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ankyrin repeat and SOCS box protein 7 [Bufo gargarizans]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
30-261 3.14e-36

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 132.00  E-value: 3.14e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113563440  30 AVAVGDVHTVRTMLEQGYSPNGRDTNGWTLLHFSAARGKERCVRVFLEHGADPTVKDLiGGFTALHYAAMHGRARIARLL 109
Cdd:COG0666    28 AALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD-GGNTLLHAAARNGDLEIVKLL 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113563440 110 LEsehRSDIINAKSNDGWTPLHVAAHYGRDSFVTLLLEFKAEVDPLSDKGTTPLQLAIIRERSSCVKILLDHNANIDIQN 189
Cdd:COG0666   107 LE---AGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARD 183

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2113563440 190 GF---LLRYAVLKSNHSYCRMFLQRGADTNLgRLEDGQTPLHISALRDDVLCARMLYNYGADTNTRNYEGQTPLD 261
Cdd:COG0666   184 NDgetPLHLAAENGHLEIVKLLLEAGADVNA-KDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALL 257
SOCS_ASB7 cd03726
SOCS (suppressors of cytokine signaling) box of ASB7-like proteins. ASB family members have a ...
 282-326 9.69e-24

SOCS (suppressors of cytokine signaling) box of ASB7-like proteins. ASB family members have a C-terminal SOCS box and an N-terminal ankyrin-related sequence. The general function of the SOCS box is the recruitment of the ubiquitin-transferase system. The SOCS box interacts with Elongins B and C, Cullin-5 or Cullin-2, Rbx-1, and E2. Therefore, SOCS-box-containing proteins probably function as E3 ubiquitin ligases and mediate the degradation of proteins associated through their N-terminal regions.


:

Pssm-ID: 239696  Cd Length: 45  Bit Score: 91.83  E-value: 9.69e-24
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2113563440 282 RQPRYLQDLCRIKIRYCIGLQNLKLLDELPIARVMKDYLKHKFDD 326
Cdd:cd03726     1 RQPRTLQDLCRIKIRHCIGLQNLKLLDELPIAKVMKDYLKHKFDD 45
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
30-261 3.14e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 132.00  E-value: 3.14e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113563440  30 AVAVGDVHTVRTMLEQGYSPNGRDTNGWTLLHFSAARGKERCVRVFLEHGADPTVKDLiGGFTALHYAAMHGRARIARLL 109
Cdd:COG0666    28 AALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD-GGNTLLHAAARNGDLEIVKLL 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113563440 110 LEsehRSDIINAKSNDGWTPLHVAAHYGRDSFVTLLLEFKAEVDPLSDKGTTPLQLAIIRERSSCVKILLDHNANIDIQN 189
Cdd:COG0666   107 LE---AGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARD 183

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2113563440 190 GF---LLRYAVLKSNHSYCRMFLQRGADTNLgRLEDGQTPLHISALRDDVLCARMLYNYGADTNTRNYEGQTPLD 261
Cdd:COG0666   184 NDgetPLHLAAENGHLEIVKLLLEAGADVNA-KDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALL 257
SOCS_ASB7 cd03726
SOCS (suppressors of cytokine signaling) box of ASB7-like proteins. ASB family members have a ...
 282-326 9.69e-24

SOCS (suppressors of cytokine signaling) box of ASB7-like proteins. ASB family members have a C-terminal SOCS box and an N-terminal ankyrin-related sequence. The general function of the SOCS box is the recruitment of the ubiquitin-transferase system. The SOCS box interacts with Elongins B and C, Cullin-5 or Cullin-2, Rbx-1, and E2. Therefore, SOCS-box-containing proteins probably function as E3 ubiquitin ligases and mediate the degradation of proteins associated through their N-terminal regions.


Pssm-ID: 239696  Cd Length: 45  Bit Score: 91.83  E-value: 9.69e-24
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2113563440 282 RQPRYLQDLCRIKIRYCIGLQNLKLLDELPIARVMKDYLKHKFDD 326
Cdd:cd03726     1 RQPRTLQDLCRIKIRHCIGLQNLKLLDELPIAKVMKDYLKHKFDD 45
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 30-262 7.98e-22

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 95.06  E-value: 7.98e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113563440  30 AVAVGDVHTVRTMLEQGYSPNGRDTNGWTLLHFSAARGKERCVRVFLEHGADPTVKdLIGGFTALHYAAMHGRARIARLL 109
Cdd:PHA02875    9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVK-YPDIESELHDAVEEGDVKAVEEL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113563440 110 LESEHRSDIINAKsnDGWTPLHVAAHYGRDSFVTLLLEFKAEVDPLSDKGTTPLQLAIIRERSSCVKILLDHNANIDIQN 189
Cdd:PHA02875   88 LDLGKFADDVFYK--DGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIED 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113563440 190 GF---LLRYAVLKSNHSYCRMFLQRGADTN-LGRleDGQTPLHISALRDDVL-CARMLYNYGADTN---TRNYEGQTPLD 261
Cdd:PHA02875  166 CCgctPLIIAMAKGDIAICKMLLDSGANIDyFGK--NGCVAALCYAIENNKIdIVRLFIKRGADCNimfMIEGEECTILD 243


                  .
gi 2113563440 262 V 262
Cdd:PHA02875  244 M 244
Ank_2 pfam12796
Ankyrin repeats (3 copies);
94-189 3.87e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 83.24  E-value: 3.87e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113563440  94 LHYAAMHGRARIARLLLESEHRsdiINAKSNDGWTPLHVAAHYGRDSFVTLLLEfKAEVDpLSDKGTTPLQLAIIRERSS 173
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGAD---ANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVN-LKDNGRTALHYAARSGHLE 75

                          90
                  ....*....|....*.
gi 2113563440 174 CVKILLDHNANIDIQN 189
Cdd:pfam12796  76 IVKLLLEKGADINVKD 91
SOCS_box pfam07525
SOCS box; The SOCS box acts as a bridge between specific substrate- binding domains and more ...
 283-321 1.48e-06

SOCS box; The SOCS box acts as a bridge between specific substrate- binding domains and more generic proteins that comprise a large family of E3 ubiquitin protein ligases.


Pssm-ID: 462192  Cd Length: 39  Bit Score: 44.08  E-value: 1.48e-06
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2113563440 283 QPRYLQDLCRIKIRYCIGLQNLKLLDELPIARVMKDYLK 321
Cdd:pfam07525   1 TPRSLQHLCRLAIRRALGKRRLGAIDKLPLPPLLKDYLL 39
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 90-260 1.29e-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: 46.54  E-value: 1.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113563440  90 GFTALHYAAMHGRARIARLLLEsEHRSDIINAKSND---GWTPLHVAAHYGRDSFVTLLLEFKAEVDPLSDKGTtplqla 166
Cdd:cd22192    51 GETALHVAALYDNLEAAVVLME-AAPELVNEPMTSDlyqGETALHIAVVNQNLNLVRELIARGADVVSPRATGT------ 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113563440 167 IIRERSSCVKILLDHnanidiqngfLLRYAVLKSNHSYCRMFLQRGADTnlgRLED--GQTPLHISALRDDVLCARMLYN 244
Cdd:cd22192   124 FFRPGPKNLIYYGEH----------PLSFAACVGNEEIVRLLIEHGADI---RAQDslGNTVLHILVLQPNKTFACQMYD 190

                         170       180
                  ....*....|....*....|....*.
gi 2113563440 245 ----YGADTNT------RNYEGQTPL 260
Cdd:cd22192   191 lilsYDKEDDLqpldlvPNNQGLTPF 216
SOCS smart00253
suppressors of cytokine signalling; suppressors of cytokine signalling
 281-323 3.72e-05

suppressors of cytokine signalling; suppressors of cytokine signalling


Pssm-ID: 128549  Cd Length: 43  Bit Score: 40.36  E-value: 3.72e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 2113563440  281 RRQPRYLQDLCRIKIRYCIGLQNLKlldELPIARVMKDYLKHK 323
Cdd:smart00253   4 PSNVPSLQHLCRFTIRRCTRTDQIK---TLPLPPKLKDYLSYY 43
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 24-116 1.64e-03

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: 40.06  E-value: 1.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113563440  24 ELRIQGAVAVGDVHTVRTMLEQGYSPNGRDTNGWTLLH-------FSAARGKERC-----VRVFLEHGADPTVKDLI--- 88
Cdd:TIGR00870 176 ESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHllvmeneFKAEYEELSCqmynfALSLLDKLRDSKELEVIlnh 255

                          90       100
                  ....*....|....*....|....*...
gi 2113563440  89 GGFTALHYAAMHGRARIARLLLESEHRS 116
Cdd:TIGR00870 256 QGLTPLKLAAKEGRIVLFRLKLAIKYKQ 283
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 125-153 3.17e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 34.49  E-value: 3.17e-03
                           10        20
                   ....*....|....*....|....*....
gi 2113563440  125 DGWTPLHVAAHYGRDSFVTLLLEFKAEVD 153
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
30-261 3.14e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 132.00  E-value: 3.14e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113563440  30 AVAVGDVHTVRTMLEQGYSPNGRDTNGWTLLHFSAARGKERCVRVFLEHGADPTVKDLiGGFTALHYAAMHGRARIARLL 109
Cdd:COG0666    28 AALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD-GGNTLLHAAARNGDLEIVKLL 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113563440 110 LEsehRSDIINAKSNDGWTPLHVAAHYGRDSFVTLLLEFKAEVDPLSDKGTTPLQLAIIRERSSCVKILLDHNANIDIQN 189
Cdd:COG0666   107 LE---AGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARD 183

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2113563440 190 GF---LLRYAVLKSNHSYCRMFLQRGADTNLgRLEDGQTPLHISALRDDVLCARMLYNYGADTNTRNYEGQTPLD 261
Cdd:COG0666   184 NDgetPLHLAAENGHLEIVKLLLEAGADVNA-KDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALL 257
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
30-189 2.07e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 116.59  E-value: 2.07e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113563440  30 AVAVGDVHTVRTMLEQGYSPNGRDTNGWTLLHFSAARGKERCVRVFLEHGADPTVKDlIGGFTALHYAAMHGRARIARLL 109
Cdd:COG0666   127 AAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARD-NDGETPLHLAAENGHLEIVKLL 205

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113563440 110 LEseHRSDIiNAKSNDGWTPLHVAAHYGRDSFVTLLLEFKAEVDPLSDKGTTPLQLAIIRERSSCVKILLDHNANIDIQN 189
Cdd:COG0666   206 LE--AGADV-NAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282
SOCS_ASB7 cd03726
SOCS (suppressors of cytokine signaling) box of ASB7-like proteins. ASB family members have a ...
 282-326 9.69e-24

SOCS (suppressors of cytokine signaling) box of ASB7-like proteins. ASB family members have a C-terminal SOCS box and an N-terminal ankyrin-related sequence. The general function of the SOCS box is the recruitment of the ubiquitin-transferase system. The SOCS box interacts with Elongins B and C, Cullin-5 or Cullin-2, Rbx-1, and E2. Therefore, SOCS-box-containing proteins probably function as E3 ubiquitin ligases and mediate the degradation of proteins associated through their N-terminal regions.


Pssm-ID: 239696  Cd Length: 45  Bit Score: 91.83  E-value: 9.69e-24
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2113563440 282 RQPRYLQDLCRIKIRYCIGLQNLKLLDELPIARVMKDYLKHKFDD 326
Cdd:cd03726     1 RQPRTLQDLCRIKIRHCIGLQNLKLLDELPIAKVMKDYLKHKFDD 45
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
85-260 5.17e-22

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 93.87  E-value: 5.17e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113563440  85 KDLIGGFTALHYAAMHGRARIARLLLESEHRSDIINAKSNDGWTPLHVAAHYGRDSFVTLLLEFKAEVDPLSDKGTTPLQ 164
Cdd:COG0666    13 AALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLH 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113563440 165 LAIIRERSSCVKILLDHNANIDIQNGF---LLRYAVLKSNHSYCRMFLQRGADTNLgRLEDGQTPLHISALRDDVLCARM 241
Cdd:COG0666    93 AAARNGDLEIVKLLLEAGADVNARDKDgetPLHLAAYNGNLEIVKLLLEAGADVNA-QDNDGNTPLHLAAANGNLEIVKL 171

                         170
                  ....*....|....*....
gi 2113563440 242 LYNYGADTNTRNYEGQTPL 260
Cdd:COG0666   172 LLEAGADVNARDNDGETPL 190
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 30-262 7.98e-22

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 95.06  E-value: 7.98e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113563440  30 AVAVGDVHTVRTMLEQGYSPNGRDTNGWTLLHFSAARGKERCVRVFLEHGADPTVKdLIGGFTALHYAAMHGRARIARLL 109
Cdd:PHA02875    9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVK-YPDIESELHDAVEEGDVKAVEEL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113563440 110 LESEHRSDIINAKsnDGWTPLHVAAHYGRDSFVTLLLEFKAEVDPLSDKGTTPLQLAIIRERSSCVKILLDHNANIDIQN 189
Cdd:PHA02875   88 LDLGKFADDVFYK--DGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIED 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113563440 190 GF---LLRYAVLKSNHSYCRMFLQRGADTN-LGRleDGQTPLHISALRDDVL-CARMLYNYGADTN---TRNYEGQTPLD 261
Cdd:PHA02875  166 CCgctPLIIAMAKGDIAICKMLLDSGANIDyFGK--NGCVAALCYAIENNKIdIVRLFIKRGADCNimfMIEGEECTILD 243


                  .
gi 2113563440 262 V 262
Cdd:PHA02875  244 M 244
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 72-264 2.77e-20

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 91.09  E-value: 2.77e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113563440  72 VRVFLEHGADPTVKDLIGGFTALHYAAMHGRARIARLLLESEHRSDIINAKSNdgwTPLHVAAHYGRDSFVTLLLEFKAE 151
Cdd:PHA02878  150 TKLLLSYGADINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNN---SPLHHAVKHYNKPIVHILLENGAS 226

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113563440 152 VDPLSDKGTTPLQLAIirersscvkilldhnanidiqnGFLLRYAVLKsnhsycrMFLQRGADTNLGRLEDGQTPLHISA 231
Cdd:PHA02878  227 TDARDKCGNTPLHISV----------------------GYCKDYDILK-------LLLEHGVDVNAKSYILGLTALHSSI 277

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2113563440 232 LRDDVLcaRMLYNYGADTNTRNYEGQTPLDVSL 264
Cdd:PHA02878  278 KSERKL--KLLLEYGADINSLNSYKLTPLSSAV 308
Ank_2 pfam12796
Ankyrin repeats (3 copies);
94-189 3.87e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 83.24  E-value: 3.87e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113563440  94 LHYAAMHGRARIARLLLESEHRsdiINAKSNDGWTPLHVAAHYGRDSFVTLLLEfKAEVDpLSDKGTTPLQLAIIRERSS 173
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGAD---ANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVN-LKDNGRTALHYAARSGHLE 75

                          90
                  ....*....|....*.
gi 2113563440 174 CVKILLDHNANIDIQN 189
Cdd:pfam12796  76 IVKLLLEKGADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 38-264 5.84e-20

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 90.02  E-value: 5.84e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113563440  38 TVRTMLEQGYSPNGRDTNGWTLLHFSAARGKERCVRVFLEHGADPTVKDlIGGFTALHYAAMHGRARIARLLLEsehRSD 117
Cdd:PHA02874  106 MIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIED-DNGCYPIHIAIKHNFFDIIKLLLE---KGA 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113563440 118 IINAKSNDGWTPLHVAAHYGRDSFVTLLLEFKAEVDPLSDKGTTPLQLAIIRERSscVKILLDHNANIDIQNgfllryav 197
Cdd:PHA02874  182 YANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRS--AIELLINNASINDQD-------- 251

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2113563440 198 lksnhsycrmflqrgadtnlgrlEDGQTPLH--ISALRDDVLCARMLYNyGADTNTRNYEGQTPLDVSL 264
Cdd:PHA02874  252 -----------------------IDGSTPLHhaINPPCDIDIIDILLYH-KADISIKDNKGENPIDTAF 296
Ank_2 pfam12796
Ankyrin repeats (3 copies);
60-153 8.23e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 77.08  E-value: 8.23e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113563440  60 LHFSAARGKERCVRVFLEHGADPTVKDLIgGFTALHYAAMHGRARIARLLLESEHRSDIinaksNDGWTPLHVAAHYGRD 139
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKN-GRTALHLAAKNGHLEIVKLLLEHADVNLK-----DNGRTALHYAARSGHL 74

                          90
                  ....*....|....
gi 2113563440 140 SFVTLLLEFKAEVD 153
Cdd:pfam12796  75 EIVKLLLEKGADIN 88
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 39-251 1.19e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 83.18  E-value: 1.19e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113563440  39 VRTMLEQGYSPNGRDTNGWTLLHF------SAARGKErCVRVFLEHGADPTVKDlIGGFTALHYAAMH--GRARIARLLL 110
Cdd:PHA03100   51 VKILLDNGADINSSTKNNSTPLHYlsnikyNLTDVKE-IVKLLLEYGANVNAPD-NNGITPLLYAISKksNSYSIVEYLL 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113563440 111 esEHRSDiINAKSNDGWTPLHVAAHYGRDSF--VTLLLEFKAEVDplsdkgttplqlAIIRersscVKILLDHNANIDIQ 188
Cdd:PHA03100  129 --DNGAN-VNIKNSDGENLLHLYLESNKIDLkiLKLLIDKGVDIN------------AKNR-----VNYLLSYGVPINIK 188

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2113563440 189 N--GFL-LRYAVLKSNHSYCRMFLQRGADTNLgRLEDGQTPLHISALRDDVLCARMLYNYGADTNT 251
Cdd:PHA03100  189 DvyGFTpLHYAVYNNNPEFVKYLLDLGANPNL-VNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
Ank_2 pfam12796
Ankyrin repeats (3 copies);
30-120 8.91e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 74.38  E-value: 8.91e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113563440  30 AVAVGDVHTVRTMLEQGYSPNGRDTNGWTLLHFSAARGKERCVRVFLEHGAdptVKDLIGGFTALHYAAMHGRARIARLL 109
Cdd:pfam12796   4 AAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD---VNLKDNGRTALHYAARSGHLEIVKLL 80

                          90
                  ....*....|.
gi 2113563440 110 LESEHRSDIIN 120
Cdd:pfam12796  81 LEKGADINVKD 91
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 9-217 1.13e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 80.04  E-value: 1.13e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113563440   9 RMLHHHCRRNPELQEELR-IQGAVAVGDVHTVRTMLEQGYSPNGRDTNGWTLLHFSAARGKERCVRVFLEHGA---DPTV 84
Cdd:PHA02875   20 RLLDIGINPNFEIYDGISpIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKfadDVFY 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113563440  85 KDligGFTALHYAAMHGRARIARLLLESEHRSDIinaKSNDGWTPLHVAAHYGRDSFVTLLLEFKAEVDPLSDKGTTPLQ 164
Cdd:PHA02875  100 KD---GMTPLHLATILKKLDIMKLLIARGADPDI---PNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLI 173

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2113563440 165 LAIIRERSSCVKILLDHNANIDI--QNG--FLLRYAVLKSNHSYCRMFLQRGADTNL 217
Cdd:PHA02875  174 IAMAKGDIAICKMLLDSGANIDYfgKNGcvAALCYAIENNKIDIVRLFIKRGADCNI 230
PHA03095 PHA03095
ankyrin-like protein; Provisional
 35-186 1.31e-16

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 80.07  E-value: 1.31e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113563440  35 DVHTVRTMLEQGYSPNGRDTNGWTLLHFSA--ARGKERCVRVFLEHGADPTVKDLIGGfTALHYAAMHGRARIARLLLES 112
Cdd:PHA03095  166 NVELLRLLIDAGADVYAVDDRFRSLLHHHLqsFKPRARIVRELIRAGCDPAATDMLGN-TPLHSMATGSSCKRSLVLPLL 244

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2113563440 113 EHRSDIiNAKSNDGWTPLHVAAHYGRDSFVTLLLEFKAEVDPLSDKGTTPLQLAIIRERSSCVKILLDHNANID 186
Cdd:PHA03095  245 IAGISI-NARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAE 317
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 22-281 5.88e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 78.57  E-value: 5.88e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113563440  22 QEELRIQGAVAVGDVHTVRTMLEQGYSPNGRDTNGWTLLHF-SAARGKERCVRVFLEHGADPTVKDlIGGFTALHYAAMH 100
Cdd:PHA02876  239 KNDLSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHaSQAPSLSRLVPKLLERGADVNAKN-IKGETPLYLMAKN 317

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113563440 101 G--RARIARLLLesehRSDIINAKSNDGWTPLHVAAHYGRDS-FVTLLLEFKAEVDPLSDKGTTPLQLAIIRERSSCVKI 177
Cdd:PHA02876  318 GydTENIRTLIM----LGADVNAADRLYITPLHQASTLDRNKdIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINT 393

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113563440 178 LLDHNANIDIQN---GFLLRYAVLKSN-HSYCRMFLQRGADTNlGRLEDGQTPLHISALRD---DVLcaRMLYNYGADTN 250
Cdd:PHA02876  394 LLDYGADIEALSqkiGTALHFALCGTNpYMSVKTLIDRGANVN-SKNKDLSTPLHYACKKNcklDVI--EMLLDNGADVN 470

                         250       260       270
                  ....*....|....*....|....*....|.
gi 2113563440 251 TRNYEGQTPLDVSLSISETSRPCLDFLQEVR 281
Cdd:PHA02876  471 AINIQNQYPLLIALEYHGIVNILLHYGAELR 501
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 30-189 1.43e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 76.93  E-value: 1.43e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113563440  30 AVAVGDVHTVRTMLEQGYSPNGRDTNGWTLLHFSAARGKERCVRVFLEHGADPTVKDLIGGfTALHYAAMHGRARIARLL 109
Cdd:PHA02874  131 AIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGE-SPLHNAAEYGDYACIKLL 209

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113563440 110 LesEHRSDIINaKSNDGWTPLHVAAHYGRdSFVTLLLEfKAEVDPLSDKGTTPLQLAIireRSSC----VKILLDHNANI 185
Cdd:PHA02874  210 I--DHGNHIMN-KCKNGFTPLHNAIIHNR-SAIELLIN-NASINDQDIDGSTPLHHAI---NPPCdidiIDILLYHKADI 281


                  ....
gi 2113563440 186 DIQN 189
Cdd:PHA02874  282 SIKD 285
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 35-193 1.69e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 76.63  E-value: 1.69e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113563440  35 DVHTVRTMLEQGYSPNGRDTNGWTLLHFSAARGKE--RCVRVFLEHGADPTVKDLIGgFTALHYAAMHGRA--RIARLLL 110
Cdd:PHA03100   85 VKEIVKLLLEYGANVNAPDNNGITPLLYAISKKSNsySIVEYLLDNGANVNIKNSDG-ENLLHLYLESNKIdlKILKLLI 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113563440 111 EseHRSDI---------------INAKSNDGWTPLHVAAHYGRDSFVTLLLEFKAEVDPLSDKGTTPLQLAIIRERSSCV 175
Cdd:PHA03100  164 D--KGVDInaknrvnyllsygvpINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIF 241

                         170
                  ....*....|....*...
gi 2113563440 176 KILLDHNANIDIQNGFLL 193
Cdd:PHA03100  242 KLLLNNGPSIKTIIETLL 259
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 67-260 1.73e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 76.63  E-value: 1.73e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113563440  67 GKERCVRVFLEHGA-------DPTVKDLIggfTALHYAAMHGRARIARLLLESEHRsdiINAKSNDGWTPLHVAAHY--- 136
Cdd:PHA03100    8 TKSRIIKVKNIKYIimeddlnDYSYKKPV---LPLYLAKEARNIDVVKILLDNGAD---INSSTKNNSTPLHYLSNIkyn 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113563440 137 -GRD-SFVTLLLEFKAEVDPLSDKGTTPLQLAIIRER--SSCVKILLDHNANIDIQN--GFLLRYAVLKSNH---SYCRM 207
Cdd:PHA03100   82 lTDVkEIVKLLLEYGANVNAPDNNGITPLLYAISKKSnsYSIVEYLLDNGANVNIKNsdGENLLHLYLESNKidlKILKL 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2113563440 208 FLQRGADTN----------LGRLED-----GQTPLHISALRDDVLCARMLYNYGADTNTRNYEGQTPL 260
Cdd:PHA03100  162 LIDKGVDINaknrvnyllsYGVPINikdvyGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPL 229
PHA03095 PHA03095
ankyrin-like protein; Provisional
 39-260 1.56e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 73.91  E-value: 1.56e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113563440  39 VRTMLEQGYSPNGRDTNGWTLLHFSAARG-KERCVRVFLEHGADPTVKDLIgGFTALH-YAA-MHGRARIARLLLesEHR 115
Cdd:PHA03095   66 VRLLLEAGADVNAPERCGFTPLHLYLYNAtTLDVIKLLIKAGADVNAKDKV-GRTPLHvYLSgFNINPKVIRLLL--RKG 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113563440 116 SDiINAKSNDGWTPLHVAAHYGRDSFVTLLLEFKAEVDPLS--DKGTTPLQ--LAIIRERSSCVKILLDHNANIDIQNGF 191
Cdd:PHA03095  143 AD-VNALDLYGMTPLAVLLKSRNANVELLRLLIDAGADVYAvdDRFRSLLHhhLQSFKPRARIVRELIRAGCDPAATDML 221

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2113563440 192 LLRYAVLKSNHSYCRM-----FLQRGADTNLgRLEDGQTPLHI-SALRDDVLCARMLyNYGADTNTRNYEGQTPL 260
Cdd:PHA03095  222 GNTPLHSMATGSSCKRslvlpLLIAGISINA-RNRYGQTPLHYaAVFNNPRACRRLI-ALGADINAVSSDGNTPL 294
Ank_2 pfam12796
Ankyrin repeats (3 copies);
130-253 1.83e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 67.83  E-value: 1.83e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113563440 130 LHVAAHYGRDSFVTLLLEFKAEVDPLSDKGTTPLQLAIIRERSSCVKILLDHnANIDIQNgfllryavlksnhsycrmfl 209
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-------------------- 59

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2113563440 210 qrgadtnlgrleDGQTPLHISALRDDVLCARMLYNYGADTNTRN 253
Cdd:pfam12796  60 ------------NGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 35-277 9.71e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 71.59  E-value: 9.71e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113563440  35 DVHTVRTMLEQGYSPNGRDTNGWTLLHFSAARGKERC---VRVFLEHGADPTVKDlIGGFTALHYAAMHG-RARIARLLL 110
Cdd:PHA03095   26 TVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVkdiVRLLLEAGADVNAPE-RCGFTPLHLYLYNAtTLDVIKLLI 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113563440 111 EseHRSDIiNAKSNDGWTPLHV-----AAHYGrdsFVTLLLEFKAEVDPLSDKGTTPLQLAIIRersscvkilldHNANI 185
Cdd:PHA03095  105 K--AGADV-NAKDKVGRTPLHVylsgfNINPK---VIRLLLRKGADVNALDLYGMTPLAVLLKS-----------RNANV 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113563440 186 DiqngfLLRYAVLKSNHSYCRMFlqrgadtnlgrleDGQTPLHISA--LRDDVLCARMLYNYGADTNTRNYEGQTPLDVS 263
Cdd:PHA03095  168 E-----LLRLLIDAGADVYAVDD-------------RFRSLLHHHLqsFKPRARIVRELIRAGCDPAATDMLGNTPLHSM 229

                         250
                  ....*....|....
gi 2113563440 264 LSISETSRPCLDFL 277
Cdd:PHA03095  230 ATGSSCKRSLVLPL 243
SOCS_ASB_like cd03716
SOCS (suppressors of cytokine signaling) box of ASB (ankyrin repeat and SOCS box) and SSB ...
 282-323 1.01e-11

SOCS (suppressors of cytokine signaling) box of ASB (ankyrin repeat and SOCS box) and SSB (SPRY domain-containing SOCS box proteins) protein families. ASB family members have a C-terminal SOCS box and an N-terminal ankyrin-related sequence of a variable number of repeats. SSB proteins contain a central SPRY domain and a C-terminal SOCS. Recently, it has been shown that all four SSB proteins interact with the MET, the receptor protein-tyrosine kinase for hepatocyte growth factor (HGF), and that SSB-1, SSB-2, and SSB-4 interact with prostate apoptosis response protein-4. Both types of interactions are mediated through the SPRY domain.


Pssm-ID: 239686  Cd Length: 42  Bit Score: 58.66  E-value: 1.01e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2113563440 282 RQPRYLQDLCRIKIRYCIGLQNLKLLDELPIARVMKDYLKHK 323
Cdd:cd03716     1 STPRSLQHLCRLAIRRCLGRRRLELIKKLPLPPRLKDYLLYE 42
SOCS cd03587
SOCS (suppressors of cytokine signaling) box. The SOCS box is found in the C-terminal region ...
 283-323 1.83e-11

SOCS (suppressors of cytokine signaling) box. The SOCS box is found in the C-terminal region of CIS/SOCS family proteins (in combination with a SH2 domain), ASBs (ankyrin repeat-containing proteins with a SOCS box), SSBs (SPRY domain-containing proteins with a SOCS box), and WSBs (WD40 repeat-containing proteins with a SOCS box), as well as, other miscellaneous proteins. The function of the SOCS box is the recruitment of the ubiquitin-transferase system. The SOCS box interacts with Elongins B and C, Cullin-5 or Cullin-2, Rbx-1, and E2. Therefore, SOCS-box-containing proteins probably function as E3 ubiquitin ligases and mediate the degradation of proteins associated through their N-terminal regions.


Pssm-ID: 239641  Cd Length: 41  Bit Score: 58.25  E-value: 1.83e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2113563440 283 QPRYLQDLCRIKIRYCIGLQNLKLLDELPIARVMKDYLKHK 323
Cdd:cd03587     1 NPRSLQHLCRLAIRRCLGKRRLDLIDKLPLPPRLKDYLLYK 41
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 22-264 4.20e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 63.93  E-value: 4.20e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113563440  22 QEELRIqgavavgdvhtVRTMLEQGYSPNGRDTNGWTLLHFSAARGKERCVRVFLEHGADPTVKDLiGGFTALHYAAMHG 101
Cdd:PHA02876  155 QDELLI-----------AEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIAL-DDLSVLECAVDSK 222

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113563440 102 RARIARLLLESehRSDI-------INAKSNDGW---------------------TPLHVAAHYGRDS-FVTLLLEFKAEV 152
Cdd:PHA02876  223 NIDTIKAIIDN--RSNInkndlslLKAIRNEDLetslllydagfsvnsiddcknTPLHHASQAPSLSrLVPKLLERGADV 300

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113563440 153 DPLSDKGTTPLQL-AIIRERSSCVKILL----DHNANIDIQNGFLLRYAVLKSNHSYCRMFLQRGADTNLGRLEDgQTPL 227
Cdd:PHA02876  301 NAKNIKGETPLYLmAKNGYDTENIRTLImlgaDVNAADRLYITPLHQASTLDRNKDIVITLLELGANVNARDYCD-KTPI 379

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 2113563440 228 HISALRDDVLCARMLYNYGADTNTRNYEGQTPLDVSL 264
Cdd:PHA02876  380 HYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAL 416
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 30-189 7.88e-11

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 62.96  E-value: 7.88e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113563440  30 AVAVGDVHTVRTMLEQGYSPNGRDTNGWTLLHFSAARGKERCVRVFLEHGADPTVKDlIGGFTALHYAAMHGRARIARLL 109
Cdd:PLN03192  532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRD-ANGNTALWNAISAKHHKIFRIL 610

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113563440 110 LESEHRSDiinakSNDGWTPLHVAAHYGRDSFVTLLLEFKAEVDPLSDKGTTPLQLAIIRERSSCVKILLDHNANIDIQN 189
Cdd:PLN03192  611 YHFASISD-----PHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAN 685
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 32-110 5.08e-10

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 60.30  E-value: 5.08e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2113563440  32 AVGDVHTVRTMLEQGYSPNGRDTNGWTLLHFSAARGKERCVRVFLEHGADPTVKDLIGGfTALHYAAMHGRARIARLLL 110
Cdd:PTZ00322   91 ASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGK-TPLELAEENGFREVVQLLS 168
Ank_4 pfam13637
Ankyrin repeats (many copies);
56-110 1.26e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.43  E-value: 1.26e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2113563440  56 GWTLLHFSAARGKERCVRVFLEHGADPTVKDlIGGFTALHYAAMHGRARIARLLL 110
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVD-GNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 81-181 8.49e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.83  E-value: 8.49e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113563440  81 DPTVKDLIGgfTALHYAAMHGRARIARLLLESEHRSdiiNAKSNDGWTPLHVAAHYGRDSFVTLLLEFKAEVDPLSDKGT 160
Cdd:PTZ00322   75 DPVVAHMLT--VELCQLAASGDAVGARILLTGGADP---NCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGK 149

                          90       100
                  ....*....|....*....|.
gi 2113563440 161 TPLQLAIIRERSSCVKILLDH 181
Cdd:PTZ00322  150 TPLELAEENGFREVVQLLSRH 170
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 93-270 1.61e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 55.38  E-value: 1.61e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113563440  93 ALHYAAMHGRARIARLLLESEHRSdiiNAKSNDGWTPLHVAAHYGRDSFVTLLLEFKAEVDPLSDKGTTPLQLAIIRERS 172
Cdd:PHA02875    5 ALCDAILFGELDIARRLLDIGINP---NFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113563440 173 SCVKILLDHNANID---IQNGFL-LRYAVLKSNHSYCRMFLQRGADTNLGRlEDGQTPLHISALRDDVLCARMLYNYGAD 248
Cdd:PHA02875   82 KAVEELLDLGKFADdvfYKDGMTpLHLATILKKLDIMKLLIARGADPDIPN-TDKFSPLHLAVMMGDIKGIELLIDHKAC 160

                         170       180
                  ....*....|....*....|..
gi 2113563440 249 TNTRNYEGQTPLDVSLSISETS 270
Cdd:PHA02875  161 LDIEDCCGCTPLIIAMAKGDIA 182
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 35-217 2.73e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 54.89  E-value: 2.73e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113563440  35 DVHTVRTMLEQGYSPNGRDTNGWTLLHFSAARGKERCVRVFLEHGADPTVKDLIGGfTALHYAAmhGRAR---IARLLLE 111
Cdd:PHA02878  180 DQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGN-TPLHISV--GYCKdydILKLLLE 256

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113563440 112 sehRSDIINAKSN-DGWTPLHVAAHYGRDsfVTLLLEFKAEVDPLSDKGTTPLQLAII-RERSSCVKILLDH-----NAN 184
Cdd:PHA02878  257 ---HGVDVNAKSYiLGLTALHSSIKSERK--LKLLLEYGADINSLNSYKLTPLSSAVKqYLCINIGRILISNicllkRIK 331

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2113563440 185 IDIQN--GFLLR------YAVLKSNHSYCRMFLQRGADTNL 217
Cdd:PHA02878  332 PDIKNseGFIDNmdcitsNKRLNQIKDKCEDELNRLASIKI 372
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 95-265 4.32e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 54.49  E-value: 4.32e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113563440  95 HYAAMHGrARIARLLLESEHRSDIINAKSNdgwtpLHVAAHYGRDSFVTLLLEFKAEVDPLSDKGTTPLQLAIIRERSSC 174
Cdd:PLN03192  500 HHKELHD-LNVGDLLGDNGGEHDDPNMASN-----LLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDC 573

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113563440 175 VKILLDHNANI---DIQNGFLLRYAVLKSNHSYCRMFLQrgadtnLGRLEDGQTP---LHISALRDDVLCARMLYNYGAD 248
Cdd:PLN03192  574 VLVLLKHACNVhirDANGNTALWNAISAKHHKIFRILYH------FASISDPHAAgdlLCTAAKRNDLTAMKELLKQGLN 647

                         170
                  ....*....|....*..
gi 2113563440 249 TNTRNYEGQTPLDVSLS 265
Cdd:PLN03192  648 VDSEDHQGATALQVAMA 664
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 136-277 5.87e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 53.90  E-value: 5.87e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113563440 136 YGRDSFVTLLLEFKA-----EVDPLSDKGTTPLQLAIIRERSSCVKILLDHNANIDIQNGFLLRYAVLKSNHSY------ 204
Cdd:PHA03100    7 LTKSRIIKVKNIKYIimeddLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvk 86

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2113563440 205 --CRMFLQRGADTNLGRLEdGQTPLH--ISALRDDVLCARMLYNYGADTNTRNYEGQTPLDVSLSISETSRPCLDFL 277
Cdd:PHA03100   87 eiVKLLLEYGANVNAPDNN-GITPLLyaISKKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLKILKLL 162
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 193-323 7.88e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 53.06  E-value: 7.88e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113563440 193 LRYAVLKSNHSYCRMFLQRGADTNLGRLEDGQTPLHISALRDDVLCARMLYNYGADTNTRNYEGQTPLDVSLSIsetsrp 272
Cdd:PHA02884   74 LIYAIDCDNDDAAKLLIRYGADVNRYAEEAKITPLYISVLHGCLKCLEILLSYGADINIQTNDMVTPIELALMI------ 147

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2113563440 273 CLDFLQEVRRQpRYLQDLCRIKIRYCIGLQNLKLLDELPIARVMKDYLKHK 323
Cdd:PHA02884  148 CNNFLAFMICD-NEISNFYKHPKKILINFDILKILVSHFILQASNDRLNEK 197
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 75-260 1.13e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 53.04  E-value: 1.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113563440  75 FLEHGADPTVKDLIGgftalhyAAMHGRARIARLLLESEHRSDIINAKSNDgwtPLHVAAHYGRDSFVTLLLefkaevdp 154
Cdd:PHA02874   27 CINISVDETTTPLID-------AIRSGDAKIVELFIKHGADINHINTKIPH---PLLTAIKIGAHDIIKLLI-------- 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113563440 155 lsDKGTTPLQLAIIRERSSCVKILLDHNANIDIQNGFL---LRYAVLKSNHSYCRMFLQRGADTNLgRLEDGQTPLHISA 231
Cdd:PHA02874   89 --DNGVDTSILPIPCIEKDMIKTILDCGIDVNIKDAELktfLHYAIKKGDLESIKMLFEYGADVNI-EDDNGCYPIHIAI 165

                         170       180
                  ....*....|....*....|....*....
gi 2113563440 232 LRDDVLCARMLYNYGADTNTRNYEGQTPL 260
Cdd:PHA02874  166 KHNFFDIIKLLLEKGAYANVKDNNGESPL 194
Ank_4 pfam13637
Ankyrin repeats (many copies);
126-179 2.20e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.88  E-value: 2.20e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2113563440 126 GWTPLHVAAHYGRDSFVTLLLEFKAEVDPLSDKGTTPLQLAIIRERSSCVKILL 179
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 206-263 2.37e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.21  E-value: 2.37e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2113563440 206 RMFLQRGADTNlGRLEDGQTPLHISALRDDVLCARMLYNYGADTNTRNYEGQTPLDVS 263
Cdd:PTZ00322   99 RILLTGGADPN-CRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELA 155
Ank_4 pfam13637
Ankyrin repeats (many copies);
92-146 2.53e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.88  E-value: 2.53e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2113563440  92 TALHYAAMHGRARIARLLLESEHRsdiINAKSNDGWTPLHVAAHYGRDSFVTLLL 146
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGAD---INAVDGNGETALHFAASNGNVEVLKLLL 54
SOCS_box pfam07525
SOCS box; The SOCS box acts as a bridge between specific substrate- binding domains and more ...
 283-321 1.48e-06

SOCS box; The SOCS box acts as a bridge between specific substrate- binding domains and more generic proteins that comprise a large family of E3 ubiquitin protein ligases.


Pssm-ID: 462192  Cd Length: 39  Bit Score: 44.08  E-value: 1.48e-06
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2113563440 283 QPRYLQDLCRIKIRYCIGLQNLKLLDELPIARVMKDYLK 321
Cdd:pfam07525   1 TPRSLQHLCRLAIRRALGKRRLGAIDKLPLPPLLKDYLL 39
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 30-274 2.01e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 49.19  E-value: 2.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113563440  30 AVAVGDVHTVRTMLEQGYSPNGRDTNGWTLLHFSAARGKERCVRVFLEHGADPTV-------KDLIggftalhyaamhgr 102
Cdd:PHA02874   42 AIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSIlpipcieKDMI-------------- 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113563440 103 ariaRLLLESEHRSDIINAKSNdgwTPLHVAAHYGRDSFVTLLLEFKAEVDPLSDKGTTPLQLAIIRERSSCVKILLDHN 182
Cdd:PHA02874  108 ----KTILDCGIDVNIKDAELK---TFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKG 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113563440 183 AnidiqngfllrYAVLKSNHsycrmflqrgadtnlgrledGQTPLHISALRDDVLCARMLYNYGADTNTRNYEGQTPLDV 262
Cdd:PHA02874  181 A-----------YANVKDNN--------------------GESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHN 229

                         250
                  ....*....|..
gi 2113563440 263 SLSISETSRPCL 274
Cdd:PHA02874  230 AIIHNRSAIELL 241
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
30-126 3.47e-06

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 48.03  E-value: 3.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113563440  30 AVAVGDVHTVRTMLEQGYSPNGRDTNGWTLLHFSAARGKERCVRVFLEHGADPTVKDLIGGfTALHYAAMHGRARIARLL 109
Cdd:COG0666   193 AAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGL-TALLLAAAAGAALIVKLL 271

                          90
                  ....*....|....*..
gi 2113563440 110 LESEHRSDIINAKSNDG 126
Cdd:COG0666   272 LLALLLLAAALLDLLTL 288
SOCS_SOCS_like cd03717
SOCS (suppressors of cytokine signaling) box of SOCS-like proteins. The CIS/SOCS family of ...
 283-321 4.22e-06

SOCS (suppressors of cytokine signaling) box of SOCS-like proteins. The CIS/SOCS family of proteins is characterized by the presence of a C-terminal SOCS box and a central SH2 domain. These intracellular proteins regulate the responses of immune cells to cytokines. Identified as negative regulators of the cytokine-JAK-STAT pathway, they seem to play a role in many immunological and pathological processes. The function of the SOCS box is the recruitment of the ubiquitin-transferase system. Related SOCS boxes are also present in Rab40-like proteins and insect proteins of unknown function that also contain a NEUZ (domain in neuralized proteins) domain.


Pssm-ID: 239687  Cd Length: 39  Bit Score: 42.97  E-value: 4.22e-06
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2113563440 283 QPRYLQDLCRIKIRYCIGLQNLkllDELPIARVMKDYLK 321
Cdd:cd03717     2 SVRSLQHLCRFVIRQCTRRDLI---DQLPLPRRLKDYLK 37
SOCS_ASB2 cd03721
SOCS (suppressors of cytokine signaling) box of ASB2-like proteins. ASB family members have a ...
 284-323 6.34e-06

SOCS (suppressors of cytokine signaling) box of ASB2-like proteins. ASB family members have a C-terminal SOCS box and an N-terminal ankyrin-related sequence. ASB2 targets specific proteins to destruction by the proteasome in leukemia cells that have been induced to differentiate. The general function of the SOCS box is the recruitment of the ubiquitin-transferase system. The SOCS box interacts with Elongins B and C, Cullin-5 or Cullin-2, Rbx-1, and E2. Therefore, SOCS-box-containing proteins probably function as E3 ubiquitin ligases and mediate the degradation of proteins associated through their N-terminal regions.


Pssm-ID: 239691  Cd Length: 45  Bit Score: 42.55  E-value: 6.34e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2113563440 284 PRYLQDLCRIKIRYCIGLQNLKLLDELPIARVMKDYLKHK 323
Cdd:cd03721     3 PRPLAHLCRLKVRTLIGINRIKLIDTLPLPPRLIRYLNHQ 42
PHA02946 PHA02946
ankyin-like protein; Provisional
 35-130 7.78e-06

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 47.36  E-value: 7.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113563440  35 DVHTVRTMLEQGYSPNGRDTNGWTLLHFSAARGKERCVRVFLEHGADPTVKDLIGGfTALHYAAMHGRARIARLLLESEH 114
Cdd:PHA02946   51 DERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHK-TPLYYLSGTDDEVIERINLLVQY 129

                          90
                  ....*....|....*.
gi 2113563440 115 RSDIINAKSNDGWTPL 130
Cdd:PHA02946  130 GAKINNSVDEEGCGPL 145
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 97-261 1.25e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 46.78  E-value: 1.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113563440  97 AAMHGRARIARLLLESEHRSDIINAKsndGWTPLHVAAHYGRDSFVTLLLEFKAEVDPLSDKGTTPLQLAIIRERSSCVK 176
Cdd:PLN03192  532 VASTGNAALLEELLKAKLDPDIGDSK---GRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFR 608

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113563440 177 ILLDHNANIDIQ-NGFLLRYAVLKSNHSYCRMFLQRGADTNlGRLEDGQTPLHISALRDDVLCARMLYNYGADTNTRN-Y 254
Cdd:PLN03192  609 ILYHFASISDPHaAGDLLCTAAKRNDLTAMKELLKQGLNVD-SEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANtD 687


                  ....*..
gi 2113563440 255 EGQTPLD 261
Cdd:PLN03192  688 DDFSPTE 694
Ank_5 pfam13857
Ankyrin repeats (many copies);
76-133 1.28e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.95  E-value: 1.28e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2113563440  76 LEHGADPTVKDLIGGFTALHYAAMHGRARIARLLLesEHRSDiINAKSNDGWTPLHVA 133
Cdd:pfam13857   2 LEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLL--AYGVD-LNLKDEEGLTALDLA 56
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 90-260 1.29e-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: 46.54  E-value: 1.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113563440  90 GFTALHYAAMHGRARIARLLLEsEHRSDIINAKSND---GWTPLHVAAHYGRDSFVTLLLEFKAEVDPLSDKGTtplqla 166
Cdd:cd22192    51 GETALHVAALYDNLEAAVVLME-AAPELVNEPMTSDlyqGETALHIAVVNQNLNLVRELIARGADVVSPRATGT------ 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113563440 167 IIRERSSCVKILLDHnanidiqngfLLRYAVLKSNHSYCRMFLQRGADTnlgRLED--GQTPLHISALRDDVLCARMLYN 244
Cdd:cd22192   124 FFRPGPKNLIYYGEH----------PLSFAACVGNEEIVRLLIEHGADI---RAQDslGNTVLHILVLQPNKTFACQMYD 190

                         170       180
                  ....*....|....*....|....*.
gi 2113563440 245 ----YGADTNT------RNYEGQTPL 260
Cdd:cd22192   191 lilsYDKEDDLqpldlvPNNQGLTPF 216
Ank_2 pfam12796
Ankyrin repeats (3 copies);
193-277 3.60e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 41.64  E-value: 3.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113563440 193 LRYAVLKSNHSYCRMFLQRGADTNLgRLEDGQTPLHISALRDDVLCARMLYNYgADTNTRNYeGQTPLDvsLSISETSRP 272
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANL-QDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALH--YAARSGHLE 75


                  ....*
gi 2113563440 273 CLDFL 277
Cdd:pfam12796  76 IVKLL 80
Ank_5 pfam13857
Ankyrin repeats (many copies);
113-166 3.71e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.79  E-value: 3.71e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2113563440 113 EHRSDIINAKSNDGWTPLHVAAHYGRDSFVTLLLEFKAEVDPLSDKGTTPLQLA 166
Cdd:pfam13857   3 EHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
SOCS smart00253
suppressors of cytokine signalling; suppressors of cytokine signalling
 281-323 3.72e-05

suppressors of cytokine signalling; suppressors of cytokine signalling


Pssm-ID: 128549  Cd Length: 43  Bit Score: 40.36  E-value: 3.72e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 2113563440  281 RRQPRYLQDLCRIKIRYCIGLQNLKlldELPIARVMKDYLKHK 323
Cdd:smart00253   4 PSNVPSLQHLCRFTIRRCTRTDQIK---TLPLPPKLKDYLSYY 43
SOCS_SSB1_4 cd03718
SOCS (suppressors of cytokine signaling) box of SSB1 and SSB4 (SPRY domain-containing SOCS box ...
 283-320 5.70e-05

SOCS (suppressors of cytokine signaling) box of SSB1 and SSB4 (SPRY domain-containing SOCS box proteins)-like proteins. SSB proteins contain a central SPRY domain and a C-terminal SOCS. SSB1 and SSB4 has been shown to bind to MET, the receptor protein-tyrosine kinase for hepatocyte growth factor (HGF) and also interacts with prostate apoptosis response protein-4. Both types of interactions are mediated through the SPRY domain. The general function of the SOCS box is the recruitment of the ubiquitin-transferase system. The SOCS box interacts with Elongins B and C, Cullin-5 or Cullin-2, Rbx-1, and E2. Therefore, SOCS-box-containing proteins probably function as E3 ubiquitin ligases and mediate the degradation of proteins associated through their N-terminal regions.


Pssm-ID: 239688  Cd Length: 42  Bit Score: 39.98  E-value: 5.70e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2113563440 283 QPRYLQDLCRIKIRYCIGLQNLKLLDELPIARVMKDYL 320
Cdd:cd03718     2 EPLPLMDLCRRRVRVALGRDRLEEIEQLPLPPSLKNYL 39
SOCS_SOCS1 cd03735
SOCS (suppressors of cytokine signaling) box of SOCS1-like proteins. Together with CIS1, the ...
 280-321 6.14e-05

SOCS (suppressors of cytokine signaling) box of SOCS1-like proteins. Together with CIS1, the CIS/SOCS family of proteins is characterized by the presence of a C-terminal SOCS box and a central SH2 domain. SOCS1, like CIS1 and SOCS3, is involved in the down-regulation of the JAK/STAT pathway. SOCS1 has a dual function as a direct potent JAK kinase inhibitor and as a component of an E3 ubiquitin-ligase complex recruiting substrates to the protein degradation machinery.


Pssm-ID: 239704  Cd Length: 43  Bit Score: 39.90  E-value: 6.14e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2113563440 280 VRRQPryLQDLCRIKIRYCIGLQNLkllDELPIARVMKDYLK 321
Cdd:cd03735     1 VRVRP--LQELCRKSIVATFGRENL---ARIPLNPVLKDYLK 37
SOCS_box smart00969
The SOCS box acts as a bridge between specific substrate- binding domains and more generic ...
 287-323 6.50e-05

The SOCS box acts as a bridge between specific substrate- binding domains and more generic proteins that comprise a large family of E3 ubiquitin protein ligases;


Pssm-ID: 198037  Cd Length: 34  Bit Score: 39.31  E-value: 6.50e-05
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 2113563440  287 LQDLCRIKIRyciglQNLKLLDELPIARVMKDYLKHK 323
Cdd:smart00969   3 LQHLCRLAIR-----RSLGGIDKLPLPPRLKDYLLYY 34
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 30-136 7.06e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 44.21  E-value: 7.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113563440  30 AVAVGDVHTVRTMLEQGYSPNGRDTNGWTLLHFSAARGKERCVRVFLEHGADPTVKDLIGGFTALHYAAMHGRARIARLL 109
Cdd:PHA02875  142 AVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIDIVRLF 221

                          90       100
                  ....*....|....*....|....*..
gi 2113563440 110 LESEHRSDIINAKSNDGWTPLHVAAHY 136
Cdd:PHA02875  222 IKRGADCNIMFMIEGEECTILDMICNM 248
Ank_4 pfam13637
Ankyrin repeats (many copies);
30-76 9.10e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.57  E-value: 9.10e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2113563440  30 AVAVGDVHTVRTMLEQGYSPNGRDTNGWTLLHFSAARGKERCVRVFL 76
Cdd:pfam13637   8 AAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
SOCS_SSB4 cd03743
SOCS (suppressors of cytokine signaling) box of SSB4 (SPRY domain-containing SOCS box ...
 283-323 2.04e-04

SOCS (suppressors of cytokine signaling) box of SSB4 (SPRY domain-containing SOCS box proteins)-like proteins. SSB proteins contain a central SPRY domain and a C-terminal SOCS. SSB4 has been shown to bind to MET, the receptor protein-tyrosine kinase for hepatocyte growth factor (HGF). SSB4, like SSB2 and SSB1, also interacts with prostate apoptosis response protein-4. Both types of interactions are mediated through the SPRY domain. The general function of the SOCS box is the recruitment of the ubiquitin-transferase system. The SOCS box interacts with Elongins B and C, Cullin-5 or Cullin-2, Rbx-1, and E2. Therefore, SOCS-box-containing proteins probably function as E3 ubiquitin ligases and mediate the degradation of proteins associated through their N-terminal regions.


Pssm-ID: 239712  Cd Length: 42  Bit Score: 38.40  E-value: 2.04e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2113563440 283 QPRYLQDLCRIKIRYCIGLQNLKLLDELPIARVMKDYLKHK 323
Cdd:cd03743     2 EPLPLMDLCRRSARQALGRHRLHHIQSLPLPQTLKNYLQYQ 42
Ank_5 pfam13857
Ankyrin repeats (many copies);
211-262 2.27e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.48  E-value: 2.27e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2113563440 211 RGADTNLGRLEdGQTPLHISALRDDVLCARMLYNYGADTNTRNYEGQTPLDV 262
Cdd:pfam13857   5 GPIDLNRLDGE-GYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDL 55
Ank_5 pfam13857
Ankyrin repeats (many copies);
48-97 2.33e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.48  E-value: 2.33e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2113563440  48 SPNGRDTNGWTLLHFSAARGKERCVRVFLEHGADPTVKDlIGGFTALHYA 97
Cdd:pfam13857   8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKD-EEGLTALDLA 56
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 113-309 3.59e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 42.17  E-value: 3.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113563440 113 EHRSDIINAKSndgWTPLHVAAHYGRDSFVTLLLEFKAEVDPLSDKGTTPLQLA-----------IIRERSSC------V 175
Cdd:PHA02878   27 ENYSTSASLIP---FIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIIckepnklgmkeMIRSINKCsvfytlV 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113563440 176 KI-LLDHNANIDIQNGFLLRYavLKSNHS------------------YCRMFLQRGADTNLGRLEDGQTPLHISALRDDV 236
Cdd:PHA02878  104 AIkDAFNNRNVEIFKIILTNR--YKNIQTidlvyidkkskddiieaeITKLLLSYGADINMKDRHKGNTALHYATENKDQ 181

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2113563440 237 LCARMLYNYGADTNTRNYEGQTPLdvSLSISETSRPCLDFLQEVRRQPRYlQDLC-----RIKIRYCIGLQNLKLLDE 309
Cdd:PHA02878  182 RLTELLLSYGANVNIPDKTNNSPL--HHAVKHYNKPIVHILLENGASTDA-RDKCgntplHISVGYCKDYDILKLLLE 256
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 55-86 3.75e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 37.27  E-value: 3.75e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2113563440  55 NGWTLLHFSAAR-GKERCVRVFLEHGADPTVKD 86
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
SOCS_ASB14 cd03730
SOCS (suppressors of cytokine signaling) box of ASB14-like proteins. ASB family members have a ...
 284-327 3.89e-04

SOCS (suppressors of cytokine signaling) box of ASB14-like proteins. ASB family members have a C-terminal SOCS box and an N-terminal ankyrin-related sequence. The general function of the SOCS box is the recruitment of the ubiquitin-transferase system. The SOCS box interacts with Elongins B and C, Cullin-5 or Cullin-2, Rbx-1, and E2. Therefore, SOCS-box-containing proteins probably function as E3 ubiquitin ligases and mediate the degradation of proteins associated through their N-terminal regions.


Pssm-ID: 239700  Cd Length: 57  Bit Score: 37.90  E-value: 3.89e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2113563440 284 PRYLQDLCRIKIRYCIGLQNLK---LLDELPIARVMKDYLKHKFDDI 327
Cdd:cd03730     3 PRSLKHLCRLKIRACMGRLRLRcpvFMSFLPLPNRLKAYILYKEYDL 49
SOCS_ASB5 cd03724
SOCS (suppressors of cytokine signaling) box of ASB5-like proteins. ASB family members have a ...
 284-323 4.41e-04

SOCS (suppressors of cytokine signaling) box of ASB5-like proteins. ASB family members have a C-terminal SOCS box and an N-terminal ankyrin-related sequence. ASB5 has been implicated in the initiation of arteriogenesis. The general function of the SOCS box is the recruitment of the ubiquitin-transferase system. The SOCS box interacts with Elongins B and C, Cullin-5 or Cullin-2, Rbx-1, and E2. Therefore, SOCS-box-containing proteins probably function as E3 ubiquitin ligases and mediate the degradation of proteins associated through their N-terminal regions.


Pssm-ID: 239694  Cd Length: 42  Bit Score: 37.55  E-value: 4.41e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2113563440 284 PRYLQDLCRIKIRYCIGLQNLKLLDELPIARVMKDYLKHK 323
Cdd:cd03724     3 PSSLCQLCRLCIRNYIGRSRLHLIPQLQLPTLLKNFLQYR 42
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 125-153 7.10e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 36.50  E-value: 7.10e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 2113563440 125 DGWTPLHVAA-HYGRDSFVTLLLEFKAEVD 153
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVN 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 158-189 8.90e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 36.11  E-value: 8.90e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2113563440 158 KGTTPLQLAIIRERS-SCVKILLDHNANIDIQN 189
Cdd:pfam00023   1 DGNTPLHLAAGRRGNlEIVKLLLSKGADVNARD 33
SOCS_ASB15 cd03731
SOCS (suppressors of cytokine signaling) box of ASB15-like proteins. ASB family members have a ...
 284-327 1.34e-03

SOCS (suppressors of cytokine signaling) box of ASB15-like proteins. ASB family members have a C-terminal SOCS box and an N-terminal ankyrin-related sequence. Human ASB15 is expressed predominantly in skeletal muscle and participates in the regulation of protein turnover and muscle cell development by stimulating protein synthesis and regulating differentiation of muscle cells. The general function of the SOCS box is the recruitment of the ubiquitin-transferase system. The SOCS box interacts with Elongins B and C, Cullin-5 or Cullin-2, Rbx-1, and E2. Therefore, SOCS-box-containing proteins probably function as E3 ubiquitin ligases and mediate the degradation of proteins associated through their N-terminal regions.


Pssm-ID: 239701  Cd Length: 56  Bit Score: 36.35  E-value: 1.34e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2113563440 284 PRYLQDLCRIKIRYCIGLQNLKLL---DELPIARVMKDYLKHKFDDI 327
Cdd:cd03731     3 PRPLKHLCRLKIRKLMGLQKLQQPssmKKLPLPPALKRYILYKEYDL 49
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 128-188 1.55e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 39.58  E-value: 1.55e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2113563440 128 TPLHVAAHYGRDSFVTLLLEFKAEVDPLSDKGT-TPLQLAIIRERSSCVKILLDHNANIDIQ 188
Cdd:PHA02884   72 NPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKiTPLYISVLHGCLKCLEILLSYGADINIQ 133
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 24-116 1.64e-03

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: 40.06  E-value: 1.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113563440  24 ELRIQGAVAVGDVHTVRTMLEQGYSPNGRDTNGWTLLH-------FSAARGKERC-----VRVFLEHGADPTVKDLI--- 88
Cdd:TIGR00870 176 ESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHllvmeneFKAEYEELSCqmynfALSLLDKLRDSKELEVIlnh 255

                          90       100
                  ....*....|....*....|....*...
gi 2113563440  89 GGFTALHYAAMHGRARIARLLLESEHRS 116
Cdd:TIGR00870 256 QGLTPLKLAAKEGRIVLFRLKLAIKYKQ 283
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 222-253 2.48e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 34.96  E-value: 2.48e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2113563440 222 DGQTPLHISALR-DDVLCARMLYNYGADTNTRN 253
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 60-137 2.56e-03

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 39.61  E-value: 2.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113563440  60 LHFSAARGKERCVRVFLEHGADPTVKDLIGGfTALHYAAMHGRARIA----RLLLESEHRSDII---NAKSNDGWTPLHV 132
Cdd:cd22192   140 LSFAACVGNEEIVRLLIEHGADIRAQDSLGN-TVLHILVLQPNKTFAcqmyDLILSYDKEDDLQpldLVPNNQGLTPFKL 218


                  ....*
gi 2113563440 133 AAHYG 137
Cdd:cd22192   219 AAKEG 223
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 125-153 2.66e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 34.93  E-value: 2.66e-03
                          10        20
                  ....*....|....*....|....*....
gi 2113563440 125 DGWTPLHVAAHYGRDSFVTLLLEFKAEVD 153
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
Ank_4 pfam13637
Ankyrin repeats (many copies);
159-209 2.74e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 35.33  E-value: 2.74e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2113563440 159 GTTPLQLAIIRERSSCVKILLDHNANIDIQNGF---LLRYAVLKSNHSYCRMFL 209
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNgetALHFAASNGNVEVLKLLL 54
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 125-153 3.17e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 34.49  E-value: 3.17e-03
                           10        20
                   ....*....|....*....|....*....
gi 2113563440  125 DGWTPLHVAAHYGRDSFVTLLLEFKAEVD 153
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 205-263 3.68e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 37.55  E-value: 3.68e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113563440 205 CRMFLQRGADTNLGRLEDGQTPLHISALRDDVLCARMLYNY-GADTNTRNYEGQTPLDVS 263
Cdd:PHA02736   74 LKLLMEWGADINGKERVFGNTPLHIAVYTQNYELATWLCNQpGVNMEILNYAFKTPYYVA 133
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 19-262 4.01e-03

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: 38.91  E-value: 4.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113563440  19 PELQEELRIQGAVAVGDVHTVRTMLE--QGYSPNGRDTNGWTLLHFSAARGK-ERCVRVFLEHGADPTVKDliggfTALH 95
Cdd:TIGR00870  13 PLSDEEKAFLPAAERGDLASVYRDLEepKKLNINCPDRLGRSALFVAAIENEnLELTELLLNLSCRGAVGD-----TLLH 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113563440  96 yAAMHGRARIARLLLEsehrsdIINAKSNDGWTPLHVAAHYGRDSFVtlllefkaevdplsdkGTTPLQLAIIRERSSCV 175
Cdd:TIGR00870  88 -AISLEYVDAVEAILL------HLLAAFRKSGPLELANDQYTSEFTP----------------GITALHLAAHRQNYEIV 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113563440 176 KILLDHNANIDI------------QNGF------LLRYAVLKSNhSYCRMFLQRGADTNLgRLEDGQTPLHISALRDDVL 237
Cdd:TIGR00870 145 KLLLERGASVPAracgdffvksqgVDSFyhgespLNAAACLGSP-SIVALLSEDPADILT-ADSLGNTLLHLLVMENEFK 222

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 2113563440 238 C-----ARMLYNYGADTNTR-----------NYEGQTPLDV 262
Cdd:TIGR00870 223 AeyeelSCQMYNFALSLLDKlrdskelevilNHQGLTPLKL 263
PHA02917 PHA02917
ankyrin-like protein; Provisional
 119-186 4.30e-03

ankyrin-like protein; Provisional


Pssm-ID: 165231 [Multi-domain]  Cd Length: 661  Bit Score: 38.83  E-value: 4.30e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2113563440 119 INAKSNDGWTPLHVAAHYGRDSFVTLLLEFKAEVDPLSDKGTTPLQLAIIRERS-SCVKILLDHNANID 186
Cdd:PHA02917  445 INMIDKRGETLLHKAVRYNKQSLVSLLLESGSDVNIRSNNGYTCIAIAINESRNiELLKMLLCHKPTLD 513
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 90-112 4.47e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 34.10  E-value: 4.47e-03
                           10        20
                   ....*....|....*....|...
gi 2113563440   90 GFTALHYAAMHGRARIARLLLES 112
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDK 24
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 158-187 4.79e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 34.10  E-value: 4.79e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 2113563440  158 KGTTPLQLAIIRERSSCVKILLDHNANIDI 187
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 56-166 5.24e-03

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 38.32  E-value: 5.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113563440  56 GWTLLHFSAARGKERCVRVFLEHGADPTVKDLIGGFT------------ALHYAAMHGRARIARLLLESEHRSDIINAKS 123
Cdd:cd21882    73 GQTALHIAIENRNLNLVRLLVENGADVSARATGRFFRkspgnlfyfgelPLSLAACTNQEEIVRLLLENGAQPAALEAQD 152

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2113563440 124 NDGWTPLHVAAHYGRDS-----FVT----LLLEFKAEVDPL-------SDKGTTPLQLA 166
Cdd:cd21882   153 SLGNTVLHALVLQADNTpensaFVCqmynLLLSYGAHLDPTqqleeipNHQGLTPLKLA 211
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 55-84 7.09e-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: 33.72  E-value: 7.09e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 2113563440   55 NGWTLLHFSAARGKERCVRVFLEHGADPTV 84
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 56-166 9.26e-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: 37.85  E-value: 9.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113563440  56 GWTLLHFSAARGKERCVRVFLEHGADPTV---------KDLIGGF----TALHYAAMHGRARIARLLLESEHRSDIINAK 122
Cdd:cd22193    76 GQTALHIAIERRQGDIVALLVENGADVHAhakgrffqpKYQGEGFyfgeLPLSLAACTNQPDIVQYLLENEHQPADIEAQ 155

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113563440 123 SNDGWTPLHVAAHYGRDS-----FVT----LLLEFKAEVDPLS-------DKGTTPLQLA 166
Cdd:cd22193   156 DSRGNTVLHALVTVADNTkentkFVTrmydMILIRGAKLCPTVeleeirnNDGLTPLQLA 215
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 56-166 9.71e-03

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 37.68  E-value: 9.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113563440  56 GWTLLHFSAARGKERCVRVFLEHGAD------------PTVKDLIG-GFTALHYAAMHGRARIARLLLesEHRSDIinaK 122
Cdd:cd22192    89 GETALHIAVVNQNLNLVRELIARGADvvspratgtffrPGPKNLIYyGEHPLSFAACVGNEEIVRLLI--EHGADI---R 163

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2113563440 123 SNDGW--TPLHVAAHYGRDSFVTLLLEFKAEVDPLSD----------KGTTPLQLA 166
Cdd:cd22192   164 AQDSLgnTVLHILVLQPNKTFACQMYDLILSYDKEDDlqpldlvpnnQGLTPFKLA 219
 
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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