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Conserved domains on  [gi|530379755|ref|XP_005271973|]
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spermatogenesis-associated protein 24 isoform X1 [Homo sapiens]

Protein Classification

SPATA24 domain-containing protein( domain architecture ID 12172058)

SPATA24 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SPATA24 pfam15175
Spermatogenesis-associated protein 24; This family of proteins bind to DNA and to TBP (TATA ...
 22-162 3.88e-78

Spermatogenesis-associated protein 24; This family of proteins bind to DNA and to TBP (TATA box binding protein), TATA-binding protein (TBP)-related protein 2 (TRF2) and several polycomb factors. It is likely to function as a transcription regulator.


:

Pssm-ID: 464544 [Multi-domain]  Cd Length: 170  Bit Score: 238.98  E-value: 3.88e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379755   22 LRDVIESQEELIHQLRNVMVLQDENFVSKEEFQAVEKKLVEEKAAHAKTKVLLAKEEEKLQFALGEVEVLSKQLEKEKLA 101
Cdd:pfam15175   1 MKDLFHVQQNTLEQLRQTARRQKENFVSKEEYEAVAKKLEEERAEHAKTKLLLAKESEKLQFALGEIEVLSKQLEREKKA 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530379755  102 FEKALSSVKSKVLQESSKKDQLITKCNEIESHIIKQEDILNGKENEIKELQQVISQQKQIF 162
Cdd:pfam15175  81 FEKALGSVKSKALRESKKADQLKTKCSEIESHCIRQEDILNGKENEIKELKQRLSKQKEIH 141
 
Name Accession Description Interval E-value
SPATA24 pfam15175
Spermatogenesis-associated protein 24; This family of proteins bind to DNA and to TBP (TATA ...
 22-162 3.88e-78

Spermatogenesis-associated protein 24; This family of proteins bind to DNA and to TBP (TATA box binding protein), TATA-binding protein (TBP)-related protein 2 (TRF2) and several polycomb factors. It is likely to function as a transcription regulator.


Pssm-ID: 464544 [Multi-domain]  Cd Length: 170  Bit Score: 238.98  E-value: 3.88e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379755   22 LRDVIESQEELIHQLRNVMVLQDENFVSKEEFQAVEKKLVEEKAAHAKTKVLLAKEEEKLQFALGEVEVLSKQLEKEKLA 101
Cdd:pfam15175   1 MKDLFHVQQNTLEQLRQTARRQKENFVSKEEYEAVAKKLEEERAEHAKTKLLLAKESEKLQFALGEIEVLSKQLEREKKA 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530379755  102 FEKALSSVKSKVLQESSKKDQLITKCNEIESHIIKQEDILNGKENEIKELQQVISQQKQIF 162
Cdd:pfam15175  81 FEKALGSVKSKALRESKKADQLKTKCSEIESHCIRQEDILNGKENEIKELKQRLSKQKEIH 141
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
17-160 7.09e-07

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 51.06  E-value: 7.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379755  17 LALDQLRDVIESQEELIHQLRNvmvLQDENFVSKEEFQAVEKKLVEEKAAHAKTKVLLAKEEEKLQFALGEVEVLSKQLE 96
Cdd:COG4372   28 ALSEQLRKALFELDKLQEELEQ---LREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELE 104

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530379755  97 ---KEKLAFEKALSSVKSKVLQESSKKDQLITKCNEIESHIIKQEDILNGKENEIKELQQVISQQKQ 160
Cdd:COG4372  105 slqEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQ 171
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 49-163 3.51e-05

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 46.17  E-value: 3.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379755   49 SKEEFQAVEKKLVEEKAAHAKTKVLLAKEEEKLQFALGEVEVLSKQ---LEKEKLAFEKALSSVKSKVLQESSKKDQL-- 123
Cdd:TIGR04523 122 LEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQkeeLENELNLLEKEKLNIQKNIDKIKNKLLKLel 201

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 530379755  124 --------ITKCNEIESHIIKQEDILNGKENEIKELQQVISQQKQIFS 163
Cdd:TIGR04523 202 llsnlkkkIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEIS 249
PRK12704 PRK12704
phosphodiesterase; Provisional
 48-161 1.66e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.53  E-value: 1.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379755  48 VSKEEFQAveKKLVEEkaahAKTKVLLAKEEEKLQfALGEVEVLSKQLEKEKLAFEKALSSVKSKVLQES---SKKDQLI 124
Cdd:PRK12704  33 IKEAEEEA--KRILEE----AKKEAEAIKKEALLE-AKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEenlDRKLELL 105

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 530379755 125 TKcneIESHIIKQEDILNGKENEIKELQQVIS--QQKQI 161
Cdd:PRK12704 106 EK---REEELEKKEKELEQKQQELEKKEEELEelIEEQL 141
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 19-161 2.06e-03

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 40.00  E-value: 2.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379755    19 LDQLRDVIESQEELIHQLrnVMVLQDENFVSKEEFQaVEKKLVEEKAAHAKTkvLLAKEEEKLQFALGEVEVLSKQLEKe 98
Cdd:smart00787 156 LKEDYKLLMKELELLNSI--KPKLRDRKDALEEELR-QLKQLEDELEDCDPT--ELDRAKEKLKKLLQEIMIKVKKLEE- 229

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530379755    99 klaFEKALSSVKSKVLQESSKKDQLITKCNEIEShiiKQEDILNGKENEIKELQQVISQQKQI 161
Cdd:smart00787 230 ---LEEELQELESKIEDLTNKKSELNTEIAEAEK---KLEQCRGFTFKEIEKLKEQLKLLQSL 286
 
Name Accession Description Interval E-value
SPATA24 pfam15175
Spermatogenesis-associated protein 24; This family of proteins bind to DNA and to TBP (TATA ...
 22-162 3.88e-78

Spermatogenesis-associated protein 24; This family of proteins bind to DNA and to TBP (TATA box binding protein), TATA-binding protein (TBP)-related protein 2 (TRF2) and several polycomb factors. It is likely to function as a transcription regulator.


Pssm-ID: 464544 [Multi-domain]  Cd Length: 170  Bit Score: 238.98  E-value: 3.88e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379755   22 LRDVIESQEELIHQLRNVMVLQDENFVSKEEFQAVEKKLVEEKAAHAKTKVLLAKEEEKLQFALGEVEVLSKQLEKEKLA 101
Cdd:pfam15175   1 MKDLFHVQQNTLEQLRQTARRQKENFVSKEEYEAVAKKLEEERAEHAKTKLLLAKESEKLQFALGEIEVLSKQLEREKKA 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530379755  102 FEKALSSVKSKVLQESSKKDQLITKCNEIESHIIKQEDILNGKENEIKELQQVISQQKQIF 162
Cdd:pfam15175  81 FEKALGSVKSKALRESKKADQLKTKCSEIESHCIRQEDILNGKENEIKELKQRLSKQKEIH 141
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 19-160 6.11e-07

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 51.65  E-value: 6.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379755   19 LDQLRDVIESQEELIHQLRNVMVLqdenfvsKEEFQAVEKKLV-----EEKAAH-AKTKVLLAKEEEklQFALGEVEVLS 92
Cdd:pfam05483 407 LEELKKILAEDEKLLDEKKQFEKI-------AEELKGKEQELIfllqaREKEIHdLEIQLTAIKTSE--EHYLKEVEDLK 477

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530379755   93 KQLEKEKL------AFEKALSSVKSKVLQESSkkDQLItkcnEIESHiikQEDILNGKENEIKELQQVISQQKQ 160
Cdd:pfam05483 478 TELEKEKLknieltAHCDKLLLENKELTQEAS--DMTL----ELKKH---QEDIINCKKQEERMLKQIENLEEK 542
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
17-160 7.09e-07

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 51.06  E-value: 7.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379755  17 LALDQLRDVIESQEELIHQLRNvmvLQDENFVSKEEFQAVEKKLVEEKAAHAKTKVLLAKEEEKLQFALGEVEVLSKQLE 96
Cdd:COG4372   28 ALSEQLRKALFELDKLQEELEQ---LREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELE 104

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530379755  97 ---KEKLAFEKALSSVKSKVLQESSKKDQLITKCNEIESHIIKQEDILNGKENEIKELQQVISQQKQ 160
Cdd:COG4372  105 slqEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQ 171
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 19-160 1.08e-05

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 46.46  E-value: 1.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379755  19 LDQLRDV--IESQ-EELIHQLRNVmvlqdenfvsKEEFQAVEKKLVEEKAAHAKTKVLLAKEEEKLQFALGEVEVLSKQL 95
Cdd:COG1579    6 LRALLDLqeLDSElDRLEHRLKEL----------PAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARI 75

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530379755  96 EKeklaFEKALSSVKS----KVLQ---ESSKKDQlitkcNEIESHIIKQEDILNGKENEIKELQQVISQQKQ 160
Cdd:COG1579   76 KK----YEEQLGNVRNnkeyEALQkeiESLKRRI-----SDLEDEILELMERIEELEEELAELEAELAELEA 138
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 49-163 3.51e-05

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 46.17  E-value: 3.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379755   49 SKEEFQAVEKKLVEEKAAHAKTKVLLAKEEEKLQFALGEVEVLSKQ---LEKEKLAFEKALSSVKSKVLQESSKKDQL-- 123
Cdd:TIGR04523 122 LEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQkeeLENELNLLEKEKLNIQKNIDKIKNKLLKLel 201

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 530379755  124 --------ITKCNEIESHIIKQEDILNGKENEIKELQQVISQQKQIFS 163
Cdd:TIGR04523 202 llsnlkkkIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEIS 249
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 19-160 1.31e-04

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 44.24  E-value: 1.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379755   19 LDQLRDVIESQ-EELIHQLRNVmvlqdenfvsKEEFQAVEKKLVEekaahaKTKVLLAKEEEKlqfalgevevlsKQLEK 97
Cdd:TIGR04523 459 LDNTRESLETQlKVLSRSINKI----------KQNLEQKQKELKS------KEKELKKLNEEK------------KELEE 510

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530379755   98 EKLAFEKALSSVKSKVLQESSKKDQLITKCNEIESHIIKQEDILN--GKENEIKELQQVISQQKQ 160
Cdd:TIGR04523 511 KVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKkeNLEKEIDEKNKEIEELKQ 575
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 18-163 2.22e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.51  E-value: 2.22e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379755    18 ALDQLRDVIESQEELIHQLrnvmvlQDENFVSKEEFQAVEKKLVEEKAAHAKTKVLLAKEEEKLQFALGEVEVLSKQLEK 97
Cdd:TIGR02168  776 ELAEAEAEIEELEAQIEQL------KEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEE 849

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530379755    98 EKLAFEKALSSVKSKVLQESSKKDQLITKCNEIESHI----------IKQEDILNGKENEIKELQQVISQQKQIFS 163
Cdd:TIGR02168  850 LSEDIESLAAEIEELEELIEELESELEALLNERASLEealallrselEELSEELRELESKRSELRRELEELREKLA 925
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
 27-153 8.88e-04

Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.


Pssm-ID: 464932 [Multi-domain]  Cd Length: 329  Bit Score: 40.95  E-value: 8.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379755   27 ESQEELIHQLRNVMVLQDENfVSKEEFQAVEK----KLVEE-KAAHA------KTKVLLAKEEEKLQFALGEVEVLSKQL 95
Cdd:pfam15905 188 VTQKNLEHSKGKVAQLEEKL-VSTEKEKIEEKseteKLLEYiTELSCvseqveKYKLDIAQLEELLKEKNDEIESLKQSL 266

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530379755   96 EKEKLAFEKALSSVKSKVLQESSKKDQLITKCNEIESHIIKQ----EDILNGKENEIKELQQ 153
Cdd:pfam15905 267 EEKEQELSKQIKDLNEKCKLLESEKEELLREYEEKEQTLNAEleelKEKLTLEEQEHQKLQQ 328
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 17-161 9.05e-04

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 41.50  E-value: 9.05e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379755    17 LALDQLRDVIESQEELIHQLRNvmvLQDENFVSKEEFQAVEKKLVEEKAAHAKTKVLLAKEEEKLQFALGEVEVLSKQLE 96
Cdd:pfam02463  227 LYLDYLKLNEERIDLLQELLRD---EQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELL 303

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530379755    97 KEKLafekaLSSVKSKVLQESSKKDQlitkcnEIESHIIKQEDILNGKENEIKELQQVISQQKQI 161
Cdd:pfam02463  304 KLER-----RKVDDEEKLKESEKEKK------KAEKELKKEKEEIEELEKELKELEIKREAEEEE 357
PRK12704 PRK12704
phosphodiesterase; Provisional
 48-161 1.66e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.53  E-value: 1.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379755  48 VSKEEFQAveKKLVEEkaahAKTKVLLAKEEEKLQfALGEVEVLSKQLEKEKLAFEKALSSVKSKVLQES---SKKDQLI 124
Cdd:PRK12704  33 IKEAEEEA--KRILEE----AKKEAEAIKKEALLE-AKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEenlDRKLELL 105

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 530379755 125 TKcneIESHIIKQEDILNGKENEIKELQQVIS--QQKQI 161
Cdd:PRK12704 106 EK---REEELEKKEKELEQKQQELEKKEEELEelIEEQL 141
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 19-161 2.06e-03

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 40.00  E-value: 2.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379755    19 LDQLRDVIESQEELIHQLrnVMVLQDENFVSKEEFQaVEKKLVEEKAAHAKTkvLLAKEEEKLQFALGEVEVLSKQLEKe 98
Cdd:smart00787 156 LKEDYKLLMKELELLNSI--KPKLRDRKDALEEELR-QLKQLEDELEDCDPT--ELDRAKEKLKKLLQEIMIKVKKLEE- 229

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530379755    99 klaFEKALSSVKSKVLQESSKKDQLITKCNEIEShiiKQEDILNGKENEIKELQQVISQQKQI 161
Cdd:smart00787 230 ---LEEELQELESKIEDLTNKKSELNTEIAEAEK---KLEQCRGFTFKEIEKLKEQLKLLQSL 286
DUF4200 pfam13863
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ...
 50-161 4.04e-03

Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil domain of unknwon function.


Pssm-ID: 464003 [Multi-domain]  Cd Length: 119  Bit Score: 37.16  E-value: 4.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379755   50 KEEFQaVEKKLVEEKAAHAKTKVLLAKEEEKLqfalgevEVLSKQLEKEKLAFEKALSSVKSKVLQESSKKDQlitkcnE 129
Cdd:pfam13863   6 REMFL-VQLALDAKREEIERLEELLKQREEEL-------EKKEQELKEDLIKFDKFLKENDAKRRRALKKAEE------E 71

                          90       100       110
                  ....*....|....*....|....*....|..
gi 530379755  130 IESHIIKQEDILNgKENEIKELQQVISQQKQI 161
Cdd:pfam13863  72 TKLKKEKEKEIKK-LTAQIEELKSEISKLEEK 102
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 18-157 4.36e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 39.27  E-value: 4.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379755    18 ALDQLRDVIESQEELIHQLRNVMVLQDENFVSKEEFQAVEKKLVEEKAAHaktKVLLAKEEEKLQFALGEVEVLSKQLEK 97
Cdd:TIGR02168  713 ELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAE---IEELEERLEEAEEELAEAEAEIEELEA 789

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530379755    98 -------EKLAFEKALSSVKSKVLQESSKKDQLITKCNEIESHIIKQEDILNGKENEIKELQQVISQ 157
Cdd:TIGR02168  790 qieqlkeELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIES 856
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
19-161 4.39e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.12  E-value: 4.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379755  19 LDQLRDVIESQEELIHQLRNvmvlqdENFVSKEEFQAVEKKLVEEKAAHAKTKVLLAKEEEKLQFALGEVEVLSKQ---L 95
Cdd:COG4372   54 LEQAREELEQLEEELEQARS------ELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKErqdL 127

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530379755  96 EKEKLAFEKALSSVKSKVLQESSKKDQLITKCNEIESHI--IKQEDILNGKENEIKELQQVISQQKQI 161
Cdd:COG4372  128 EQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELaaLEQELQALSEAEAEQALDELLKEANRN 195
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 20-163 4.78e-03

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 39.18  E-value: 4.78e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379755    20 DQLRDVIESQEELIHQLRNVMVLQDENFVSKEEFQAVEKKLVEEKAAHAKTKVLLAKEEEKLQfalgevEVLSKQLEKEK 99
Cdd:pfam02463  271 LKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKE------KEEIEELEKEL 344

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530379755   100 LAFEKALSSVKSKVLQESSKKDQLITKCNEI-------ESHIIKQEDILNGKENEIKELQQVISQQKQIFS 163
Cdd:pfam02463  345 KELEIKREAEEEEEEELEKLQEKLEQLEEELlakkkleSERLSSAAKLKEEELELKSEEEKEAQLLLELAR 415
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
 35-163 5.16e-03

Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.


Pssm-ID: 464932 [Multi-domain]  Cd Length: 329  Bit Score: 38.64  E-value: 5.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379755   35 QLRNVMVLQDENFVSKEEFQAVEKKLVEEKAAHAKTKVllAKEEEKLQFAlgEVEVLSKQLEKEKL-AFEKALSSVKSKV 113
Cdd:pfam15905 163 KLRNKLEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKV--AQLEEKLVST--EKEKIEEKSETEKLlEYITELSCVSEQV 238

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 530379755  114 lqESSKKDqlitkcneieshIIKQEDILNGKENEIKELQQVISQQKQIFS 163
Cdd:pfam15905 239 --EKYKLD------------IAQLEELLKEKNDEIESLKQSLEEKEQELS 274
Tropomyosin pfam00261
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ...
 54-154 5.92e-03

Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.


Pssm-ID: 459736 [Multi-domain]  Cd Length: 235  Bit Score: 38.09  E-value: 5.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379755   54 QAVEKKL--VEEKAAHAKTKvlLAKEEEKLQFALGEVEVLSK---QLEKEKLAFEKALSSVKSKVLQESSKKDQLITKCN 128
Cdd:pfam00261   4 QQIKEELdeAEERLKEAMKK--LEEAEKRAEKAEAEVAALNRriqLLEEELERTEERLAEALEKLEEAEKAADESERGRK 81

                          90       100
                  ....*....|....*....|....*.
gi 530379755  129 EIESHIIKQEDILNGKENEIKELQQV 154
Cdd:pfam00261  82 VLENRALKDEEKMEILEAQLKEAKEI 107
PTZ00440 PTZ00440
reticulocyte binding protein 2-like protein; Provisional
 19-157 6.90e-03

reticulocyte binding protein 2-like protein; Provisional


Pssm-ID: 240419 [Multi-domain]  Cd Length: 2722  Bit Score: 39.04  E-value: 6.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379755   19 LDQLRDVIESQEELIHQLRNVMVLQDENFVSKEEFQAVEKKLveekaaHAKTKVLLAK-EEEKLQFALGEvevLSKQLEK 97
Cdd:PTZ00440  580 VDHIKDIISLNDEIDNIIQQIEELINEALFNKEKFINEKNDL------QEKVKYILNKfYKGDLQELLDE---LSHFLDD 650

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530379755   98 EKLAFEKALSSVKSKVLQESSKKDQliTKCNEIESHIIKQ---------EDILNGKENEIKELQQVISQ 157
Cdd:PTZ00440  651 HKYLYHEAKSKEDLQTLLNTSKNEY--EKLEFMKSDNIDNiiknlkkelQNLLSLKENIIKKQLNNIEQ 717
 
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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