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Conserved domains on  [gi|1584775672|ref|NP_001355758|]
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protein phosphatase 1 regulatory subunit 12B isoform 3 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRKG1_interact pfam15898
cGMP-dependent protein kinase interacting domain; This domain is found at the C-terminus of ...
 707-808 8.33e-44

cGMP-dependent protein kinase interacting domain; This domain is found at the C-terminus of protein phosphatase 1 regulatory subunits 12A, 12B and 12C. In protein phosphatase 1 regulatory subunit 12A it has been found to bind to cGMP-dependent protein kinase 1 via a leucine zipper motif located at the C-terminus of this domain.


:

Pssm-ID: 464927 [Multi-domain]  Cd Length: 102  Bit Score: 153.23  E-value: 8.33e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584775672 707 DYKKLYESALTENQKLKTKLQEAQLELADIKAKLEKMAQQKQEKTSDRSSVLEVEKRERRALERKMSEMEEEMKVLTELK 786
Cdd:pfam15898   1 DYKKLYEEELQENERLKRKLQDAQQELAELKSQLERLTQQRQESFSDRSSLLETEKREKRALERKISEMEEELKVLEDLR 80

                          90       100
                  ....*....|....*....|..
gi 1584775672 787 SDNQRLKDENGALIRVISKLSK 808
Cdd:pfam15898  81 AENQRLKDENGALIRVISKLSK 102
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
45-137 1.54e-18

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 86.93  E-value: 1.54e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584775672  45 QARSGATALHVAAAKGYSEVLRLLIQAGYELNVQDHDGWTPLHAAAHWGVKEACSILAEALCDMDIRNKLGQTPFDVA-D 123
Cdd:COG0666   149 QDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAaE 228

                          90
                  ....*....|....
gi 1584775672 124 EGLVEHLEMLQKKQ 137
Cdd:COG0666   229 NGNLEIVKLLLEAG 242
IPD_PPP1R12 super family cl40436
inhibitory phosphorylation domain of protein phosphatase 1 regulatory subunit 12 (PPP1R12) ...
 442-494 2.58e-17

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: 76.28  E-value: 2.58e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1584775672 442 EAREKRRSYLTPVRDEEAESLRKARSRQARQTRRSTQGVTLTDLQEAEKTFSR 494
Cdd:cd21945     2 DSRDRRRSYQTPVRDEESESQRKARSRLMRQSRRSTQGVTLTDLKEAEKSIGK 54
 
Name Accession Description Interval E-value
PRKG1_interact pfam15898
cGMP-dependent protein kinase interacting domain; This domain is found at the C-terminus of ...
 707-808 8.33e-44

cGMP-dependent protein kinase interacting domain; This domain is found at the C-terminus of protein phosphatase 1 regulatory subunits 12A, 12B and 12C. In protein phosphatase 1 regulatory subunit 12A it has been found to bind to cGMP-dependent protein kinase 1 via a leucine zipper motif located at the C-terminus of this domain.


Pssm-ID: 464927 [Multi-domain]  Cd Length: 102  Bit Score: 153.23  E-value: 8.33e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584775672 707 DYKKLYESALTENQKLKTKLQEAQLELADIKAKLEKMAQQKQEKTSDRSSVLEVEKRERRALERKMSEMEEEMKVLTELK 786
Cdd:pfam15898   1 DYKKLYEEELQENERLKRKLQDAQQELAELKSQLERLTQQRQESFSDRSSLLETEKREKRALERKISEMEEELKVLEDLR 80

                          90       100
                  ....*....|....*....|..
gi 1584775672 787 SDNQRLKDENGALIRVISKLSK 808
Cdd:pfam15898  81 AENQRLKDENGALIRVISKLSK 102
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
45-137 1.54e-18

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 86.93  E-value: 1.54e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584775672  45 QARSGATALHVAAAKGYSEVLRLLIQAGYELNVQDHDGWTPLHAAAHWGVKEACSILAEALCDMDIRNKLGQTPFDVA-D 123
Cdd:COG0666   149 QDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAaE 228

                          90
                  ....*....|....
gi 1584775672 124 EGLVEHLEMLQKKQ 137
Cdd:COG0666   229 NGNLEIVKLLLEAG 242
IPD_PPP1R12C cd21945
inhibitory phosphorylation domain of protein phosphatase 1 regulatory subunit 12C (PPP1R12C); ...
 442-494 2.58e-17

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: 76.28  E-value: 2.58e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1584775672 442 EAREKRRSYLTPVRDEEAESLRKARSRQARQTRRSTQGVTLTDLQEAEKTFSR 494
Cdd:cd21945     2 DSRDRRRSYQTPVRDEESESQRKARSRLMRQSRRSTQGVTLTDLKEAEKSIGK 54
Ank_2 pfam12796
Ankyrin repeats (3 copies);
53-133 2.08e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.07  E-value: 2.08e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584775672  53 LHVAAAKGYSEVLRLLIQAGYELNVQDHDGWTPLHAAAHWGVKEACSILAEaLCDMDIRNKlGQTPFDVA-DEGLVEHLE 131
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYAaRSGHLEIVK 78


                  ..
gi 1584775672 132 ML 133
Cdd:pfam12796  79 LL 80
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 57-124 3.76e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.20  E-value: 3.76e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1584775672  57 AAKGYSEVLRLLIQAGYELNVQDHDGWTPLHAAAHWGVKEACSILAEALCDMDIRNKLGQTPFDVADE 124
Cdd:PTZ00322   90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEE 157
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
718-808 3.09e-04

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 44.46  E-value: 3.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584775672 718 ENQKLKTKLQEAQLELADIKAKLEKM-AQQKQEKTSDRssvlEVEKRERR--ALERKMSEMEEEMKvltELKSDNQRLKD 794
Cdd:COG2433   428 EVEELEAELEEKDERIERLERELSEArSEERREIRKDR----EISRLDREieRLERELEEERERIE---ELKRKLERLKE 500

                          90       100
                  ....*....|....*....|.
gi 1584775672 795 -------ENGALIRVISKLSK 808
Cdd:COG2433   501 lwklehsGELVPVKVVEKFTK 521
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 49-77 8.28e-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: 37.18  E-value: 8.28e-04
                           10        20
                   ....*....|....*....|....*....
gi 1584775672   49 GATALHVAAAKGYSEVLRLLIQAGYELNV 77
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 53-137 2.25e-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: 41.54  E-value: 2.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584775672  53 LHVAAAKGYSEVLRLLIQAGYELNVQDHDGWTPLHAAAHWGVKE-ACSILaEALCDMD----------IRNKLGQTPFDV 121
Cdd:cd22192   140 LSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPNKTfACQMY-DLILSYDkeddlqpldlVPNNQGLTPFKL 218

                          90
                  ....*....|....*..
gi 1584775672 122 A-DEGLVEHLEMLQKKQ 137
Cdd:cd22192   219 AaKEGNIVMFQHLVQKR 235
PRK12704 PRK12704
phosphodiesterase; Provisional
 702-808 5.50e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.15  E-value: 5.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584775672 702 EDSNRDYKKLYESALTE-NQKLKTKLQEAQLELADIKAKL---EKMAQQKQEKTSDRSSVLevEKRERRaLERKMSEMEE 777
Cdd:PRK12704   45 EEAKKEAEAIKKEALLEaKEEIHKLRNEFEKELRERRNELqklEKRLLQKEENLDRKLELL--EKREEE-LEKKEKELEQ 121

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1584775672 778 EMKVLTELKSDNQRLKDENGALIRVISKLSK 808
Cdd:PRK12704  122 KQQELEKKEEELEELIEEQLQELERISGLTA 152
 
Name Accession Description Interval E-value
PRKG1_interact pfam15898
cGMP-dependent protein kinase interacting domain; This domain is found at the C-terminus of ...
 707-808 8.33e-44

cGMP-dependent protein kinase interacting domain; This domain is found at the C-terminus of protein phosphatase 1 regulatory subunits 12A, 12B and 12C. In protein phosphatase 1 regulatory subunit 12A it has been found to bind to cGMP-dependent protein kinase 1 via a leucine zipper motif located at the C-terminus of this domain.


Pssm-ID: 464927 [Multi-domain]  Cd Length: 102  Bit Score: 153.23  E-value: 8.33e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584775672 707 DYKKLYESALTENQKLKTKLQEAQLELADIKAKLEKMAQQKQEKTSDRSSVLEVEKRERRALERKMSEMEEEMKVLTELK 786
Cdd:pfam15898   1 DYKKLYEEELQENERLKRKLQDAQQELAELKSQLERLTQQRQESFSDRSSLLETEKREKRALERKISEMEEELKVLEDLR 80

                          90       100
                  ....*....|....*....|..
gi 1584775672 787 SDNQRLKDENGALIRVISKLSK 808
Cdd:pfam15898  81 AENQRLKDENGALIRVISKLSK 102
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
45-137 1.54e-18

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 86.93  E-value: 1.54e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584775672  45 QARSGATALHVAAAKGYSEVLRLLIQAGYELNVQDHDGWTPLHAAAHWGVKEACSILAEALCDMDIRNKLGQTPFDVA-D 123
Cdd:COG0666   149 QDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAaE 228

                          90
                  ....*....|....
gi 1584775672 124 EGLVEHLEMLQKKQ 137
Cdd:COG0666   229 NGNLEIVKLLLEAG 242
IPD_PPP1R12C cd21945
inhibitory phosphorylation domain of protein phosphatase 1 regulatory subunit 12C (PPP1R12C); ...
 442-494 2.58e-17

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: 76.28  E-value: 2.58e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1584775672 442 EAREKRRSYLTPVRDEEAESLRKARSRQARQTRRSTQGVTLTDLQEAEKTFSR 494
Cdd:cd21945     2 DSRDRRRSYQTPVRDEESESQRKARSRLMRQSRRSTQGVTLTDLKEAEKSIGK 54
IPD_MYPT1 cd21944
inhibitory phosphorylation domain of myosin phosphatase targeting subunit 1(MYPT1); MYPT1, ...
 440-495 2.96e-17

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: 76.48  E-value: 2.96e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1584775672 440 SVEAREKRRSYLTPVRDEEAESLRKARSRQARQTRRSTQGVTLTDLQEAEKTFSRS 495
Cdd:cd21944     2 TSEVRERRRSYLTPVRDEESESQRKARSRQARQSRRSTQGVTLTDLQEAEKTIGRS 57
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
45-133 7.82e-17

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 81.92  E-value: 7.82e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584775672  45 QARSGATALHVAAAKGYSEVLRLLIQAGYELNVQDHDGWTPLHAAAHWGVKEACSILAEALCDMDIRNKLGQTPFDVA-D 123
Cdd:COG0666   116 RDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAaE 195

                          90
                  ....*....|
gi 1584775672 124 EGLVEHLEML 133
Cdd:COG0666   196 NGHLEIVKLL 205
IPD_PPP1R12 cd21930
inhibitory phosphorylation domain of protein phosphatase 1 regulatory subunit 12 (PPP1R12) ...
 444-490 1.62e-16

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: 73.92  E-value: 1.62e-16
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1584775672 444 REKRRSYLTPVRDEEAESLRKARSRQARQTRRSTQGVTLTDLQEAEK 490
Cdd:cd21930     1 RSRRRSYLPPVRDEESETQRKARAKRARQTRRSTQGVTLEDLEEAEK 47
IPD_MYPT2 cd21946
inhibitory phosphorylation domain of myosin phosphatase targeting subunit 2 (MYPT2); MYPT2, ...
 444-496 8.81e-16

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: 72.00  E-value: 8.81e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1584775672 444 REKRRSYLTPVRDEEAESLRKARSRQARQTRRSTQGVTLTDLQEAEKTFSRSR 496
Cdd:cd21946     1 REKRRSYLTPVRDEEAESLRKARSRQARQTRRSTQGVTLTDLQEAERTFSRSR 53
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
30-133 1.12e-15

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 78.46  E-value: 1.12e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584775672  30 DARQWLNSGRIEDVRQARSGATALHVAAAKGYSEVLRLLIQAGYELNVQDHDGWTPLHAAAHWGVKEACSILAEALCDMD 109
Cdd:COG0666    68 LVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVN 147

                          90       100
                  ....*....|....*....|....*
gi 1584775672 110 IRNKLGQTPFDVA-DEGLVEHLEML 133
Cdd:COG0666   148 AQDNDGNTPLHLAaANGNLEIVKLL 172
Ank_2 pfam12796
Ankyrin repeats (3 copies);
53-133 2.08e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.07  E-value: 2.08e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584775672  53 LHVAAAKGYSEVLRLLIQAGYELNVQDHDGWTPLHAAAHWGVKEACSILAEaLCDMDIRNKlGQTPFDVA-DEGLVEHLE 131
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYAaRSGHLEIVK 78


                  ..
gi 1584775672 132 ML 133
Cdd:pfam12796  79 LL 80
IPD_PPP1R12A-like cd22527
inhibitory phosphorylation domain of protein phosphatase 1 regulatory subunit 12A-like, and ...
 442-491 2.20e-12

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: 62.20  E-value: 2.20e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1584775672 442 EAREKRRSYLTPVRDEEAESLRKARSRQARQTRRSTQGVTLTDLQEAEKT 491
Cdd:cd22527     1 ETKERRRSYLTPVRDEEAEAQRKARSRHARQSRRSTQGVTLTDLKEAEKT 50
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
45-122 4.86e-12

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 67.67  E-value: 4.86e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1584775672  45 QARSGATALHVAAAKGYSEVLRLLIQAGYELNVQDHDGWTPLHAAAHWGVKEACSILAEALCDMDIRNKLGQTPFDVA 122
Cdd:COG0666   182 RDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLA 259
Ank_4 pfam13637
Ankyrin repeats (many copies);
51-101 5.03e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 58.44  E-value: 5.03e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1584775672  51 TALHVAAAKGYSEVLRLLIQAGYELNVQDHDGWTPLHAAAHWGVKEACSIL 101
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
Ank_2 pfam12796
Ankyrin repeats (3 copies);
49-112 5.24e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 59.74  E-value: 5.24e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1584775672  49 GATALHVAAAKGYSEVLRLLIQAGyELNVQDHdGWTPLHAAAHWGVKEACSILAEALCDMDIRN 112
Cdd:pfam12796  30 GRTALHLAAKNGHLEIVKLLLEHA-DVNLKDN-GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
Ank_5 pfam13857
Ankyrin repeats (many copies);
35-89 1.54e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.50  E-value: 1.54e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1584775672  35 LNSGRIEDVRQARSGATALHVAAAKGYSEVLRLLIQAGYELNVQDHDGWTPLHAA 89
Cdd:pfam13857   2 LEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
35-134 8.75e-07

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 51.49  E-value: 8.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584775672  35 LNSGRIEDVRQARSGATALHVAAAKGYSEVLRLLIQAGYELNVQDHDGWTPLHAAAHWGVKEACSILAEALCDMDIRNKL 114
Cdd:COG0666    40 LLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKD 119

                          90       100
                  ....*....|....*....|
gi 1584775672 115 GQTPFDVADEGlvEHLEMLQ 134
Cdd:COG0666   120 GETPLHLAAYN--GNLEIVK 137
Ank_2 pfam12796
Ankyrin repeats (3 copies);
42-79 1.83e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 43.95  E-value: 1.83e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1584775672  42 DVRQARSGATALHVAAAKGYSEVLRLLIQAGYELNVQD 79
Cdd:pfam12796  54 DVNLKDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 57-124 3.76e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.20  E-value: 3.76e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1584775672  57 AAKGYSEVLRLLIQAGYELNVQDHDGWTPLHAAAHWGVKEACSILAEALCDMDIRNKLGQTPFDVADE 124
Cdd:PTZ00322   90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEE 157
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 2-122 6.71e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 46.41  E-value: 6.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584775672   2 KDLLLEQVKK-QGVDLEQSRKEEEQQMLQDA--RQWLNSGRIEDVRQARSGATALHVAAAKGYSEVLRLLIQAGYELNVQ 78
Cdd:PHA02878  118 KIILTNRYKNiQTIDLVYIDKKSKDDIIEAEitKLLLSYGADINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIP 197

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1584775672  79 DHDGWTPLHAAAHWGVKEACSILAEALCDMDIRNKLGQTPFDVA 122
Cdd:PHA02878  198 DKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHIS 241
Ank_4 pfam13637
Ankyrin repeats (many copies);
82-134 7.40e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.11  E-value: 7.40e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1584775672  82 GWTPLHAAAHWGVKEACSILAEALCDMDIRNKLGQTPFDVADEGlvEHLEMLQ 134
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASN--GNVEVLK 51
PHA03095 PHA03095
ankyrin-like protein; Provisional
 47-122 9.11e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 45.79  E-value: 9.11e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1584775672  47 RSGATALHVAAAKGYSE--VLRLLIQAGYELNVQDHDGWTPLHAAAHWGVKEACSILAEALCDMDIRNKLGQTPFDVA 122
Cdd:PHA03095  220 MLGNTPLHSMATGSSCKrsLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLM 297
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 49-80 9.19e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 40.35  E-value: 9.19e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1584775672  49 GATALHVAAAK-GYSEVLRLLIQAGYELNVQDH 80
Cdd:pfam00023   2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 47-136 2.07e-04

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 42.56  E-value: 2.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584775672  47 RSGATALHVAAAKGYS---EVLRLLIQAGYELNVQDH-DGWTPLHAAAHWGVKEacsiLAEALC-----DMDIRNKLGQT 117
Cdd:PHA02736   53 RHGKQCVHIVSNPDKAdpqEKLKLLMEWGADINGKERvFGNTPLHIAVYTQNYE----LATWLCnqpgvNMEILNYAFKT 128

                          90       100
                  ....*....|....*....|
gi 1584775672 118 PFDVA-DEGLVEHLEMLQKK 136
Cdd:PHA02736  129 PYYVAcERHDAKMMNILRAK 148
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
718-808 3.09e-04

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 44.46  E-value: 3.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584775672 718 ENQKLKTKLQEAQLELADIKAKLEKM-AQQKQEKTSDRssvlEVEKRERR--ALERKMSEMEEEMKvltELKSDNQRLKD 794
Cdd:COG2433   428 EVEELEAELEEKDERIERLERELSEArSEERREIRKDR----EISRLDREieRLERELEEERERIE---ELKRKLERLKE 500

                          90       100
                  ....*....|....*....|.
gi 1584775672 795 -------ENGALIRVISKLSK 808
Cdd:COG2433   501 lwklehsGELVPVKVVEKFTK 521
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 40-122 3.90e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 43.80  E-value: 3.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584775672  40 IEDVrqarSGATALHVAAAKGYSEVLRLLIQAGYELNVQDHDGWTPLHAAAHWGVKEACSILAEALCDMDIRNKLGQTPF 119
Cdd:PHA02874  152 IEDD----NGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPL 227


                  ...
gi 1584775672 120 DVA 122
Cdd:PHA02874  228 HNA 230
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 49-77 8.28e-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: 37.18  E-value: 8.28e-04
                           10        20
                   ....*....|....*....|....*....
gi 1584775672   49 GATALHVAAAKGYSEVLRLLIQAGYELNV 77
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 45-122 9.41e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 42.64  E-value: 9.41e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1584775672  45 QARSGATALHVAAAKGYSeVLRLLIQaGYELNVQDHDGWTPLHAAAHWGV-KEACSILAEALCDMDIRNKLGQTPFDVA 122
Cdd:PHA02874  219 KCKNGFTPLHNAIIHNRS-AIELLIN-NASINDQDIDGSTPLHHAINPPCdIDIIDILLYHKADISIKDNKGENPIDTA 295
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 35-124 1.27e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 42.26  E-value: 1.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584775672  35 LNSGRIEDVRQARSgATALHVAAAKGYSEVLRLLIQAGYELNVQDHDGWTPLHAAAHWGVKEACSILAEALCDMDIRNKL 114
Cdd:PHA02874  111 LDCGIDVNIKDAEL-KTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNN 189

                          90
                  ....*....|
gi 1584775672 115 GQTPFDVADE 124
Cdd:PHA02874  190 GESPLHNAAE 199
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 53-137 2.25e-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: 41.54  E-value: 2.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584775672  53 LHVAAAKGYSEVLRLLIQAGYELNVQDHDGWTPLHAAAHWGVKE-ACSILaEALCDMD----------IRNKLGQTPFDV 121
Cdd:cd22192   140 LSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPNKTfACQMY-DLILSYDkeddlqpldlVPNNQGLTPFKL 218

                          90
                  ....*....|....*..
gi 1584775672 122 A-DEGLVEHLEMLQKKQ 137
Cdd:cd22192   219 AaKEGNIVMFQHLVQKR 235
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
45-117 2.53e-03

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 40.71  E-value: 2.53e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1584775672  45 QARSGATALHVAAAKGYSEVLRLLIQAGYELNVQDHDGWTPLHAAAHWGVKEACSILAEALCDMDIRNKLGQT 117
Cdd:COG0666   215 KDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 1-89 2.68e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 41.39  E-value: 2.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584775672   1 MKDLLLEQVKKQGV---DLEQSRKEEEQQMLQDARQWL-----NSGRIEDVRQAR--------SGATALHVAAAKGYSEV 64
Cdd:PLN03192  494 LKNFLQHHKELHDLnvgDLLGDNGGEHDDPNMASNLLTvastgNAALLEELLKAKldpdigdsKGRTPLHIAASKGYEDC 573

                          90       100
                  ....*....|....*....|....*
gi 1584775672  65 LRLLIQAGYELNVQDHDGWTPLHAA 89
Cdd:PLN03192  574 VLVLLKHACNVHIRDANGNTALWNA 598
PHA03095 PHA03095
ankyrin-like protein; Provisional
 47-121 3.32e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 40.78  E-value: 3.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584775672  47 RSGATALHVAAAKGYSE-VLRLLIQAGYELNVQDHDGWTPLHA-----AAHWGVKEacsILAEALCDMDIRNKLGQTPFD 120
Cdd:PHA03095   81 RCGFTPLHLYLYNATTLdVIKLLIKAGADVNAKDKVGRTPLHVylsgfNINPKVIR---LLLRKGADVNALDLYGMTPLA 157


                  .
gi 1584775672 121 V 121
Cdd:PHA03095  158 V 158
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 81-113 3.64e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 35.73  E-value: 3.64e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1584775672  81 DGWTPLHAAA-HWGVKEACSILAEALCDMDIRNK 113
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 18-117 3.67e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 41.01  E-value: 3.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584775672  18 QSRKEEEQQMLQDARQW---LNSGRIEDVRQARSG-------ATALHVAAAKGYSEVLRLLIQAGYELNVQDHDGWTPLH 87
Cdd:PLN03192  484 QTRQEDNVVILKNFLQHhkeLHDLNVGDLLGDNGGehddpnmASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLH 563

                          90       100       110
                  ....*....|....*....|....*....|
gi 1584775672  88 AAAHWGVKEACSILAEALCDMDIRNKLGQT 117
Cdd:PLN03192  564 IAASKGYEDCVLVLLKHACNVHIRDANGNT 593
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 49-77 4.24e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 35.31  E-value: 4.24e-03
                          10        20
                  ....*....|....*....|....*....
gi 1584775672  49 GATALHVAAAKGYSEVLRLLIQAGYELNV 77
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
PRK12704 PRK12704
phosphodiesterase; Provisional
 702-808 5.50e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.15  E-value: 5.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584775672 702 EDSNRDYKKLYESALTE-NQKLKTKLQEAQLELADIKAKL---EKMAQQKQEKTSDRSSVLevEKRERRaLERKMSEMEE 777
Cdd:PRK12704   45 EEAKKEAEAIKKEALLEaKEEIHKLRNEFEKELRERRNELqklEKRLLQKEENLDRKLELL--EKREEE-LEKKEKELEQ 121

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1584775672 778 EMKVLTELKSDNQRLKDENGALIRVISKLSK 808
Cdd:PRK12704  122 KQQELEKKEEELEELIEEQLQELERISGLTA 152
 
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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