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Conserved domains on  [gi|1236650|gb|AAA92961|]
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PP-1M, partial [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
34-288 1.80e-41

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 152.42  E-value: 1.80e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236650   34 FLAACSSGDTDEVLKLLHRGADINYANVDGLTALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASCGYLDIAE 113
Cdd:COG0666  91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236650  114 FLIGQGAHVGAVNsegdtpldiaeeeameellqnevnrqgvdieaarkeeerimlrdarqwlnsghisdvrhaKSGGTAL 193
Cdd:COG0666 171 LLLEAGADVNARD------------------------------------------------------------NDGETPL 190

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236650  194 HVAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKEEACRILVDNLCDMETVNKVGQTAFDVADEDILGYLEEL 273
Cdd:COG0666 191 HLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKL 270

                       250
                ....*....|....*
gi 1236650  274 QKKQNLLHSEKRDKK 288
Cdd:COG0666 271 LLLALLLLAAALLDL 285
IPD_PPP1R12 super family cl40436
inhibitory phosphorylation domain of protein phosphatase 1 regulatory subunit 12 (PPP1R12) ...
 598-644 3.16e-14

inhibitory phosphorylation domain of protein phosphatase 1 regulatory subunit 12 (PPP1R12) family; The PPP1R12 family includes PPP1R12A/MYPT1, PPP1R12B/MYPT2, and PPP1R12C. PPP1R12A/MYPT1, also called myosin phosphatase target subunit 1, or protein phosphatase myosin-binding subunit, is a substrate for the asparaginyl hydroxylase factor inhibiting hypoxia-inducible factor (FIH). It acts as a key regulator of protein phosphatase 1C (PPP1C). It mediates binding to myosin. As part of the PPP1C complex, PPP1R12A/MYPT1 is involved in dephosphorylation of PLK1. It is capable of inhibiting HIF1A inhibitor (HIF1AN)-dependent suppression of HIF1A activity. PPP1R12B/MYPT2, also called myosin phosphatase target subunit 2, is the targeting subunit of smooth-muscle myosin phosphatase that regulates myosin phosphatase activity and augments Ca(2+) sensitivity of the contractile apparatus. PPP1R12C, also called protein phosphatase 1 myosin-binding subunit of 85 kDa (MBS85), protein phosphatase 1 myosin-binding subunit p85, or LENG3, regulates myosin phosphatase activity. All family members contain an inhibitory phosphorylation domain.


The actual alignment was detected with superfamily member cd21945:

Pssm-ID: 424067  Cd Length: 54  Bit Score: 67.42  E-value: 3.16e-14
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 1236650  598 RSYLTPVRDEESESHRKARSRQARQSRRSTQGVTLTDLQEAEKTIGR 644
Cdd:cd21945   8 RSYQTPVRDEESESQRKARSRLMRQSRRSTQGVTLTDLKEAEKSIGK 54
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
34-288 1.80e-41

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 152.42  E-value: 1.80e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236650   34 FLAACSSGDTDEVLKLLHRGADINYANVDGLTALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASCGYLDIAE 113
Cdd:COG0666  91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236650  114 FLIGQGAHVGAVNsegdtpldiaeeeameellqnevnrqgvdieaarkeeerimlrdarqwlnsghisdvrhaKSGGTAL 193
Cdd:COG0666 171 LLLEAGADVNARD------------------------------------------------------------NDGETPL 190

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236650  194 HVAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKEEACRILVDNLCDMETVNKVGQTAFDVADEDILGYLEEL 273
Cdd:COG0666 191 HLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKL 270

                       250
                ....*....|....*
gi 1236650  274 QKKQNLLHSEKRDKK 288
Cdd:COG0666 271 LLLALLLLAAALLDL 285
PHA03095 PHA03095
ankyrin-like protein; Provisional
 33-262 8.67e-22

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 98.94  E-value: 8.67e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236650    33 VFLAACSSGDTDEVLKLLHRGADINYANVDGLTALH-QACIDDNVDMVKFLVENGANINQPDNEGWIPLHAaascgYL-- 109
Cdd:PHA03095  53 LYLHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHlYLYNATTLDVIKLLIKAGADVNAKDKVGRTPLHV-----YLsg 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236650   110 -----DIAEFLIGQGAHVGAVNSEGDTPLDIAeeeameellqneVNRQGVDIEAARkeeeriMLRDArqwlnsghISDVR 184
Cdd:PHA03095 128 fninpKVIRLLLRKGADVNALDLYGMTPLAVL------------LKSRNANVELLR------LLIDA--------GADVY 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236650   185 HAKS-GGTALHVAA--AKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGkeeACR-ILVDNL----CDMETVNKVGQ 256
Cdd:PHA03095 182 AVDDrFRSLLHHHLqsFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGS---SCKrSLVLPLliagISINARNRYGQ 258


                 ....*.
gi 1236650   257 TAFDVA 262
Cdd:PHA03095 259 TPLHYA 264
Ank_2 pfam12796
Ankyrin repeats (3 copies);
37-126 2.63e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 88.63  E-value: 2.63e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236650     37 ACSSGDTDEVLKLLHRGADINYANVDGLTALHQACIDDNVDMVKFLVENgANINQPDNeGWIPLHAAASCGYLDIAEFLI 116
Cdd:pfam12796   4 AAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVKLLL 81

                          90
                  ....*....|
gi 1236650    117 GQGAHVGAVN 126
Cdd:pfam12796  82 EKGADINVKD 91
IPD_PPP1R12C cd21945
inhibitory phosphorylation domain of protein phosphatase 1 regulatory subunit 12C (PPP1R12C); ...
 598-644 3.16e-14

inhibitory phosphorylation domain of protein phosphatase 1 regulatory subunit 12C (PPP1R12C); PPP1R12C, also called protein phosphatase 1 myosin-binding subunit of 85 kDa (MBS85), protein phosphatase 1 myosin-binding subunit p85, or LENG3, regulates myosin phosphatase activity. This model corresponds to a conserved region of PPP1R12C, which shows high sequence similarity to the inhibitory phosphorylation domain of MYPT1.


Pssm-ID: 412020  Cd Length: 54  Bit Score: 67.42  E-value: 3.16e-14
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 1236650  598 RSYLTPVRDEESESHRKARSRQARQSRRSTQGVTLTDLQEAEKTIGR 644
Cdd:cd21945   8 RSYQTPVRDEESESQRKARSRLMRQSRRSTQGVTLTDLKEAEKSIGK 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 63-210 3.16e-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: 50.40  E-value: 3.16e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236650   63 GLTALHQACIDDNVDMVKFLVENGANINQPDNEGWI--------------PLHAAASCGYLDIAEFLIGQGAHVGAVNSE 128
Cdd:cd22192  89 GETALHIAVVNQNLNLVRELIARGADVVSPRATGTFfrpgpknliyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSL 168

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236650  129 GDTPLDIaeeeaMEELLQNEVNRQGVDIeaarkeeerIMLRDARQwlNSGHISDVRHaKSGGTALHVAAAKGYTEVLKLL 208
Cdd:cd22192 169 GNTVLHI-----LVLQPNKTFACQMYDL---------ILSYDKED--DLQPLDLVPN-NQGLTPFKLAAKEGNIVMFQHL 231


                ..
gi 1236650  209 IQ 210
Cdd:cd22192 232 VQ 233
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 62-90 3.84e-06

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: 43.73  E-value: 3.84e-06
                           10        20
                   ....*....|....*....|....*....
gi 1236650      62 DGLTALHQACIDDNVDMVKFLVENGANIN 90
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
34-288 1.80e-41

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 152.42  E-value: 1.80e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236650   34 FLAACSSGDTDEVLKLLHRGADINYANVDGLTALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASCGYLDIAE 113
Cdd:COG0666  91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236650  114 FLIGQGAHVGAVNsegdtpldiaeeeameellqnevnrqgvdieaarkeeerimlrdarqwlnsghisdvrhaKSGGTAL 193
Cdd:COG0666 171 LLLEAGADVNARD------------------------------------------------------------NDGETPL 190

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236650  194 HVAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKEEACRILVDNLCDMETVNKVGQTAFDVADEDILGYLEEL 273
Cdd:COG0666 191 HLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKL 270

                       250
                ....*....|....*
gi 1236650  274 QKKQNLLHSEKRDKK 288
Cdd:COG0666 271 LLLALLLLAAALLDL 285
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
29-321 2.96e-41

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 152.03  E-value: 2.96e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236650   29 DDGAVFLAACSSGDTDEVLKLLHRGADINYANVDGLTALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASCGY 108
Cdd:COG0666  53 LGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGN 132

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236650  109 LDIAEFLIGQGAHVGAVNSEGDTPldiaeeeameellqnevnrqgvdieaarkeeerimlrdarqwlnsghisdvrhaks 188
Cdd:COG0666 133 LEIVKLLLEAGADVNAQDNDGNTP-------------------------------------------------------- 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236650  189 ggtaLHVAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKEEACRILVDNLCDMETVNKVGQTAFDVADEDILG 268
Cdd:COG0666 157 ----LHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNL 232

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 1236650  269 YLEELQKKQNLLHSEKRDKKSPLIESTANMENNQPQKNFKNKETLIIEPEKNA 321
Cdd:COG0666 233 EIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDL 285
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
29-259 1.48e-31

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 124.68  E-value: 1.48e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236650   29 DDGAVFLAACSSGDTDEVLKLLHRGADINYANVDGLTALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASCGY 108
Cdd:COG0666 119 DGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGH 198

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236650  109 LDIAEFLIGQGAHVGAVNSEGDTPLDIaeeeameellqnevnrqgvdieaarkeeerimlrdarqwlnsghisdvrhaks 188
Cdd:COG0666 199 LEIVKLLLEAGADVNAKDNDGKTALDL----------------------------------------------------- 225

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1236650  189 ggtalhvAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKEEACRILVDNLCDMETVNKVGQTAF 259
Cdd:COG0666 226 -------AAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
PHA03095 PHA03095
ankyrin-like protein; Provisional
 33-262 8.67e-22

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 98.94  E-value: 8.67e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236650    33 VFLAACSSGDTDEVLKLLHRGADINYANVDGLTALH-QACIDDNVDMVKFLVENGANINQPDNEGWIPLHAaascgYL-- 109
Cdd:PHA03095  53 LYLHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHlYLYNATTLDVIKLLIKAGADVNAKDKVGRTPLHV-----YLsg 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236650   110 -----DIAEFLIGQGAHVGAVNSEGDTPLDIAeeeameellqneVNRQGVDIEAARkeeeriMLRDArqwlnsghISDVR 184
Cdd:PHA03095 128 fninpKVIRLLLRKGADVNALDLYGMTPLAVL------------LKSRNANVELLR------LLIDA--------GADVY 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236650   185 HAKS-GGTALHVAA--AKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGkeeACR-ILVDNL----CDMETVNKVGQ 256
Cdd:PHA03095 182 AVDDrFRSLLHHHLqsFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGS---SCKrSLVLPLliagISINARNRYGQ 258


                 ....*.
gi 1236650   257 TAFDVA 262
Cdd:PHA03095 259 TPLHYA 264
Ank_2 pfam12796
Ankyrin repeats (3 copies);
37-126 2.63e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 88.63  E-value: 2.63e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236650     37 ACSSGDTDEVLKLLHRGADINYANVDGLTALHQACIDDNVDMVKFLVENgANINQPDNeGWIPLHAAASCGYLDIAEFLI 116
Cdd:pfam12796   4 AAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVKLLL 81

                          90
                  ....*....|
gi 1236650    117 GQGAHVGAVN 126
Cdd:pfam12796  82 EKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
67-219 3.33e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.77  E-value: 3.33e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236650     67 LHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASCGYLDIAEFLIGQGahvgavnsegdtpldiaeeeameellq 146
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA--------------------------- 53

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1236650    147 nevnrqgvdieaarkeeerimlrdarqwlnsghisDVRHAKSGGTALHVAAAKGYTEVLKLLIQAGYDVNIKD 219
Cdd:pfam12796  54 -----------------------------------DVNLKDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 40-226 3.02e-17

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 85.08  E-value: 3.02e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236650    40 SGDTDEVLKLLHR-GADINYANVDGLTALHQACIDDNVD--MVKFLVENGANINQPDNEGWIPLHA-----AAScgyLDI 111
Cdd:PHA03095  93 NATTLDVIKLLIKaGADVNAKDKVGRTPLHVYLSGFNINpkVIRLLLRKGADVNALDLYGMTPLAVllksrNAN---VEL 169

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236650   112 AEFLIGQGAHVGAVNSEGDTPLDIAEEEAMEELLQN-EVNRQGVDiEAARKEEERIMLRDA-----------RQWLNSGH 179
Cdd:PHA03095 170 LRLLIDAGADVYAVDDRFRSLLHHHLQSFKPRARIVrELIRAGCD-PAATDMLGNTPLHSMatgssckrslvLPLLIAGI 248

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 1236650   180 ISDVRHaKSGGTALHVAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPL 226
Cdd:PHA03095 249 SINARN-RYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPL 294
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 45-230 5.57e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 83.56  E-value: 5.57e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236650    45 EVLK-LLHRGADINYANVDGLTALH-----QACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASC--GYLDIAEFLI 116
Cdd:PHA03100  49 DVVKiLLDNGADINSSTKNNSTPLHylsniKYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLL 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236650   117 GQGAHVGAVNSEGDTPLDIAEEEAMEELL--QNEVNRqGVDIEAARKEEeriMLrdarqwLNSGHISDVRHAKsGGTALH 194
Cdd:PHA03100 129 DNGANVNIKNSDGENLLHLYLESNKIDLKilKLLIDK-GVDINAKNRVN---YL------LSYGVPINIKDVY-GFTPLH 197

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 1236650   195 VAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAA 230
Cdd:PHA03100 198 YAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAI 233
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 42-253 4.24e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 81.46  E-value: 4.24e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236650    42 DTDEVLKLLHRGADINYANVDGL-TALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASCGYLDIAEFLIGQGA 120
Cdd:PHA02878 146 EAEITKLLLSYGADINMKDRHKGnTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGA 225

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236650   121 HVGAVNSEGDTPLDIAEEEAMEELLQNEVNRQGVDIEAArkeeerimlrdarqwlnsghiSDVRhaksGGTALHVAAAKg 200
Cdd:PHA02878 226 STDARDKCGNTPLHISVGYCKDYDILKLLLEHGVDVNAK---------------------SYIL----GLTALHSSIKS- 279

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 1236650   201 yTEVLKLLIQAGYDVNIKDYDGWTPLHAAA-HWGKEEACRILVDNLCDMETVNK 253
Cdd:PHA02878 280 -ERKLKLLLEYGADINSLNSYKLTPLSSAVkQYLCINIGRILISNICLLKRIKP 332
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 34-135 1.57e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 79.32  E-value: 1.57e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236650    34 FLAACSSGDTDEVLKLLHRGADINYANVDGLTALHQA--CIDDNVDMVKFLVENGANINQ----------------PDNE 95
Cdd:PHA03100 112 YAISKKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYleSNKIDLKILKLLIDKGVDINAknrvnyllsygvpiniKDVY 191

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 1236650    96 GWIPLHAAASCGYLDIAEFLIGQGAHVGAVNSEGDTPLDI 135
Cdd:PHA03100 192 GFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHI 231
Ank_2 pfam12796
Ankyrin repeats (3 copies);
193-262 2.18e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 71.69  E-value: 2.18e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236650    193 LHVAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKEEACRILVDNlCDMETVNKvGQTAFDVA 262
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYA 68
Ank_4 pfam13637
Ankyrin repeats (many copies);
63-116 5.43e-15

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 69.61  E-value: 5.43e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1236650     63 GLTALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASCGYLDIAEFLI 116
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
IPD_PPP1R12C cd21945
inhibitory phosphorylation domain of protein phosphatase 1 regulatory subunit 12C (PPP1R12C); ...
 598-644 3.16e-14

inhibitory phosphorylation domain of protein phosphatase 1 regulatory subunit 12C (PPP1R12C); PPP1R12C, also called protein phosphatase 1 myosin-binding subunit of 85 kDa (MBS85), protein phosphatase 1 myosin-binding subunit p85, or LENG3, regulates myosin phosphatase activity. This model corresponds to a conserved region of PPP1R12C, which shows high sequence similarity to the inhibitory phosphorylation domain of MYPT1.


Pssm-ID: 412020  Cd Length: 54  Bit Score: 67.42  E-value: 3.16e-14
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 1236650  598 RSYLTPVRDEESESHRKARSRQARQSRRSTQGVTLTDLQEAEKTIGR 644
Cdd:cd21945   8 RSYQTPVRDEESESQRKARSRLMRQSRRSTQGVTLTDLKEAEKSIGK 54
IPD_MYPT1 cd21944
inhibitory phosphorylation domain of myosin phosphatase targeting subunit 1(MYPT1); MYPT1, ...
 590-645 7.25e-14

inhibitory phosphorylation domain of myosin phosphatase targeting subunit 1(MYPT1); MYPT1, also called protein phosphatase 1 regulatory subunit 12A (PPP1R12A), myosin phosphatase target subunit 1, or protein phosphatase myosin-binding subunit, is the targeting subunit of smooth-muscle myosin phosphatase. It is a substrate for the asparaginyl hydroxylase factor inhibiting hypoxia-inducible factor (FIH). MYPT1 acts as a key regulator of protein phosphatase 1C (PPP1C). It mediates binding to myosin. As part of the PPP1C complex, MYPT1 is involved in dephosphorylation of the mitosis regulator polo-like kinase 1 (PLK1). It is capable of inhibiting HIF1A inhibitor (HIF1AN)-dependent suppression of HIF1A activity. This model corresponds to the inhibitory phosphorylation domain of MYPT1.


Pssm-ID: 412019  Cd Length: 57  Bit Score: 66.47  E-value: 7.25e-14
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 1236650  590 SSPAGTQSRSYLTPVRDEESESHRKARSRQARQSRRSTQGVTLTDLQEAEKTIGRS 645
Cdd:cd21944   2 TSEVRERRRSYLTPVRDEESESQRKARSRQARQSRRSTQGVTLTDLQEAEKTIGRS 57
Ank_2 pfam12796
Ankyrin repeats (3 copies);
100-252 3.88e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 65.52  E-value: 3.88e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236650    100 LHAAASCGYLDIAEFLIGQGAHVGAVNSEGDTPLdiaeeeameellqnevnrqgvdieaarkeeerimlrdarqwlnsgh 179
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTAL---------------------------------------------- 34

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1236650    180 isdvrhaksggtalHVAAAKGYTEVLKLLIQAGyDVNIKDYdGWTPLHAAAHWGKEEACRILVDNLCDMETVN 252
Cdd:pfam12796  35 --------------HLAAKNGHLEIVKLLLEHA-DVNLKDN-GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
Ank_4 pfam13637
Ankyrin repeats (many copies);
189-242 5.34e-13

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 63.83  E-value: 5.34e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1236650    189 GGTALHVAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKEEACRILV 242
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 37-262 3.85e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 69.32  E-value: 3.85e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236650    37 ACSSGDTDEVLKLLHRGADINYANVDGLTALHQACIDDNVDMVKFLVENGANINQPDnegwIPLHAAASCGYLDIAEFLI 116
Cdd:PHA02876 185 AAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKND----LSLLKAIRNEDLETSLLLY 260

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236650   117 GQGAHVGAVNSEGDTPLDIAEEEAMEELLQNEVNRQGVDIEAARKEEERIMLRDARQWLNSGHI-------SDVRHAKS- 188
Cdd:PHA02876 261 DAGFSVNSIDDCKNTPLHHASQAPSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYDTENIrtlimlgADVNAADRl 340

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1236650   189 GGTALHVAAA-KGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKEEACRILVDNLCDMETVNKVGQTAFDVA 262
Cdd:PHA02876 341 YITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFA 415
IPD_MYPT2 cd21946
inhibitory phosphorylation domain of myosin phosphatase targeting subunit 2 (MYPT2); MYPT2, ...
 596-646 1.15e-11

inhibitory phosphorylation domain of myosin phosphatase targeting subunit 2 (MYPT2); MYPT2, also called protein phosphatase 1 regulatory subunit 12B (PPP1R12B), or myosin phosphatase target subunit 2, is the targeting subunit of smooth-muscle myosin phosphatase that regulates myosin phosphatase activity and augments Ca(2+) sensitivity of the contractile apparatus. This model corresponds to the inhibitory phosphorylation domain of MYPT2.


Pssm-ID: 412021  Cd Length: 53  Bit Score: 60.06  E-value: 1.15e-11
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 1236650  596 QSRSYLTPVRDEESESHRKARSRQARQSRRSTQGVTLTDLQEAEKTIGRSR 646
Cdd:cd21946   3 KRRSYLTPVRDEEAESLRKARSRQARQTRRSTQGVTLTDLQEAERTFSRSR 53
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 43-257 1.45e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 67.00  E-value: 1.45e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236650    43 TDEVLKLLHRGADINYANV-DGLTALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASCGY-----LDIAEFLI 116
Cdd:PHA03100  14 KVKNIKYIIMEDDLNDYSYkKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLL 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236650   117 GQGAHVGAVNSEGDTPLDIaeeeameellqnevnrqgvdieAARKEeerimlrdarqwLNSGHI--------SDVRHAKS 188
Cdd:PHA03100  94 EYGANVNAPDNNGITPLLY----------------------AISKK------------SNSYSIveylldngANVNIKNS 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236650   189 -GGTALHVAAAKGY--TEVLKLLIQAGYDVNIKD-------YD---------GWTPLHAAAHWGKEEACRILVDNLCDME 249
Cdd:PHA03100 140 dGENLLHLYLESNKidLKILKLLIDKGVDINAKNrvnyllsYGvpinikdvyGFTPLHYAVYNNNPEFVKYLLDLGANPN 219


                 ....*...
gi 1236650   250 TVNKVGQT 257
Cdd:PHA03100 220 LVNKYGDT 227
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 42-262 3.43e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 65.76  E-value: 3.43e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236650    42 DTDEVLKLLHRGADINYANVDGLTALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASCGYLDIAEFLIGQGAH 121
Cdd:PHA02874 103 EKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAY 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236650   122 VGAVNSEGDTPLDIAeeeameellqnevnrqgvdIEAARKEEERIMLRdarqwlNSGHISDvrHAKSGGTALHVAAAKGY 201
Cdd:PHA02874 183 ANVKDNNGESPLHNA-------------------AEYGDYACIKLLID------HGNHIMN--KCKNGFTPLHNAIIHNR 235

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1236650   202 TeVLKLLIQaGYDVNIKDYDGWTPLHAAAHWG-KEEACRILVDNLCDMETVNKVGQTAFDVA 262
Cdd:PHA02874 236 S-AIELLIN-NASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKADISIKDNKGENPIDTA 295
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 37-277 6.64e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 64.98  E-value: 6.64e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236650    37 ACSSGDTDEVLKLLHRGADINYANVDGLTALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASCGYLDIAEFLI 116
Cdd:PHA02874 131 AIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLI 210

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236650   117 GQGAHVGAVNSEGDTPLdiaeeeameellQNEV--NRQGVDIeaarkeeerimlrdarqWLNSGHISDvrHAKSGGTALH 194
Cdd:PHA02874 211 DHGNHIMNKCKNGFTPL------------HNAIihNRSAIEL-----------------LINNASIND--QDIDGSTPLH 259

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236650   195 VAAAKGYT-EVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKEEAcrILVDNLCDMETVNKVGQtafdVADEDILGYLEEL 273
Cdd:PHA02874 260 HAINPPCDiDIIDILLYHKADISIKDNKGENPIDTAFKYINKDP--VIKDIIANAVLIKEADK----LKDSDFLEHIEIK 333


                 ....
gi 1236650   274 QKKQ 277
Cdd:PHA02874 334 DNKE 337
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 33-269 5.74e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 62.39  E-value: 5.74e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236650    33 VFLAACSSGDTDEVLKLLHRGADINYANVDGLTALHQAC-IDDNVDMVKFLVENGANINQPDNEGWIPLHAAASCGYLDI 111
Cdd:PHA02876 311 LYLMAKNGYDTENIRTLIMLGADVNAADRLYITPLHQAStLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVI 390

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236650   112 AEFLIGQGAhvgavnsegdtpldiaeeeameellqnevnrqgvDIEAArkeeerimlrdarqwlnsghisdvrhAKSGGT 191
Cdd:PHA02876 391 INTLLDYGA----------------------------------DIEAL--------------------------SQKIGT 410

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236650   192 ALHVA--AAKGYTEVlKLLIQAGYDVNIKDYDGWTPLHAAAHWG-KEEACRILVDNLCDMETVNKVGQTAFDVAdediLG 268
Cdd:PHA02876 411 ALHFAlcGTNPYMSV-KTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIA----LE 485


                 .
gi 1236650   269 Y 269
Cdd:PHA02876 486 Y 486
Ank_5 pfam13857
Ankyrin repeats (many copies);
82-135 1.95e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 53.89  E-value: 1.95e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1236650     82 LVENG-ANINQPDNEGWIPLHAAASCGYLDIAEFLIGQGAHVGAVNSEGDTPLDI 135
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDL 55
Ank_5 pfam13857
Ankyrin repeats (many copies);
49-103 2.15e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 53.50  E-value: 2.15e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1236650     49 LLHRGADINYANVDGLTALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAA 103
Cdd:pfam13857   2 LEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 37-258 2.79e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 59.62  E-value: 2.79e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236650    37 ACSSGDTDEVLKLLHRGADINYANVDGLTALHQACIDDNVDMVKFLVENGA--NINQPDNEGwiPLHAAASCGYLDIAEF 114
Cdd:PHA02875   9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAipDVKYPDIES--ELHDAVEEGDVKAVEE 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236650   115 LIGQGAHVGAV-NSEGDTPLDIAEEEameellqnevnrQGVDIeaarkeeerimlrdARQWLNSGHISDVRHAKSgGTAL 193
Cdd:PHA02875  87 LLDLGKFADDVfYKDGMTPLHLATIL------------KKLDI--------------MKLLIARGADPDIPNTDK-FSPL 139

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1236650   194 HVAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKEEACRILVDNLCDMETVNKVGQTA 258
Cdd:PHA02875 140 HLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVA 204
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 40-244 5.88e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 58.82  E-value: 5.88e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236650    40 SGDTDEVLKLL-HRGADINYANVDGLTALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASCGYLDIAEFLIGQ 118
Cdd:PHA02874  11 SGDIEAIEKIIkNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDN 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236650   119 GAHVG----------AVNSEGDTPLDIAEEEAMEELLQNEVNRQGvDIEAARkeeeriMLRDARQWLNsghISDVrhakS 188
Cdd:PHA02874  91 GVDTSilpipciekdMIKTILDCGIDVNIKDAELKTFLHYAIKKG-DLESIK------MLFEYGADVN---IEDD----N 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 1236650   189 GGTALHVAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKEEACRILVDN 244
Cdd:PHA02874 157 GCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDH 212
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 44-127 8.56e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 58.14  E-value: 8.56e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236650    44 DEVLKLLHRGADINYANVDGLTALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASCGYLDIAEFLIGQGAHVG 123
Cdd:PHA03100 173 NRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252


                 ....
gi 1236650   124 AVNS 127
Cdd:PHA03100 253 TIIE 256
IPD_PPP1R12 cd21930
inhibitory phosphorylation domain of protein phosphatase 1 regulatory subunit 12 (PPP1R12) ...
 598-640 1.11e-08

inhibitory phosphorylation domain of protein phosphatase 1 regulatory subunit 12 (PPP1R12) family; The PPP1R12 family includes PPP1R12A/MYPT1, PPP1R12B/MYPT2, and PPP1R12C. PPP1R12A/MYPT1, also called myosin phosphatase target subunit 1, or protein phosphatase myosin-binding subunit, is a substrate for the asparaginyl hydroxylase factor inhibiting hypoxia-inducible factor (FIH). It acts as a key regulator of protein phosphatase 1C (PPP1C). It mediates binding to myosin. As part of the PPP1C complex, PPP1R12A/MYPT1 is involved in dephosphorylation of PLK1. It is capable of inhibiting HIF1A inhibitor (HIF1AN)-dependent suppression of HIF1A activity. PPP1R12B/MYPT2, also called myosin phosphatase target subunit 2, is the targeting subunit of smooth-muscle myosin phosphatase that regulates myosin phosphatase activity and augments Ca(2+) sensitivity of the contractile apparatus. PPP1R12C, also called protein phosphatase 1 myosin-binding subunit of 85 kDa (MBS85), protein phosphatase 1 myosin-binding subunit p85, or LENG3, regulates myosin phosphatase activity. All family members contain an inhibitory phosphorylation domain.


Pssm-ID: 412018  Cd Length: 47  Bit Score: 51.19  E-value: 1.11e-08
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 1236650  598 RSYLTPVRDEESESHRKARSRQARQSRRSTQGVTLTDLQEAEK 640
Cdd:cd21930   5 RSYLPPVRDEESETQRKARAKRARQTRRSTQGVTLEDLEEAEK 47
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 44-269 1.93e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 57.20  E-value: 1.93e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236650    44 DEVLKLLHRGADINYANVDGLTALHQACI--------------------------------------------------- 72
Cdd:PHA02878  51 DVVKSLLTRGHNVNQPDHRDLTPLHIICKepnklgmkemirsinkcsvfytlvaikdafnnrnveifkiiltnrykniqt 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236650    73 -----------DDNVD--MVKFLVENGANINQPD-NEGWIPLHAAASCGYLDIAEFLIGQGAHVGAVNSEGDTPLDiaee 138
Cdd:PHA02878 131 idlvyidkkskDDIIEaeITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLH---- 206

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236650   139 eameellqnevnrqgvdiEAARKEEERIMlrdaRQWLNSGHISDVRHaKSGGTALHVAAA--KGYtEVLKLLIQAGYDVN 216
Cdd:PHA02878 207 ------------------HAVKHYNKPIV----HILLENGASTDARD-KCGNTPLHISVGycKDY-DILKLLLEHGVDVN 262

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 1236650   217 IKDY-DGWTPLHAAAHwgKEEACRILVDNLCDMETVNKVGQTAFDVADEDILGY 269
Cdd:PHA02878 263 AKSYiLGLTALHSSIK--SERKLKLLLEYGADINSLNSYKLTPLSSAVKQYLCI 314
Ank_4 pfam13637
Ankyrin repeats (many copies);
33-83 1.95e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 50.74  E-value: 1.95e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1236650     33 VFLAACSSGDTDEVLKLLHRGADINYANVDGLTALHQACIDDNVDMVKFLV 83
Cdd:pfam13637   4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
IPD_PPP1R12A-like cd22527
inhibitory phosphorylation domain of protein phosphatase 1 regulatory subunit 12A-like, and ...
 596-641 2.58e-08

inhibitory phosphorylation domain of protein phosphatase 1 regulatory subunit 12A-like, and similar proteins; Protein phosphatase 1 regulatory subunit 12A-like (PPP1R12A-like) is a homolog of MYPT1, also called protein phosphatase 1 regulatory subunit 12A (PPP1R12A), myosin phosphatase target subunit 1, or protein phosphatase myosin-binding subunit. MYPT1 is the targeting subunit of smooth-muscle myosin phosphatase. It is a substrate for the asparaginyl hydroxylase factor inhibiting hypoxia-inducible factor (FIH). MYPT1 acts as a key regulator of protein phosphatase 1C (PPP1C). It mediates binding to myosin. As part of the PPP1C complex, MYPT1 is involved in dephosphorylation of the mitosis regulator polo-like kinase 1 (PLK1). It is capable of inhibiting HIF1A inhibitor (HIF1AN)-dependent suppression of HIF1A activity. This model corresponds to the inhibitory phosphorylation domain of PPP1R12A-like protein.


Pssm-ID: 412022  Cd Length: 50  Bit Score: 50.64  E-value: 2.58e-08
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 1236650  596 QSRSYLTPVRDEESESHRKARSRQARQSRRSTQGVTLTDLQEAEKT 641
Cdd:cd22527   5 RRRSYLTPVRDEEAEAQRKARSRHARQSRRSTQGVTLTDLKEAEKT 50
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 35-131 3.57e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.83  E-value: 3.57e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236650    35 LAAcsSGDTDEVLKLLHRGADINYANVDGLTALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASCGYLDIAEF 114
Cdd:PTZ00322  89 LAA--SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166

                         90
                 ....*....|....*....
gi 1236650   115 LIG--QGAHVGAVNSEGDT 131
Cdd:PTZ00322 167 LSRhsQCHFELGANAKPDS 185
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
147-270 1.81e-07

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 53.42  E-value: 1.81e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236650  147 NEVNRQGVDIEAARKEEERIMLRDARQWLNSGHISDVRHAKSGGTALHVAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPL 226
Cdd:COG0666  12 LAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLL 91

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 1236650  227 HAAAHWGKEEACRILVDNLCDMETVNKVGQTAFDVA----DEDILGYL 270
Cdd:COG0666  92 HAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAayngNLEIVKLL 139
Ank_5 pfam13857
Ankyrin repeats (many copies);
175-229 2.00e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.11  E-value: 2.00e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1236650    175 LNSGHISDVRHAKSGGTALHVAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAA 229
Cdd:pfam13857   2 LEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 62-94 2.47e-07

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: 47.28  E-value: 2.47e-07
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1236650     62 DGLTALHQACID-DNVDMVKFLVENGANINQPDN 94
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 57-269 2.53e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 53.73  E-value: 2.53e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236650    57 NYANVDGLTALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASC-GYLDIAEFL--------------IGQGAH 121
Cdd:PHA02878  31 TSASLIPFIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEpNKLGMKEMIrsinkcsvfytlvaIKDAFN 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236650   122 VGAVNSEGDTPLDIAEeeameellqnevNRQGVDIEAARK--EEERIMLRDARQWLNSGHISDVRHAKSGGTALHVAAAK 199
Cdd:PHA02878 111 NRNVEIFKIILTNRYK------------NIQTIDLVYIDKksKDDIIEAEITKLLLSYGADINMKDRHKGNTALHYATEN 178

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236650   200 GYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKEEACRILVDNLCDMETVNKVGQTAFDVADEDILGY 269
Cdd:PHA02878 179 KDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKDY 248
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 42-226 2.78e-07

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 53.76  E-value: 2.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236650    42 DTDEVLKLLHRGADINYANVDGLTALHQACIDDNV--DMVKFLVENGANINQPDNEGWIPLHAAASCG------------ 107
Cdd:PHA02716 296 DISVVYSFLQPGVKLHYKDSAGRTCLHQYILRHNIstDIIKLLHEYGNDLNEPDNIGNTVLHTYLSMLsvvnildpetdn 375

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236650   108 --YLDIAEFLIGQGAHVGAVNSEGDTPL-------------DIAEEEAMEELLQNEVNRQGVDIEAARKEEERIM----- 167
Cdd:PHA02716 376 diRLDVIQCLISLGADITAVNCLGYTPLtsyictaqnymyyDIIDCLISDKVLNMVKHRILQDLLIRVDDTPCIIhhiia 455

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236650   168 --------LRDARQWLNSGHISDVRHAK------------SGGTALHVAA-----AKGYTEVLKLLIQAGYDVNIKDYDG 222
Cdd:PHA02716 456 kyniptdlYTDEYEPYDSTKIHDVYHCAiierynnavcetSGMTPLHVSIishtnANIVMDSFVYLLSIQYNINIPTKNG 535


                 ....
gi 1236650   223 WTPL 226
Cdd:PHA02716 536 VTPL 539
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 197-283 5.05e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.98  E-value: 5.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236650   197 AAKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKEEACRILVDNLCDMETVNKVGQTAFDVADEDILGYLEELQKK 276
Cdd:PTZ00322  90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169


                 ....*..
gi 1236650   277 QNLLHSE 283
Cdd:PTZ00322 170 HSQCHFE 176
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 45-135 1.00e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 49.82  E-value: 1.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236650    45 EVLKLL-HRGADINYANVDGLTALHQAC--IDDNVDMVKFLVENGANINQPDNEGWIPLHAaascgYL------DIAEFL 115
Cdd:PHA02859 104 EILKILiDSGSSITEEDEDGKNLLHMYMcnFNVRINVIKLLIDSGVSFLNKDFDNNNILYS-----YIlfhsdkKIFDFL 178

                         90       100
                 ....*....|....*....|
gi 1236650   116 IGQGAHVGAVNSEGDTPLDI 135
Cdd:PHA02859 179 TSLGIDINETNKSGYNCYDL 198
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 26-133 1.02e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 51.53  E-value: 1.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236650    26 VKFDDGAVFLAACSSGDTDEVLK-LLHRGADINYANVDGLTALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAA 104
Cdd:PHA02875  97 VFYKDGMTPLHLATILKKLDIMKlLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAM 176

                         90       100
                 ....*....|....*....|....*....
gi 1236650   105 SCGYLDIAEFLIGQGAHVGAVNSEGDTPL 133
Cdd:PHA02875 177 AKGDIAICKMLLDSGANIDYFGKNGCVAA 205
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 62-90 1.06e-06

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 45.33  E-value: 1.06e-06
                          10        20
                  ....*....|....*....|....*....
gi 1236650     62 DGLTALHQACIDDNVDMVKFLVENGANIN 90
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 46-278 1.58e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 51.22  E-value: 1.58e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236650    46 VLKLLHRGADINY----ANVDGLTALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASCGYLDIAEFLIGQGAH 121
Cdd:PHA02876 124 ILKEAISGNDIHYdkinESIEYMKLIKERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGAD 203

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236650   122 VGAVNSEGDTPLDIAEEEAMEELLQNEV-NRQGVD------IEAARKE--EERIMLRDARQWLNSghISDVRHaksggTA 192
Cdd:PHA02876 204 VNIIALDDLSVLECAVDSKNIDTIKAIIdNRSNINkndlslLKAIRNEdlETSLLLYDAGFSVNS--IDDCKN-----TP 276

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236650   193 LHVAA-AKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKE-EACRILVDNLCDMETVNKVGQTAFDVA-----DED 265
Cdd:PHA02876 277 LHHASqAPSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYDtENIRTLIMLGADVNAADRLYITPLHQAstldrNKD 356

                        250
                 ....*....|...
gi 1236650   266 ILGYLEELQKKQN 278
Cdd:PHA02876 357 IVITLLELGANVN 369
Ank_4 pfam13637
Ankyrin repeats (many copies);
222-270 2.94e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.57  E-value: 2.94e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1236650    222 GWTPLHAAAHWGKEEACRILVDNLCDMETVNKVGQTAFDVA----DEDILGYL 270
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAasngNVEVLKLL 53
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 63-210 3.16e-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: 50.40  E-value: 3.16e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236650   63 GLTALHQACIDDNVDMVKFLVENGANINQPDNEGWI--------------PLHAAASCGYLDIAEFLIGQGAHVGAVNSE 128
Cdd:cd22192  89 GETALHIAVVNQNLNLVRELIARGADVVSPRATGTFfrpgpknliyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSL 168

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236650  129 GDTPLDIaeeeaMEELLQNEVNRQGVDIeaarkeeerIMLRDARQwlNSGHISDVRHaKSGGTALHVAAAKGYTEVLKLL 208
Cdd:cd22192 169 GNTVLHI-----LVLQPNKTFACQMYDL---------ILSYDKED--DLQPLDLVPN-NQGLTPFKLAAKEGNIVMFQHL 231


                ..
gi 1236650  209 IQ 210
Cdd:cd22192 232 VQ 233
PHA03095 PHA03095
ankyrin-like protein; Provisional
 76-270 3.67e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 50.02  E-value: 3.67e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236650    76 VDMVKFLVENGANINQPDNEGWIPLHAAASCG---YLDIAEFLIGQGAHVGAVNSEGDTPLdiaeeeameellqnevnrq 152
Cdd:PHA03095  27 VEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSsekVKDIVRLLLEAGADVNAPERCGFTPL------------------- 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236650   153 gvdieaarkeeerimlrdarqwlnsghisdvrhaksggtalHVAAAKGYTE-VLKLLIQAGYDVNIKDYDGWTPLHA--A 229
Cdd:PHA03095  88 -----------------------------------------HLYLYNATTLdVIKLLIKAGADVNAKDKVGRTPLHVylS 126

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 1236650   230 AHWGKEEACRILVDNLCDMETVNKVGQTAFDV------ADEDILGYL 270
Cdd:PHA03095 127 GFNINPKVIRLLLRKGADVNALDLYGMTPLAVllksrnANVELLRLL 173
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 62-90 3.84e-06

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: 43.73  E-value: 3.84e-06
                           10        20
                   ....*....|....*....|....*....
gi 1236650      62 DGLTALHQACIDDNVDMVKFLVENGANIN 90
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 189-219 3.87e-06

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 43.82  E-value: 3.87e-06
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1236650    189 GGTALHVAAAK-GYTEVLKLLIQAGYDVNIKD 219
Cdd:pfam00023   2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 37-217 8.88e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 48.45  E-value: 8.88e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236650    37 ACSSGDTDEVLKLLHRGA---DINYAnvDGLTALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASCGYLDIAE 113
Cdd:PHA02875  75 AVEEGDVKAVEELLDLGKfadDVFYK--DGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIE 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236650   114 FLIGQGAHVGAVNSEGDTPLDIAEEEAmeellqnevnrqgvDIEAARkeeeriMLrdarqwLNSGHISDVRHAKSGGTAL 193
Cdd:PHA02875 153 LLIDHKACLDIEDCCGCTPLIIAMAKG--------------DIAICK------ML------LDSGANIDYFGKNGCVAAL 206

                        170       180
                 ....*....|....*....|....
gi 1236650   194 HVAAAKGYTEVLKLLIQAGYDVNI 217
Cdd:PHA02875 207 CYAIENNKIDIVRLFIKRGADCNI 230
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 31-89 1.23e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 48.71  E-value: 1.23e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 1236650    31 GAVFLAACSSGDTDEVLKLLHRGADINYANVDGLTALHQACIDDNVDMVKFLVENGANI 89
Cdd:PLN03192 623 GDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 35-226 1.78e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 47.94  E-value: 1.78e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236650    35 LAACSSGDTDEVLKLLHRGADINYANVDGLTALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASCGYLDIAEF 114
Cdd:PLN03192 530 LTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRI 609

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236650   115 LIgQGAHVGAVNSEGDtpldiaeeeameellqnevnrqgVDIEAARKEEERIMLRDARQWLNSGhiSDVRHaksGGTALH 194
Cdd:PLN03192 610 LY-HFASISDPHAAGD-----------------------LLCTAAKRNDLTAMKELLKQGLNVD--SEDHQ---GATALQ 660

                        170       180       190
                 ....*....|....*....|....*....|...
gi 1236650   195 VAAAKGYTEVLKLLIQAGYDVNIKD-YDGWTPL 226
Cdd:PLN03192 661 VAMAEDHVDMVRLLIMNGADVDKANtDDDFSPT 693
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 175-291 2.32e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 47.56  E-value: 2.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236650   175 LNSGHISDVRHAKsGGTALHVAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKEEACRIL--VDNLCDMETVN 252
Cdd:PLN03192 545 LKAKLDPDIGDSK-GRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILyhFASISDPHAAG 623

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 1236650   253 KVGQTAfdvADEDILGYLEELQKKQNLLHSEKRDKKSPL 291
Cdd:PLN03192 624 DLLCTA---AKRNDLTAMKELLKQGLNVDSEDHQGATAL 659
PHA02798 PHA02798
ankyrin-like protein; Provisional
 43-227 2.55e-05

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 47.14  E-value: 2.55e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236650    43 TDEVLKLLHRGADINYANVDGLTALhqaC------IDDN--VDMVKFLVENGANINQPDNEGWIPLHAAASCGYLDIAE- 113
Cdd:PHA02798  51 TDIVKLFINLGANVNGLDNEYSTPL---CtilsniKDYKhmLDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEi 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236650   114 --FLIGQGAHVGAVNSEGDTPLDIaeeeameellqnevnrqgvdieaarkeeerimlrdarqWLNSGHISDVrhaksggt 191
Cdd:PHA02798 128 llFMIENGADTTLLDKDGFTMLQV--------------------------------------YLQSNHHIDI-------- 161

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 1236650   192 alhvaaakgytEVLKLLIQAGYDVN-IKDYDGWTPLH 227
Cdd:PHA02798 162 -----------EIIKLLLEKGVDINtHNNKEKYDTLH 187
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 32-122 3.36e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 46.98  E-value: 3.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236650    32 AVFLAACSSGDTDEVLKLLHRGADINYANVDGLTALHQACIDD-NVDMVKFLVENGANINQPDNEGWIPLHAAasCGYLD 110
Cdd:PHA02876 411 ALHFALCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIA--LEYHG 488

                         90
                 ....*....|..
gi 1236650   111 IAEFLIGQGAHV 122
Cdd:PHA02876 489 IVNILLHYGAEL 500
Ank_5 pfam13857
Ankyrin repeats (many copies);
208-262 3.82e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.56  E-value: 3.82e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1236650    208 LIQAGY-DVNIKDYDGWTPLHAAAHWGKEEACRILVDNLCDMETVNKVGQTAFDVA 262
Cdd:pfam13857   1 LLEHGPiDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 191-217 7.56e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.88  E-value: 7.56e-05
                           10        20
                   ....*....|....*....|....*..
gi 1236650     191 TALHVAAAKGYTEVLKLLIQAGYDVNI 217
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 56-210 1.46e-04

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: 44.80  E-value: 1.46e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236650   56 INYANVD----GLTALHQACIDDNVDMVKFLVENGANINQPDNE--------------GWIPLHAAASCGYLDIAEFLIG 117
Cdd:cd22196  83 VNAAYTDsyykGQTALHIAIERRNMHLVELLVQNGADVHARASGeffkkkkggpgfyfGELPLSLAACTNQLDIVKFLLE 162

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236650  118 ---QGAHVGAVNSEGDTPL--------DIAEEEAMEELLQNEVNRQGVDIEAARKEEErimlrdarqwlnsghISDvrha 186
Cdd:cd22196 163 nphSPADISARDSMGNTVLhalvevadNTPENTKFVTKMYNEILILGAKIRPLLKLEE---------------ITN---- 223

                       170       180
                ....*....|....*....|....
gi 1236650  187 KSGGTALHVAAAKGYTEVLKLLIQ 210
Cdd:cd22196 224 KKGLTPLKLAAKTGKIGIFAYILG 247
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 70-133 1.72e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 43.27  E-value: 1.72e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1236650    70 ACIDD---NVDMVKFLVENGANIN-QPDNEGWIPLHAaascgYL--------DIAEFLIGQGAHVGAVNSEGDTPL 133
Cdd:PHA02859  57 SCLEKdkvNVEILKFLIENGADVNfKTRDNNLSALHH-----YLsfnknvepEILKILIDSGSSITEEDEDGKNLL 127
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 79-135 2.38e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.12  E-value: 2.38e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 1236650    79 VKFLVENGANINQPDNEGWIPLHAAASCGYLDIAEFLIGQGAHVGAVNSEGDTPLDI 135
Cdd:PTZ00322  98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLEL 154
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 45-119 2.65e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 42.88  E-value: 2.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236650    45 EVLKLL-HRGADINYANVD-GLTALHQ-ACIDDNV--DMVKFLVENGANINQPDNEGWIPLHAaascgYLD-------IA 112
Cdd:PHA02859  67 EILKFLiENGADVNFKTRDnNLSALHHyLSFNKNVepEILKILIDSGSSITEEDEDGKNLLHM-----YMCnfnvrinVI 141


                 ....*..
gi 1236650   113 EFLIGQG 119
Cdd:PHA02859 142 KLLIDSG 148
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 95-126 2.83e-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: 38.42  E-value: 2.83e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1236650     95 EGWIPLHAAA-SCGYLDIAEFLIGQGAHVGAVN 126
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
Ank_4 pfam13637
Ankyrin repeats (many copies);
99-135 3.93e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.79  E-value: 3.93e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1236650     99 PLHAAASCGYLDIAEFLIGQGAHVGAVNSEGDTPLDI 135
Cdd:pfam13637   4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHF 40
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 189-217 7.32e-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: 7.32e-04
                          10        20
                  ....*....|....*....|....*....
gi 1236650    189 GGTALHVAAAKGYTEVLKLLIQAGYDVNI 217
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 63-210 8.40e-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: 42.48  E-value: 8.40e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236650   63 GLTALHQACIDDNVDMVKFLVENGANIN--------QPDNE------GWIPLHAAASCGYLDIAEFLIG---QGAHVGAV 125
Cdd:cd22193  76 GQTALHIAIERRQGDIVALLVENGADVHahakgrffQPKYQgegfyfGELPLSLAACTNQPDIVQYLLEnehQPADIEAQ 155

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236650  126 NSEGDTPLDIAEEEAMEELLQNEVNRQGVDIeaarkeeerIMLRDARqWLNSGHISDVRHAKsGGTALHVAAAKGYTEVL 205
Cdd:cd22193 156 DSRGNTVLHALVTVADNTKENTKFVTRMYDM---------ILIRGAK-LCPTVELEEIRNND-GLTPLQLAAKMGKIEIL 224


                ....*
gi 1236650  206 KLLIQ 210
Cdd:cd22193 225 KYILQ 229
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 221-253 9.28e-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: 37.27  E-value: 9.28e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1236650    221 DGWTPLHAAA-HWGKEEACRILVDNLCDMETVNK 253
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 33-122 1.04e-03

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: 42.31  E-value: 1.04e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236650   33 VFLAAcSSGDTDEVLKLL-HRGADINYANVDGLTALHQACIDDNVDMVKFLVENGAN-INQPDN----EGWIPLHAAASC 106
Cdd:cd22192  21 LLLAA-KENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElVNEPMTsdlyQGETALHIAVVN 99

                        90
                ....*....|....*.
gi 1236650  107 GYLDIAEFLIGQGAHV 122
Cdd:cd22192 100 QNLNLVRELIARGADV 115
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 63-135 1.15e-03

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: 42.17  E-value: 1.15e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236650   63 GLTALHQACIDDNVDMVKFLVENGANINQPDNE-------------GWIPLHAAASCGYLDIAEFLIGQGAHVGAV---N 126
Cdd:cd21882  73 GQTALHIAIENRNLNLVRLLVENGADVSARATGrffrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGAQPAALeaqD 152


                ....*....
gi 1236650  127 SEGDTPLDI 135
Cdd:cd21882 153 SLGNTVLHA 161
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 196-258 1.44e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 41.78  E-value: 1.44e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1236650   196 AAAKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKEEACRILVDNLCDMETVNKVGQTA 258
Cdd:PLN03192 532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTA 594
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 60-206 1.87e-03

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 41.28  E-value: 1.87e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236650   60 NVDGLTALHQACIDDNVDMVKFLVENGANIN--------QPDNE------GWIPLHAAASCGYLDIAEFLIGQGAHVGAV 125
Cdd:cd22194 138 AYEGQTALNIAIERRQGDIVKLLIAKGADVNahakgvffNPKYKhegfyfGETPLALAACTNQPEIVQLLMEKESTDITS 217

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236650  126 -NSEGDTPLDIAEEEAMEELLQNEVNRQGVDieaarkeeerIMLRDARQWlnsgHISDVRHaKSGGTALHVAAAKGYTEV 204
Cdd:cd22194 218 qDSRGNTVLHALVTVAEDSKTQNDFVKRMYD----------MILLKSENK----NLETIRN-NEGLTPLQLAAKMGKAEI 282


                ..
gi 1236650  205 LK 206
Cdd:cd22194 283 LK 284
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 171-241 1.88e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 41.42  E-value: 1.88e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1236650   171 ARQWLNSGHISDVRHAkSGGTALHVAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKEEACRIL 241
Cdd:PTZ00322  98 ARILLTGGADPNCRDY-DGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
PHA02946 PHA02946
ankyin-like protein; Provisional
 33-266 4.49e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 40.04  E-value: 4.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236650    33 VFLAACSSGDTDE--VLKLLHRGADINYANVDGLTALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASCG--Y 108
Cdd:PHA02946  40 ILHAYCGIKGLDErfVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDdeV 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236650   109 LDIAEFLIGQGAHV-GAVNSEGDTPLDIAEEEAMEELLQnevnRQGVDIEA------ARKEEERIMLRDARQ-----WLN 176
Cdd:PHA02946 120 IERINLLVQYGAKInNSVDEEGCGPLLACTDPSERVFKK----IMSIGFEArivdkfGKNHIHRHLMSDNPKastisWMM 195

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236650   177 SGHISDVRHAKSGGTALHVAAAKGY--TEVLKLLIQAGyDVNIKDYDGWTPLhaaahwgkeeacRILVDNLCDMETVNKV 254
Cdd:PHA02946 196 KLGISPSKPDHDGNTPLHIVCSKTVknVDIINLLLPST-DVNKQNKFGDSPL------------TLLIKTLSPAHLINKL 262

                        250
                 ....*....|..
gi 1236650   255 GQTAFDVADEDI 266
Cdd:PHA02946 263 LSTSNVITDQTV 274
PHA02795 PHA02795
ankyrin-like protein; Provisional
 76-135 7.08e-03

ankyrin-like protein; Provisional


Pssm-ID: 165157 [Multi-domain]  Cd Length: 437  Bit Score: 39.21  E-value: 7.08e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236650    76 VDMVKFLVENGANINQPDNEGWIPLHAAASCGYLDIAEFLIGQGAHVGAVNSEGDTPLDI 135
Cdd:PHA02795 201 LEIYKLCIPYIEDINQLDAGGRTLLYRAIYAGYIDLVSWLLENGANVNAVMSNGYTCLDV 260
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 203-282 8.37e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 38.26  E-value: 8.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236650   203 EVLKLLIQAGYDVNIK-DYDGWTPLHAAAHWGK---EEACRILVDNLCDMETVNKVGQTAFDV------ADEDILGYLEE 272
Cdd:PHA02859  67 EILKFLIENGADVNFKtRDNNLSALHHYLSFNKnvePEILKILIDSGSSITEEDEDGKNLLHMymcnfnVRINVIKLLID 146

                         90
                 ....*....|....*...
gi 1236650   273 L--------QKKQNLLHS 282
Cdd:PHA02859 147 SgvsflnkdFDNNNILYS 164
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 221-249 8.88e-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: 34.10  E-value: 8.88e-03
                           10        20
                   ....*....|....*....|....*....
gi 1236650     221 DGWTPLHAAAHWGKEEACRILVDNLCDME 249
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
 
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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