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Conserved domains on  [gi|1207186342|ref|XP_021326790|]
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kinetochore scaffold 1 isoform X2 [Danio rerio]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DRWD-C_Knl1 cd22892
C-terminal double-RWD domain of kinetochore scaffold 1 and related proteins; Kinetochore ...
 1576-1676 6.50e-49

C-terminal double-RWD domain of kinetochore scaffold 1 and related proteins; Kinetochore scaffold 1 (KNL1 or Knl1, also known as Spc105, Spc7, and Blinkin) coordinates the spindle assembly checkpoint (SAC), a signaling pathway that delays chromosome segregation until all sister chromatids are properly attached to spindle microtubules (MTs). Knl1 is part of the KMN network, a conserved kinetochore protein complex that connects kinetochores to MTs. Knl1 has been shown to play an effective role in decreasing apoptosis and promoting the proliferation of colorectal cancer cells, suggesting that its inhibition may represent a promising therapeutic approach for colorectal cancer patients. Knl1 contains tandem RWD domains, also known as a double-RWD domain, DRWD, which has been shown to bind the Mis12 complex, consisting of Dsn1 and Nsl1, that tethers directly onto the underlying chromatin layer and mediates kinetochore targeting of Knl1. The model corresponds to the C-terminal double-RWD domain (DRWD-C).


:

Pssm-ID: 467644  Cd Length: 99  Bit Score: 169.10  E-value: 6.50e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186342 1576 LLGEEIHRLKKWGGlRLRILKITCTDTRVHVIFSSLKAFEKFELSLTVTPDYPfGPLHIQDFKNHMGNTRLDQLEEIISS 1655
Cdd:cd22892      1 LLGEEIEYLKRWGG-KYNILKIDINDTNVHLLFSSSAAFAKFEITLSLTSGYP-SVPLPFTFENHIGNTSQDQIEEVISK 78

                           90       100
                   ....*....|....*....|.
gi 1207186342 1656 VKPAKNYLSKILKKIHDDLLC 1676
Cdd:cd22892     79 VPPGKNYLKRVVKKIHQDLLQ 99
DRWD-N_Knl1 cd22817
N-terminal double-RWD domain of kinetochore scaffold 1 and related proteins; Kinetochore ...
 1458-1569 1.50e-45

N-terminal double-RWD domain of kinetochore scaffold 1 and related proteins; Kinetochore scaffold 1 (KNL1 or Knl1, also known as Spc105, Spc7, and Blinkin) coordinates the spindle assembly checkpoint (SAC), a signaling pathway that delays chromosome segregation until all sister chromatids are properly attached to spindle microtubules (MTs). Knl1 is part of the KMN network, a conserved kinetochore protein complex that connects kinetochores to MTs. Knl1 has been shown to play an effective role in decreasing apoptosis and promoting the proliferation of colorectal cancer cells, suggesting that its inhibition may represent a promising therapeutic approach for colorectal cancer patients. Knl1 contains tandem RWD domains, also known as a double-RWD domain, DRWD, which has been shown to bind the Mis12 complex, consisting of Dsn1 and Nsl1, that tethers directly onto the underlying chromatin layer and mediates kinetochore targeting of Knl1. The model corresponds to N-terminal double-RWD domain (DRWD-N).


:

Pssm-ID: 467642  Cd Length: 112  Bit Score: 159.75  E-value: 1.50e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186342 1458 SSSLKSHLATLNSLNEWRLEATDETGALFSFLHKTVHLQVNLQTPAGKEWMAEDVERNVDVVFQLQLDGQKSECHASMIH 1537
Cdd:cd22817      1 TQELESHLELLNSLSEWRLEEWDENQAVFTFLYDSLELEVKFEDSKDGTAFEKPERKIVDISFQSLLDEEKAPPSARLVH 80

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1207186342 1538 NLLATKIESQSHWKQRYTTTRHIPELLHTMSL 1569
Cdd:cd22817     81 KLIFQFIESKESWKETYPTQRDLPKLLHDVSL 112
SMC_N super family cl47134
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 1266-1485 1.84e-05

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.


The actual alignment was detected with superfamily member TIGR02169:

Pssm-ID: 481474 [Multi-domain]  Cd Length: 1164  Bit Score: 49.68  E-value: 1.84e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186342 1266 EDLLK-EKYISHPKQRVYEQDCKNITEIVERLKEQMSAQEKSLRSINGALQQEicTLSEEQLKSFGSKLKERRAYFGKKS 1344
Cdd:TIGR02169  772 EDLHKlEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRL--TLEKEYLEKEIQELQEQRIDLKEQI 849

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186342 1345 KAVSHEMKgvlysELIKKtqdaKLSLISKIKETDEMIEDLDGCIKDLEtdlasvdamitGDRLDLPQAGPALKAKEEDlh 1424
Cdd:TIGR02169  850 KSIEKEIE-----NLNGK----KEELEEELEELEAALRDLESRLGDLK-----------KERDELEAQLRELERKIEE-- 907

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207186342 1425 rLNSAVTFKEREIGELEIQLKTLESQQ---EKLQGESSSLKSHLATLNSLNEWRLEATDETGAL 1485
Cdd:TIGR02169  908 -LEAQIEKKRKRLSELKAKLEALEEELseiEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRAL 970
 
Name Accession Description Interval E-value
DRWD-C_Knl1 cd22892
C-terminal double-RWD domain of kinetochore scaffold 1 and related proteins; Kinetochore ...
 1576-1676 6.50e-49

C-terminal double-RWD domain of kinetochore scaffold 1 and related proteins; Kinetochore scaffold 1 (KNL1 or Knl1, also known as Spc105, Spc7, and Blinkin) coordinates the spindle assembly checkpoint (SAC), a signaling pathway that delays chromosome segregation until all sister chromatids are properly attached to spindle microtubules (MTs). Knl1 is part of the KMN network, a conserved kinetochore protein complex that connects kinetochores to MTs. Knl1 has been shown to play an effective role in decreasing apoptosis and promoting the proliferation of colorectal cancer cells, suggesting that its inhibition may represent a promising therapeutic approach for colorectal cancer patients. Knl1 contains tandem RWD domains, also known as a double-RWD domain, DRWD, which has been shown to bind the Mis12 complex, consisting of Dsn1 and Nsl1, that tethers directly onto the underlying chromatin layer and mediates kinetochore targeting of Knl1. The model corresponds to the C-terminal double-RWD domain (DRWD-C).


Pssm-ID: 467644  Cd Length: 99  Bit Score: 169.10  E-value: 6.50e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186342 1576 LLGEEIHRLKKWGGlRLRILKITCTDTRVHVIFSSLKAFEKFELSLTVTPDYPfGPLHIQDFKNHMGNTRLDQLEEIISS 1655
Cdd:cd22892      1 LLGEEIEYLKRWGG-KYNILKIDINDTNVHLLFSSSAAFAKFEITLSLTSGYP-SVPLPFTFENHIGNTSQDQIEEVISK 78

                           90       100
                   ....*....|....*....|.
gi 1207186342 1656 VKPAKNYLSKILKKIHDDLLC 1676
Cdd:cd22892     79 VPPGKNYLKRVVKKIHQDLLQ 99
DRWD-N_Knl1 cd22817
N-terminal double-RWD domain of kinetochore scaffold 1 and related proteins; Kinetochore ...
 1458-1569 1.50e-45

N-terminal double-RWD domain of kinetochore scaffold 1 and related proteins; Kinetochore scaffold 1 (KNL1 or Knl1, also known as Spc105, Spc7, and Blinkin) coordinates the spindle assembly checkpoint (SAC), a signaling pathway that delays chromosome segregation until all sister chromatids are properly attached to spindle microtubules (MTs). Knl1 is part of the KMN network, a conserved kinetochore protein complex that connects kinetochores to MTs. Knl1 has been shown to play an effective role in decreasing apoptosis and promoting the proliferation of colorectal cancer cells, suggesting that its inhibition may represent a promising therapeutic approach for colorectal cancer patients. Knl1 contains tandem RWD domains, also known as a double-RWD domain, DRWD, which has been shown to bind the Mis12 complex, consisting of Dsn1 and Nsl1, that tethers directly onto the underlying chromatin layer and mediates kinetochore targeting of Knl1. The model corresponds to N-terminal double-RWD domain (DRWD-N).


Pssm-ID: 467642  Cd Length: 112  Bit Score: 159.75  E-value: 1.50e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186342 1458 SSSLKSHLATLNSLNEWRLEATDETGALFSFLHKTVHLQVNLQTPAGKEWMAEDVERNVDVVFQLQLDGQKSECHASMIH 1537
Cdd:cd22817      1 TQELESHLELLNSLSEWRLEEWDENQAVFTFLYDSLELEVKFEDSKDGTAFEKPERKIVDISFQSLLDEEKAPPSARLVH 80

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1207186342 1538 NLLATKIESQSHWKQRYTTTRHIPELLHTMSL 1569
Cdd:cd22817     81 KLIFQFIESKESWKETYPTQRDLPKLLHDVSL 112
Knl1_RWD_C pfam18210
Knl1 RWD C-terminal domain; This domain is found in Knl1, a sub-unit of the KMN network, ...
 1416-1578 2.51e-22

Knl1 RWD C-terminal domain; This domain is found in Knl1, a sub-unit of the KMN network, present in Homo sapiens. The KMN network is the core of the outer kinetochore which is responsible for microtubule binding/stabilization and controls the spindle assembly checkpoint. This domain is the second of two RING finger, WD repeat, DEAD-like helicase (RWD) domains. The tandem RWD domains mediate kinetochore targeting of the microtubule-binding subunits by interacting with the Mis12 complex. The Mis12 complex is a KMN sub-complex that tethers directly onto the underlying chromatin layer.


Pssm-ID: 465680 [Multi-domain]  Cd Length: 152  Bit Score: 94.83  E-value: 2.51e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186342 1416 LKAKEEDLhrlnsavtfkEREIGELEIQLKTLESQ---QEKLQGESSS------LKSHLATLNSLNEWRLEATDETGALF 1486
Cdd:pfam18210    2 LKEELEEL----------EEKLEELEERKQELLAAigeAERIREECWTseevlrLKEELEALESLHGWRITEVSDDTLVF 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186342 1487 SFLHKtVHLQVNLqtpagkewmaEDVERNVDVVFQLQLDGQKSECHASMIHNLLATKIESQSHWKQRYTTTRHIPELLHT 1566
Cdd:pfam18210   72 TYLSD-IELTFDF----------GASPKISSIDLESYLDDEKAPPSSLLVHRLAFFFLQSARDWVRKYPTQTSLPKLLQD 140

                          170
                   ....*....|..
gi 1207186342 1567 MSLVVGRLRLLG 1578
Cdd:pfam18210  141 VSLVWSRCRLLG 152
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 1266-1485 1.84e-05

chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 49.68  E-value: 1.84e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186342 1266 EDLLK-EKYISHPKQRVYEQDCKNITEIVERLKEQMSAQEKSLRSINGALQQEicTLSEEQLKSFGSKLKERRAYFGKKS 1344
Cdd:TIGR02169  772 EDLHKlEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRL--TLEKEYLEKEIQELQEQRIDLKEQI 849

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186342 1345 KAVSHEMKgvlysELIKKtqdaKLSLISKIKETDEMIEDLDGCIKDLEtdlasvdamitGDRLDLPQAGPALKAKEEDlh 1424
Cdd:TIGR02169  850 KSIEKEIE-----NLNGK----KEELEEELEELEAALRDLESRLGDLK-----------KERDELEAQLRELERKIEE-- 907

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207186342 1425 rLNSAVTFKEREIGELEIQLKTLESQQ---EKLQGESSSLKSHLATLNSLNEWRLEATDETGAL 1485
Cdd:TIGR02169  908 -LEAQIEKKRKRLSELKAKLEALEEELseiEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRAL 970
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 1360-1485 6.73e-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: 46.07  E-value: 6.73e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186342 1360 IKKTQDAKLSLISKIKETDEMIEDLDGCIKDLETDLASVDAMITGDRLDLPQAgpalkAKEEDLHRLNSAVTFKEREIGE 1439
Cdd:COG1579     33 LAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNV-----RNNKEYEALQKEIESLKRRISD 107

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1207186342 1440 LEIQLKTLESQQEKLQGESSSLKSHLATLNS-LNEWRLEATDETGAL 1485
Cdd:COG1579    108 LEDEILELMERIEELEEELAELEAELAELEAeLEEKKAELDEELAEL 154
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 1262-1465 9.58e-04

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: 43.94  E-value: 9.58e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186342 1262 TRTIEDLLKEKYISHPKQRVYEQDCKNITEIVERLKEQMSAQEKSLRSINGA-------LQQEICTLsEEQLKSFGSKLK 1334
Cdd:pfam05483  295 TKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAhsfvvteFEATTCSL-EELLRTEQQRLE 373

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186342 1335 ErrayfgkkskavSHEMKGVLYSELIKKTqdAKLSLISKIKETDEmIEdldgcIKDLETDLASvDAMITGDRLDLPQAGP 1414
Cdd:pfam05483  374 K------------NEDQLKIITMELQKKS--SELEEMTKFKNNKE-VE-----LEELKKILAE-DEKLLDEKKQFEKIAE 432

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1207186342 1415 ALKAKEEDLHRLNSAvtfKEREIGELEIQLKTLESQQEKLQGESSSLKSHL 1465
Cdd:pfam05483  433 ELKGKEQELIFLLQA---REKEIHDLEIQLTAIKTSEEHYLKEVEDLKTEL 480
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
1282-1485 2.96e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.36  E-value: 2.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186342 1282 YEQDCKNITEIVERLKEQMSAQEKSLRSingalQQEICTLSEEQLKSFGSKLKERRAyFGKKSKAVSHEMKGV--LYSEL 1359
Cdd:PRK03918   160 YENAYKNLGEVIKEIKRRIERLEKFIKR-----TENIEELIKEKEKELEEVLREINE-ISSELPELREELEKLekEVKEL 233

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186342 1360 -------------IKKTQDAKLSLISKIKETDEMIEDLDGCIKDLETDLASVdamitgdrldlpqagPALKAKEEDLHRL 1426
Cdd:PRK03918   234 eelkeeieelekeLESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKEL---------------KELKEKAEEYIKL 298

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1207186342 1427 NSAVTFKEREIGELEIQLKTLESQQEKLQGESSSLKSHLATLNSLNEWRLEATDETGAL 1485
Cdd:PRK03918   299 SEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEEL 357
 
Name Accession Description Interval E-value
DRWD-C_Knl1 cd22892
C-terminal double-RWD domain of kinetochore scaffold 1 and related proteins; Kinetochore ...
 1576-1676 6.50e-49

C-terminal double-RWD domain of kinetochore scaffold 1 and related proteins; Kinetochore scaffold 1 (KNL1 or Knl1, also known as Spc105, Spc7, and Blinkin) coordinates the spindle assembly checkpoint (SAC), a signaling pathway that delays chromosome segregation until all sister chromatids are properly attached to spindle microtubules (MTs). Knl1 is part of the KMN network, a conserved kinetochore protein complex that connects kinetochores to MTs. Knl1 has been shown to play an effective role in decreasing apoptosis and promoting the proliferation of colorectal cancer cells, suggesting that its inhibition may represent a promising therapeutic approach for colorectal cancer patients. Knl1 contains tandem RWD domains, also known as a double-RWD domain, DRWD, which has been shown to bind the Mis12 complex, consisting of Dsn1 and Nsl1, that tethers directly onto the underlying chromatin layer and mediates kinetochore targeting of Knl1. The model corresponds to the C-terminal double-RWD domain (DRWD-C).


Pssm-ID: 467644  Cd Length: 99  Bit Score: 169.10  E-value: 6.50e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186342 1576 LLGEEIHRLKKWGGlRLRILKITCTDTRVHVIFSSLKAFEKFELSLTVTPDYPfGPLHIQDFKNHMGNTRLDQLEEIISS 1655
Cdd:cd22892      1 LLGEEIEYLKRWGG-KYNILKIDINDTNVHLLFSSSAAFAKFEITLSLTSGYP-SVPLPFTFENHIGNTSQDQIEEVISK 78

                           90       100
                   ....*....|....*....|.
gi 1207186342 1656 VKPAKNYLSKILKKIHDDLLC 1676
Cdd:cd22892     79 VPPGKNYLKRVVKKIHQDLLQ 99
DRWD-N_Knl1 cd22817
N-terminal double-RWD domain of kinetochore scaffold 1 and related proteins; Kinetochore ...
 1458-1569 1.50e-45

N-terminal double-RWD domain of kinetochore scaffold 1 and related proteins; Kinetochore scaffold 1 (KNL1 or Knl1, also known as Spc105, Spc7, and Blinkin) coordinates the spindle assembly checkpoint (SAC), a signaling pathway that delays chromosome segregation until all sister chromatids are properly attached to spindle microtubules (MTs). Knl1 is part of the KMN network, a conserved kinetochore protein complex that connects kinetochores to MTs. Knl1 has been shown to play an effective role in decreasing apoptosis and promoting the proliferation of colorectal cancer cells, suggesting that its inhibition may represent a promising therapeutic approach for colorectal cancer patients. Knl1 contains tandem RWD domains, also known as a double-RWD domain, DRWD, which has been shown to bind the Mis12 complex, consisting of Dsn1 and Nsl1, that tethers directly onto the underlying chromatin layer and mediates kinetochore targeting of Knl1. The model corresponds to N-terminal double-RWD domain (DRWD-N).


Pssm-ID: 467642  Cd Length: 112  Bit Score: 159.75  E-value: 1.50e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186342 1458 SSSLKSHLATLNSLNEWRLEATDETGALFSFLHKTVHLQVNLQTPAGKEWMAEDVERNVDVVFQLQLDGQKSECHASMIH 1537
Cdd:cd22817      1 TQELESHLELLNSLSEWRLEEWDENQAVFTFLYDSLELEVKFEDSKDGTAFEKPERKIVDISFQSLLDEEKAPPSARLVH 80

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1207186342 1538 NLLATKIESQSHWKQRYTTTRHIPELLHTMSL 1569
Cdd:cd22817     81 KLIFQFIESKESWKETYPTQRDLPKLLHDVSL 112
Knl1_RWD_C pfam18210
Knl1 RWD C-terminal domain; This domain is found in Knl1, a sub-unit of the KMN network, ...
 1416-1578 2.51e-22

Knl1 RWD C-terminal domain; This domain is found in Knl1, a sub-unit of the KMN network, present in Homo sapiens. The KMN network is the core of the outer kinetochore which is responsible for microtubule binding/stabilization and controls the spindle assembly checkpoint. This domain is the second of two RING finger, WD repeat, DEAD-like helicase (RWD) domains. The tandem RWD domains mediate kinetochore targeting of the microtubule-binding subunits by interacting with the Mis12 complex. The Mis12 complex is a KMN sub-complex that tethers directly onto the underlying chromatin layer.


Pssm-ID: 465680 [Multi-domain]  Cd Length: 152  Bit Score: 94.83  E-value: 2.51e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186342 1416 LKAKEEDLhrlnsavtfkEREIGELEIQLKTLESQ---QEKLQGESSS------LKSHLATLNSLNEWRLEATDETGALF 1486
Cdd:pfam18210    2 LKEELEEL----------EEKLEELEERKQELLAAigeAERIREECWTseevlrLKEELEALESLHGWRITEVSDDTLVF 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186342 1487 SFLHKtVHLQVNLqtpagkewmaEDVERNVDVVFQLQLDGQKSECHASMIHNLLATKIESQSHWKQRYTTTRHIPELLHT 1566
Cdd:pfam18210   72 TYLSD-IELTFDF----------GASPKISSIDLESYLDDEKAPPSSLLVHRLAFFFLQSARDWVRKYPTQTSLPKLLQD 140

                          170
                   ....*....|..
gi 1207186342 1567 MSLVVGRLRLLG 1578
Cdd:pfam18210  141 VSLVWSRCRLLG 152
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 1266-1485 1.84e-05

chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 49.68  E-value: 1.84e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186342 1266 EDLLK-EKYISHPKQRVYEQDCKNITEIVERLKEQMSAQEKSLRSINGALQQEicTLSEEQLKSFGSKLKERRAYFGKKS 1344
Cdd:TIGR02169  772 EDLHKlEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRL--TLEKEYLEKEIQELQEQRIDLKEQI 849

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186342 1345 KAVSHEMKgvlysELIKKtqdaKLSLISKIKETDEMIEDLDGCIKDLEtdlasvdamitGDRLDLPQAGPALKAKEEDlh 1424
Cdd:TIGR02169  850 KSIEKEIE-----NLNGK----KEELEEELEELEAALRDLESRLGDLK-----------KERDELEAQLRELERKIEE-- 907

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207186342 1425 rLNSAVTFKEREIGELEIQLKTLESQQ---EKLQGESSSLKSHLATLNSLNEWRLEATDETGAL 1485
Cdd:TIGR02169  908 -LEAQIEKKRKRLSELKAKLEALEEELseiEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRAL 970
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 1360-1485 6.73e-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: 46.07  E-value: 6.73e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186342 1360 IKKTQDAKLSLISKIKETDEMIEDLDGCIKDLETDLASVDAMITGDRLDLPQAgpalkAKEEDLHRLNSAVTFKEREIGE 1439
Cdd:COG1579     33 LAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNV-----RNNKEYEALQKEIESLKRRISD 107

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1207186342 1440 LEIQLKTLESQQEKLQGESSSLKSHLATLNS-LNEWRLEATDETGAL 1485
Cdd:COG1579    108 LEDEILELMERIEELEEELAELEAELAELEAeLEEKKAELDEELAEL 154
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
1373-1481 1.70e-04

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 46.39  E-value: 1.70e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186342 1373 KIKETDEMIEDLDGCIKDLETDLASVDAMIT--GDRLDLpqagpaLKAKEEDLHRLNSAVTFKEREIGELEIQLKTLESQ 1450
Cdd:COG2433    414 EIRRLEEQVERLEAEVEELEAELEEKDERIErlERELSE------ARSEERREIRKDREISRLDREIERLERELEEERER 487

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1207186342 1451 QEKLQGESSSLKSHlatlnslneWRLEATDE 1481
Cdd:COG2433    488 IEELKRKLERLKEL---------WKLEHSGE 509
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 1357-1487 3.09e-04

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: 45.14  E-value: 3.09e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186342 1357 SELIKKTQDAKLSLISKIKETDEMIEDLDGCIKDLETDLASVDAmitgdrldlpqagpALKAKEEDLHRLNSAVTFKERE 1436
Cdd:COG4942     19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALER--------------RIAALARRIRALEQELAALEAE 84

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1207186342 1437 IGELEIQLKTLESQQEKLQGEsssLKSHLATLnslneWRLEATDETGALFS 1487
Cdd:COG4942     85 LAELEKEIAELRAELEAQKEE---LAELLRAL-----YRLGRQPPLALLLS 127
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1278-1500 4.01e-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: 45.43  E-value: 4.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186342 1278 KQRVYEQDCKNITEIVERLKEQMSAQEKSLRSIN---GALQQEICTLSEEQLKSFGSKLKERRAYFGKKSKAVSHEMKGV 1354
Cdd:TIGR02168  706 ELEELEEELEQLRKELEELSRQISALRKDLARLEaevEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIE 785

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186342 1355 LYSELIKKTQDAKLSLISKIKETDEMIEDLDGCIKDLETDLASVDAMITGDRLDLPQAGPALKAKEEDLHRLNSAVTFKE 1434
Cdd:TIGR02168  786 ELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELE 865

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207186342 1435 REIGELEIQLKTLESQQEKLQGESSSLKSHLATLNS-LNEWRLEATDETGALFSFLHKTVHLQVNLQ 1500
Cdd:TIGR02168  866 ELIEELESELEALLNERASLEEALALLRSELEELSEeLRELESKRSELRRELEELREKLAQLELRLE 932
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 1262-1465 9.58e-04

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: 43.94  E-value: 9.58e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186342 1262 TRTIEDLLKEKYISHPKQRVYEQDCKNITEIVERLKEQMSAQEKSLRSINGA-------LQQEICTLsEEQLKSFGSKLK 1334
Cdd:pfam05483  295 TKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAhsfvvteFEATTCSL-EELLRTEQQRLE 373

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186342 1335 ErrayfgkkskavSHEMKGVLYSELIKKTqdAKLSLISKIKETDEmIEdldgcIKDLETDLASvDAMITGDRLDLPQAGP 1414
Cdd:pfam05483  374 K------------NEDQLKIITMELQKKS--SELEEMTKFKNNKE-VE-----LEELKKILAE-DEKLLDEKKQFEKIAE 432

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1207186342 1415 ALKAKEEDLHRLNSAvtfKEREIGELEIQLKTLESQQEKLQGESSSLKSHL 1465
Cdd:pfam05483  433 ELKGKEQELIFLLQA---REKEIHDLEIQLTAIKTSEEHYLKEVEDLKTEL 480
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
1370-1490 9.73e-04

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.14  E-value: 9.73e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186342 1370 LISKIKETDEMIEDLDGCIKDLETDLASVD---------AMITGDRLDLPQAGPALKAKEEDLHRL---NSAVTFKEREI 1437
Cdd:COG4913    615 LEAELAELEEELAEAEERLEALEAELDALQerrealqrlAEYSWDEIDVASAEREIAELEAELERLdasSDDLAALEEQL 694

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1207186342 1438 GELEIQLKTLESQQEKLQGESSSLKSHLATLNSL---NEWRLEATDETGALFSFLH 1490
Cdd:COG4913    695 EELEAELEELEEELDELKGEIGRLEKELEQAEEEldeLQDRLEAAEDLARLELRAL 750
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1357-1597 2.01e-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: 43.12  E-value: 2.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186342 1357 SELIKKTQDAKLSLISKIKETDEMIEDLDGCIKDLETDLASVDAMITGDRLDLPQAGPALKAKEEDLHRLNSAVTFKERE 1436
Cdd:TIGR02168  683 EEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAE 762

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186342 1437 IGELEIQL--------------KTLESQQEKLQGESSSLKSHLATLNS-LNEWRLEATDETGALFSFLHKTVHLQVNLQT 1501
Cdd:TIGR02168  763 IEELEERLeeaeeelaeaeaeiEELEAQIEQLKEELKALREALDELRAeLTLLNEEAANLRERLESLERRIAATERRLED 842

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186342 1502 PAG-KEWMAEDVERNVDVVFQLQLDGQKSECHASMIHNLLATKIE-SQSHWKQRYTTTRHIPELLHTMSLVVGRLRLLGE 1579
Cdd:TIGR02168  843 LEEqIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEaLALLRSELEELSEELRELESKRSELRRELEELRE 922

                          250
                   ....*....|....*....
gi 1207186342 1580 EIHRLK-KWGGLRLRILKI 1597
Cdd:TIGR02168  923 KLAQLElRLEGLEVRIDNL 941
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 1263-1451 2.52e-03

chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 42.75  E-value: 2.52e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186342 1263 RTIEDLLKEKYISHPKQRVYEQDCKNITEIVERL----------KEQMSAQEKSLRSINGALQQEICTLSEEQLKSFgSK 1332
Cdd:TIGR02169  308 RSIAEKERELEDAEERLAKLEAEIDKLLAEIEELereieeerkrRDKLTEEYAELKEELEDLRAELEEVDKEFAETR-DE 386

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186342 1333 LKERRayfgKKSKAVSHEMKGVLYSelIKKTQDAKLSLISKIKETDEMIEDLDGCIKDLETDLASVDAMITGDRLDLPQA 1412
Cdd:TIGR02169  387 LKDYR----EKLEKLKREINELKRE--LDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQL 460

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1207186342 1413 GPALK-------AKEEDLHRLNSAVTFKEREIGELEIQLKTLESQQ 1451
Cdd:TIGR02169  461 AADLSkyeqelyDLKEEYDRVEKELSKLQRELAEAEAQARASEERV 506
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 1258-1481 2.94e-03

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 42.73  E-value: 2.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186342 1258 GAGETRTIEDLLKEKYISHPKQRVyeqdcKNITEIVERLKEQMSAQEKSLRSINGALQ-QEICTLSEEQLKSFGSKLKE- 1335
Cdd:TIGR00606  730 GLAPGRQSIIDLKEKEIPELRNKL-----QKVNRDIQRLKNDIEEQETLLGTIMPEEEsAKVCLTDVTIMERFQMELKDv 804

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186342 1336 RRAYFGKKSKAVSHEMKgVLYSELIKKTQDAKLSL---ISKIKETDEMIEDLDGCIKDLETDLASVDAmitgDRLDLPQA 1412
Cdd:TIGR00606  805 ERKIAQQAAKLQGSDLD-RTVQQVNQEKQEKQHELdtvVSKIELNRKLIQDQQEQIQHLKSKTNELKS----EKLQIGTN 879

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207186342 1413 GPALKAKEEDLHRLNSAVTFKEREIGELEIQLKTLESQQEKLQGESSSLKSHLATLNSLNEWRLEATDE 1481
Cdd:TIGR00606  880 LQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKE 948
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
1282-1485 2.96e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.36  E-value: 2.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186342 1282 YEQDCKNITEIVERLKEQMSAQEKSLRSingalQQEICTLSEEQLKSFGSKLKERRAyFGKKSKAVSHEMKGV--LYSEL 1359
Cdd:PRK03918   160 YENAYKNLGEVIKEIKRRIERLEKFIKR-----TENIEELIKEKEKELEEVLREINE-ISSELPELREELEKLekEVKEL 233

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186342 1360 -------------IKKTQDAKLSLISKIKETDEMIEDLDGCIKDLETDLASVdamitgdrldlpqagPALKAKEEDLHRL 1426
Cdd:PRK03918   234 eelkeeieelekeLESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKEL---------------KELKEKAEEYIKL 298

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1207186342 1427 NSAVTFKEREIGELEIQLKTLESQQEKLQGESSSLKSHLATLNSLNEWRLEATDETGAL 1485
Cdd:PRK03918   299 SEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEEL 357
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1283-1451 3.89e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.43  E-value: 3.89e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186342 1283 EQDCKNITEIVERLKEQMSAQEKSLRSINGALQQeictlSEEQLKSFGSKLKERRAYFGKKSkavshemkgvlysELIKK 1362
Cdd:COG4372     44 QEELEQLREELEQAREELEQLEEELEQARSELEQ-----LEEELEELNEQLQAAQAELAQAQ-------------EELES 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186342 1363 TQDAKLSLISKIKETDEMIEDLDGCIKDLETDLASVDAmitgdrldlpqagpALKAKEEDLHRLNSAVTFKEREIGELEI 1442
Cdd:COG4372    106 LQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQS--------------EIAEREEELKELEEQLESLQEELAALEQ 171


                   ....*....
gi 1207186342 1443 QLKTLESQQ 1451
Cdd:COG4372    172 ELQALSEAE 180
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 1265-1470 6.34e-03

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: 41.16  E-value: 6.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186342 1265 IEDLLKEKyishpkqRVYEQDCKNITEIVERLKEQMSAQEKslrsINGALQQEICTLSEEQLKsfgsKLKERRayfgkks 1344
Cdd:TIGR04523  372 IEKLKKEN-------QSYKQEIKNLESQINDLESKIQNQEK----LNQQKDEQIKKLQQEKEL----LEKEIE------- 429

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186342 1345 kavshemkgvLYSELIKKTQDAKLSLISKIKETDEMIEDLDGCIKDLETDLASVDAMITGDRLDLPQAGPALKAKEEDLH 1424
Cdd:TIGR04523  430 ----------RLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELK 499

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1207186342 1425 RLNSAVTFKEREIGELEIQLKTLESQQEKLQGESSSLKSHLATLNS 1470
Cdd:TIGR04523  500 KLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLED 545
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 1283-1465 7.26e-03

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: 39.91  E-value: 7.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186342 1283 EQDCKNITEIVERLKEQMSAQEKSLRSINGALQQEictlsEEQLKSFGSKLKERRAyfgkkskavshemkgvlyseLIKK 1362
Cdd:COG1579     23 EHRLKELPAELAELEDELAALEARLEAAKTELEDL-----EKEIKRLELEIEEVEA--------------------RIKK 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186342 1363 TQDaKLSLISKIKETDEM---IEDLDGCIKDLETDLASVDAMITGDRLDLPQAGPALKAKEEDLhrlnsavtfkEREIGE 1439
Cdd:COG1579     78 YEE-QLGNVRNNKEYEALqkeIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAEL----------EEKKAE 146

                          170       180
                   ....*....|....*....|....*.
gi 1207186342 1440 LEIQLKTLESQQEKLQGESSSLKSHL 1465
Cdd:COG1579    147 LDEELAELEAELEELEAEREELAAKI 172
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 1264-1471 9.20e-03

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: 40.77  E-value: 9.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186342 1264 TIEDLLKEKYishpkqrVYEQDCKNITEIVERLKEQMSAQEKSLRSINGALQQ----------EICTLSEE--QLKSFGS 1331
Cdd:TIGR04523  441 EIKDLTNQDS-------VKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQkqkelkskekELKKLNEEkkELEEKVK 513

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186342 1332 KLKERRAYFGKKSKAVSHEMKGV------LYSELIKKTQDAKLSLISK-IKETDEMIEDLDGCIKDLETDLASVDAMItg 1404
Cdd:TIGR04523  514 DLTKKISSLKEKIEKLESEKKEKeskisdLEDELNKDDFELKKENLEKeIDEKNKEIEELKQTQKSLKKKQEEKQELI-- 591

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207186342 1405 drldlpqagpalKAKEEDLHRLNSAVTFKEREIGELEIQLKTLESQQEKLQGESSSLKSHLATLNSL 1471
Cdd:TIGR04523  592 ------------DQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQE 646
 
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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