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Conserved domains on  [gi|14149716|ref|NP_060077|]
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protein phosphatase 1 regulatory subunit 12C isoform a [Homo sapiens]

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 ...
 683-782 2.14e-40

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: 143.60  E-value: 2.14e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716   683 FRTLYAELRRENERLREALTETTLRLAQLKVELERAT-QRQERFAERPALLELERFERRALERKAAELEEELKALSDLRA 761
Cdd:pfam15898   2 YKKLYEEELQENERLKRKLQDAQQELAELKSQLERLTqQRQESFSDRSSLLETEKREKRALERKISEMEEELKVLEDLRA 81

                          90       100
                  ....*....|....*....|.
gi 14149716   762 DNQRLKDENAALIRVISKLSK 782
Cdd:pfam15898  82 ENQRLKDENGALIRVISKLSK 102
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
52-322 3.11e-40

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 150.10  E-value: 3.11e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716  52 AAEFLAACAGGDLDEARLMLRAADPGPGAELDPAAPPPARAVLDSTNADGISALHQACIDENLEVVRFLVEQGATVNQAD 131
Cdd:COG0666  38 LLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARD 117

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716 132 NEGWTPLHVAASCGYLDIARYLLSHGANIAAVNSDGDLPLDLAesdamegllkaeiARRGvDVEAAKraeeeLLlhdtrc 211
Cdd:COG0666 118 KDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA-------------AANG-NLEIVK-----LL------ 172

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716 212 wLNGGAMPEARHPRtGASALHVAAAKGYIEVMRLLLQAGYDPELRDGDGWTPLHAAAHWGVEDACRLLAEHGGGMDSLTH 291
Cdd:COG0666 173 -LEAGADVNARDND-GETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDK 250

                       250       260       270
                ....*....|....*....|....*....|.
gi 14149716 292 AGQRPCDLADEEVLSLLEELARKQEDLRNQK 322
Cdd:COG0666 251 DGLTALLLAAAAGAALIVKLLLLALLLLAAA 281
IPD_PPP1R12C cd21945
inhibitory phosphorylation domain of protein phosphatase 1 regulatory subunit 12C (PPP1R12C); ...
 524-577 1.83e-27

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: 105.17  E-value: 1.83e-27
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 14149716 524 ADSRDRRRSYQMPVRDEESESQRKARSRLMRQSRRSTQGVTLTDLKEAEKAAGK 577
Cdd:cd21945   1 TDSRDRRRSYQTPVRDEESESQRKARSRLMRQSRRSTQGVTLTDLKEAEKSIGK 54
PTZ00449 super family cl33186
104 kDa microneme/rhoptry antigen; Provisional
 371-619 2.94e-07

104 kDa microneme/rhoptry antigen; Provisional


The actual alignment was detected with superfamily member PTZ00449:

Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 54.31  E-value: 2.94e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716  371 PPIQDED-EGEEGPTEPPPAE--PRTLNGVSSPPHPSPKSPVQLEEAPFSRRFGLLKTGSSGAL-GPPERRTAEGAP--- 443
Cdd:PTZ00449 497 APIEEEDsDKHDEPPEGPEASglPPKAPGDKEGEEGEHEDSKESDEPKEGGKPGETKEGEVGKKpGPAKEHKPSKIPtls 576

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716  444 --GAGLQRSASSSWLEGTSTQAKELRLARITPTPSPKLPEpsvLSEVTKPPPCLENSSPPSRIPEPESPAKPNVPTASTA 521
Cdd:PTZ00449 577 kkPEFPKDPKHPKDPEEPKKPKRPRSAQRPTRPKSPKLPE---LLDIPKSPKRPESPKSPKRPPPPQRPSSPERPEGPKI 653

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716  522 PPADsrdrrRSYQMPVRDEESESQRKARSRLMRQSRRSTQGVTLTDLKEAEKAAGKAPESEKPAQSLD-----PSRRPRV 596
Cdd:PTZ00449 654 IKSP-----KPPKSPKPPFDPKFKEKFYDDYLDAAAKSKETKTTVVLDESFESILKETLPETPGTPFTtprplPPKLPRD 728

                        250       260
                 ....*....|....*....|...
gi 14149716  597 PgvensDSPAQRAEAPDGQGPGP 619
Cdd:PTZ00449 729 E-----EFPFEPIGDPDAEQPDD 746
 
Name Accession Description Interval E-value
PRKG1_interact pfam15898
cGMP-dependent protein kinase interacting domain; This domain is found at the C-terminus of ...
 683-782 2.14e-40

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: 143.60  E-value: 2.14e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716   683 FRTLYAELRRENERLREALTETTLRLAQLKVELERAT-QRQERFAERPALLELERFERRALERKAAELEEELKALSDLRA 761
Cdd:pfam15898   2 YKKLYEEELQENERLKRKLQDAQQELAELKSQLERLTqQRQESFSDRSSLLETEKREKRALERKISEMEEELKVLEDLRA 81

                          90       100
                  ....*....|....*....|.
gi 14149716   762 DNQRLKDENAALIRVISKLSK 782
Cdd:pfam15898  82 ENQRLKDENGALIRVISKLSK 102
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
52-322 3.11e-40

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 150.10  E-value: 3.11e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716  52 AAEFLAACAGGDLDEARLMLRAADPGPGAELDPAAPPPARAVLDSTNADGISALHQACIDENLEVVRFLVEQGATVNQAD 131
Cdd:COG0666  38 LLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARD 117

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716 132 NEGWTPLHVAASCGYLDIARYLLSHGANIAAVNSDGDLPLDLAesdamegllkaeiARRGvDVEAAKraeeeLLlhdtrc 211
Cdd:COG0666 118 KDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA-------------AANG-NLEIVK-----LL------ 172

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716 212 wLNGGAMPEARHPRtGASALHVAAAKGYIEVMRLLLQAGYDPELRDGDGWTPLHAAAHWGVEDACRLLAEHGGGMDSLTH 291
Cdd:COG0666 173 -LEAGADVNARDND-GETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDK 250

                       250       260       270
                ....*....|....*....|....*....|.
gi 14149716 292 AGQRPCDLADEEVLSLLEELARKQEDLRNQK 322
Cdd:COG0666 251 DGLTALLLAAAAGAALIVKLLLLALLLLAAA 281
IPD_PPP1R12C cd21945
inhibitory phosphorylation domain of protein phosphatase 1 regulatory subunit 12C (PPP1R12C); ...
 524-577 1.83e-27

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: 105.17  E-value: 1.83e-27
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 14149716 524 ADSRDRRRSYQMPVRDEESESQRKARSRLMRQSRRSTQGVTLTDLKEAEKAAGK 577
Cdd:cd21945   1 TDSRDRRRSYQTPVRDEESESQRKARSRLMRQSRRSTQGVTLTDLKEAEKSIGK 54
Ank_2 pfam12796
Ankyrin repeats (3 copies);
95-160 1.36e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 78.23  E-value: 1.36e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 14149716    95 DSTNADGISALHQACIDENLEVVRFLVEQGATvnQADNEGWTPLHVAASCGYLDIARYLLSHGANI 160
Cdd:pfam12796  24 NLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVKLLLEKGADI 87
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 110-268 8.04e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 80.48  E-value: 8.04e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716  110 IDENLEVVRFLVEQGATVNQADNEGWTPLHVAASC--GYLDIARYLLSHGANIAAVNSDGDLPLDLA------ESDAMEG 181
Cdd:PHA03100  82 LTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYlesnkiDLKILKL 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716  182 LLKaeiarRGVDVEAAKRAEeelllhdtrCWLNGGAMPEARHPRtGASALHVAAAKGYIEVMRLLLQAGYDPELRDGDGW 261
Cdd:PHA03100 162 LID-----KGVDINAKNRVN---------YLLSYGVPINIKDVY-GFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGD 226


                 ....*..
gi 14149716  262 TPLHAAA 268
Cdd:PHA03100 227 TPLHIAI 233
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 101-282 1.16e-07

Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 55.27  E-value: 1.16e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716 101 GISALHQACIDENLEVVRFLVEQGATVNQADNE-------------GWTPLHVAASCGYLDIARYLLSHGANIAAVNSDg 167
Cdd:cd21882  73 GQTALHIAIENRNLNLVRLLVENGADVSARATGrffrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGAQPAALEAQ- 151

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716 168 dlplDLAESDAMEGLLkaEIARRGVDVEA-AKRAEEELLLHDTRcwLNGGAMPEARHPRTGASALHVAAAKGYIEVMRLL 246
Cdd:cd21882 152 ----DSLGNTVLHALV--LQADNTPENSAfVCQMYNLLLSYGAH--LDPTQQLEEIPNHQGLTPLKLAAVEGKIVMFQHI 223

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 14149716 247 LQ----AGYDPELRDGDGWT--PLHAAAH-------WGVEDACRLLAEH 282
Cdd:cd21882 224 LQrefsGPYQPLSRKFTEWTygPVTSSLYdlseidsWEKNSVLELIAFS 272
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 371-619 2.94e-07

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 54.31  E-value: 2.94e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716  371 PPIQDED-EGEEGPTEPPPAE--PRTLNGVSSPPHPSPKSPVQLEEAPFSRRFGLLKTGSSGAL-GPPERRTAEGAP--- 443
Cdd:PTZ00449 497 APIEEEDsDKHDEPPEGPEASglPPKAPGDKEGEEGEHEDSKESDEPKEGGKPGETKEGEVGKKpGPAKEHKPSKIPtls 576

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716  444 --GAGLQRSASSSWLEGTSTQAKELRLARITPTPSPKLPEpsvLSEVTKPPPCLENSSPPSRIPEPESPAKPNVPTASTA 521
Cdd:PTZ00449 577 kkPEFPKDPKHPKDPEEPKKPKRPRSAQRPTRPKSPKLPE---LLDIPKSPKRPESPKSPKRPPPPQRPSSPERPEGPKI 653

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716  522 PPADsrdrrRSYQMPVRDEESESQRKARSRLMRQSRRSTQGVTLTDLKEAEKAAGKAPESEKPAQSLD-----PSRRPRV 596
Cdd:PTZ00449 654 IKSP-----KPPKSPKPPFDPKFKEKFYDDYLDAAAKSKETKTTVVLDESFESILKETLPETPGTPFTtprplPPKLPRD 728

                        250       260
                 ....*....|....*....|...
gi 14149716  597 PgvensDSPAQRAEAPDGQGPGP 619
Cdd:PTZ00449 729 E-----EFPFEPIGDPDAEQPDD 746
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 133-160 3.56e-07

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: 46.81  E-value: 3.56e-07
                           10        20
                   ....*....|....*....|....*...
gi 14149716    133 EGWTPLHVAASCGYLDIARYLLSHGANI 160
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 101-270 1.50e-06

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 51.62  E-value: 1.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716   101 GISALHQACIDENLEVVRFLVEQGATVNQADN--------------EGWTPLHVAASCGYLDIARYLLSHGANIAAVNSD 166
Cdd:TIGR00870 128 GITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsfyHGESPLNAAACLGSPSIVALLSEDPADILTADSL 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716   167 GDlplDLAESDAMEGLLKAEiarrgvDVEAAKRAEEELLLHDTRCwlnggampeaRHPRT--------GASALHVAAAKG 238
Cdd:TIGR00870 208 GN---TLLHLLVMENEFKAE------YEELSCQMYNFALSLLDKL----------RDSKElevilnhqGLTPLKLAAKEG 268

                         170       180       190
                  ....*....|....*....|....*....|....
gi 14149716   239 YIEVMRLLLQAGYdpELRDGDGWT--PLHAAAHW 270
Cdd:TIGR00870 269 RIVLFRLKLAIKY--KQKKFVAWPngQQLLSLYW 300
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
688-782 1.56e-04

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 45.23  E-value: 1.56e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716 688 AELRRENERLREALTETTLRLAQLKVELERATQRQERFAERPAllELERFERR--ALERkaaELEEELKALSDLRADNQR 765
Cdd:COG2433 423 ERLEAEVEELEAELEEKDERIERLERELSEARSEERREIRKDR--EISRLDREieRLER---ELEEERERIEELKRKLER 497

                        90       100
                ....*....|....*....|....
gi 14149716 766 LKD-------ENAALIRVISKLSK 782
Cdd:COG2433 498 LKElwklehsGELVPVKVVEKFTK 521
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 636-782 6.83e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.51  E-value: 6.83e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716    636 AEGEEAEPADRSQESSTLEGGPSARRQRWQRDLNPEPEPESEepdggFRTLYAELRRENERLREALTETTLRLAQL---- 711
Cdd:TIGR02168  759 LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKA-----LREALDELRAELTLLNEEAANLRERLESLerri 833

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 14149716    712 ---KVELERATQRQERFAERPALLELERFErraLERKAAELEEELKALSDLRADNQR----LKDENAALIRVISKLSK 782
Cdd:TIGR02168  834 aatERRLEDLEEQIEELSEDIESLAAEIEE---LEELIEELESELEALLNERASLEEalalLRSELEELSEELRELES 908
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
 695-772 8.56e-03

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 39.55  E-value: 8.56e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 14149716   695 ERLREALTETTLRLAQLKVELERATQRQERFAERpalLELERFERRALERKAAELEEELKAlsdLRADNQRLKDENAA 772
Cdd:PRK11448  138 EDPENLLHALQQEVLTLKQQLELQAREKAQSQAL---AEAQQQELVALEGLAAELEEKQQE---LEAQLEQLQEKAAE 209
 
Name Accession Description Interval E-value
PRKG1_interact pfam15898
cGMP-dependent protein kinase interacting domain; This domain is found at the C-terminus of ...
 683-782 2.14e-40

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: 143.60  E-value: 2.14e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716   683 FRTLYAELRRENERLREALTETTLRLAQLKVELERAT-QRQERFAERPALLELERFERRALERKAAELEEELKALSDLRA 761
Cdd:pfam15898   2 YKKLYEEELQENERLKRKLQDAQQELAELKSQLERLTqQRQESFSDRSSLLETEKREKRALERKISEMEEELKVLEDLRA 81

                          90       100
                  ....*....|....*....|.
gi 14149716   762 DNQRLKDENAALIRVISKLSK 782
Cdd:pfam15898  82 ENQRLKDENGALIRVISKLSK 102
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
52-322 3.11e-40

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 150.10  E-value: 3.11e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716  52 AAEFLAACAGGDLDEARLMLRAADPGPGAELDPAAPPPARAVLDSTNADGISALHQACIDENLEVVRFLVEQGATVNQAD 131
Cdd:COG0666  38 LLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARD 117

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716 132 NEGWTPLHVAASCGYLDIARYLLSHGANIAAVNSDGDLPLDLAesdamegllkaeiARRGvDVEAAKraeeeLLlhdtrc 211
Cdd:COG0666 118 KDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA-------------AANG-NLEIVK-----LL------ 172

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716 212 wLNGGAMPEARHPRtGASALHVAAAKGYIEVMRLLLQAGYDPELRDGDGWTPLHAAAHWGVEDACRLLAEHGGGMDSLTH 291
Cdd:COG0666 173 -LEAGADVNARDND-GETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDK 250

                       250       260       270
                ....*....|....*....|....*....|.
gi 14149716 292 AGQRPCDLADEEVLSLLEELARKQEDLRNQK 322
Cdd:COG0666 251 DGLTALLLAAAAGAALIVKLLLLALLLLAAA 281
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
50-300 9.71e-35

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 134.31  E-value: 9.71e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716  50 ERAAEFLAACAGGDLDEARLMLRAADPGPGAELDPAAPPPARAVLDSTNADGISALHQACIDENLEVVRFLVEQGATVNQ 129
Cdd:COG0666   3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716 130 ADNEGWTPLHVAASCGYLDIARYLLSHGANIAAVNSDGDLPLDLAesdamegllkaeiARRGvDVEAAKraeeeLLlhdt 209
Cdd:COG0666  83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLA-------------AYNG-NLEIVK-----LL---- 139

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716 210 rcwLNGGAMPEARHPRtGASALHVAAAKGYIEVMRLLLQAGYDPELRDGDGWTPLHAAAHWGVEDACRLLAEHGGGMDSL 289
Cdd:COG0666 140 ---LEAGADVNAQDND-GNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAK 215

                       250
                ....*....|.
gi 14149716 290 THAGQRPCDLA 300
Cdd:COG0666 216 DNDGKTALDLA 226
IPD_PPP1R12C cd21945
inhibitory phosphorylation domain of protein phosphatase 1 regulatory subunit 12C (PPP1R12C); ...
 524-577 1.83e-27

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: 105.17  E-value: 1.83e-27
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 14149716 524 ADSRDRRRSYQMPVRDEESESQRKARSRLMRQSRRSTQGVTLTDLKEAEKAAGK 577
Cdd:cd21945   1 TDSRDRRRSYQTPVRDEESESQRKARSRLMRQSRRSTQGVTLTDLKEAEKSIGK 54
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
55-204 1.71e-19

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 89.63  E-value: 1.71e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716  55 FLAACAGGDLDEARLMLRAadpgpGAELDPaappparavldsTNADGISALHQACIDENLEVVRFLVEQGATVNQADNEG 134
Cdd:COG0666 157 LHLAAANGNLEIVKLLLEA-----GADVNA------------RDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDG 219

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716 135 WTPLHVAASCGYLDIARYLLSHGANIAAVNSDGDLPLDLAESDAMEGLLKAEIARRGVDVEAAKRAEEEL 204
Cdd:COG0666 220 KTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
Ank_2 pfam12796
Ankyrin repeats (3 copies);
95-160 1.36e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 78.23  E-value: 1.36e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 14149716    95 DSTNADGISALHQACIDENLEVVRFLVEQGATvnQADNEGWTPLHVAASCGYLDIARYLLSHGANI 160
Cdd:pfam12796  24 NLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVKLLLEKGADI 87
IPD_PPP1R12 cd21930
inhibitory phosphorylation domain of protein phosphatase 1 regulatory subunit 12 (PPP1R12) ...
 527-573 1.59e-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.


Pssm-ID: 412018  Cd Length: 47  Bit Score: 76.61  E-value: 1.59e-17
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 14149716 527 RDRRRSYQMPVRDEESESQRKARSRLMRQSRRSTQGVTLTDLKEAEK 573
Cdd:cd21930   1 RSRRRSYLPPVRDEESETQRKARAKRARQTRRSTQGVTLEDLEEAEK 47
Ank_2 pfam12796
Ankyrin repeats (3 copies);
105-257 2.07e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 77.85  E-value: 2.07e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716   105 LHQACIDENLEVVRFLVEQGATVNQADNEGWTPLHVAASCGYLDIARYLLSHganiAAVNSDGDlpldlaesdamegllk 184
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH----ADVNLKDN---------------- 60

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14149716   185 aeiarrgvdveaakraeeelllhdtrcwlnggampearhprtGASALHVAAAKGYIEVMRLLLQAGYDPELRD 257
Cdd:pfam12796  61 ------------------------------------------GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
IPD_MYPT1 cd21944
inhibitory phosphorylation domain of myosin phosphatase targeting subunit 1(MYPT1); MYPT1, ...
 524-578 2.27e-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: 2.27e-17
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 14149716 524 ADSRDRRRSYQMPVRDEESESQRKARSRLMRQSRRSTQGVTLTDLKEAEKAAGKA 578
Cdd:cd21944   3 SEVRERRRSYLTPVRDEESESQRKARSRQARQSRRSTQGVTLTDLQEAEKTIGRS 57
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 110-268 8.04e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 80.48  E-value: 8.04e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716  110 IDENLEVVRFLVEQGATVNQADNEGWTPLHVAASC--GYLDIARYLLSHGANIAAVNSDGDLPLDLA------ESDAMEG 181
Cdd:PHA03100  82 LTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYlesnkiDLKILKL 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716  182 LLKaeiarRGVDVEAAKRAEeelllhdtrCWLNGGAMPEARHPRtGASALHVAAAKGYIEVMRLLLQAGYDPELRDGDGW 261
Cdd:PHA03100 162 LID-----KGVDINAKNRVN---------YLLSYGVPINIKDVY-GFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGD 226


                 ....*..
gi 14149716  262 TPLHAAA 268
Cdd:PHA03100 227 TPLHIAI 233
PHA03095 PHA03095
ankyrin-like protein; Provisional
 63-300 1.27e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 76.99  E-value: 1.27e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716   63 DLDEARLMLRAadpgpGAELDPAAPPparavldstnadGISALH-QACIDENLEVVRFLVEQGATVNQADNEGWTPLHVa 141
Cdd:PHA03095  62 VKDIVRLLLEA-----GADVNAPERC------------GFTPLHlYLYNATTLDVIKLLIKAGADVNAKDKVGRTPLHV- 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716  142 ascgYL-------DIARYLLSHGANIAAVNSDGDLPLDLaesdamegLLKaeiaRRGVDVEAAKraeeeLLlhdtrcwLN 214
Cdd:PHA03095 124 ----YLsgfninpKVIRLLLRKGADVNALDLYGMTPLAV--------LLK----SRNANVELLR-----LL-------ID 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716  215 GGAMPEARHPRtGASALHVAA--AKGYIEVMRLLLQAGYDPELRDGDGWTPLHAAAHWGvedACRL-----LAEHGGGMD 287
Cdd:PHA03095 176 AGADVYAVDDR-FRSLLHHHLqsFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGS---SCKRslvlpLLIAGISIN 251

                        250
                 ....*....|...
gi 14149716  288 SLTHAGQRPCDLA 300
Cdd:PHA03095 252 ARNRYGQTPLHYA 264
Ank_2 pfam12796
Ankyrin repeats (3 copies);
231-282 3.89e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 68.60  E-value: 3.89e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 14149716   231 LHVAAAKGYIEVMRLLLQAGYDPELRDGDGWTPLHAAAHWGVEDACRLLAEH 282
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH 52
Ank_4 pfam13637
Ankyrin repeats (many copies);
103-154 3.94e-13

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 64.22  E-value: 3.94e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 14149716   103 SALHQACIDENLEVVRFLVEQGATVNQADNEGWTPLHVAASCGYLDIARYLL 154
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
IPD_PPP1R12A-like cd22527
inhibitory phosphorylation domain of protein phosphatase 1 regulatory subunit 12A-like, and ...
 525-573 4.17e-13

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: 64.13  E-value: 4.17e-13
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 14149716 525 DSRDRRRSYQMPVRDEESESQRKARSRLMRQSRRSTQGVTLTDLKEAEK 573
Cdd:cd22527   1 ETKERRRSYLTPVRDEEAEAQRKARSRHARQSRRSTQGVTLTDLKEAEK 49
IPD_MYPT2 cd21946
inhibitory phosphorylation domain of myosin phosphatase targeting subunit 2 (MYPT2); MYPT2, ...
 527-578 6.14e-13

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: 63.91  E-value: 6.14e-13
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 14149716 527 RDRRRSYQMPVRDEESESQRKARSRLMRQSRRSTQGVTLTDLKEAEKAAGKA 578
Cdd:cd21946   1 REKRRSYLTPVRDEEAESLRKARSRQARQTRRSTQGVTLTDLQEAERTFSRS 52
PHA03095 PHA03095
ankyrin-like protein; Provisional
 109-264 5.22e-12

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 68.90  E-value: 5.22e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716  109 CIDENleVVRFLVEQGATVNQADNEGWTPLHV-----AAScgyLDIARYLLSHGANIAAVNSDGDLPLD-LAES-DAMEG 181
Cdd:PHA03095 129 NINPK--VIRLLLRKGADVNALDLYGMTPLAVllksrNAN---VELLRLLIDAGADVYAVDDRFRSLLHhHLQSfKPRAR 203

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716  182 LLKaEIARRGVDVeAAKRAEEELLLHD----TRCW-------LNGGAMPEARHpRTGASALHVAAAKGYIEVMRLLLQAG 250
Cdd:PHA03095 204 IVR-ELIRAGCDP-AATDMLGNTPLHSmatgSSCKrslvlplLIAGISINARN-RYGQTPLHYAAVFNNPRACRRLIALG 280

                        170
                 ....*....|....
gi 14149716  251 YDPELRDGDGWTPL 264
Cdd:PHA03095 281 ADINAVSSDGNTPL 294
PHA03095 PHA03095
ankyrin-like protein; Provisional
 114-266 1.79e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 66.97  E-value: 1.79e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716  114 LEVVRFLVEQGATVNQADNEGWTPLHVAASCG---YLDIARYLLSHGANIAAVNSDGDLPLDL-AESDAMEGLLKAEIaR 189
Cdd:PHA03095  27 VEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSsekVKDIVRLLLEAGADVNAPERCGFTPLHLyLYNATTLDVIKLLI-K 105

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14149716  190 RGVDVEAAKRAeeelllhdtrcwlnggampearhprtGASALHVAAAKGYI--EVMRLLLQAGYDPELRDGDGWTPLHA 266
Cdd:PHA03095 106 AGADVNAKDKV--------------------------GRTPLHVYLSGFNInpKVIRLLLRKGADVNALDLYGMTPLAV 158
Ank_4 pfam13637
Ankyrin repeats (many copies);
229-279 2.63e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 59.21  E-value: 2.63e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 14149716   229 SALHVAAAKGYIEVMRLLLQAGYDPELRDGDGWTPLHAAAHWGVEDACRLL 279
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 94-174 4.63e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 65.46  E-value: 4.63e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716   94 LDSTNADGISALHQA--CIDENLEVVRFLVEQGATVNQ----------------ADNEGWTPLHVAASCGYLDIARYLLS 155
Cdd:PHA03100 134 VNIKNSDGENLLHLYleSNKIDLKILKLLIDKGVDINAknrvnyllsygvpiniKDVYGFTPLHYAVYNNNPEFVKYLLD 213

                         90
                 ....*....|....*....
gi 14149716  156 HGANIAAVNSDGDLPLDLA 174
Cdd:PHA03100 214 LGANPNLVNKYGDTPLHIA 232
Ank_5 pfam13857
Ankyrin repeats (many copies);
120-174 2.01e-10

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 56.59  E-value: 2.01e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 14149716   120 LVEQG-ATVNQADNEGWTPLHVAASCGYLDIARYLLSHGANIAAVNSDGDLPLDLA 174
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 94-165 5.16e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 59.29  E-value: 5.16e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14149716   94 LDSTNADGISALHQACIDENLEVVRFLVEQGATVNQADNEGWTPLHVAASCGYLDIARYLLSHGANIAAVNS 165
Cdd:PHA03100 185 INIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIE 256
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 120-287 7.01e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 59.50  E-value: 7.01e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716  120 LVEQGATVNQADNEGWTPLHVAASCGYLDIARYLLSHGANIAAVNSDGDLPLdlaesdamegllkaeiarrgVDVEAAKR 199
Cdd:PLN03192 544 LLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTAL--------------------WNAISAKH 603

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716  200 AEEELLLHDtrcwlnggaMPEARHPRTGASALHVAAAKGYIEVMRLLLQAGYDPELRDGDGWTPLHAAAHWGVEDACRLL 279
Cdd:PLN03192 604 HKIFRILYH---------FASISDPHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLL 674


                 ....*...
gi 14149716  280 AEHGGGMD 287
Cdd:PLN03192 675 IMNGADVD 682
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 115-300 1.27e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 57.97  E-value: 1.27e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716  115 EVVRFLVEQGATVNQAD-NEGWTPLHVAASCGYLDIARYLLSHGANIAAVNSDGDLPLDLAESDAMEGLLKAeiarrgvd 193
Cdd:PHA02878 148 EITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHI-------- 219

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716  194 veaakraeeelllhdtrcWLNGGAMPEARHpRTGASALHVAAakGY---IEVMRLLLQAGYDPELRDG-DGWTPLHAAAH 269
Cdd:PHA02878 220 ------------------LLENGASTDARD-KCGNTPLHISV--GYckdYDILKLLLEHGVDVNAKSYiLGLTALHSSIK 278

                        170       180       190
                 ....*....|....*....|....*....|.
gi 14149716  270 wgVEDACRLLAEHGGGMDSLTHAGQRPCDLA 300
Cdd:PHA02878 279 --SERKLKLLLEYGADINSLNSYKLTPLSSA 307
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 101-282 2.17e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 57.20  E-value: 2.17e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716  101 GISALHQACIDENLEVVRFLVEQGATVNQADNEGWTPLHVAASCGYLDIARYLLSHGANIAAVNSDGDLPLDLAESdame 180
Cdd:PHA02878 168 GNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVG---- 243

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716  181 gllkaeiarRGVDVEAAKRaeeeLLLHdtrcwlngGAMPEARHPRTGASALHVAAAKGyiEVMRLLLQAGYDPELRDGDG 260
Cdd:PHA02878 244 ---------YCKDYDILKL----LLEH--------GVDVNAKSYILGLTALHSSIKSE--RKLKLLLEYGADINSLNSYK 300

                        170       180
                 ....*....|....*....|....
gi 14149716  261 WTPLHAAA--HWGVEdACRLLAEH 282
Cdd:PHA02878 301 LTPLSSAVkqYLCIN-IGRILISN 323
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 99-296 2.35e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 57.20  E-value: 2.35e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716   99 ADGISA-----LHQACIDENLEVVRFLVEQGATVNQADNEGWTPLHVAASCGYLDIARYLlshganIAAVNSDGDLPLDL 173
Cdd:PHA02878  30 STSASLipfipLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEM------IRSINKCSVFYTLV 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716  174 AESDAMEG---------LLKAEIARRGVD-VEAAKRAEEELLLHD-TRCWLNGGAMPEARHPRTGASALHVAAAKGYIEV 242
Cdd:PHA02878 104 AIKDAFNNrnveifkiiLTNRYKNIQTIDlVYIDKKSKDDIIEAEiTKLLLSYGADINMKDRHKGNTALHYATENKDQRL 183

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 14149716  243 MRLLLQAGYDPELRDGDGWTPLHAAAHWGVEDACRLLAEHGGGMDSLTHAGQRP 296
Cdd:PHA02878 184 TELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTP 237
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 117-175 4.47e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.83  E-value: 4.47e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 14149716  117 VRFLVEQGATVNQADNEGWTPLHVAASCGYLDIARYLLSHGANIAAVNSDGDLPLDLAE 175
Cdd:PTZ00322  98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAE 156
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 133-164 5.02e-08

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: 49.21  E-value: 5.02e-08
                          10        20        30
                  ....*....|....*....|....*....|...
gi 14149716   133 EGWTPLHVAA-SCGYLDIARYLLSHGANIAAVN 164
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 101-282 1.16e-07

Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 55.27  E-value: 1.16e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716 101 GISALHQACIDENLEVVRFLVEQGATVNQADNE-------------GWTPLHVAASCGYLDIARYLLSHGANIAAVNSDg 167
Cdd:cd21882  73 GQTALHIAIENRNLNLVRLLVENGADVSARATGrffrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGAQPAALEAQ- 151

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716 168 dlplDLAESDAMEGLLkaEIARRGVDVEA-AKRAEEELLLHDTRcwLNGGAMPEARHPRTGASALHVAAAKGYIEVMRLL 246
Cdd:cd21882 152 ----DSLGNTVLHALV--LQADNTPENSAfVCQMYNLLLSYGAH--LDPTQQLEEIPNHQGLTPLKLAAVEGKIVMFQHI 223

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 14149716 247 LQ----AGYDPELRDGDGWT--PLHAAAH-------WGVEDACRLLAEH 282
Cdd:cd21882 224 LQrefsGPYQPLSRKFTEWTygPVTSSLYdlseidsWEKNSVLELIAFS 272
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 371-619 2.94e-07

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 54.31  E-value: 2.94e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716  371 PPIQDED-EGEEGPTEPPPAE--PRTLNGVSSPPHPSPKSPVQLEEAPFSRRFGLLKTGSSGAL-GPPERRTAEGAP--- 443
Cdd:PTZ00449 497 APIEEEDsDKHDEPPEGPEASglPPKAPGDKEGEEGEHEDSKESDEPKEGGKPGETKEGEVGKKpGPAKEHKPSKIPtls 576

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716  444 --GAGLQRSASSSWLEGTSTQAKELRLARITPTPSPKLPEpsvLSEVTKPPPCLENSSPPSRIPEPESPAKPNVPTASTA 521
Cdd:PTZ00449 577 kkPEFPKDPKHPKDPEEPKKPKRPRSAQRPTRPKSPKLPE---LLDIPKSPKRPESPKSPKRPPPPQRPSSPERPEGPKI 653

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716  522 PPADsrdrrRSYQMPVRDEESESQRKARSRLMRQSRRSTQGVTLTDLKEAEKAAGKAPESEKPAQSLD-----PSRRPRV 596
Cdd:PTZ00449 654 IKSP-----KPPKSPKPPFDPKFKEKFYDDYLDAAAKSKETKTTVVLDESFESILKETLPETPGTPFTtprplPPKLPRD 728

                        250       260
                 ....*....|....*....|...
gi 14149716  597 PgvensDSPAQRAEAPDGQGPGP 619
Cdd:PTZ00449 729 E-----EFPFEPIGDPDAEQPDD 746
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 210-282 3.10e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 54.13  E-value: 3.10e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14149716  210 RCWLNGGAMPEARHpRTGASALHVAAAKGYIEVMRLLLQAGYDPELRDGDGWTPLHAAAHWGVEDACRLLAEH 282
Cdd:PTZ00322  99 RILLTGGADPNCRD-YDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 133-160 3.56e-07

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: 46.81  E-value: 3.56e-07
                           10        20
                   ....*....|....*....|....*...
gi 14149716    133 EGWTPLHVAASCGYLDIARYLLSHGANI 160
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 113-225 4.17e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 53.72  E-value: 4.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716  113 NLEVVRFLVEQGATVNQADNEGWTPLHVAASCGYLDIARYLLSHGANIAAVNSDGDL-PLDLAESdamegLLKAEIARRG 191
Cdd:PLN03192 634 DLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDDDFsPTELREL-----LQKRELGHSI 708

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 14149716  192 VDVEAAKRAEEELLL--HDTRCWLNGGAMPEARHPR 225
Cdd:PLN03192 709 TIVDSVPADEPDLGRdgGSRPGRLQGTSSDNQCRPR 744
Ank_4 pfam13637
Ankyrin repeats (many copies);
134-174 5.71e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.88  E-value: 5.71e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 14149716   134 GWTPLHVAASCGYLDIARYLLSHGANIAAVNSDGDLPLDLA 174
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFA 41
PHA03095 PHA03095
ankyrin-like protein; Provisional
 96-174 6.43e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 52.72  E-value: 6.43e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716   96 STNADGISALHQACIDENLE--VVRFLVEQGATVNQADNEGWTPLHVAASCGYLDIARYLLSHGANIAAVNSDGDLPLDL 173
Cdd:PHA03095 217 ATDMLGNTPLHSMATGSSCKrsLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSL 296


                 .
gi 14149716  174 A 174
Cdd:PHA03095 297 M 297
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 52-156 1.00e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.21  E-value: 1.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716   52 AAEFLAACAGGDLDEARLMLRA-ADPgpgaeldpaappparavlDSTNADGISALHQACIDENLEVVRFLVEQGATVNQA 130
Cdd:PTZ00322  83 TVELCQLAASGDAVGARILLTGgADP------------------NCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLL 144

                         90       100
                 ....*....|....*....|....*.
gi 14149716  131 DNEGWTPLHVAASCGYLDIARYLLSH 156
Cdd:PTZ00322 145 DKDGKTPLELAEENGFREVVQLLSRH 170
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 95-171 1.22e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 51.53  E-value: 1.22e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 14149716   95 DSTNADGISALHQACIDENLEVVRFLVEQGATVNQADNEGWTPLHVAASCGYLDIARYLLSHGANIAAVNSDGDLPL 171
Cdd:PHA02875 129 DIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAA 205
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 101-270 1.50e-06

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 51.62  E-value: 1.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716   101 GISALHQACIDENLEVVRFLVEQGATVNQADN--------------EGWTPLHVAASCGYLDIARYLLSHGANIAAVNSD 166
Cdd:TIGR00870 128 GITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsfyHGESPLNAAACLGSPSIVALLSEDPADILTADSL 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716   167 GDlplDLAESDAMEGLLKAEiarrgvDVEAAKRAEEELLLHDTRCwlnggampeaRHPRT--------GASALHVAAAKG 238
Cdd:TIGR00870 208 GN---TLLHLLVMENEFKAE------YEELSCQMYNFALSLLDKL----------RDSKElevilnhqGLTPLKLAAKEG 268

                         170       180       190
                  ....*....|....*....|....*....|....
gi 14149716   239 YIEVMRLLLQAGYdpELRDGDGWT--PLHAAAHW 270
Cdd:TIGR00870 269 RIVLFRLKLAIKY--KQKKFVAWPngQQLLSLYW 300
Ank_5 pfam13857
Ankyrin repeats (many copies);
225-267 1.52e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.80  E-value: 1.52e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 14149716   225 RTGASALHVAAAKGYIEVMRLLLQAGYDPELRDGDGWTPLHAA 267
Cdd:pfam13857  14 GEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 100-297 1.66e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 51.15  E-value: 1.66e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716  100 DGISALHQACIDENLEVVRFLVEQGATVNQADNEGWTPLHVAASCGYLDIARYLLSHGANIAAV-NSDGDLPLDLAESDA 178
Cdd:PHA02875  34 DGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDVfYKDGMTPLHLATILK 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716  179 MEGLLKAEIARRG-VDVEAAKRAeeelllhdtrcwlnggampearhprtgaSALHVAAAKGYIEVMRLLLQAGYDPELRD 257
Cdd:PHA02875 114 KLDIMKLLIARGAdPDIPNTDKF----------------------------SPLHLAVMMGDIKGIELLIDHKACLDIED 165

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 14149716  258 GDGWTPLHAAAHWGVEDACRLLAEHGGGMDsltHAGQRPC 297
Cdd:PHA02875 166 CCGCTPLIIAMAKGDIAICKMLLDSGANID---YFGKNGC 202
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 113-283 1.86e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 51.12  E-value: 1.86e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716  113 NLEVVRFLVEQGATVNQADNEGWTPLHVAASCGYLDIARYLLSHGANIAAvnsdgdLPLDLAESDAMEGLLKAeiarrGV 192
Cdd:PHA02874  47 DAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSI------LPIPCIEKDMIKTILDC-----GI 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716  193 DVEAAKRAEEELL--------LHDTRCWLNGGAMPEARHPrTGASALHVAAAKGYIEVMRLLLQAGYDPELRDGDGWTPL 264
Cdd:PHA02874 116 DVNIKDAELKTFLhyaikkgdLESIKMLFEYGADVNIEDD-NGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPL 194

                        170
                 ....*....|....*....
gi 14149716  265 HAAAHWGVEDACRLLAEHG 283
Cdd:PHA02874 195 HNAAEYGDYACIKLLIDHG 213
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 94-300 3.30e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 50.35  E-value: 3.30e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716   94 LDSTNADGISALHQACIDENLEVVRFLVEQGATVNQADNEGWTPLHVAASCGYLDIARYLLSHGANIAAVNSDGDLPLDL 173
Cdd:PHA02874 117 VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHN 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716  174 AesdamegllkaeiarrgvdVEAAKRAEEELLLHDTRCWLNggampearHPRTGASALHVAAAKGYIEVMRLLLQAGYDp 253
Cdd:PHA02874 197 A-------------------AEYGDYACIKLLIDHGNHIMN--------KCKNGFTPLHNAIIHNRSAIELLINNASIN- 248

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 14149716  254 eLRDGDGWTPLHAAAHWGVE-DACRLLAEHGGGMDSLTHAGQRPCDLA 300
Cdd:PHA02874 249 -DQDIDGSTPLHHAINPPCDiDIIDILLYHKADISIKDNKGENPIDTA 295
PHA03247 PHA03247
large tegument protein UL36; Provisional
 319-629 3.89e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 50.71  E-value: 3.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716   319 RNQKEASQSRGQEPQAPSSSKHRRS---SVCRLSSREKISLQDLSKERRP----GGAGGPPIQDEDEGEEGPTEPPPAEP 391
Cdd:PHA03247 2663 RPRRARRLGRAAQASSPPQRPRRRAarpTVGSLTSLADPPPPPPTPEPAPhalvSATPLPPGPAAARQASPALPAAPAPP 2742

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716   392 RTLNGVSSPPHPSPKSPVQLEEAPFSrrfgllKTGSSGALGPPERRT--AEGAPGAGLQRSASSSWLEGTSTQAKELRLA 469
Cdd:PHA03247 2743 AVPAGPATPGGPARPARPPTTAGPPA------PAPPAAPAAGPPRRLtrPAVASLSESRESLPSPWDPADPPAAVLAPAA 2816

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716   470 RITPTPSPKLPEPsvlsevtkPPPclenSSPPSRIPEPESPAKPNVPTASTAPPADSRDRRRSYQMPVRDEESESQRKAR 549
Cdd:PHA03247 2817 ALPPAASPAGPLP--------PPT----SAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVR 2884

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716   550 SRLMRQSRRSTQGVTLTDLKEAEKAAGKAPESEKPAQSLDPSRRPRVPGVENSDSPAQRAEAPDGQG-PGPQAAREHRKV 628
Cdd:PHA03247 2885 RLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGaGEPSGAVPQPWL 2964


                  .
gi 14149716   629 G 629
Cdd:PHA03247 2965 G 2965
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 133-162 5.22e-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: 43.40  E-value: 5.22e-06
                          10        20        30
                  ....*....|....*....|....*....|
gi 14149716   133 EGWTPLHVAASCGYLDIARYLLSHGANIAA 162
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 104-287 5.33e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 49.60  E-value: 5.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716  104 ALHQACIDENLEVVRFLVEQGATVNQADNEGWTPLHVAASCGYLDIARYLLSHGAnIAAVNSDGdlpldlAESDAMEGLL 183
Cdd:PHA02875   5 ALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGA-IPDVKYPD------IESELHDAVE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716  184 KAEIarrgvdveaakRAEEELLLHDTrcWLNGGAMpearhpRTGASALHVAAAKGYIEVMRLLLQAGYDPELRDGDGWTP 263
Cdd:PHA02875  78 EGDV-----------KAVEELLDLGK--FADDVFY------KDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSP 138

                        170       180
                 ....*....|....*....|....
gi 14149716  264 LHAAAHWGVEDACRLLAEHGGGMD 287
Cdd:PHA02875 139 LHLAVMMGDIKGIELLIDHKACLD 162
PRK13335 PRK13335
superantigen-like protein SSL3; Reviewed;
425-543 1.95e-05

superantigen-like protein SSL3; Reviewed;


Pssm-ID: 139494 [Multi-domain]  Cd Length: 356  Bit Score: 47.43  E-value: 1.95e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716  425 TGSSGALGPPERRTA--EGAPGAGLQRSASSSWLEGTSTQAKELRLARITPTPSPKLPEPSVLSEVTKPPPCLenSSPPS 502
Cdd:PRK13335  60 SATTQAANTRQERTPklEKAPNTNEEKTSASKIEKISQPKQEEQKSLNISATPAPKQEQSQTTTESTTPKTKV--TTPPS 137

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 14149716  503 -RIPEPESPAKPNVPTASTAPPADS------RDRRRSYQMPVRDEESE 543
Cdd:PRK13335 138 tNTPQPMQSTKSDTPQSPTIKQAQTdmtpkyEDLRAYYTKPSFEFEKQ 185
Ank_5 pfam13857
Ankyrin repeats (many copies);
94-141 2.29e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.33  E-value: 2.29e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 14149716    94 LDSTNADGISALHQACIDENLEVVRFLVEQGATVNQADNEGWTPLHVA 141
Cdd:pfam13857   9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 101-171 3.14e-05

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 47.31  E-value: 3.14e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716 101 GISALHQACIDENLEVVRFLVEQGATVNQA-----------DNE---GWTPLHVAASCGYLDIARYLLSHGANIAAVNSD 166
Cdd:cd22192  89 GETALHIAVVNQNLNLVRELIARGADVVSPratgtffrpgpKNLiyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSL 168


                ....*
gi 14149716 167 GDLPL 171
Cdd:cd22192 169 GNTVL 173
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 100-252 5.42e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 46.52  E-value: 5.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716  100 DGISALHQACIDENLEVVRFLVEQGATVNQADNEGWTPLHVAASCGYLDIARYLLSHGANIAAVNSDGDLPLDLAesdam 179
Cdd:PHA02875 101 DGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIA----- 175

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14149716  180 egllkaeIARRGVDVeaakraeeelllhdTRCWLNGGAMPEARHPRTGASALHVAAAKGYIEVMRLLLQAGYD 252
Cdd:PHA02875 176 -------MAKGDIAI--------------CKMLLDSGANIDYFGKNGCVAALCYAIENNKIDIVRLFIKRGAD 227
PHA02795 PHA02795
ankyrin-like protein; Provisional
 114-174 6.29e-05

ankyrin-like protein; Provisional


Pssm-ID: 165157 [Multi-domain]  Cd Length: 437  Bit Score: 46.14  E-value: 6.29e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14149716  114 LEVVRFLVEQGATVNQADNEGWTPLHVAASCGYLDIARYLLSHGANIAAVNSDGDLPLDLA 174
Cdd:PHA02795 201 LEIYKLCIPYIEDINQLDAGGRTLLYRAIYAGYIDLVSWLLENGANVNAVMSNGYTCLDVA 261
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 94-268 7.12e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 46.21  E-value: 7.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716   94 LDSTNADGISA--------------LHQACIDENLEVVRFLVEQGATVNQADNEGWTPLHVAASCGYLD-IARYLLSHGA 158
Cdd:PHA02876 219 VDSKNIDTIKAiidnrsninkndlsLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGA 298

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716  159 NIAAVNSDGDLPLDLAESDAMEGLLKAEIARRGVDVEAAKRaeeellLHDTrcwlnggampearhPRTGASALhvaaaKG 238
Cdd:PHA02876 299 DVNAKNIKGETPLYLMAKNGYDTENIRTLIMLGADVNAADR------LYIT--------------PLHQASTL-----DR 353

                        170       180       190
                 ....*....|....*....|....*....|
gi 14149716  239 YIEVMRLLLQAGYDPELRDGDGWTPLHAAA 268
Cdd:PHA02876 354 NKDIVITLLELGANVNARDYCDKTPIHYAA 383
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 93-174 9.13e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 45.72  E-value: 9.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716   93 VLDSTN------ADGISALHQACIdENLEVVRFLVEQgATVNQADNEGWTPLHVAAS--CGyLDIARYLLSHGANIAAVN 164
Cdd:PHA02874 209 LIDHGNhimnkcKNGFTPLHNAII-HNRSAIELLINN-ASINDQDIDGSTPLHHAINppCD-IDIIDILLYHKADISIKD 285

                         90
                 ....*....|
gi 14149716  165 SDGDLPLDLA 174
Cdd:PHA02874 286 NKGENPIDTA 295
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 100-128 1.09e-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: 39.93  E-value: 1.09e-04
                          10        20
                  ....*....|....*....|....*....
gi 14149716   100 DGISALHQACIDENLEVVRFLVEQGATVN 128
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 100-132 1.17e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 39.97  E-value: 1.17e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 14149716   100 DGISALHQACIDE-NLEVVRFLVEQGATVNQADN 132
Cdd:pfam00023   1 DGNTPLHLAAGRRgNLEIVKLLLSKGADVNARDK 34
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 235-300 1.32e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 45.27  E-value: 1.32e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 14149716  235 AAKGYIEVMRLLLQAGYDPELRDGDGWTPLHAAAHWGVEDACRLLAEHGGGMDSLTHAGQRPCDLA 300
Cdd:PTZ00322  90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELA 155
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
688-782 1.56e-04

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 45.23  E-value: 1.56e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716 688 AELRRENERLREALTETTLRLAQLKVELERATQRQERFAERPAllELERFERR--ALERkaaELEEELKALSDLRADNQR 765
Cdd:COG2433 423 ERLEAEVEELEAELEEKDERIERLERELSEARSEERREIRKDR--EISRLDREieRLER---ELEEERERIEELKRKLER 497

                        90       100
                ....*....|....*....|....
gi 14149716 766 LKD-------ENAALIRVISKLSK 782
Cdd:COG2433 498 LKElwklehsGELVPVKVVEKFTK 521
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 112-268 1.58e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 45.05  E-value: 1.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716  112 ENLEVVRFLVEQGATVNQADNEGWTPLHVAASCGYLDIARYLLSHGANIAAVNSDGDLPLDLAESDAMEGLLKAEIARRG 191
Cdd:PHA02876 156 DELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRS 235

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716  192 ---------VDVEAAKRAEEELLLHDTRCWLNG----------------------------GAMPEARHPRtGASALHVA 234
Cdd:PHA02876 236 ninkndlslLKAIRNEDLETSLLLYDAGFSVNSiddckntplhhasqapslsrlvpkllerGADVNAKNIK-GETPLYLM 314

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 14149716  235 AAKGY-IEVMRLLLQAGYDPELRDGDGWTPLHAAA 268
Cdd:PHA02876 315 AKNGYdTENIRTLIMLGADVNAADRLYITPLHQAS 349
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 227-257 1.62e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 39.58  E-value: 1.62e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 14149716   227 GASALHVAAAK-GYIEVMRLLLQAGYDPELRD 257
Cdd:pfam00023   2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
PHA02798 PHA02798
ankyrin-like protein; Provisional
 114-167 1.96e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 44.83  E-value: 1.96e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 14149716  114 LEVVRFLVEQGATVNQADNEGWTPLHVAASCGY---LDIARYLLSHGANIAAVNSDG 167
Cdd:PHA02798  89 LDIVKILIENGADINKKNSDGETPLYCLLSNGYinnLEILLFMIENGADTTLLDKDG 145
Ank_2 pfam12796
Ankyrin repeats (3 copies);
57-131 2.02e-04

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 40.87  E-value: 2.02e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 14149716    57 AACAGGDLDEARLMLRAADpgpgaeldpaappparavLDSTNaDGISALHQACIDENLEVVRFLVEQGATVNQAD 131
Cdd:pfam12796  36 LAAKNGHLEIVKLLLEHAD------------------VNLKD-NGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 364-543 2.17e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 44.98  E-value: 2.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716  364 RPGGAGGPPIQDEDEGEEGPTEPPPAEPRTLNGVSSPPHPSPKSPVQL-EEAPFSRRFGLLKTGSSGALGPPERRTAEGA 442
Cdd:PRK07764 626 APAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAgGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAP 705

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716  443 PGAGLQRSASSSWLEGTSTQAKELRLARITPTPSPKLPEP------SVLSEVTKPPPCLENSSPPSRIPEPESPAKPNVP 516
Cdd:PRK07764 706 AATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPddppdpAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEM 785

                        170       180
                 ....*....|....*....|....*..
gi 14149716  517 TASTAPPADSRDRRRSYQMPVRDEESE 543
Cdd:PRK07764 786 AEDDAPSMDDEDRRDAEEVAMELLEEE 812
PRK12678 PRK12678
transcription termination factor Rho; Provisional
 437-699 2.84e-04

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 44.51  E-value: 2.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716  437 RTAEGAPGAGL--------QRSASSSWLEGTSTQAKELRLARIT----PTPSPKLPEPSVLSEVTKPPPCLENSSPPSRI 504
Cdd:PRK12678  13 DTAPRARGGGLagmklpelRALAKQLGIKGTSGMRKGELIAAIKeargGGAAAAAATPAAPAAAARRAARAAAAARQAEQ 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716  505 PEPESPAKPNVPTASTAPPADSRDRRRSYQMPVRdEESESQRKARSRLMRQSRRSTQGvtltdlkEAEKAAGKAPESEKP 584
Cdd:PRK12678  93 PAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQ-ARERRERGEAARRGAARKAGEGG-------EQPATEARADAAERT 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716  585 AQSlDPSRRPRVPGVENSDSPAQRAEAPDGQGPGPQAAREHRKVGKEwrgpaEGEEAEPADRSQESSTLEGGPSARRQRW 664
Cdd:PRK12678 165 EEE-ERDERRRRGDREDRQAEAERGERGRREERGRDGDDRDRRDRRE-----QGDRREERGRRDGGDRRGRRRRRDRRDA 238

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 14149716  665 QRDLNPEPEPESEEPDGGFRtlyAELRRENERLRE 699
Cdd:PRK12678 239 RGDDNREDRGDRDGDDGEGR---GGRRGRRFRDRD 270
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 685-782 2.88e-04

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 43.98  E-value: 2.88e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716 685 TLYAELRRENERLREALTETTLRLAQLKVELERATQRQERF-----AERPALLELERFERRALERKAAELEEELKALSDL 759
Cdd:COG4942 139 QYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALlaeleEERAALEALKAERQKLLARLEKELAELAAELAEL 218

                        90       100
                ....*....|....*....|...
gi 14149716 760 RADNQRLKDENAALIRVISKLSK 782
Cdd:COG4942 219 QQEAEELEALIARLEAEAAAAAE 241
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 93-171 3.78e-04

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 44.13  E-value: 3.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716   93 VLDSTNADGISALHQACIDENL--EVVRFLVEQGATVNQADNEGWTPLHVAASCG--------------YLDIARYLLSH 156
Cdd:PHA02716 309 KLHYKDSAGRTCLHQYILRHNIstDIIKLLHEYGNDLNEPDNIGNTVLHTYLSMLsvvnildpetdndiRLDVIQCLISL 388

                         90
                 ....*....|....*
gi 14149716  157 GANIAAVNSDGDLPL 171
Cdd:PHA02716 389 GADITAVNCLGYTPL 403
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 228-283 5.45e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 43.70  E-value: 5.45e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 14149716  228 ASALHVAAAKGYIEVMRLLLQAGYDPELRDGDGWTPLHAAAHWGVEDACRLLAEHG 283
Cdd:PLN03192 526 ASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHA 581
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 636-782 6.83e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.51  E-value: 6.83e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716    636 AEGEEAEPADRSQESSTLEGGPSARRQRWQRDLNPEPEPESEepdggFRTLYAELRRENERLREALTETTLRLAQL---- 711
Cdd:TIGR02168  759 LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKA-----LREALDELRAELTLLNEEAANLRERLESLerri 833

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 14149716    712 ---KVELERATQRQERFAERPALLELERFErraLERKAAELEEELKALSDLRADNQR----LKDENAALIRVISKLSK 782
Cdd:TIGR02168  834 aatERRLEDLEEQIEELSEDIESLAAEIEE---LEELIEELESELEALLNERASLEEalalLRSELEELSEELRELES 908
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 101-171 6.87e-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: 43.26  E-value: 6.87e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716 101 GISALHQACIDENLEVVRFLVEQGATVN-QADNE-------------GWTPLHVAASCGYLDIARYLLSH---GANIAAV 163
Cdd:cd22196  94 GQTALHIAIERRNMHLVELLVQNGADVHaRASGEffkkkkggpgfyfGELPLSLAACTNQLDIVKFLLENphsPADISAR 173


                ....*...
gi 14149716 164 NSDGDLPL 171
Cdd:cd22196 174 DSMGNTVL 181
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 227-255 7.33e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.57  E-value: 7.33e-04
                           10        20
                   ....*....|....*....|....*....
gi 14149716    227 GASALHVAAAKGYIEVMRLLLQAGYDPEL 255
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 101-265 7.35e-04

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 43.08  E-value: 7.35e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716 101 GISALHQACIDENLEVVRFLVEQGAT-VNQADN----EGWTPLHvaascgyldiaryllshganIAAVNSDgdlpldlae 175
Cdd:cd22192  51 GETALHVAALYDNLEAAVVLMEAAPElVNEPMTsdlyQGETALH--------------------IAVVNQN--------- 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716 176 sdamEGLLKAEIaRRGVDVEAAkRAEEELLLHDTRCWLNGGampeaRHPrtgasaLHVAAAKGYIEVMRLLLQAGYDPEL 255
Cdd:cd22192 102 ----LNLVRELI-ARGADVVSP-RATGTFFRPGPKNLIYYG-----EHP------LSFAACVGNEEIVRLLIEHGADIRA 164

                       170
                ....*....|
gi 14149716 256 RDGDGWTPLH 265
Cdd:cd22192 165 QDSLGNTVLH 174
PHA02798 PHA02798
ankyrin-like protein; Provisional
 111-171 7.92e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 42.90  E-value: 7.92e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 14149716  111 DENLEVVRFLVEQGATVNQADNEGWTPLHVAASC-----GYLDIARYLLSHGANIAAVNSDGDLPL 171
Cdd:PHA02798  48 SPSTDIVKLFINLGANVNGLDNEYSTPLCTILSNikdykHMLDIVKILIENGADINKKNSDGETPL 113
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 94-164 8.36e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 42.74  E-value: 8.36e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14149716   94 LDSTNADGISALHQA-CIDENLEVVRFLVEQGATVNQADNEGWTPLHVAASCGYLDIARYLLSHGANIAAVN 164
Cdd:PHA02876 334 VNAADRLYITPLHQAsTLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALS 405
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 414-631 8.99e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 42.67  E-value: 8.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716  414 APFSRRFGLLKTGSSGALGPPERRTAEGAPGAGLQRSASSSWLEGTSTQAkelrlaRITPTPSPKLPEPSVLSEVTKPPP 493
Cdd:PRK07764 595 AGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPA------PGVAAPEHHPKHVAVPDASDGGDG 668

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716  494 CLENSSPPSRIPEPESPAKPNVPTASTAPPADSRDRRRSYQMPVRDEESESQ-RKARSRLMRQSRRSTQGVTLTDLKEAE 572
Cdd:PRK07764 669 WPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQpPQAAQGASAPSPAADDPVPLPPEPDDP 748

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 14149716  573 KAAGKAPESEKPAQSLDPSRRPRVPGVENSDSPAQRAEAPDGQGPGPQAAREHRKVGKE 631
Cdd:PRK07764 749 PDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMAEDDAPSMDDEDRRDAEEVAME 807
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 101-267 9.47e-04

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


Pssm-ID: 411981 [Multi-domain]  Cd Length: 640  Bit Score: 42.53  E-value: 9.47e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716 101 GISALHQACIDENLEVVRFLVEQGATVN-QADNE------------GWTPLHVAASCGYLDIARYLLSHGANIAAV---N 164
Cdd:cd22197  94 GHSALHIAIEKRSLQCVKLLVENGADVHaRACGRffqkkqgtcfyfGELPLSLAACTKQWDVVNYLLENPHQPASLqaqD 173

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716 165 SDGDLPL--------DLAESDAMEGLLKAEIARRGVDVEAAKRAEEelllhdtrcwlnggaMPEarhpRTGASALHVAAA 236
Cdd:cd22197 174 SLGNTVLhalvmiadNSPENSALVIKMYDGLLQAGARLCPTVQLEE---------------ISN----HEGLTPLKLAAK 234

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 14149716 237 KGYIEVMRLLLQ----AGYDPELRDGDGWT--PLHAA 267
Cdd:cd22197 235 EGKIEIFRHILQrefsGPYQHLSRKFTEWCygPVRVS 271
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 101-256 1.21e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are thermo-sensing channels that function directly in temperature-sensing and nociception; they share substantial structural and functional properties. Transient Receptor Potential (TRP) ion channels activated by temperature (thermo TRPs) are important molecular players in acute, inflammatory, and chronic pain states. So far, 11 TRP channels in mammalian cells have been identified as thermosensitive TRP (thermo-TRP) channels. TRPV1-4 channels are activated by different heat temperatures, for example, TRPV1 and TRPV2 are activated by high temperatures (>43C and >55C, respectively). TRPV1-4 belong to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 42.48  E-value: 1.21e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716 101 GISALHQACIDENLEVVRFLVEQGATVNQADNE--------------GWTPLHVAASCGYLDIARYLLSHG---ANIAAV 163
Cdd:cd22193  76 GQTALHIAIERRQGDIVALLVENGADVHAHAKGrffqpkyqgegfyfGELPLSLAACTNQPDIVQYLLENEhqpADIEAQ 155

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716 164 NSDGDLPLdlaesDAMegllkAEIARRGVDVEA-AKRAEEELLLHDTRcWLNGGAMPEARHpRTGASALHVAAAKGYIEV 242
Cdd:cd22193 156 DSRGNTVL-----HAL-----VTVADNTKENTKfVTRMYDMILIRGAK-LCPTVELEEIRN-NDGLTPLQLAAKMGKIEI 223

                       170
                ....*....|....*
gi 14149716 243 MRLLLQAGY-DPELR 256
Cdd:cd22193 224 LKYILQREIkEPELR 238
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 696-773 1.24e-03

Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.


Pssm-ID: 462536 [Multi-domain]  Cd Length: 176  Bit Score: 40.30  E-value: 1.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716   696 RLREALTETTLR---LAQLKVELERATQRQERF--AERPALLELERfERRALERKAAELEEELKALSDLradNQRLKDEN 770
Cdd:pfam08614  61 QLREELAELYRSrgeLAQRLVDLNEELQELEKKlrEDERRLAALEA-ERAQLEEKLKDREEELREKRKL---NQDLQDEL 136


                  ...
gi 14149716   771 AAL 773
Cdd:pfam08614 137 VAL 139
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 100-128 1.25e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.80  E-value: 1.25e-03
                           10        20
                   ....*....|....*....|....*....
gi 14149716    100 DGISALHQACIDENLEVVRFLVEQGATVN 128
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
PHA03247 PHA03247
large tegument protein UL36; Provisional
 472-663 1.27e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.62  E-value: 1.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716   472 TPTPSPKLPEPSVLSEVTKPPPCLENSSPPSRIPEPESPAKPNVPTAstAPPADSRDRRRSYQMPVRDEESESQRKARSR 551
Cdd:PHA03247 2570 PPRPAPRPSEPAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSP--LPPDTHAPDPPPPSPSPAANEPDPHPPPTVP 2647

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716   552 LMRQSRRSTQGVTLTDLKEAEKAAGKAPESEKPAQSLDPSRRPRVPGVENSDSPAQRAEAPDGQGPGPQAAREHRKVGKE 631
Cdd:PHA03247 2648 PPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAA 2727

                         170       180       190
                  ....*....|....*....|....*....|..
gi 14149716   632 WRGPAEGEEAEPADRSQESSTLEGGPSARRQR 663
Cdd:PHA03247 2728 ARQASPALPAAPAPPAVPAGPATPGGPARPAR 2759
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 688-780 1.31e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.23  E-value: 1.31e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716 688 AELRRENERLREALTETTLRLAQLKVELERATQRQERFAERPALLELERFE-RRALERKAAELEEELKALSDLRADNQRL 766
Cdd:COG1196 312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEaEEALLEAEAELAEAEEELEELAEELLEA 391

                        90
                ....*....|....
gi 14149716 767 KDENAALIRVISKL 780
Cdd:COG1196 392 LRAAAELAAQLEEL 405
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 108-171 1.68e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 40.57  E-value: 1.68e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 14149716  108 ACIDE---NLEVVRFLVEQGATVN-QADNEGWTPLHvaascGYL--------DIARYLLSHGANIAAVNSDGDLPL 171
Cdd:PHA02859  57 SCLEKdkvNVEILKFLIENGADVNfKTRDNNLSALH-----HYLsfnknvepEILKILIDSGSSITEEDEDGKNLL 127
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 97-168 1.82e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 40.57  E-value: 1.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716   97 TNADGISALHQ-ACIDENL--EVVRFLVEQGATVNQADNEGWTPLHVaascgYLD-------IARYLLSHGANIAAVNSD 166
Cdd:PHA02859  83 TRDNNLSALHHyLSFNKNVepEILKILIDSGSSITEEDEDGKNLLHM-----YMCnfnvrinVIKLLIDSGVSFLNKDFD 157


                 ..
gi 14149716  167 GD 168
Cdd:PHA02859 158 NN 159
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 684-781 2.06e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.85  E-value: 2.06e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716 684 RTLYAELRRENERLREALTETTLRLAQLKVELERATQRQERFAERpaLLELERFERRALERKAAELEEELKALSDLRADN 763
Cdd:COG1196 273 RLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER--LEELEEELAELEEELEELEEELEELEEELEEAE 350

                        90
                ....*....|....*...
gi 14149716 764 QRLKDENAALIRVISKLS 781
Cdd:COG1196 351 EELEEAEAELAEAEEALL 368
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 103-174 2.52e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 41.20  E-value: 2.52e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 14149716  103 SALHQACIDEN-LEVVRFLVEQGATVNQADNEGWTPLHVAA--SCGyLDIARYLLSHGANIAAVNSDGDLPLDLA 174
Cdd:PHA02876 410 TALHFALCGTNpYMSVKTLIDRGANVNSKNKDLSTPLHYACkkNCK-LDVIEMLLDNGADVNAINIQNQYPLLIA 483
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 427-660 3.01e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 41.31  E-value: 3.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716   427 SSGALGPPERRTAEGAPGAGLQRSASSSWLEGTSTQAKELRLARITPTPSPKLPEPSVLSEVTKPPPCLENSSPPSR--- 503
Cdd:PHA03307   73 PGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAasp 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716   504 -----------------------IPEPESPAKPNVPTASTAPPADSRDRRRSYQMPVRDEESESQRKARSRLMRQSRRST 560
Cdd:PHA03307  153 paagaspaavasdaassrqaalpLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDA 232

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716   561 QGVTLTDLKEAEKAAGKAPESEKPAQSLDPSRRPRVPG------VENSDSPAQRAEAPDgQGPGPQAAREHRKVGKEWRG 634
Cdd:PHA03307  233 GASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWeasgwnGPSSRPGPASSSSSP-RERSPSPSPSSPGSGPAPSS 311

                         250       260
                  ....*....|....*....|....*.
gi 14149716   635 PAEGEEAEPADRSQESSTLEGGPSAR 660
Cdd:PHA03307  312 PRASSSSSSSRESSSSSTSSSSESSR 337
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
687-778 3.82e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.52  E-value: 3.82e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716 687 YAELRRENERLREALTETTLRLAQLKVE---LERATQRQERFAERPALL-ELERFERR--ALERKAAELEEELKALSDLR 760
Cdd:COG4717  90 YAELQEELEELEEELEELEAELEELREElekLEKLLQLLPLYQELEALEaELAELPERleELEERLEELRELEEELEELE 169

                        90
                ....*....|....*...
gi 14149716 761 ADNQRLKDENAALIRVIS 778
Cdd:COG4717 170 AELAELQEELEELLEQLS 187
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 687-781 4.00e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.69  E-value: 4.00e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716 687 YAELRRENERLREALTETTLRLAQLKVELERATQRQERFAERpalLELERFERRALERKAAELEEELKALSDLRAD-NQR 765
Cdd:COG1196 290 EYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEE---LEELEEELEELEEELEEAEEELEEAEAELAEaEEA 366

                        90
                ....*....|....*.
gi 14149716 766 LKDENAALIRVISKLS 781
Cdd:COG1196 367 LLEAEAELAEAEEELE 382
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 688-780 7.52e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.92  E-value: 7.52e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716 688 AELRRENERLREALTETTLRLAQLKVELERATQRQERF-AERPALLELERFERRALERKAAELEEELKALSDLRADNQRL 766
Cdd:COG1196 382 EELAEELLEALRAAAELAAQLEELEEAEEALLERLERLeEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL 461

                        90
                ....*....|....
gi 14149716 767 KDENAALIRVISKL 780
Cdd:COG1196 462 LELLAELLEEAALL 475
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 259-283 7.82e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 34.57  E-value: 7.82e-03
                          10        20
                  ....*....|....*....|....*.
gi 14149716   259 DGWTPLHAAA-HWGVEDACRLLAEHG 283
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKG 26
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
426-623 8.18e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 39.83  E-value: 8.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716  426 GSSGALGPPERRTAEGAPGAGLQRSASSSwLEGTSTQAKELRLARITPTPSPKLPEPSVLSEVTKPPPCLENSSPPSRIP 505
Cdd:PRK07003 439 GDDAADGDAPVPAKANARASADSRCDERD-AQPPADSGSASAPASDAPPDAAFEPAPRAAAPSAATPAAVPDARAPAAAS 517

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716  506 EPESPAKPNVPTASTAP--PADSRDRRRSyqmpvrDEESESQRKARSRLMR-QSRRSTQGVTltdlkeAEKAAGKAPESE 582
Cdd:PRK07003 518 REDAPAAAAPPAPEARPptPAAAAPAARA------GGAAAALDVLRNAGMRvSSDRGARAAA------AAKPAAAPAAAP 585

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 14149716  583 KPAqsldpSRRPRVPgvensdSPAQRAEAPDGQGPGPQAAR 623
Cdd:PRK07003 586 KPA-----APRVAVQ------VPTPRARAATGDAPPNGAAR 615
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
 695-772 8.56e-03

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 39.55  E-value: 8.56e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 14149716   695 ERLREALTETTLRLAQLKVELERATQRQERFAERpalLELERFERRALERKAAELEEELKAlsdLRADNQRLKDENAA 772
Cdd:PRK11448  138 EDPENLLHALQQEVLTLKQQLELQAREKAQSQAL---AEAQQQELVALEGLAAELEEKQQE---LEAQLEQLQEKAAE 209
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 688-772 9.54e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.53  E-value: 9.54e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149716 688 AELRRENERLREALTETTLRLAQLKVELERATQRQERFAERPALLELERF----ERRALERKAAELEEELKALSDLRADN 763
Cdd:COG1196 298 ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEeaeeELEEAEAELAEAEEALLEAEAELAEA 377


                ....*....
gi 14149716 764 QRLKDENAA 772
Cdd:COG1196 378 EEELEELAE 386
 
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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