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Conserved domains on  [gi|222352175|ref|NP_001138433|]
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NF-kappa-B inhibitor-like protein 1 isoform 2 [Homo sapiens]

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];
43-138 2.48e-10

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 60.74  E-value: 2.48e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352175  43 AGRLVRAQALLQRhpGLDVDA---GQPPPLHRACARHDAPALCLLLRLGADPAHQDRHGDTALHAAARQGpdaYTDFFLP 119
Cdd:COG0666  130 NGNLEIVKLLLEA--GADVNAqdnDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENG---HLEIVKL 204

                         90       100
                 ....*....|....*....|...
gi 222352175 120 LLSRcpsamG----IKNKDGETP 138
Cdd:COG0666  205 LLEA-----GadvnAKDNDGKTA 222
DDRGK super family cl25550
DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and ...
 190-254 3.67e-03

DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and vertebrates. They contain a highly conserved DDRGK motif.


The actual alignment was detected with superfamily member pfam09756:

Pssm-ID: 370664 [Multi-domain]  Cd Length: 188  Bit Score: 38.10  E-value: 3.67e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 222352175  190 LAREHAQKCQQQQREAEGSRRPPRAEGSSQSWRQQEEEQRLFRERARAKEEELR---ESRARRAQEAL 254
Cdd:pfam09756   8 RAKLELKEAKRQQREAEEEEREEREKLEEKREEEYKEREEREEEAEKEKEEEERkqeEEQERKEQEEY 75
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
43-138 2.48e-10

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 60.74  E-value: 2.48e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352175  43 AGRLVRAQALLQRhpGLDVDA---GQPPPLHRACARHDAPALCLLLRLGADPAHQDRHGDTALHAAARQGpdaYTDFFLP 119
Cdd:COG0666  130 NGNLEIVKLLLEA--GADVNAqdnDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENG---HLEIVKL 204

                         90       100
                 ....*....|....*....|...
gi 222352175 120 LLSRcpsamG----IKNKDGETP 138
Cdd:COG0666  205 LLEA-----GadvnAKDNDGKTA 222
Ank_2 pfam12796
Ankyrin repeats (3 copies);
69-109 1.93e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 45.49  E-value: 1.93e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 222352175   69 LHRACARHDAPALCLLLRLGADPAHQDRHGDTALHAAARQG 109
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNG 41
DDRGK pfam09756
DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and ...
 190-254 3.67e-03

DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and vertebrates. They contain a highly conserved DDRGK motif.


Pssm-ID: 370664 [Multi-domain]  Cd Length: 188  Bit Score: 38.10  E-value: 3.67e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 222352175  190 LAREHAQKCQQQQREAEGSRRPPRAEGSSQSWRQQEEEQRLFRERARAKEEELR---ESRARRAQEAL 254
Cdd:pfam09756   8 RAKLELKEAKRQQREAEEEEREEREKLEEKREEEYKEREEREEEAEKEKEEEERkqeEEQERKEQEEY 75
PHA03095 PHA03095
ankyrin-like protein; Provisional
 58-132 6.26e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 38.47  E-value: 6.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352175  58 GLDVDA----GQPPpLHRAcARHDAPALCL-LLRLGADPAHQDRHGDTALHAAARQGpdaYTDFFLPLLSRCPSAMGIKN 132
Cdd:PHA03095 247 GISINArnryGQTP-LHYA-AVFNNPRACRrLIALGADINAVSSDGNTPLSLMVRNN---NGRAVRAALAKNPSAETVAA 321
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
43-138 2.48e-10

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 60.74  E-value: 2.48e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352175  43 AGRLVRAQALLQRhpGLDVDA---GQPPPLHRACARHDAPALCLLLRLGADPAHQDRHGDTALHAAARQGpdaYTDFFLP 119
Cdd:COG0666  130 NGNLEIVKLLLEA--GADVNAqdnDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENG---HLEIVKL 204

                         90       100
                 ....*....|....*....|...
gi 222352175 120 LLSRcpsamG----IKNKDGETP 138
Cdd:COG0666  205 LLEA-----GadvnAKDNDGKTA 222
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
44-138 2.65e-10

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 60.74  E-value: 2.65e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352175  44 GRLVRAQALLQRhpGLDV---DAGQPPPLHRACARHDAPALCLLLRLGADPAHQDRHGDTALHAAARQGpdaYTDFFLPL 120
Cdd:COG0666   98 GDLEIVKLLLEA--GADVnarDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANG---NLEIVKLL 172

                         90       100
                 ....*....|....*....|..
gi 222352175 121 LSRcpsamG----IKNKDGETP 138
Cdd:COG0666  173 LEA-----GadvnARDNDGETP 189
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
46-138 6.27e-08

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 53.42  E-value: 6.27e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352175  46 LVRAQALLQRHPGLDVDAGQPPPLHRACARHDAPALCLLLRLGADPAHQDRHGDTALHAAARQGPDAYTDFFLpllsrcp 125
Cdd:COG0666   68 LVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLL------- 140

                         90
                 ....*....|....*..
gi 222352175 126 sAMG----IKNKDGETP 138
Cdd:COG0666  141 -EAGadvnAQDNDGNTP 156
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
49-109 6.62e-08

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 53.42  E-value: 6.62e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 222352175  49 AQALLQRhpGLDVDAGQP---PPLHRACARHDAPALCLLLRLGADPAHQDRHGDTALHAAARQG 109
Cdd:COG0666  169 VKLLLEA--GADVNARDNdgeTPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENG 230
Ank_2 pfam12796
Ankyrin repeats (3 copies);
69-109 1.93e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 45.49  E-value: 1.93e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 222352175   69 LHRACARHDAPALCLLLRLGADPAHQDRHGDTALHAAARQG 109
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNG 41
Ank_4 pfam13637
Ankyrin repeats (many copies);
67-109 2.02e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.49  E-value: 2.02e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 222352175   67 PPLHRACARHDAPALCLLLRLGADPAHQDRHGDTALHAAARQG 109
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNG 45
Ank_5 pfam13857
Ankyrin repeats (many copies);
68-105 2.65e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.79  E-value: 2.65e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 222352175   68 PLHRACARHDAPALCLLLRLGADPAHQDRHGDTALHAA 105
Cdd:pfam13857  19 PLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
DDRGK pfam09756
DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and ...
 190-254 3.67e-03

DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and vertebrates. They contain a highly conserved DDRGK motif.


Pssm-ID: 370664 [Multi-domain]  Cd Length: 188  Bit Score: 38.10  E-value: 3.67e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 222352175  190 LAREHAQKCQQQQREAEGSRRPPRAEGSSQSWRQQEEEQRLFRERARAKEEELR---ESRARRAQEAL 254
Cdd:pfam09756   8 RAKLELKEAKRQQREAEEEEREEREKLEEKREEEYKEREEREEEAEKEKEEEERkqeEEQERKEQEEY 75
PHA03095 PHA03095
ankyrin-like protein; Provisional
 58-132 6.26e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 38.47  E-value: 6.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352175  58 GLDVDA----GQPPpLHRAcARHDAPALCL-LLRLGADPAHQDRHGDTALHAAARQGpdaYTDFFLPLLSRCPSAMGIKN 132
Cdd:PHA03095 247 GISINArnryGQTP-LHYA-AVFNNPRACRrLIALGADINAVSSDGNTPLSLMVRNN---NGRAVRAALAKNPSAETVAA 321
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 189-274 9.77e-03

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 36.17  E-value: 9.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352175  189 RLAREHAQKCQQQQREAEGSRRPPRAE----GSSQSWRQQEEEQRLFRERARAKEEELRESRARRAQEALGDREPKPTRA 264
Cdd:pfam05672  21 RQAREQREREEQERLEKEEEERLRKEElrrrAEEERARREEEARRLEEERRREEEERQRKAEEEAEEREQREQEEQERLQ 100

                          90
                  ....*....|
gi 222352175  265 GPREEHPRGA 274
Cdd:pfam05672 101 KQKEEAEAKA 110
 
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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