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Conserved domains on  [gi|1043392481|ref|NP_001316372|]
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protein phosphatase 1 regulatory subunit 16A [Homo sapiens]

Protein Classification

ankyrin repeat domain-containing protein( domain architecture ID 11429852)

ankyrin repeat domain-containing protein; ANK proteins mediate specific protein-protein interactions without necessarily recognizing specific primary sequences which allows for one ankyrin repeat domain to recognize and bind to a variety of intracellular substrates and may be involved in a wide array of functions

Gene Ontology:  GO:0005515
PubMed:  17176038
SCOP:  4000366

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
75-327 1.43e-35

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 134.70  E-value: 1.43e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043392481  75 LLEAAARNDLEEVRQFLGSGVSPDLANEDGLTALHQCCIDDFREMVQQLLEAGANINACDSECWTPLHAAATCGHLHLVE 154
Cdd:COG0666    58 LLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVK 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043392481 155 LLIASGANLLAVNTDGNMPydlcddeqtldcLETAmadrgITQDSIEAARavpelrMLddirsrLQAGADLHAPLDHGAT 234
Cdd:COG0666   138 LLLEAGADVNAQDNDGNTP------------LHLA-----AANGNLEIVK------LL------LEAGADVNARDNDGET 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043392481 235 LLHVAAANGFSEAAALLLEHRASLSAKDQDGWEPLHAAAYWGQVPLVELLVAHGADLNAKSLMDETPLD---VCGDEEVR 311
Cdd:COG0666   189 PLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLlaaAAGAALIV 268

                         250
                  ....*....|....*.
gi 1043392481 312 AKLLELKHKHDALLRA 327
Cdd:COG0666   269 KLLLLALLLLAAALLD 284
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
75-327 1.43e-35

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 134.70  E-value: 1.43e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043392481  75 LLEAAARNDLEEVRQFLGSGVSPDLANEDGLTALHQCCIDDFREMVQQLLEAGANINACDSECWTPLHAAATCGHLHLVE 154
Cdd:COG0666    58 LLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVK 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043392481 155 LLIASGANLLAVNTDGNMPydlcddeqtldcLETAmadrgITQDSIEAARavpelrMLddirsrLQAGADLHAPLDHGAT 234
Cdd:COG0666   138 LLLEAGADVNAQDNDGNTP------------LHLA-----AANGNLEIVK------LL------LEAGADVNARDNDGET 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043392481 235 LLHVAAANGFSEAAALLLEHRASLSAKDQDGWEPLHAAAYWGQVPLVELLVAHGADLNAKSLMDETPLD---VCGDEEVR 311
Cdd:COG0666   189 PLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLlaaAAGAALIV 268

                         250
                  ....*....|....*.
gi 1043392481 312 AKLLELKHKHDALLRA 327
Cdd:COG0666   269 KLLLLALLLLAAALLD 284
PHA03095 PHA03095
ankyrin-like protein; Provisional
 74-327 5.81e-18

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 86.62  E-value: 5.81e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043392481  74 VLLEAAARNDLEEVRQFLGSGVSPDLANEDGLTALHQC-CIDDFREMVQQLLEAGANINACDSECWTPLHAAAT--CGHL 150
Cdd:PHA03095   53 LYLHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYlYNATTLDVIKLLIKAGADVNAKDKVGRTPLHVYLSgfNINP 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043392481 151 HLVELLIASGANLLAVNTDGNMPYDL------CDDEqTLDCLETAMADRgITQDSI---------EAARAVPELrmlddI 215
Cdd:PHA03095  133 KVIRLLLRKGADVNALDLYGMTPLAVllksrnANVE-LLRLLIDAGADV-YAVDDRfrsllhhhlQSFKPRARI-----V 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043392481 216 RSRLQAGADLHAPLDHGATLLHVAAANGFSEAAAL--LLEHRASLSAKDQDGWEPLHAAAYWGQVPLVELLVAHGADLNA 293
Cdd:PHA03095  206 RELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINA 285

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1043392481 294 KSLMDETPLdvcgdeevrakLLELKHKHDALLRA 327
Cdd:PHA03095  286 VSSDGNTPL-----------SLMVRNNNGRAVRA 308
Ank_2 pfam12796
Ankyrin repeats (3 copies);
75-167 3.66e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 76.69  E-value: 3.66e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043392481  75 LLEAAARNDLEEVRQFLGSGVSPDLANEDGLTALHQCCIDDFREMVQQLLEaGANINACDSEcWTPLHAAATCGHLHLVE 154
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDNG-RTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 1043392481 155 LLIASGANLLAVN 167
Cdd:pfam12796  79 LLLEKGADINVKD 91
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 37-196 8.78e-06

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 48.47  E-value: 8.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043392481  37 WAQAEKEA--QGKKGPGERPRKEAASQ---GLLKQVLFPPSVVL----------LEAAARNDLEEVRQFLGSGVsPDLAN 101
Cdd:cd22192     1 WAQMLDELhlLQQKRISESPLLLAAKEndvQAIKKLLKCPSCDLfqrgalgetaLHVAALYDNLEAAVVLMEAA-PELVN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043392481 102 E-------DGLTALHQCCIDDFREMVQQLLEAGANIN---AC--------DSECW---TPLHAAATCGHLHLVELLIASG 160
Cdd:cd22192    80 EpmtsdlyQGETALHIAVVNQNLNLVRELIARGADVVsprATgtffrpgpKNLIYygeHPLSFAACVGNEEIVRLLIEHG 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1043392481 161 ANLLAVNTDGNMP----------------YDLC---DDEQTLDCLETAMADRGIT 196
Cdd:cd22192   160 ADIRAQDSLGNTVlhilvlqpnktfacqmYDLIlsyDKEDDLQPLDLVPNNQGLT 214
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 264-293 3.74e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.95  E-value: 3.74e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 1043392481  264 DGWEPLHAAAYWGQVPLVELLVAHGADLNA 293
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
75-327 1.43e-35

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 134.70  E-value: 1.43e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043392481  75 LLEAAARNDLEEVRQFLGSGVSPDLANEDGLTALHQCCIDDFREMVQQLLEAGANINACDSECWTPLHAAATCGHLHLVE 154
Cdd:COG0666    58 LLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVK 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043392481 155 LLIASGANLLAVNTDGNMPydlcddeqtldcLETAmadrgITQDSIEAARavpelrMLddirsrLQAGADLHAPLDHGAT 234
Cdd:COG0666   138 LLLEAGADVNAQDNDGNTP------------LHLA-----AANGNLEIVK------LL------LEAGADVNARDNDGET 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043392481 235 LLHVAAANGFSEAAALLLEHRASLSAKDQDGWEPLHAAAYWGQVPLVELLVAHGADLNAKSLMDETPLD---VCGDEEVR 311
Cdd:COG0666   189 PLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLlaaAAGAALIV 268

                         250
                  ....*....|....*.
gi 1043392481 312 AKLLELKHKHDALLRA 327
Cdd:COG0666   269 KLLLLALLLLAAALLD 284
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
75-302 3.82e-32

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 125.07  E-value: 3.82e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043392481  75 LLEAAARNDLEEVRQFLGSGVSPDLANEDGLTALHQCCIDDFREMVQQLLEAGANINACDSECWTPLHAAATCGHLHLVE 154
Cdd:COG0666    91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043392481 155 LLIASGANLLAVNTDGNMPYDLCddeqtldcletamadrgITQDSIEAAravpelRMLddirsrLQAGADLHAPLDHGAT 234
Cdd:COG0666   171 LLLEAGADVNARDNDGETPLHLA-----------------AENGHLEIV------KLL------LEAGADVNAKDNDGKT 221

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1043392481 235 LLHVAAANGFSEAAALLLEHRASLSAKDQDGWEPLHAAAYWGQVPLVELLVAHGADLNAKSLMDETPL 302
Cdd:COG0666   222 ALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
150-316 3.60e-19

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 88.09  E-value: 3.60e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043392481 150 LHLVELLIASGANLLAVNTDGNMPYDLCDDEQTLDCLETAMADRGITQDSIEAARAVPELRMLDDIRSRLQAGADLHAPL 229
Cdd:COG0666     5 LLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKD 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043392481 230 DHGATLLHVAAANGFSEAAALLLEHRASLSAKDQDGWEPLHAAAYWGQVPLVELLVAHGADLNAKSLMDETPLDV---CG 306
Cdd:COG0666    85 DGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLaaaNG 164

                         170
                  ....*....|
gi 1043392481 307 DEEVRAKLLE 316
Cdd:COG0666   165 NLEIVKLLLE 174
PHA03095 PHA03095
ankyrin-like protein; Provisional
 74-327 5.81e-18

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 86.62  E-value: 5.81e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043392481  74 VLLEAAARNDLEEVRQFLGSGVSPDLANEDGLTALHQC-CIDDFREMVQQLLEAGANINACDSECWTPLHAAAT--CGHL 150
Cdd:PHA03095   53 LYLHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYlYNATTLDVIKLLIKAGADVNAKDKVGRTPLHVYLSgfNINP 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043392481 151 HLVELLIASGANLLAVNTDGNMPYDL------CDDEqTLDCLETAMADRgITQDSI---------EAARAVPELrmlddI 215
Cdd:PHA03095  133 KVIRLLLRKGADVNALDLYGMTPLAVllksrnANVE-LLRLLIDAGADV-YAVDDRfrsllhhhlQSFKPRARI-----V 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043392481 216 RSRLQAGADLHAPLDHGATLLHVAAANGFSEAAAL--LLEHRASLSAKDQDGWEPLHAAAYWGQVPLVELLVAHGADLNA 293
Cdd:PHA03095  206 RELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINA 285

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1043392481 294 KSLMDETPLdvcgdeevrakLLELKHKHDALLRA 327
Cdd:PHA03095  286 VSSDGNTPL-----------SLMVRNNNGRAVRA 308
Ank_2 pfam12796
Ankyrin repeats (3 copies);
75-167 3.66e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 76.69  E-value: 3.66e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043392481  75 LLEAAARNDLEEVRQFLGSGVSPDLANEDGLTALHQCCIDDFREMVQQLLEaGANINACDSEcWTPLHAAATCGHLHLVE 154
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDNG-RTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 1043392481 155 LLIASGANLLAVN 167
Cdd:pfam12796  79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
219-294 2.52e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 65.52  E-value: 2.52e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1043392481 219 LQAGADLHAPLDHGATLLHVAAANGFSEAAALLLEHrASLSAKDqDGWEPLHAAAYWGQVPLVELLVAHGADLNAK 294
Cdd:pfam12796  17 LENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVKLLLEKGADINVK 90
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 114-302 5.14e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 71.63  E-value: 5.14e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043392481 114 DDFReMVQQLLEAGANINACDSECWTPLHAAATCGHLHLVELLIASGANLLAVNTDGNMPYDLCDDEQTLDCLETAMADR 193
Cdd:PHA02876  156 DELL-IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNR 234

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043392481 194 G-ITQDSIEAARAVPElrmlDDIRSRL---QAGADLHAPLDHGATLLHVAA-ANGFSEAAALLLEHRASLSAKDQDGWEP 268
Cdd:PHA02876  235 SnINKNDLSLLKAIRN----EDLETSLllyDAGFSVNSIDDCKNTPLHHASqAPSLSRLVPKLLERGADVNAKNIKGETP 310

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1043392481 269 LHAAAYWG-QVPLVELLVAHGADLNAKSLMDETPL 302
Cdd:PHA02876  311 LYLMAKNGyDTENIRTLIMLGADVNAADRLYITPL 345
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 118-302 9.06e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 70.38  E-value: 9.06e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043392481 118 EMVQQLLEAGAN-INACDSECWTPLHAAATCGHLHLVELLIASGANLLAVNTdgNMPYDLCDDEQT-LDCLETAMADRGI 195
Cdd:PHA02874   15 EAIEKIIKNKGNcINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINT--KIPHPLLTAIKIgAHDIIKLLIDNGV 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043392481 196 TQDSIeaarAVPELRMlDDIRSRLQAGADLHAPLDHGATLLHVAAANGFSEAAALLLEHRASLSAKDQDGWEPLHAAAYW 275
Cdd:PHA02874   93 DTSIL----PIPCIEK-DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKH 167

                         170       180
                  ....*....|....*....|....*..
gi 1043392481 276 GQVPLVELLVAHGADLNAKSLMDETPL 302
Cdd:PHA02874  168 NFFDIIKLLLEKGAYANVKDNNGESPL 194
Ank_2 pfam12796
Ankyrin repeats (3 copies);
236-322 3.18e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 59.74  E-value: 3.18e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043392481 236 LHVAAANGFSEAAALLLEHRASLSAKDQDGWEPLHAAAYWGQVPLVELLVAHgADLNAKSlMDETPLDVC---GDEEVrA 312
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAarsGHLEI-V 77

                          90
                  ....*....|
gi 1043392481 313 KLLeLKHKHD 322
Cdd:pfam12796  78 KLL-LEKGAD 86
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 113-302 3.91e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 65.07  E-value: 3.91e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043392481 113 IDDFREMVQQLLEAGANINACDSECWTPLHAAATC--GHLHLVELLIASGANLLAVNTDGNMPYdlcddeqtldcletAM 190
Cdd:PHA03100   82 LTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLL--------------HL 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043392481 191 ADRGITQDSieaaravpelrmldDIRSRLqagadlhapLDHGAtllHVAAANGFSeaaaLLLEHRASLSAKDQDGWEPLH 270
Cdd:PHA03100  148 YLESNKIDL--------------KILKLL---------IDKGV---DINAKNRVN----YLLSYGVPINIKDVYGFTPLH 197

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1043392481 271 AAAYWGQVPLVELLVAHGADLNAKSLMDETPL 302
Cdd:PHA03100  198 YAVYNNNPEFVKYLLDLGANPNLVNKYGDTPL 229
Ank_2 pfam12796
Ankyrin repeats (3 copies);
108-262 3.97e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 59.36  E-value: 3.97e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043392481 108 LHQCCIDDFREMVQQLLEAGANINACDSECWTPLHAAATCGHLHLVELLIAsganllavNTDGNMPydlcddeqtldcle 187
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE--------HADVNLK-------------- 58

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1043392481 188 tamadrgitqdsieaaravpelrmlddirsrlqagadlhaplDHGATLLHVAAANGFSEAAALLLEHRASLSAKD 262
Cdd:pfam12796  59 ------------------------------------------DNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 73-292 4.12e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 61.93  E-value: 4.12e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043392481  73 VVLLEAAARNDLEEVRQFLGSGVSPDLANEDGLTALHQCCIDDFREMVQQLLEAGA--NINACDSEcwTPLHAAATCGHL 150
Cdd:PHA02875    4 VALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAipDVKYPDIE--SELHDAVEEGDV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043392481 151 HLVELLIASGANLLAV-NTDGNMPYDLCDDEQTLDCLETAMAdrgitqdsieaaravpelrmlddirsrlqAGADLHAPL 229
Cdd:PHA02875   82 KAVEELLDLGKFADDVfYKDGMTPLHLATILKKLDIMKLLIA-----------------------------RGADPDIPN 132

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1043392481 230 DHGATLLHVAAANGFSEAAALLLEHRASLSAKDQDGWEPLHAAAYWGQVPLVELLVAHGADLN 292
Cdd:PHA02875  133 TDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANID 195
Ank_4 pfam13637
Ankyrin repeats (many copies);
104-157 5.42e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.97  E-value: 5.42e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1043392481 104 GLTALHQCCIDDFREMVQQLLEAGANINACDSECWTPLHAAATCGHLHLVELLI 157
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 108-316 2.27e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 59.51  E-value: 2.27e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043392481 108 LHQCCIDDFREMVQQLLEAGANINACDSECWTPLHAAATCGHLHLVELLIAS------GANLLAVNTDGN---------M 172
Cdd:PHA02878   41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSinkcsvFYTLVAIKDAFNnrnveifkiI 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043392481 173 PYDLCDDEQTLDCLETAMADRgitQDSIEAaravpelrmlDDIRSRLQAGADLHAPLDH-GATLLHVAAANGFSEAAALL 251
Cdd:PHA02878  121 LTNRYKNIQTIDLVYIDKKSK---DDIIEA----------EITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELL 187

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1043392481 252 LEHRASLSAKDQDGWEPLHAAAYWGQVPLVELLVAHGADLNAKSLMDETPLDV----CGDEEVRAKLLE 316
Cdd:PHA02878  188 LSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHIsvgyCKDYDILKLLLE 256
PHA03095 PHA03095
ankyrin-like protein; Provisional
 212-317 4.41e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 58.88  E-value: 4.41e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043392481 212 LDDIRSRLQAGADLHAPLDHGATLLHVAAANGFS---EAAALLLEHRASLSAKDQDGWEPLHAAAYWGQV-PLVELLVAH 287
Cdd:PHA03095   27 VEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEkvkDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIKA 106

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1043392481 288 GADLNAKSLMDETPLDVC-GDEEVRAKLLEL 317
Cdd:PHA03095  107 GADVNAKDKVGRTPLHVYlSGFNINPKVIRL 137
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 85-304 1.23e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 57.28  E-value: 1.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043392481  85 EEVRQFLGSGVSPDLANEDGLTALHQCCIDDFREMVQQLLEAGANINACDSECWTPLHAAATCGHLHLVELLIASGANLL 164
Cdd:PHA02874  105 DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYAN 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043392481 165 AVNTDGNMPYDLCDDEQTLDCletamadrgitqdsieaaravpelrmlddIRSRLQAGADLHAPLDHGATLLHVAAAngF 244
Cdd:PHA02874  185 VKDNNGESPLHNAAEYGDYAC-----------------------------IKLLIDHGNHIMNKCKNGFTPLHNAII--H 233

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1043392481 245 SEAAALLLEHRASLSAKDQDGWEPLH-AAAYWGQVPLVELLVAHGADLNAKSLMDETPLDV 304
Cdd:PHA02874  234 NRSAIELLINNASINDQDIDGSTPLHhAINPPCDIDIIDILLYHKADISIKDNKGENPIDT 294
Ank_4 pfam13637
Ankyrin repeats (many copies);
234-285 4.66e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.58  E-value: 4.66e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1043392481 234 TLLHVAAANGFSEAAALLLEHRASLSAKDQDGWEPLHAAAYWGQVPLVELLV 285
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 78-303 6.96e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 54.97  E-value: 6.96e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043392481  78 AAARNDLEEVRQFLGSGVSPDLANEDGLTALHQCCIDDFREMVQQLLEAGANINACDSECWTPLHAAATCGHLHLVELLI 157
Cdd:PHA02874  131 AIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLI 210

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043392481 158 ASGANLLAVNTDGNMPydlcddeqtldcLETAMadrgitqdsIEAARAVPELrmlddIRSRLQAGADLhapldHGATLLH 237
Cdd:PHA02874  211 DHGNHIMNKCKNGFTP------------LHNAI---------IHNRSAIELL-----INNASINDQDI-----DGSTPLH 259

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1043392481 238 VAAANGFS-EAAALLLEHRASLSAKDQDGWEPLHAA-AYWGQVPLVELLVAHGADLN-AKSLMDETPLD 303
Cdd:PHA02874  260 HAINPPCDiDIIDILLYHKADISIKDNKGENPIDTAfKYINKDPVIKDIIANAVLIKeADKLKDSDFLE 328
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 118-304 7.18e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 54.89  E-value: 7.18e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043392481 118 EMVQQLLEAGANINACDSECW-TPLHAAATCGHLHLVELLIASGANLLAVNTDGNMPydlcddeqtldcLETAMADRgiT 196
Cdd:PHA02878  148 EITKLLLSYGADINMKDRHKGnTALHYATENKDQRLTELLLSYGANVNIPDKTNNSP------------LHHAVKHY--N 213

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043392481 197 QDSIEAAravpelrmlddirsrLQAGADLHAPLDHGATLLHVAAANGFS-EAAALLLEHRASLSAKDQ-DGWEPLHAAAY 274
Cdd:PHA02878  214 KPIVHIL---------------LENGASTDARDKCGNTPLHISVGYCKDyDILKLLLEHGVDVNAKSYiLGLTALHSSIK 278

                         170       180       190
                  ....*....|....*....|....*....|
gi 1043392481 275 WGQVplVELLVAHGADLNAKSLMDETPLDV 304
Cdd:PHA02878  279 SERK--LKLLLEYGADINSLNSYKLTPLSS 306
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 75-302 1.71e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 53.91  E-value: 1.71e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043392481  75 LLEAAARNDLEEVRQFLGSGVSPDLANEDGLTALHQCC-IDDFREMVQQLLEAGANINACDSECWTPLHAAATCGH-LHL 152
Cdd:PHA02876  244 LLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASqAPSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTEN 323

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043392481 153 VELLIASGANLLAVNTDGNMPYDLC-------DDEQTLDCLETAMADRGITQDSIEAARAVPELRMLddIRSRLQAGADL 225
Cdd:PHA02876  324 IRTLIMLGADVNAADRLYITPLHQAstldrnkDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVI--INTLLDYGADI 401

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043392481 226 HAPLDHGATLLHVA--AANGFSeAAALLLEHRASLSAKDQDGWEPLHAAAYWGQVP-LVELLVAHGADLNAKSLMDETPL 302
Cdd:PHA02876  402 EALSQKIGTALHFAlcGTNPYM-SVKTLIDRGANVNSKNKDLSTPLHYACKKNCKLdVIEMLLDNGADVNAINIQNQYPL 480
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 117-302 2.61e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 53.04  E-value: 2.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043392481 117 REMVQQLLEAGANINACDSECWTPLHAAATCGHLHLVELLIASGANLLAVNTDGNMPYDLCDDEQTLDCletamadrgit 196
Cdd:PHA02874  104 KDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDI----------- 172

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043392481 197 qdsieaaravpelrmlddIRSRLQAGADLHAPLDHGATLLHVAAANGFSEAAALLLEHRASLSAKDQDGWEPLHAAAYWG 276
Cdd:PHA02874  173 ------------------IKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHN 234

                         170       180
                  ....*....|....*....|....*.
gi 1043392481 277 QvPLVELLVaHGADLNAKSLMDETPL 302
Cdd:PHA02874  235 R-SAIELLI-NNASINDQDIDGSTPL 258
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 120-208 2.76e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 53.36  E-value: 2.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043392481 120 VQQLLEAGANINACDSECWTPLHAAATCGHLHLVELLIASGANLLAVNTDGNMPYDLCDDEQTLDCLETAMadRGITQDS 199
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS--RHSQCHF 175


                  ....*....
gi 1043392481 200 IEAARAVPE 208
Cdd:PTZ00322  176 ELGANAKPD 184
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 82-162 7.53e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 51.59  E-value: 7.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043392481  82 NDLEEVRQFLGSGVSPDLANEDGLTALHQCCIDDFREMVQQLLEAGANINACDSECWTPLHAAATCGHLHLVELLIASGA 161
Cdd:PHA03100  170 NAKNRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGP 249


                  .
gi 1043392481 162 N 162
Cdd:PHA03100  250 S 250
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 119-364 1.16e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 51.41  E-value: 1.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043392481 119 MVQQLLEAGANINACDSECWTPLHAAATCGHLHLVELLIASGANLLAVNTDGNmpydlcddeqtldcleTAMadrgitQD 198
Cdd:PLN03192  540 LLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGN----------------TAL------WN 597

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043392481 199 SIEAARavpelRMLDDIRSRLQAGADLHApldhGATLLHVAAANGFSEAAALLLEHRASLSAKDQDGWEPLHAAAYWGQV 278
Cdd:PLN03192  598 AISAKH-----HKIFRILYHFASISDPHA----AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHV 668

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043392481 279 PLVELLVAHGADLNAKSLMDE-TPLDVcgdEEVRAKlLELKHK------HDALLRAQSRQRSLLRRRTSSAGSRGKVVRR 351
Cdd:PLN03192  669 DMVRLLIMNGADVDKANTDDDfSPTEL---RELLQK-RELGHSitivdsVPADEPDLGRDGGSRPGRLQGTSSDNQCRPR 744

                         250
                  ....*....|...
gi 1043392481 352 VSLTQRTDLYRKQ 364
Cdd:PLN03192  745 VSIYKGHPLLRNE 757
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 54-156 1.39e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.05  E-value: 1.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043392481  54 PRKEAASQGLLKQ-VLFPPSVVLLEAAARNDLEEVRQFLGSGVSPDLANEDGLTALHQCCIDDFREMVQQLLEAGANINA 132
Cdd:PTZ00322   64 PDHNLTTEEVIDPvVAHMLTVELCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTL 143

                          90       100
                  ....*....|....*....|....
gi 1043392481 133 CDSECWTPLHAAATCGHLHLVELL 156
Cdd:PTZ00322  144 LDKDGKTPLELAEENGFREVVQLL 167
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 215-299 1.98e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 50.67  E-value: 1.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043392481 215 IRSRLQAGADLHAPLDHGATLLHVAAANGFSEAAALLLEHRASLSAKDQDGWEPLHAAAYWGQVPLVELLVAHGA---DL 291
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQchfEL 177


                  ....*...
gi 1043392481 292 NAKSLMDE 299
Cdd:PTZ00322  178 GANAKPDS 185
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 81-173 6.89e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 48.51  E-value: 6.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043392481  81 RNDLEEVRQFLGSGVSPDLANEDGLTALHQ---CCIDDFrEMVQQLLEAGANINACDS---------------EC-WTPL 141
Cdd:PHA03100  118 SNSYSIVEYLLDNGANVNIKNSDGENLLHLyleSNKIDL-KILKLLIDKGVDINAKNRvnyllsygvpinikdVYgFTPL 196

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1043392481 142 HAAATCGHLHLVELLIASGANLLAVNTDGNMP 173
Cdd:PHA03100  197 HYAVYNNNPEFVKYLLDLGANPNLVNKYGDTP 228
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 37-196 8.78e-06

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 48.47  E-value: 8.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043392481  37 WAQAEKEA--QGKKGPGERPRKEAASQ---GLLKQVLFPPSVVL----------LEAAARNDLEEVRQFLGSGVsPDLAN 101
Cdd:cd22192     1 WAQMLDELhlLQQKRISESPLLLAAKEndvQAIKKLLKCPSCDLfqrgalgetaLHVAALYDNLEAAVVLMEAA-PELVN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043392481 102 E-------DGLTALHQCCIDDFREMVQQLLEAGANIN---AC--------DSECW---TPLHAAATCGHLHLVELLIASG 160
Cdd:cd22192    80 EpmtsdlyQGETALHIAVVNQNLNLVRELIARGADVVsprATgtffrpgpKNLIYygeHPLSFAACVGNEEIVRLLIEHG 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1043392481 161 ANLLAVNTDGNMP----------------YDLC---DDEQTLDCLETAMADRGIT 196
Cdd:cd22192   160 ADIRAQDSLGNTVlhilvlqpnktfacqmYDLIlsyDKEDDLQPLDLVPNNQGLT 214
Ank_5 pfam13857
Ankyrin repeats (many copies);
123-177 1.68e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.33  E-value: 1.68e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1043392481 123 LLEAG-ANINACDSECWTPLHAAATCGHLHLVELLIASGANLLAVNTDGNMPYDLC 177
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 77-302 2.37e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 46.98  E-value: 2.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043392481  77 EAAARNDLEEVRQFLGSGVSPDLANEDGLTALHQCCIDDFREMVQQLLEAGANINACDSECWTPLHAAATCGHLHLVELL 156
Cdd:PHA02876  151 ERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAI 230

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043392481 157 IASGANllaVNTDGNMPYDLCDDEQtldcLETAMA--DRGITQDSIEA--------ARAVPELRMLddIRSRLQAGADLH 226
Cdd:PHA02876  231 IDNRSN---INKNDLSLLKAIRNED----LETSLLlyDAGFSVNSIDDckntplhhASQAPSLSRL--VPKLLERGADVN 301

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043392481 227 APLDHGATLLHVAAANGF-SEAAALLLEHRASLSAKDQDGWEPLHAAAYWGQ-----VPLVELlvahGADLNAKSLMDET 300
Cdd:PHA02876  302 AKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTLDRnkdivITLLEL----GANVNARDYCDKT 377


                  ..
gi 1043392481 301 PL 302
Cdd:PHA02876  378 PI 379
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 240-311 2.54e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.82  E-value: 2.54e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1043392481 240 AANGFSEAAALLLEHRASLSAKDQDGWEPLHAAAYWGQVPLVELLVAHGADLNAKSLMDETPLDVCGDEEVR 311
Cdd:PTZ00322   90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFR 161
Ank_5 pfam13857
Ankyrin repeats (many copies);
251-305 3.65e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.56  E-value: 3.65e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1043392481 251 LLEHR-ASLSAKDQDGWEPLHAAAYWGQVPLVELLVAHGADLNAKSLMDETPLDVC 305
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
265-315 5.40e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 40.72  E-value: 5.40e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1043392481 265 GWEPLHAAAYWGQVPLVELLVAHGADLNAKSLMDETPLDVC---GDEEVrAKLL 315
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAasnGNVEV-LKLL 53
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 138-167 1.12e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 39.58  E-value: 1.12e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1043392481 138 WTPLHAAAT-CGHLHLVELLIASGANLLAVN 167
Cdd:pfam00023   3 NTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
Ank_4 pfam13637
Ankyrin repeats (many copies);
74-124 2.63e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.79  E-value: 2.63e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1043392481  74 VLLEAAARNDLEEVRQFLGSGVSPDLANEDGLTALHQCCIDDFREMVQQLL 124
Cdd:pfam13637   4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 264-294 3.21e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 38.04  E-value: 3.21e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1043392481 264 DGWEPLHAAAY-WGQVPLVELLVAHGADLNAK 294
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNAR 32
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 264-293 3.74e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.95  E-value: 3.74e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 1043392481  264 DGWEPLHAAAYWGQVPLVELLVAHGADLNA 293
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 219-290 3.93e-04

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 43.08  E-value: 3.93e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1043392481 219 LQAGADLHAPLDHGATLLHVAAANGFSEAAALLLEHRASL------SAKDQdGWEPLHAAAYWGQVPLVELLVAHGAD 290
Cdd:cd22192    38 KCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELvnepmtSDLYQ-GETALHIAVVNQNLNLVRELIARGAD 114
PHA02946 PHA02946
ankyin-like protein; Provisional
 87-302 4.33e-04

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 42.73  E-value: 4.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043392481  87 VRQFLGSGVSPDLANEDGLTALHQCCIDDFREMVQQLLEAGANINACDSECWTPLHAAATCGH--LHLVELLIASGANL- 163
Cdd:PHA02946   55 VEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDevIERINLLVQYGAKIn 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043392481 164 LAVNTDGNMPYDLCDDeqtldcletamadrgitqdsieaaravPELRMLDDIRSrLQAGADLHAPLDHGATLLHVAAANG 243
Cdd:PHA02946  135 NSVDEEGCGPLLACTD---------------------------PSERVFKKIMS-IGFEARIVDKFGKNHIHRHLMSDNP 186

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1043392481 244 FSEAAALLLEHRASLSAKDQDGWEPLH--AAAYWGQVPLVELLVAhGADLNAKSLMDETPL 302
Cdd:PHA02946  187 KASTISWMMKLGISPSKPDHDGNTPLHivCSKTVKNVDIINLLLP-STDVNKQNKFGDSPL 246
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 74-132 4.46e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 42.93  E-value: 4.46e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1043392481  74 VLLEAAARNDLEEVRQFLGSGVSPDLANEDGLTALHQCCIDDFREMVQQLLEAGANINA 132
Cdd:PLN03192  625 LLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDK 683
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 264-293 4.48e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 37.62  E-value: 4.48e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 1043392481 264 DGWEPLHAAAYWGQVPLVELLVAHGADLNA 293
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 138-163 5.39e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.57  E-value: 5.39e-04
                           10        20
                   ....*....|....*....|....*.
gi 1043392481  138 WTPLHAAATCGHLHLVELLIASGANL 163
Cdd:smart00248   3 RTPLHLAAENGNLEVVKLLLDKGADI 28
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 248-303 6.54e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 42.36  E-value: 6.54e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1043392481 248 AALLLEHRASLSAKDQDGWEPLHAAAYWGQVPLVELLVAHGADLNAKSLMDETPLD 303
Cdd:PHA02876  161 AEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLE 216
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 103-132 6.96e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 37.24  E-value: 6.96e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 1043392481 103 DGLTALHQCCIDDFREMVQQLLEAGANINA 132
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_4 pfam13637
Ankyrin repeats (many copies);
137-173 8.49e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 37.64  E-value: 8.49e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1043392481 137 CWTPLHAAATCGHLHLVELLIASGANLLAVNTDGNMP 173
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETA 37
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 103-134 9.74e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 36.88  E-value: 9.74e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1043392481 103 DGLTALHQCCID-DFREMVQQLLEAGANINACD 134
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 103-132 1.56e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.03  E-value: 1.56e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1043392481  103 DGLTALHQCCIDDFREMVQQLLEAGANINA 132
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
95-144 2.21e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.56  E-value: 2.21e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1043392481  95 VSPDLANEDGLTALHQCCIDDFREMVQQLLEAGANINACDSECWTPLHAA 144
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 138-165 4.42e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 34.93  E-value: 4.42e-03
                          10        20
                  ....*....|....*....|....*...
gi 1043392481 138 WTPLHAAATCGHLHLVELLIASGANLLA 165
Cdd:pfam13606   3 NTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
223-272 5.15e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.40  E-value: 5.15e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1043392481 223 ADLHAPLDHGATLLHVAAANGFSEAAALLLEHRASLSAKDQDGWEPLHAA 272
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 75-132 7.35e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 38.88  E-value: 7.35e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1043392481  75 LLEAAARNDLEEVRQFLGSGVSPDLANEDGLTALHQCCIDDFREMVQQLLEAGANINA 132
Cdd:PHA03100  196 LHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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