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Conserved domains on  [gi|564330588|ref|XP_006230157|]
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nucleobindin-2 isoform X1 [Rattus norvegicus]

Protein Classification

EF-hand domain-containing protein( domain architecture ID 12144783)

EF-hand (EFh) domain-containing protein may be involved in binding intracellular calcium and in calcium signal transduction

CATH:  1.10.238.10
Gene Ontology:  GO:0005509
PubMed:  2479149|10191494
SCOP:  3001983

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 307-400 1.64e-05

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


:

Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 46.75  E-value: 1.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330588 307 NNKDRLVTLEEFLRATEKKEFLepDSWETLDQQQLFTEEELKEYESIIAIQEN---ELKKKADELQKQKEELQRQHDHLE 383
Cdd:COG3883   97 RSGGSVSYLDVLLGSESFSDFL--DRLSALSKIADADADLLEELKADKAELEAkkaELEAKLAELEALKAELEAAKAELE 174

                         90
                 ....*....|....*..
gi 564330588 384 AQKQEYQQAVQQLEQKK 400
Cdd:COG3883  175 AQQAEQEALLAQLSAEE 191
EF-hand_7 pfam13499
EF-hand domain pair;
247-322 2.39e-05

EF-hand domain pair;


:

Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 41.86  E-value: 2.39e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564330588  247 KTFFKLHDVNNDGFLDEQELEALFTKeldkvynpqnaeddMIEMEEERLRMREHVMNEIDNNKDRLVTLEEFLRAT 322
Cdd:pfam13499   5 KEAFKLLDSDGDGYLDVEELKKLLRK--------------LEEGEPLSDEEVEELFKEFDLDKDGRISFEEFLELY 66
 
Name Accession Description Interval E-value
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 307-400 1.64e-05

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 46.75  E-value: 1.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330588 307 NNKDRLVTLEEFLRATEKKEFLepDSWETLDQQQLFTEEELKEYESIIAIQEN---ELKKKADELQKQKEELQRQHDHLE 383
Cdd:COG3883   97 RSGGSVSYLDVLLGSESFSDFL--DRLSALSKIADADADLLEELKADKAELEAkkaELEAKLAELEALKAELEAAKAELE 174

                         90
                 ....*....|....*..
gi 564330588 384 AQKQEYQQAVQQLEQKK 400
Cdd:COG3883  175 AQQAEQEALLAQLSAEE 191
EF-hand_7 pfam13499
EF-hand domain pair;
247-322 2.39e-05

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 41.86  E-value: 2.39e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564330588  247 KTFFKLHDVNNDGFLDEQELEALFTKeldkvynpqnaeddMIEMEEERLRMREHVMNEIDNNKDRLVTLEEFLRAT 322
Cdd:pfam13499   5 KEAFKLLDSDGDGYLDVEELKKLLRK--------------LEEGEPLSDEEVEELFKEFDLDKDGRISFEEFLELY 66
PRK12704 PRK12704
phosphodiesterase; Provisional
 316-399 1.22e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 44.00  E-value: 1.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330588 316 EEFLRATEK--KEFLEPDswETLDQQqlftEEELKEYESIIAIQENELKKKADELQKQKEELQRQHDHLEAQKQEYQQAV 393
Cdd:PRK12704  64 EEIHKLRNEfeKELRERR--NELQKL----EKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELI 137


                 ....*.
gi 564330588 394 QQLEQK 399
Cdd:PRK12704 138 EEQLQE 143
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 294-399 1.64e-03

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 40.88  E-value: 1.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330588  294 RLRMREHVMNE-----IDNNKDRLVTLEEFLRATEKKEFLEPDSWETldqqQLFTEEELKEYESIIAIQENELKkkadEL 368
Cdd:pfam05557  59 LLEKREAEAEEalreqAELNRLKKKYLEALNKKLNEKESQLADAREV----ISCLKNELSELRRQIQRAELELQ----ST 130

                          90       100       110
                  ....*....|....*....|....*....|.
gi 564330588  369 QKQKEELQRQHDHLEAQKQEYQQAVQQLEQK 399
Cdd:pfam05557 131 NSELEELQERLDLLKAKASEAEQLRQNLEKQ 161
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 338-403 5.73e-03

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 37.18  E-value: 5.73e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564330588   338 QQQLFTEEELKEYESIIAIQENELKKKADELQKQKEELQRQHDHL-EAQKQEYQQAVQQLEQkKFQQ 403
Cdd:smart00935  11 QESPAGKAAQKQLEKEFKKRQAELEKLEKELQKLKEKLQKDAATLsEAAREKKEKELQKKVQ-EFQR 76
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
247-332 8.76e-03

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 36.31  E-value: 8.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330588 247 KTFFKLHDVNNDGFLDEQELEALFTkelDKVYNPQNAeddmiemeeerlrmrEHVMNEIDNNKDRLVTLEEFLRATekKE 326
Cdd:COG5126   72 RAAFDLLDTDGDGKISADEFRRLLT---ALGVSEEEA---------------DELFARLDTDGDGKISFEEFVAAV--RD 131


                 ....*.
gi 564330588 327 FLEPDS 332
Cdd:COG5126  132 YYTPDA 137
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 250-321 9.88e-03

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 34.45  E-value: 9.88e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564330588 250 FKLHDVNNDGFLDEQELEALFTKELDKVYNPQnaeddmiemeeerlrmREHVMNEIDNNKDRLVTLEEFLRA 321
Cdd:cd00051    6 FRLFDKDGDGTISADELKAALKSLGEGLSEEE----------------IDEMIREVDKDGDGKIDFEEFLEL 61
 
Name Accession Description Interval E-value
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 307-400 1.64e-05

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 46.75  E-value: 1.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330588 307 NNKDRLVTLEEFLRATEKKEFLepDSWETLDQQQLFTEEELKEYESIIAIQEN---ELKKKADELQKQKEELQRQHDHLE 383
Cdd:COG3883   97 RSGGSVSYLDVLLGSESFSDFL--DRLSALSKIADADADLLEELKADKAELEAkkaELEAKLAELEALKAELEAAKAELE 174

                         90
                 ....*....|....*..
gi 564330588 384 AQKQEYQQAVQQLEQKK 400
Cdd:COG3883  175 AQQAEQEALLAQLSAEE 191
EF-hand_7 pfam13499
EF-hand domain pair;
247-322 2.39e-05

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 41.86  E-value: 2.39e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564330588  247 KTFFKLHDVNNDGFLDEQELEALFTKeldkvynpqnaeddMIEMEEERLRMREHVMNEIDNNKDRLVTLEEFLRAT 322
Cdd:pfam13499   5 KEAFKLLDSDGDGYLDVEELKKLLRK--------------LEEGEPLSDEEVEELFKEFDLDKDGRISFEEFLELY 66
PRK12704 PRK12704
phosphodiesterase; Provisional
 316-399 1.22e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 44.00  E-value: 1.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330588 316 EEFLRATEK--KEFLEPDswETLDQQqlftEEELKEYESIIAIQENELKKKADELQKQKEELQRQHDHLEAQKQEYQQAV 393
Cdd:PRK12704  64 EEIHKLRNEfeKELRERR--NELQKL----EKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELI 137


                 ....*.
gi 564330588 394 QQLEQK 399
Cdd:PRK12704 138 EEQLQE 143
PRK12704 PRK12704
phosphodiesterase; Provisional
 343-400 2.04e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 43.61  E-value: 2.04e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 564330588 343 TEEELKEYESIIAIQENELKKKADELQKQKEELQRQHDHLEAQKQEYQQAVQQLEQKK 400
Cdd:PRK12704  73 FEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKE 130
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 334-398 3.93e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 42.89  E-value: 3.93e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564330588 334 ETLDQQQLFTEEELKEYESIIAiqenELKKKADELQKQKEELQRQHDHL-EAQKQEYQQAVQQLEQ 398
Cdd:PRK00409 523 ASLEELERELEQKAEEAEALLK----EAEKLKEELEEKKEKLQEEEDKLlEEAEKEAQQAIKEAKK 584
PRK12704 PRK12704
phosphodiesterase; Provisional
 344-403 8.99e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 41.30  E-value: 8.99e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330588 344 EEELKEYESIIAIQENELKKKADELQKQKEELQRQHDHLEAQKQEYQQAVQQLEQKKFQQ 403
Cdd:PRK12704  81 RNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQ 140
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 320-400 9.97e-04

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 40.95  E-value: 9.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330588 320 RATEKKEFLEPDSWETLDQQQLFTEEELKEYEsiiaiQEnelKKKADELQKQKEELQRQhdHLEAQKQEYQQAVQQLEQK 399
Cdd:PRK09510  76 RAEEQRKKKEQQQAEELQQKQAAEQERLKQLE-----KE---RLAAQEQKKQAEEAAKQ--AALKQKQAEEAAAKAAAAA 145


                 .
gi 564330588 400 K 400
Cdd:PRK09510 146 K 146
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 294-399 1.64e-03

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 40.88  E-value: 1.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330588  294 RLRMREHVMNE-----IDNNKDRLVTLEEFLRATEKKEFLEPDSWETldqqQLFTEEELKEYESIIAIQENELKkkadEL 368
Cdd:pfam05557  59 LLEKREAEAEEalreqAELNRLKKKYLEALNKKLNEKESQLADAREV----ISCLKNELSELRRQIQRAELELQ----ST 130

                          90       100       110
                  ....*....|....*....|....*....|.
gi 564330588  369 QKQKEELQRQHDHLEAQKQEYQQAVQQLEQK 399
Cdd:pfam05557 131 NSELEELQERLDLLKAKASEAEQLRQNLEKQ 161
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 348-403 1.82e-03

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 461098 [Multi-domain]  Cd Length: 140  Bit Score: 38.33  E-value: 1.82e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 564330588  348 KEYESIIAIQENELKKKADELQKQKEELQRQHDHLEAQKQEYQQAVQQLEQ--KKFQQ 403
Cdd:pfam03938  22 AQLEKKFKKRQAELEAKQKELQKLYEELQKDGALLEEEREEKEQELQKKEQelQQLQQ 79
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 345-400 1.82e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.13  E-value: 1.82e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 564330588 345 EELKEYESIIAIQENELKKKADELQKQKEELQRQHDHLEAQKQEYQQAVQQLEQKK 400
Cdd:COG4942  153 EELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKEL 208
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 338-403 5.73e-03

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 37.18  E-value: 5.73e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564330588   338 QQQLFTEEELKEYESIIAIQENELKKKADELQKQKEELQRQHDHL-EAQKQEYQQAVQQLEQkKFQQ 403
Cdd:smart00935  11 QESPAGKAAQKQLEKEFKKRQAELEKLEKELQKLKEKLQKDAATLsEAAREKKEKELQKKVQ-EFQR 76
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 262-403 7.91e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 38.76  E-value: 7.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330588 262 DEQELEALFTKELDKVYNPQNAEDDMIEMEEERLRMREHVMNEIDNNKDRLVTLEEFLRATEKKEFLEPDSWETLDQQQL 341
Cdd:COG1196  691 EELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELE 770

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564330588 342 FTEEELKEYESI--IAIQEnelkkkADELQKQKEELQRQHDHLEAQKQEYQQAVQQLEQKKFQQ 403
Cdd:COG1196  771 RLEREIEALGPVnlLAIEE------YEELEERYDFLSEQREDLEEARETLEEAIEEIDRETRER 828
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 294-400 7.98e-03

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 38.52  E-value: 7.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330588 294 RLRMREHVM-NEIDNNKDRLVTLEEFLRATEKKEflEPDSWETLDQQQLFTEEELKEYESIIAIQENElKKKADELQKQK 372
Cdd:COG0542  401 RVRMEIDSKpEELDELERRLEQLEIEKEALKKEQ--DEASFERLAELRDELAELEEELEALKARWEAE-KELIEEIQELK 477

                         90       100
                 ....*....|....*....|....*...
gi 564330588 373 EELQRQHDHLEAQKQEYQQAVQQLEQKK 400
Cdd:COG0542  478 EELEQRYGKIPELEKELAELEEELAELA 505
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
247-332 8.76e-03

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 36.31  E-value: 8.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330588 247 KTFFKLHDVNNDGFLDEQELEALFTkelDKVYNPQNAeddmiemeeerlrmrEHVMNEIDNNKDRLVTLEEFLRATekKE 326
Cdd:COG5126   72 RAAFDLLDTDGDGKISADEFRRLLT---ALGVSEEEA---------------DELFARLDTDGDGKISFEEFVAAV--RD 131


                 ....*.
gi 564330588 327 FLEPDS 332
Cdd:COG5126  132 YYTPDA 137
Borrelia_P83 pfam05262
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
 346-410 9.01e-03

Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.


Pssm-ID: 114011 [Multi-domain]  Cd Length: 489  Bit Score: 38.06  E-value: 9.01e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330588  346 ELKEYESIIA-----IQENELKKKADELQKQKEELQRQHDHLEAQKQEYQQAVQqlEQKKFQQGIAPSGP 410
Cdd:pfam05262 202 DLKERESQEDakraqQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQ--EAKNLPKPADTSSP 269
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 250-321 9.88e-03

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 34.45  E-value: 9.88e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564330588 250 FKLHDVNNDGFLDEQELEALFTKELDKVYNPQnaeddmiemeeerlrmREHVMNEIDNNKDRLVTLEEFLRA 321
Cdd:cd00051    6 FRLFDKDGDGTISADELKAALKSLGEGLSEEE----------------IDEMIREVDKDGDGKIDFEEFLEL 61
 
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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