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Conserved domains on  [gi|966965853|ref|XP_015004207|]
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ankyrin repeat domain-containing protein 60 [Macaca mulatta]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Ubl_ANKRD60 cd17063
ubiquitin-like (Ubl) domain found in ankyrin repeat domain-containing protein 60 (ANKRD60) and ...
 92-168 1.03e-39

ubiquitin-like (Ubl) domain found in ankyrin repeat domain-containing protein 60 (ANKRD60) and similar proteins; ANKRD60 is an uncharacterized ankyrin repeat domain-containing protein which also harbors a conserved ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, a common structure involved in protein-protein interactions.


:

Pssm-ID: 340583  Cd Length: 77  Bit Score: 134.71  E-value: 1.03e-39
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 966965853  92 DVFFLRVRLEETGEIFRVANCRGDMTVRELKEELDLMVGIPFNLQRLQYLDEGVLMDDTTLKFHDVVPGGIISLCIW 168
Cdd:cd17063    1 RLFSLKLRLPETEETFTVPNCYPGMKVKELKSRLELVTGIPSHLQRLSYLDEGDLMDDSTLKYNDIVPGATITLRVW 77
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
223-320 2.44e-19

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 86.55  E-value: 2.44e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966965853 223 ALYVASHRGHSDAVQYLLEHGASCLSRSPLGRTPLHVAAAMGRSDCISLLLQHGASIHDKDAKGETPISIAHRLNHTQSE 302
Cdd:COG0666  123 PLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIV 202

                         90
                 ....*....|....*...
gi 966965853 303 RqmFLLHQIAKSGIRDLN 320
Cdd:COG0666  203 K--LLLEAGADVNAKDND 218
 
Name Accession Description Interval E-value
Ubl_ANKRD60 cd17063
ubiquitin-like (Ubl) domain found in ankyrin repeat domain-containing protein 60 (ANKRD60) and ...
 92-168 1.03e-39

ubiquitin-like (Ubl) domain found in ankyrin repeat domain-containing protein 60 (ANKRD60) and similar proteins; ANKRD60 is an uncharacterized ankyrin repeat domain-containing protein which also harbors a conserved ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, a common structure involved in protein-protein interactions.


Pssm-ID: 340583  Cd Length: 77  Bit Score: 134.71  E-value: 1.03e-39
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 966965853  92 DVFFLRVRLEETGEIFRVANCRGDMTVRELKEELDLMVGIPFNLQRLQYLDEGVLMDDTTLKFHDVVPGGIISLCIW 168
Cdd:cd17063    1 RLFSLKLRLPETEETFTVPNCYPGMKVKELKSRLELVTGIPSHLQRLSYLDEGDLMDDSTLKYNDIVPGATITLRVW 77
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
223-320 2.44e-19

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 86.55  E-value: 2.44e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966965853 223 ALYVASHRGHSDAVQYLLEHGASCLSRSPLGRTPLHVAAAMGRSDCISLLLQHGASIHDKDAKGETPISIAHRLNHTQSE 302
Cdd:COG0666  123 PLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIV 202

                         90
                 ....*....|....*...
gi 966965853 303 RqmFLLHQIAKSGIRDLN 320
Cdd:COG0666  203 K--LLLEAGADVNAKDND 218
Ank_2 pfam12796
Ankyrin repeats (3 copies);
224-318 1.36e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 68.60  E-value: 1.36e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966965853  224 LYVASHRGHSDAVQYLLEHGASCLSRSPLGRTPLHVAAAMGRSDCISLLLQHGASihDKDAKGETPISIAHRLNHTQSER 303
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|....*
gi 966965853  304 qmFLLHQIAKSGIRD 318
Cdd:pfam12796  79 --LLLEKGADINVKD 91
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 231-314 1.50e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.06  E-value: 1.50e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966965853 231 GHSDAVQYLLEHGASCLSRSPLGRTPLHVAAAMGRSDCISLLLQHGASIHDKDAKGETPISIAHRlNHTQSERQMFLLHQ 310
Cdd:PTZ00322  93 GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEE-NGFREVVQLLSRHS 171


                 ....
gi 966965853 311 IAKS 314
Cdd:PTZ00322 172 QCHF 175
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 253-281 1.46e-06

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 44.12  E-value: 1.46e-06
                           10        20
                   ....*....|....*....|....*....
gi 966965853   253 GRTPLHVAAAMGRSDCISLLLQHGASIHD 281
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 204-306 9.29e-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: 44.23  E-value: 9.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966965853 204 SEHFEGEkwkqwtsqrafVALYVASHRGHSDAVQYLLEHGA---------SCLSRSP-----LGRTPLHVAAAMGRSDCI 269
Cdd:cd22192   84 SDLYQGE-----------TALHIAVVNQNLNLVRELIARGAdvvspratgTFFRPGPknliyYGEHPLSFAACVGNEEIV 152

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 966965853 270 SLLLQHGASIHDKDAKGETPISIAHRLNHTQSERQMF 306
Cdd:cd22192  153 RLLIEHGADIRAQDSLGNTVLHILVLQPNKTFACQMY 189
UBQ smart00213
Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of ...
 113-165 1.55e-04

Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of proteins required for controlling cell cycle progression


Pssm-ID: 214563 [Multi-domain]  Cd Length: 72  Bit Score: 39.55  E-value: 1.55e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 966965853   113 RGDMTVRELKEELDLMVGIPFNLQRLQYlDEGVLMDDTTLKFHDVVPGGIISL 165
Cdd:smart00213  18 KPSDTVSELKEKIAELTGIPPEQQRLIY-KGKVLEDDRTLADYGIQDGSTIHL 69
Ubiquitin_2 pfam14560
Ubiquitin-like domain; This entry contains ubiquitin-like domains.
 115-152 1.28e-03

Ubiquitin-like domain; This entry contains ubiquitin-like domains.


Pssm-ID: 405277  Cd Length: 83  Bit Score: 37.12  E-value: 1.28e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 966965853  115 DMTVRELKEELDLMVGIPFNLQRLQYLDEG-----VLMDDTTL 152
Cdd:pfam14560  22 SLTIEELKEKLELITGTPPSSMRLQLYDDDdnlvaKLDDDDAL 64
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 223-288 1.70e-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: 1.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966965853  223 ALYVASHRGHSDAVQYLLEHGAS---------CLSRSPL-----GRTPLHVAAAMGRSDCISLLLQHGASIHDKDAKGET 288
Cdd:TIGR00870 131 ALHLAAHRQNYEIVKLLLERGASvparacgdfFVKSQGVdsfyhGESPLNAAACLGSPSIVALLSEDPADILTADSLGNT 210
 
Name Accession Description Interval E-value
Ubl_ANKRD60 cd17063
ubiquitin-like (Ubl) domain found in ankyrin repeat domain-containing protein 60 (ANKRD60) and ...
 92-168 1.03e-39

ubiquitin-like (Ubl) domain found in ankyrin repeat domain-containing protein 60 (ANKRD60) and similar proteins; ANKRD60 is an uncharacterized ankyrin repeat domain-containing protein which also harbors a conserved ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, a common structure involved in protein-protein interactions.


Pssm-ID: 340583  Cd Length: 77  Bit Score: 134.71  E-value: 1.03e-39
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 966965853  92 DVFFLRVRLEETGEIFRVANCRGDMTVRELKEELDLMVGIPFNLQRLQYLDEGVLMDDTTLKFHDVVPGGIISLCIW 168
Cdd:cd17063    1 RLFSLKLRLPETEETFTVPNCYPGMKVKELKSRLELVTGIPSHLQRLSYLDEGDLMDDSTLKYNDIVPGATITLRVW 77
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
223-320 2.44e-19

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 86.55  E-value: 2.44e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966965853 223 ALYVASHRGHSDAVQYLLEHGASCLSRSPLGRTPLHVAAAMGRSDCISLLLQHGASIHDKDAKGETPISIAHRLNHTQSE 302
Cdd:COG0666  123 PLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIV 202

                         90
                 ....*....|....*...
gi 966965853 303 RqmFLLHQIAKSGIRDLN 320
Cdd:COG0666  203 K--LLLEAGADVNAKDND 218
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
223-330 2.82e-19

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 86.55  E-value: 2.82e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966965853 223 ALYVASHRGHSDAVQYLLEHGASCLSRSPLGRTPLHVAAAMGRSDCISLLLQHGASIHDKDAKGETPISIAHRLNHTQSE 302
Cdd:COG0666  156 PLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIV 235

                         90       100
                 ....*....|....*....|....*...
gi 966965853 303 RqMFLLHQIAKSGIRDLNDLVMKNALQR 330
Cdd:COG0666  236 K-LLLEAGADLNAKDKDGLTALLLAAAA 262
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
223-299 9.75e-17

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 79.23  E-value: 9.75e-17
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 966965853 223 ALYVASHRGHSDAVQYLLEHGASCLSRSPLGRTPLHVAAAMGRSDCISLLLQHGASIHDKDAKGETPISIAHRLNHT 299
Cdd:COG0666   90 LLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNL 166
Ank_2 pfam12796
Ankyrin repeats (3 copies);
224-318 1.36e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 68.60  E-value: 1.36e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966965853  224 LYVASHRGHSDAVQYLLEHGASCLSRSPLGRTPLHVAAAMGRSDCISLLLQHGASihDKDAKGETPISIAHRLNHTQSER 303
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|....*
gi 966965853  304 qmFLLHQIAKSGIRD 318
Cdd:pfam12796  79 --LLLEKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
223-322 2.77e-14

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 72.29  E-value: 2.77e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966965853 223 ALYVASHRGHSDAVQYLLEHGASCLSRSPLGRTPLHVAAAMGRSDCISLLLQHGASIHDKDAKGETPISIAHRLNHTQSE 302
Cdd:COG0666  189 PLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIV 268

                         90       100
                 ....*....|....*....|
gi 966965853 303 RQMFLLHQIAKSGIRDLNDL 322
Cdd:COG0666  269 KLLLLALLLLAAALLDLLTL 288
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
223-299 1.24e-09

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 58.43  E-value: 1.24e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 966965853 223 ALYVASHRGHSDAVQYLLEHGASCLSRSPLGRTPLHVAAAMGRSDCISLLLQHGASIHDKDAKGETPISIAHRLNHT 299
Cdd:COG0666   57 LLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNL 133
Ank_4 pfam13637
Ankyrin repeats (many copies);
223-273 3.82e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.89  E-value: 3.82e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 966965853  223 ALYVASHRGHSDAVQYLLEHGASCLSRSPLGRTPLHVAAAMGRSDCISLLL 273
Cdd:pfam13637   4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ubl_ubiquitin_like cd17039
ubiquitin-like (Ubl) domain found in ubiquitin and ubiquitin-like Ubl proteins; Ubiquitin-like ...
 96-165 6.01e-09

ubiquitin-like (Ubl) domain found in ubiquitin and ubiquitin-like Ubl proteins; Ubiquitin-like (Ubl) proteins have a similar ubiquitin (Ub) beta-grasp fold and attach to other proteins in a Ubl manner but with biochemically distinct roles. Ub and Ubl proteins conjugate and deconjugate via ligases and peptidases to covalently modify target polypeptides. Some Ubl domains have adaptor roles in Ub-signaling by mediating protein-protein interaction. Prokaryotic sulfur carrier proteins are Ub-related proteins that can be activated in an ATP-dependent manner. Polyubiquitination signals for a diverse set of cellular events via different isopeptide linkages formed between the C terminus of one ubiquitin (Ub) and the epsilon-amine of K6, K11, K27, K29, K33, K48, or K63 of a second Ub. One of these seven lysine residues (K27, Ub numbering) is conserved in this Ubl_ubiquitin_like family. K27-linked Ub chains are versatile and can be recognized by several downstream receptor proteins. K27 has roles beyond chain linkage, such as in Ubl NEDD8 (which contains many of the same lysines (K6, K11, K27, K33, K48) as Ub) where K27 has a role (other than conjugation) in the mechanism of protein neddylation.


Pssm-ID: 340559 [Multi-domain]  Cd Length: 68  Bit Score: 51.83  E-value: 6.01e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966965853  96 LRVRLEeTGEIFRVANCRgDMTVRELKEELDLMVGIPFNLQRLQYlDEGVLMDDTTLKFHDVVPGGIISL 165
Cdd:cd17039    1 ITVKTL-DGKTYTVEVDP-DDTVADLKEKIEEKTGIPVEQQRLIY-NGKELKDDKTLSDYGIKDGSTIHL 67
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 231-314 1.50e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.06  E-value: 1.50e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966965853 231 GHSDAVQYLLEHGASCLSRSPLGRTPLHVAAAMGRSDCISLLLQHGASIHDKDAKGETPISIAHRlNHTQSERQMFLLHQ 310
Cdd:PTZ00322  93 GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEE-NGFREVVQLLSRHS 171


                 ....
gi 966965853 311 IAKS 314
Cdd:PTZ00322 172 QCHF 175
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 220-288 1.12e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 53.33  E-value: 1.12e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 966965853 220 AFVALYVAShRGHSDAVQYLLEHGASCLSRSPLGRTPLHVAAAMGRSDCISLLLQHGASIHDKDAKGET 288
Cdd:PLN03192 526 ASNLLTVAS-TGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNT 593
Ank_5 pfam13857
Ankyrin repeats (many copies);
239-293 1.62e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 47.34  E-value: 1.62e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 966965853  239 LLEHG-ASCLSRSPLGRTPLHVAAAMGRSDCISLLLQHGASIHDKDAKGETPISIA 293
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 253-283 1.23e-06

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 44.59  E-value: 1.23e-06
                          10        20        30
                  ....*....|....*....|....*....|..
gi 966965853  253 GRTPLHVAAAM-GRSDCISLLLQHGASIHDKD 283
Cdd:pfam00023   2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
Ank_4 pfam13637
Ankyrin repeats (many copies);
253-293 1.42e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.96  E-value: 1.42e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 966965853  253 GRTPLHVAAAMGRSDCISLLLQHGASIHDKDAKGETPISIA 293
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFA 41
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 253-281 1.46e-06

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 44.12  E-value: 1.46e-06
                           10        20
                   ....*....|....*....|....*....
gi 966965853   253 GRTPLHVAAAMGRSDCISLLLQHGASIHD 281
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 234-299 6.06e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 47.74  E-value: 6.06e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 966965853 234 DAVQYLLEHGASCLSRSPLGRTPLHVAAAMGRSDCISLLLQHGASIHDKDAKGETPISIAHRLNHT 299
Cdd:PHA03100 173 NRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNK 238
Ubl_UBFD1 cd17047
ubiquitin-like (Ubl) domain found in ubiquitin domain-containing protein UBFD1 and similar ...
 115-160 1.45e-05

ubiquitin-like (Ubl) domain found in ubiquitin domain-containing protein UBFD1 and similar proteins; UBFD1, also termed ubiquitin-binding protein homolog (UBPH), is a polyubiquitin binding protein containing a conserved ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, a common structure involved in protein-protein interactions. It may play a role as nuclear factor-kappaB (NF-kappaB) regulator.


Pssm-ID: 340567  Cd Length: 70  Bit Score: 42.23  E-value: 1.45e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 966965853 115 DMTVRELKEELDLMVGIPFNLQRLQYldEGVLMDDTTLKFHDVVPG 160
Cdd:cd17047   19 DSTIAELKEHIETLTGVPPAMQKLMY--KGLLKDDKTLRELKVTKG 62
Ank_5 pfam13857
Ankyrin repeats (many copies);
214-260 1.84e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.56  E-value: 1.84e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 966965853  214 QWTSQRAFVALYVASHRGHSDAVQYLLEHGASCLSRSPLGRTPLHVA 260
Cdd:pfam13857  10 NRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ubl_IQUB cd17061
ubiquitin-like (Ubl) domain found in IQ and ubiquitin-like domain-containing protein (IQUB) ...
 104-165 2.07e-05

ubiquitin-like (Ubl) domain found in IQ and ubiquitin-like domain-containing protein (IQUB) and similar proteins; IQUB is an IQ motif and ubiquitin domain-containing protein that may play roles in cilia formation and/or maintenance. It contains a conserved ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, a common structure involved in protein-protein interactions.


Pssm-ID: 340581  Cd Length: 79  Bit Score: 42.25  E-value: 2.07e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966965853 104 GEIFRVAnCRGDMTVRELKEELDLMVGIPFNLQRLQYLDEgVLMDDTTLKFHDVVPGGIISL 165
Cdd:cd17061   13 GQVITLA-FTLGQTIGELKEHFSSELKIPPDVLQIMFDGK-LVEDNTTLVDLGVRPNGTIQL 72
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 253-280 2.11e-05

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 40.70  E-value: 2.11e-05
                          10        20
                  ....*....|....*....|....*...
gi 966965853  253 GRTPLHVAAAMGRSDCISLLLQHGASIH 280
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADIN 29
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 223-322 2.35e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 46.03  E-value: 2.35e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966965853 223 ALYVASHRGHSDAVQYLLEHGASCLSRSPLGRTPLHVAAAMGRSDCISLLLQHGASIHDKDAKGETPISIAHRLNHTQSE 302
Cdd:PHA02878 171 ALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKDYDI 250

                         90       100
                 ....*....|....*....|...
gi 966965853 303 RQMFLLHQI---AKSGIRDLNDL 322
Cdd:PHA02878 251 LKLLLEHGVdvnAKSYILGLTAL 273
Ubl_TBCEL cd17045
ubiquitin-like (Ubl) domain found in tubulin-specific chaperone cofactor E-like protein (TBCEL) ...
 88-154 2.52e-05

ubiquitin-like (Ubl) domain found in tubulin-specific chaperone cofactor E-like protein (TBCEL) and similar proteins; TBCEL, also termed leucine-rich repeat-containing protein 35 (LRRC35), or E-like (EL), is a novel regulator of tubulin stability, suggesting a link between tubulin turnover and vesicle transport. TBCEL is abundantly expressed in testis, but is also present in several tissues at a much lower level. It is required for the synchronous movement of the investment cones and is important for normal male fertility. TBCEL shows high sequence similarity to tubulin-specific chaperone cofactor E (TBCE), a component of the multimolecular complex required for tubulin heterodimer formation in all eukaryotic cells. It contains a leucine-rich repeat protein-protein interaction domain and a C-terminal ubiquitin-like (Ubl) domain, but does not harbor the cytoskeleton-associated protein with glycine-rich segment (CAP-Gly) domain found in TBCE.


Pssm-ID: 340565  Cd Length: 87  Bit Score: 42.23  E-value: 2.52e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 966965853  88 DLAPD-VFFLRVRLEETGEifrVANCRGDMTVRELKEELDLMVGIPFNLQRLQYLD-EGVLMDDTTLKF 154
Cdd:cd17045    1 DLTPPkSAKVTVHFEDQVE---SMDIDLDQTVAELKKQLKNLVGLPPSKMRLYYIDiEMSIFGPEELRF 66
Ubl_TBCB cd01789
ubiquitin-like (Ubl) domain found in tubulin-folding cofactor B (TBCB) and similar proteins; ...
 115-163 3.45e-05

ubiquitin-like (Ubl) domain found in tubulin-folding cofactor B (TBCB) and similar proteins; TBCB, also termed cytoskeleton-associated protein 1, or cytoskeleton-associated protein CKAPI, or tubulin-specific chaperone B, is one of protein cofactors A through E that is required for the folding of tubulins prior to their incorporation into microtubules and heterodimer assembly. TBCB comprises an N-terminal ubiquitin-like (Ubl) domain and a C-terminal cytoskeleton-associated protein with glycine-rich segment (CAP-Gly) domain. The Ubl domain of TBCB is essential for proper folding and assembly of tubulin alpha. It has a beta-grasp Ubl fold, a common structure involved in protein-protein interactions. Ubiquitin (Ub) is a protein modifier in eukaryotes that is involved in various cellular processes, including transcriptional regulation, cell cycle control, and DNA repair. TBC-A through E are necessary for the biogenesis of microtubules and for cell viability.


Pssm-ID: 340487  Cd Length: 80  Bit Score: 41.79  E-value: 3.45e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 966965853 115 DMTVRELKEELDLMVGIPFNLQRLQYLDE-----GVLMDDT-TLKFHDVVPGGII 163
Cdd:cd01789   22 SLTIGELKEKLELITGTPPSSMKLQLYDEdgkliGTLDDDDaLLGSYPVRDGMRI 76
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 224-293 3.56e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 45.34  E-value: 3.56e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966965853 224 LYVASHRGHSDAVQYLLEHGASCLSRSPLGRTPLHVAAAMGRSDCISLLLQHGASIHDKDAKGETPISIA 293
Cdd:PHA02874 161 IHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNA 230
Ubl_BAG6 cd01809
ubiquitin-like (Ubl) domain found in BCL2-associated athanogene 6 (BAG6) and similar proteins; ...
 115-157 5.36e-05

ubiquitin-like (Ubl) domain found in BCL2-associated athanogene 6 (BAG6) and similar proteins; BAG6, also termed large proline-rich protein BAG6, or BAG family molecular chaperone regulator 6, or HLA-B-associated transcript 3 (Bat3), or protein Scythe, or protein G3, is a nucleo-cytoplasmic shuttling chaperone protein that is highly conserved in eukaryotes. It functions in two distinct biological pathways, ubiquitin-mediated protein degradation of defective polypeptides and tail-anchored transmembrane protein biogenesis in mammals. BAG6 is a component of the heterotrimeric BAG6 sortase complex composed of BAG6, transmembrane recognition complex 35 (TRC35) and ubiquitin-like protein 4A (UBL4A). The BAG6 complex together with the cochaperone small, glutamine-rich, tetratricopeptide repeat-containing, protein alpha (SGTA) plays a role in the biogenesis of tail-anchored membrane proteins and subsequently shown to regulate the ubiquitination and proteasomal degradation of mislocalized proteins. Moreover, BAG6 acts as an apoptotic regulator that binds reaper, a potent apoptotic inducer. BAG6/reaper is thought to signal apoptosis, in part through regulating the folding and activity of apoptotic signaling molecules. It is also likely a key regulator of the molecular chaperone Heat Shock Protein A2 (HSPA2) stability/function in human germ cells. Furthermore, aspartyl protease-mediated cleavage of BAG6 is necessary for autophagy and fungal resistance in plants. BAG6 contains a ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, which provides a platform for discriminating substrates with shorter hydrophobicity stretches as a signal for defective proteins.


Pssm-ID: 340507 [Multi-domain]  Cd Length: 71  Bit Score: 40.79  E-value: 5.36e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 966965853 115 DMTVRELKEELDLMVGIPFNLQRLQYldEG-VLMDDTTLKFHDV 157
Cdd:cd01809   20 EITVKEFKEHIASSVNIPAEKQRLIF--QGrVLQDDKKLKEYDV 61
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 224-294 8.12e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.50  E-value: 8.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966965853 224 LYVASHRGHSDAVQYLLEHGASCLSRSPLGRTPLHVAAAMGRSDCISLLLQHGASIHDKDAKG-------------ETPI 290
Cdd:PTZ00322 119 LHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFELGANAkpdsftgkppsleDSPI 198


                 ....
gi 966965853 291 SIAH 294
Cdd:PTZ00322 199 SSHH 202
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 224-325 8.54e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 44.18  E-value: 8.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966965853 224 LYVASHRGHSDAVQYLLEHGASCLSRSPLGRTPLHVAAAMGRSdCISLLLQHgASIHDKDAKGETPISiaHRLNHTQSER 303
Cdd:PHA02874 194 LHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRS-AIELLINN-ASINDQDIDGSTPLH--HAINPPCDID 269

                         90       100
                 ....*....|....*....|....*...
gi 966965853 304 QM-FLLHQIAKSGIRDLN-----DLVMK 325
Cdd:PHA02874 270 IIdILLYHKADISIKDNKgenpiDTAFK 297
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 204-306 9.29e-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: 44.23  E-value: 9.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966965853 204 SEHFEGEkwkqwtsqrafVALYVASHRGHSDAVQYLLEHGA---------SCLSRSP-----LGRTPLHVAAAMGRSDCI 269
Cdd:cd22192   84 SDLYQGE-----------TALHIAVVNQNLNLVRELIARGAdvvspratgTFFRPGPknliyYGEHPLSFAACVGNEEIV 152

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 966965853 270 SLLLQHGASIHDKDAKGETPISIAHRLNHTQSERQMF 306
Cdd:cd22192  153 RLLIEHGADIRAQDSLGNTVLHILVLQPNKTFACQMY 189
PHA03095 PHA03095
ankyrin-like protein; Provisional
 234-326 9.42e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 43.86  E-value: 9.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966965853 234 DAVQYLLEHGASCLSRSPLGRTPLHVAAAmG---RSDCISLLLQHGASIHDKDAKGETPISI---AHRLN---------- 297
Cdd:PHA03095  98 DVIKLLIKAGADVNAKDKVGRTPLHVYLS-GfniNPKVIRLLLRKGADVNALDLYGMTPLAVllkSRNANvellrllida 176

                         90       100       110
                 ....*....|....*....|....*....|...
gi 966965853 298 ----HTQSERQMFLLHQIAKSgIRDLNDLVMKN 326
Cdd:PHA03095 177 gadvYAVDDRFRSLLHHHLQS-FKPRARIVREL 208
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 234-293 1.19e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 43.72  E-value: 1.19e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 966965853 234 DAVQYLLEHGASCLSRSP-LGRTPLHVAaaMGRSDCISLLLQHGASIHDKDAKGETPISIA 293
Cdd:PHA02878 249 DILKLLLEHGVDVNAKSYiLGLTALHSS--IKSERKLKLLLEYGADINSLNSYKLTPLSSA 307
UBQ smart00213
Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of ...
 113-165 1.55e-04

Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of proteins required for controlling cell cycle progression


Pssm-ID: 214563 [Multi-domain]  Cd Length: 72  Bit Score: 39.55  E-value: 1.55e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 966965853   113 RGDMTVRELKEELDLMVGIPFNLQRLQYlDEGVLMDDTTLKFHDVVPGGIISL 165
Cdd:smart00213  18 KPSDTVSELKEKIAELTGIPPEQQRLIY-KGKVLEDDRTLADYGIQDGSTIHL 69
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 219-284 3.47e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 42.34  E-value: 3.47e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 966965853 219 RAFVALYVASHRGHSDAVQYLLEHGASCLSRSPLGRTPLHVAAAMGRSDCISLLLQHGASIHDKDA 284
Cdd:PHA03100 191 YGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIE 256
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 224-290 5.85e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 41.49  E-value: 5.85e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 966965853 224 LYVASHRGHSDAVQYLLEHGASCLSRSPLGRTPLHVAAAMGRSDCISLLLQHGASIHDKDAKGETPI 290
Cdd:PHA02874 128 LHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPL 194
Ubl_Dsk2p_like cd16106
ubiquitin-like (Ubl) domain found in Saccharomyces cerevisiae proteasome interacting protein ...
 115-165 9.08e-04

ubiquitin-like (Ubl) domain found in Saccharomyces cerevisiae proteasome interacting protein Dsk2p and similar proteins; The family contains several fungal multiubiquitin receptors, including Saccharomyces cerevisiae Dsk2p and Schizosaccharomyces pombe Dph1p, both of which have been characterized as shuttle proteins transporting ubiquitinated substrates destined for degradation from the E3 ligase to the 26S proteasome. They interact with the proteasome through their N-terminal ubiquitin-like domain (Ubl) and with ubiquitin (Ub) through their C-terminal Ub-associated domain (UBA). S. cerevisiae Dsk2p is a nuclear-enriched protein that may involve in the ubiquitin-proteasome proteolytic pathway through interacting with K48-linked polyubiquitin and the proteasome. Moreover, it has been implicated in spindle pole duplication through assisting in Cdc31 assembly into the new spindle pole body (SPB). S. pombe Dph1p is an ubiquitin (Ub0 receptor working in concert with the class V myosin, Myo52, to target the degradation of the S. pombe CLIP-170 homolog, Tip1. It also can protect Ub chains against disassembly by deubiquitinating enzymes.


Pssm-ID: 340523 [Multi-domain]  Cd Length: 73  Bit Score: 37.23  E-value: 9.08e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 966965853 115 DMTVRELKEELDLMVGIPFNLQRLQYldEG-VLMDDTTLKFHDVVPGGIISL 165
Cdd:cd16106   20 DATVLELKELIAEKSDIPAEQQRLIY--KGkILKDEETLSSYKIQDGHTVHL 69
Ubiquitin_2 pfam14560
Ubiquitin-like domain; This entry contains ubiquitin-like domains.
 115-152 1.28e-03

Ubiquitin-like domain; This entry contains ubiquitin-like domains.


Pssm-ID: 405277  Cd Length: 83  Bit Score: 37.12  E-value: 1.28e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 966965853  115 DMTVRELKEELDLMVGIPFNLQRLQYLDEG-----VLMDDTTL 152
Cdd:pfam14560  22 SLTIEELKEKLELITGTPPSSMRLQLYDDDdnlvaKLDDDDAL 64
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 224-293 1.28e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 40.36  E-value: 1.28e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966965853 224 LYVASHRGHSDAVQYLLEHGASCLSRSPLGRTPLHVAAAMGRSDCISLLLQHGASIHDKDAKGETPISIA 293
Cdd:PHA02875 106 LHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIA 175
PHA03095 PHA03095
ankyrin-like protein; Provisional
 236-299 1.56e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 40.01  E-value: 1.56e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 966965853 236 VQYLLEHGASCLSRSPLGRTPLHVAAAMGRSDCISLLLQHGASIHDKDAKGETPISIAHRLNHT 299
Cdd:PHA03095 240 VLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNG 303
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 223-288 1.70e-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: 1.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966965853  223 ALYVASHRGHSDAVQYLLEHGAS---------CLSRSPL-----GRTPLHVAAAMGRSDCISLLLQHGASIHDKDAKGET 288
Cdd:TIGR00870 131 ALHLAAHRQNYEIVKLLLERGASvparacgdfFVKSQGVdsfyhGESPLNAAACLGSPSIVALLSEDPADILTADSLGNT 210
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 236-302 5.54e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 38.49  E-value: 5.54e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 966965853 236 VQYLLEHGASCLSRSPLGRTPLHVAAA--MGRSDCISLLLQHGASIHDKDAKGETPISIAHRLNHTQSE 302
Cdd:PHA03100  89 VKLLLEYGANVNAPDNNGITPLLYAISkkSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLK 157
Ubl_SF3a120 cd01800
ubiquitin-like (Ubl) domain found in splicing factor 3A 120kDa subunit (SF3a120) and similar ...
 117-165 5.62e-03

ubiquitin-like (Ubl) domain found in splicing factor 3A 120kDa subunit (SF3a120) and similar proteins; Mammalian splicing factor SF3a consists of three subunits of 60, 66, and 120 kDa and functions early during pre-mRNA splicing by converting the U2 snRNP to its active form. The 120kDa subunit SF3a120, also termed splicing factor 3A subunit 1 (SF3A1), or spliceosome-associated protein 114 (SAP114), is the U2 snRNP-specific protein that is critical for spliceosome assembly and normal splicing events. During splicing, SF3a120, together with the U2 snRNP and other proteins, are recruited to the 3' splicing site to generate the splicing complex A after the recognition of the 3' splicing site. SF3a120 contains two N-terminal SWAP (suppressor-of-white-apricot) domains, referred to collectively as the SURP module, as well as a C-terminal ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, a common structure involved in protein-protein interactions.


Pssm-ID: 340498  Cd Length: 84  Bit Score: 35.63  E-value: 5.62e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 966965853 117 TVRELKEELDLMVGIPFNLQRLQYLDEGVLMDDTTLKFHDVVPGGIISL 165
Cdd:cd01800   33 TISVLKEKIHEELGMPANKQKLQVEGGGFLKDSNSLAFYNLGSGTVLTL 81
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 170-296 5.89e-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: 5.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966965853 170 HDGWTELVLAAAEGDPSKLSCLGLTEDSfyrtANSEHFEGEkwkqwtsqrafVALYVASHRGHSDAVQYLLEHGASC--- 246
Cdd:cd21882   38 NDGVNEAIMLLLEAAPDSGNPKELVNAP----CTDEFYQGQ-----------TALHIAIENRNLNLVRLLVENGADVsar 102

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 966965853 247 -----LSRSP-----LGRTPLHVAAAMGRSDCISLLLQHGASIHDKDAKGETPISIAHRL 296
Cdd:cd21882  103 atgrfFRKSPgnlfyFGELPLSLAACTNQEEIVRLLLENGAQPAALEAQDSLGNTVLHAL 162
ubiquitin pfam00240
Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog) ...
 117-165 6.32e-03

Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog), Nedd8, Elongin B, Rub1, and Parkin. A number of them are thought to carry a distinctive five-residue motif termed the proteasome-interacting motif (PIM), which may have a biologically significant role in protein delivery to proteasomes and recruitment of proteasomes to transcription sites.


Pssm-ID: 459726 [Multi-domain]  Cd Length: 72  Bit Score: 34.84  E-value: 6.32e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 966965853  117 TVRELKEELDLMVGIPFNLQRLQYldEG-VLMDDTTLKFHDVVPGGIISL 165
Cdd:pfam00240  20 TVLELKEKIAEKEGVPPEQQRLIY--SGkVLEDDQTLGEYGIEDGSTIHL 67
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 234-297 6.77e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 38.02  E-value: 6.77e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 966965853 234 DAVQYLLEHGASCLSRSPLGRTPLHVAAAMGRSDCISLLLQHGASIHDKDAKGETPISIAHRLN 297
Cdd:PHA02874 105 DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHN 168
PHA03095 PHA03095
ankyrin-like protein; Provisional
 234-292 7.28e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 38.08  E-value: 7.28e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 966965853 234 DAVQYLLEHGASCLSRSPLGRTPLHVAAAMG-RSDCISLLLQHGASIHDKDAKGETPISI 292
Cdd:PHA03095  64 DIVRLLLEAGADVNAPERCGFTPLHLYLYNAtTLDVIKLLIKAGADVNAKDKVGRTPLHV 123
 
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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