKQDEDGKTPIMLAAQEG-RIEVVM 1258
Cdd:PHA03095   31 RRLLAAGADVNFRGEY--------GKTPLHLYLHYSSEKvkdIVRLLL-EAGADVNAPERCGFTPLHLYLYNAtTLDVIK 101

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 17554212  1259 YLIQQGASVEAVDATDHTARQ--LAQANNHHNIVDI 1292
Cdd:PHA03095  102 LLIKAGADVNAKDKVGRTPLHvyLSGFNINPKVIRL 137
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1057-1149 8.22e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 42.80  E-value: 8.22e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554212   1057 LHWIASNSSAEksedlIVHEAkecIAAGADVNAMDCDENTPLMLAVLARRRRLVAYLM-KAGADPTIYNkseRSALHQAA 1135
Cdd:pfam12796    1 LHLAAKNGNLE-----LVKLL---LENGADANLQDKNGRTALHLAAKNGHLEIVKLLLeHADVNLKDNG---RTALHYAA 69

                           90
                   ....*....|....
gi 17554212   1136 ANRDFGMMVYMLNS 1149
Cdd:pfam12796   70 RSGHLEIVKLLLEK 83
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 1029-1149 1.29e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.43  E-value: 1.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554212  1029 EAAGSYAITEPITRESVNIIDPrhnrTVLHWIASN-SSAEKSEDLIvhEAKECIAAGADVNAMDCDENTPLMLAVLARRR 1107
Cdd:PTZ00322   55 EATENKDATPDHNLTTEEVIDP----VVAHMLTVElCQLAASGDAV--GARILLTGGADPNCRDYDGRTPLHIACANGHV 128

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 17554212  1108 RLVAYLMKAGADPTIYNKSERSALHQAAANrDFGMMVYMLNS 1149
Cdd:PTZ00322  129 QVVRVLLEFGADPTLLDKDGKTPLELAEEN-GFREVVQLLSR 169
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 1240-1269 1.60e-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: 40.26  E-value: 1.60e-04
                            10        20        30
                    ....*....|....*....|....*....|
gi 17554212    1240 DGKTPIMLAAQEGRIEVVMYLIQQGASVEA 1269
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
EGF_CA pfam07645
Calcium-binding EGF domain;
152-183 3.31e-04

Calcium-binding EGF domain;


Pssm-ID: 429571  Cd Length: 32  Bit Score: 39.14  E-value: 3.31e-04
                           10        20        30
                   ....*....|....*....|....*....|..
gi 17554212    152 DVNECEENKNACGNRSTCMNTLGTYICVCPQG 183
Cdd:pfam07645    1 DVDECATGTHNCPANTVCVNTIGSFECRCPDG 32
Ank_5 pfam13857
Ankyrin repeats (many copies);
1085-1134 3.85e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.64  E-value: 3.85e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 17554212   1085 ADVNAMDCDENTPLMLAVLARRRRLVAYLMKAGADPTIYNKSERSALHQA 1134
Cdd:pfam13857    7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02798 PHA02798
ankyrin-like protein; Provisional
 1183-1292 3.94e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 44.83  E-value: 3.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554212  1183 KLLVEKGAKVDydgaaRKDSEKYKGRTAL--HYAAQVSNMPIVKYLVgEKGSNKDKQDEDGKTPIMLAAQEGRI---EVV 1257
Cdd:PHA02798   55 KLFINLGANVN-----GLDNEYSTPLCTIlsNIKDYKHMLDIVKILI-ENGADINKKNSDGETPLYCLLSNGYInnlEIL 128

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 17554212  1258 MYLIQQGASVEAVDATDHTARQLAQANNHHNIVDI 1292
Cdd:PHA02798  129 LFMIENGADTTLLDKDGFTMLQVYLQSNHHIDIEI 163
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 1045-1248 4.20e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 44.57  E-value: 4.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554212  1045 VNIIDpRHNRTVLHWIASNSSAEKSEDLIVHeakeciaaGADVNAMDCDENTPLMLAVLARRRRLVAYLMKAGADPTIYN 1124
Cdd:PHA02874  117 VNIKD-AELKTFLHYAIKKGDLESIKMLFEY--------GADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKD 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554212  1125 KSERSALHQAAANRDFGMMVYMLNSTKlkgDIEELDRNGMTALmivaHNEGRDQVASAKLLVEKGAKVDYDgaarkdsek 1204
Cdd:PHA02874  188 NNGESPLHNAAEYGDYACIKLLIDHGN---HIMNKCKNGFTPL----HNAIIHNRSAIELLINNASINDQD--------- 251

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 17554212  1205 YKGRTALHYAAQVS-NMPIVKYLVGEKgSNKDKQDEDGKTPIMLA 1248
Cdd:PHA02874  252 IDGSTPLHHAINPPcDIDIIDILLYHK-ADISIKDNKGENPIDTA 295
EGF_CA smart00179
Calcium-binding EGF-like domain;
545-579 4.49e-04

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 39.15  E-value: 4.49e-04
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 17554212     545 DLCLE-NPCSNGGVCHQHRESFSCDCPPGFY-GNGCE 579
Cdd:smart00179    3 DECASgNPCQNGGTCVNTVGSYRCECPPGYTdGRNCE 39
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 1203-1276 6.68e-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: 44.02  E-value: 6.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554212 1203 EKYKGRTALHYAAQVSNMPIVKYLVgEKGS-----------NKDKQDED---GKTPIMLAAQEGRIEVVMYLIQ---QGA 1265
Cdd:cd22193   72 EYYEGQTALHIAIERRQGDIVALLV-ENGAdvhahakgrffQPKYQGEGfyfGELPLSLAACTNQPDIVQYLLEnehQPA 150

                         90
                 ....*....|.
gi 17554212 1266 SVEAVDATDHT 1276
Cdd:cd22193  151 DIEAQDSRGNT 161
Ank_4 pfam13637
Ankyrin repeats (many copies);
1127-1186 6.94e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.79  E-value: 6.94e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554212   1127 ERSALHQAAANRDFGMMVYMLNSTKlkgDIEELDRNGMTALMIVAHNEgrdQVASAKLLV 1186
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGA---DINAVDGNGETALHFAASNG---NVEVLKLLL 54
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 293-323 7.17e-04

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 38.39  E-value: 7.17e-04
                         10        20        30
                 ....*....|....*....|....*....|.
gi 17554212  293 NNKCEAGSKCINGVNSYFCDCPPERTGPYCE 323
Cdd:cd00054    8 GNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
EGF cd00053
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ...
 550-579 1.08e-03

Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large number of proteins, mostly animal; the list of proteins currently known to contain one or more copies of an EGF-like pattern is large and varied; the functional significance of EGF-like domains in what appear to be unrelated proteins is not yet clear; a common feature is that these repeats are found in the extracellular domain of membrane-bound proteins or in proteins known to be secreted (exception: prostaglandin G/H synthase); the domain includes six cysteine residues which have been shown to be involved in disulfide bonds; the main structure is a two-stranded beta-sheet followed by a loop to a C-terminal short two-stranded sheet; Subdomains between the conserved cysteines vary in length; the region between the 5th and 6th cysteine contains two conserved glycines of which at least one is present in most EGF-like domains; a subset of these bind calcium.


Pssm-ID: 238010  Cd Length: 36  Bit Score: 37.84  E-value: 1.08e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 17554212  550 NPCSNGGVCHQHRESFSCDCPPGFYGNG-CE 579
Cdd:cd00053    6 NPCSNGGTCVNTPGSYRCVCPPGYTGDRsCE 36
Ank_4 pfam13637
Ankyrin repeats (many copies);
1094-1147 1.18e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.41  E-value: 1.18e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 17554212   1094 ENTPLMLAVLARRRRLVAYLMKAGADPTIYNKSERSALHQAAANRDFGMMVYML 1147
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 252-285 1.67e-03

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 37.23  E-value: 1.67e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 17554212  252 DSCAS-NPCS-HGVCISFSGGFQCICDDGYSGSYCQ 285
Cdd:cd00054    3 DECASgNPCQnGGTCVNTVGSYRCSCPPGYTGRNCE 38
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 1206-1239 3.19e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 36.50  E-value: 3.19e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 17554212   1206 KGRTALHYAA-QVSNMPIVKYLVgEKGSNKDKQDE 1239
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLL-SKGADVNARDK 34
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 371-399 4.35e-03

EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.


Pssm-ID: 394967  Cd Length: 31  Bit Score: 36.21  E-value: 4.35e-03
                           10        20
                   ....*....|....*....|....*....
gi 17554212    371 SENMCLNNGTCVNLPGSFRCDCARGFGGK 399
Cdd:pfam00008    2 APNPCSNGGTCVDTPGGYTCICPEGYTGK 30
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 1231-1296 4.36e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 41.78  E-value: 4.36e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17554212  1231 GSNKDKQDEDGKTPIMLAAQEGRIEVVMYLIQQGASVEAVDATDHTARQLAQANNHHNIVDIFDRC 1296
Cdd:PLN03192  548 KLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHF 613
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 505-541 4.70e-03

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 36.08  E-value: 4.70e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 17554212  505 NLCLS-DPCMNNATCIDVDAhiGYACICKQGFEGDICE 541
Cdd:cd00054    3 DECASgNPCQNGGTCVNTVG--SYRCSCPPGYTGRNCE 38
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 507-538 5.04e-03

EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.


Pssm-ID: 394967  Cd Length: 31  Bit Score: 35.82  E-value: 5.04e-03
                           10        20        30
                   ....*....|....*....|....*....|..
gi 17554212    507 CLSDPCMNNATCIDVDahIGYACICKQGFEGD 538
Cdd:pfam00008    1 CAPNPCSNGGTCVDTP--GGYTCICPEGYTGK 30
Ank_4 pfam13637
Ankyrin repeats (many copies);
1243-1293 5.38e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.48  E-value: 5.38e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 17554212   1243 TPIMLAAQEGRIEVVMYLIQQGASVEAVDATDHTARQLAQANNHHNIVDIF 1293
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
EGF_2 pfam07974
EGF-like domain; This family contains EGF domains found in a variety of extracellular proteins.
 220-245 7.47e-03

EGF-like domain; This family contains EGF domains found in a variety of extracellular proteins.


Pssm-ID: 400365  Cd Length: 26  Bit Score: 35.40  E-value: 7.47e-03
                           10        20
                   ....*....|....*....|....*.
gi 17554212    220 YCQNGGFCDKASSKCQCPPGYHGSTC 245
Cdd:pfam07974    1 ICSGRGTCVNQCGKCVCDSGYQGATC 26
PHA02798 PHA02798
ankyrin-like protein; Provisional
 1078-1227 9.30e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 40.20  E-value: 9.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554212  1078 KECIAAGADVNAMDCDENTPL--MLAVLARRRR---LVAYLMKAGADPTIYNKSERSALHQAAANRDFGMMVYMLNSTKL 1152
Cdd:PHA02798   55 KLFINLGANVNGLDNEYSTPLctILSNIKDYKHmldIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILLFMIEN 134

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17554212  1153 KGDIEELDRNGMTALMIVAHNEGRDQVASAKLLVEKGAKVDydgaARKDSEKYkgrTALH----YAAQVSNMPIVKYLV 1227
Cdd:PHA02798  135 GADTTLLDKDGFTMLQVYLQSNHHIDIEIIKLLLEKGVDIN----THNNKEKY---DTLHcyfkYNIDRIDADILKLFV 206
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 1124-1276 9.30e-03

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


Pssm-ID: 411981 [Multi-domain]  Cd Length: 640  Bit Score: 40.61  E-value: 9.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554212 1124 NKSERSALHQAAANRD----FGMMVYMLNSTKLKGDIEELD-RNGMTALMIVAHNEGRDQVASAKLLVEKGAK------- 1191
Cdd:cd22197    3 NRFDRDRLFSVVSRGNpeelAGLLEYLRRTSKYLTDSEYTEgSTGKTCLMKAVLNLQDGVNACIMPLLEIDKDsgnpkpl 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554212 1192 VDydgaARKDSEKYKGRTALHYAAQVSNMPIVKYLVgEKGSN----------KDKQDED---GKTPIMLAAQEGRIEVVM 1258
Cdd:cd22197   83 VN----AQCTDEYYRGHSALHIAIEKRSLQCVKLLV-ENGADvharacgrffQKKQGTCfyfGELPLSLAACTKQWDVVN 157

                        170       180
                 ....*....|....*....|.
gi 17554212 1259 YLIQ---QGASVEAVDATDHT 1276
Cdd:cd22197  158 YLLEnphQPASLQAQDSLGNT 178
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 1162-1193 9.89e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 34.96  E-value: 9.89e-03
                           10        20        30
                   ....*....|....*....|....*....|..
gi 17554212   1162 NGMTALMIVAHNEGRDQVasAKLLVEKGAKVD 1193
Cdd:pfam00023    1 DGNTPLHLAAGRRGNLEI--VKLLLSKGADVN 30
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH