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Conserved domains on  [gi|1647818745|ref|NP_001357527|]
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homeobox protein cut-like 2 isoform 2 [Homo sapiens]

Protein Classification

CUT and homeodomain domain-containing protein( domain architecture ID 11131078)

CUT and homeodomain domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CUT pfam02376
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in ...
 981-1057 1.60e-31

CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in cooperation with the homeodomain, often found downstream of the CUT domain. Multiple copies of the CUT domain can exist in one protein.


:

Pssm-ID: 460543  Cd Length: 78  Bit Score: 118.46  E-value: 1.60e-31
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1647818745  981 MSPELDTYSITKRVKEVLTDNNLGQRLFGESILGLTQGSVSDLLSRPKPWHKLSLKGREpFVRMQLWLNDPHNVEKL 1057
Cdd:pfam02376    1 DSEELDTKDIADRIKEELKRHKISQAVFAEKVLNRSQGTLSDLLRKPKPWEKLKSGGRT-FIRMYNWLSLPEDERME 76
CUT pfam02376
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in ...
 830-903 2.88e-29

CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in cooperation with the homeodomain, often found downstream of the CUT domain. Multiple copies of the CUT domain can exist in one protein.


:

Pssm-ID: 460543  Cd Length: 78  Bit Score: 111.92  E-value: 2.88e-29
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1647818745  830 MYREVDTLELTRQVKEKLAKNGICQRIFGEKVLGLSQGSVSDMLSRPKPWSKLTQKGREpFIRMQLWLSDQLGQ 903
Cdd:pfam02376    1 DSEELDTKDIADRIKEELKRHKISQAVFAEKVLNRSQGTLSDLLRKPKPWEKLKSGGRT-FIRMYNWLSLPEDE 73
CUT pfam02376
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in ...
 491-563 2.65e-26

CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in cooperation with the homeodomain, often found downstream of the CUT domain. Multiple copies of the CUT domain can exist in one protein.


:

Pssm-ID: 460543  Cd Length: 78  Bit Score: 103.44  E-value: 2.65e-26
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1647818745  491 LDTAEIAFQVKEQLLKHNIGQRVFGHYVLGLSQGSVSEILARPKPWRKLTVKGKEpFIKMKQFLSDEQNVLAL 563
Cdd:pfam02376    5 LDTKDIADRIKEELKRHKISQAVFAEKVLNRSQGTLSDLLRKPKPWEKLKSGGRT-FIRMYNWLSLPEDERME 76
Homeodomain pfam00046
Homeodomain;
1107-1163 1.26e-14

Homeodomain;


:

Pssm-ID: 459649 [Multi-domain]  Cd Length: 57  Bit Score: 69.45  E-value: 1.26e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1647818745 1107 KKPRVVLAPEEKEALRKAYQLEPYPSQQTIELLSFQLNLKTNTVINWFHNYRSRMRR 1163
Cdd:pfam00046    1 RRKRTTFTPEQLEELEKEFQENPYPSAEEREELAAQLGLTERQVKVWFQNRRAKWKR 57
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 117-317 7.80e-09

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 60.34  E-value: 7.80e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1647818745  117 QRNEAEK----QKGLQEVQITLAA-RLGEAEEKIKVLHSALKATQAELLELRRKYDEEAASkadevglimtnLEKANQRA 191
Cdd:COG1196    208 QAEKAERyrelKEELKELEAELLLlKLRELEAELEELEAELEELEAELEELEAELAELEAE-----------LEELRLEL 276

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1647818745  192 EAAQREVESLREQLASVNSSIRlaccspqgpsgdkvnftlcsgpRLEAALASKDREILRLLKDVQHLQSSLQELEEASAN 271
Cdd:COG1196    277 EELELELEEAQAEEYELLAELA----------------------RLEQDIARLEERRRELEERLEELEEELAELEEELEE 334

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1647818745  272 QIADLERQLTAKSEAIEKLEEKLQAQSDYEEIKTELSILKAMKLAS 317
Cdd:COG1196    335 LEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380
 
Name Accession Description Interval E-value
CUT pfam02376
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in ...
 981-1057 1.60e-31

CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in cooperation with the homeodomain, often found downstream of the CUT domain. Multiple copies of the CUT domain can exist in one protein.


Pssm-ID: 460543  Cd Length: 78  Bit Score: 118.46  E-value: 1.60e-31
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1647818745  981 MSPELDTYSITKRVKEVLTDNNLGQRLFGESILGLTQGSVSDLLSRPKPWHKLSLKGREpFVRMQLWLNDPHNVEKL 1057
Cdd:pfam02376    1 DSEELDTKDIADRIKEELKRHKISQAVFAEKVLNRSQGTLSDLLRKPKPWEKLKSGGRT-FIRMYNWLSLPEDERME 76
CUT pfam02376
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in ...
 830-903 2.88e-29

CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in cooperation with the homeodomain, often found downstream of the CUT domain. Multiple copies of the CUT domain can exist in one protein.


Pssm-ID: 460543  Cd Length: 78  Bit Score: 111.92  E-value: 2.88e-29
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1647818745  830 MYREVDTLELTRQVKEKLAKNGICQRIFGEKVLGLSQGSVSDMLSRPKPWSKLTQKGREpFIRMQLWLSDQLGQ 903
Cdd:pfam02376    1 DSEELDTKDIADRIKEELKRHKISQAVFAEKVLNRSQGTLSDLLRKPKPWEKLKSGGRT-FIRMYNWLSLPEDE 73
CUT pfam02376
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in ...
 491-563 2.65e-26

CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in cooperation with the homeodomain, often found downstream of the CUT domain. Multiple copies of the CUT domain can exist in one protein.


Pssm-ID: 460543  Cd Length: 78  Bit Score: 103.44  E-value: 2.65e-26
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1647818745  491 LDTAEIAFQVKEQLLKHNIGQRVFGHYVLGLSQGSVSEILARPKPWRKLTVKGKEpFIKMKQFLSDEQNVLAL 563
Cdd:pfam02376    5 LDTKDIADRIKEELKRHKISQAVFAEKVLNRSQGTLSDLLRKPKPWEKLKSGGRT-FIRMYNWLSLPEDERME 76
Homeodomain pfam00046
Homeodomain;
1107-1163 1.26e-14

Homeodomain;


Pssm-ID: 459649 [Multi-domain]  Cd Length: 57  Bit Score: 69.45  E-value: 1.26e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1647818745 1107 KKPRVVLAPEEKEALRKAYQLEPYPSQQTIELLSFQLNLKTNTVINWFHNYRSRMRR 1163
Cdd:pfam00046    1 RRKRTTFTPEQLEELEKEFQENPYPSAEEREELAAQLGLTERQVKVWFQNRRAKWKR 57
homeodomain cd00086
Homeodomain; DNA binding domains involved in the transcriptional regulation of key eukaryotic ...
 1107-1165 1.20e-11

Homeodomain; DNA binding domains involved in the transcriptional regulation of key eukaryotic developmental processes; may bind to DNA as monomers or as homo- and/or heterodimers, in a sequence-specific manner.


Pssm-ID: 238039 [Multi-domain]  Cd Length: 59  Bit Score: 61.11  E-value: 1.20e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1647818745 1107 KKPRVVLAPEEKEALRKAYQLEPYPSQQTIELLSFQLNLKTNTVINWFHNYRSRMRREM 1165
Cdd:cd00086      1 RRKRTRFTPEQLEELEKEFEKNPYPSREEREELAKELGLTERQVKIWFQNRRAKLKRSE 59
HOX smart00389
Homeodomain; DNA-binding factors that are involved in the transcriptional regulation of key ...
 1107-1162 9.32e-11

Homeodomain; DNA-binding factors that are involved in the transcriptional regulation of key developmental processes


Pssm-ID: 197696 [Multi-domain]  Cd Length: 57  Bit Score: 58.42  E-value: 9.32e-11
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 1647818745  1107 KKPRVVLAPEEKEALRKAYQLEPYPSQQTIELLSFQLNLKTNTVINWFHNYRSRMR 1162
Cdd:smart00389    2 RRKRTSFTPEQLEELEKEFQKNPYPSREEREELAKKLGLSERQVKVWFQNRRAKWK 57
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 117-317 7.80e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 60.34  E-value: 7.80e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1647818745  117 QRNEAEK----QKGLQEVQITLAA-RLGEAEEKIKVLHSALKATQAELLELRRKYDEEAASkadevglimtnLEKANQRA 191
Cdd:COG1196    208 QAEKAERyrelKEELKELEAELLLlKLRELEAELEELEAELEELEAELEELEAELAELEAE-----------LEELRLEL 276

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1647818745  192 EAAQREVESLREQLASVNSSIRlaccspqgpsgdkvnftlcsgpRLEAALASKDREILRLLKDVQHLQSSLQELEEASAN 271
Cdd:COG1196    277 EELELELEEAQAEEYELLAELA----------------------RLEQDIARLEERRRELEERLEELEEELAELEEELEE 334

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1647818745  272 QIADLERQLTAKSEAIEKLEEKLQAQSDYEEIKTELSILKAMKLAS 317
Cdd:COG1196    335 LEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 111-308 2.50e-08

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: 58.91  E-value: 2.50e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1647818745  111 LTETLLQRNEAEKQKGLQEVQI-TLAARLGEAEEKIKVLHSALKATQAELLELRrkydEEAASKADEVGLIMTNLEKANQ 189
Cdd:TIGR02168  763 IEELEERLEEAEEELAEAEAEIeELEAQIEQLKEELKALREALDELRAELTLLN----EEAANLRERLESLERRIAATER 838

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1647818745  190 RAEAAQREVESLREQLASVNSSIrlaccSPQGPSGDKVNFTLCSgprLEAALASKDREILRLLKDVQHLQSSLQELEEas 269
Cdd:TIGR02168  839 RLEDLEEQIEELSEDIESLAAEI-----EELEELIEELESELEA---LLNERASLEEALALLRSELEELSEELRELES-- 908

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1647818745  270 anQIADLERQLTAKSEAIEKLEEKLQ-AQSDYEEIKTELS 308
Cdd:TIGR02168  909 --KRSELRRELEELREKLAQLELRLEgLEVRIDNLQERLS 946
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
 76-302 3.46e-06

HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.


Pssm-ID: 461694 [Multi-domain]  Cd Length: 528  Bit Score: 51.61  E-value: 3.46e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1647818745   76 NPELLSPKEQREGTSPAGPTLTEGSRLPGIPGKALLT----ETL--LQR-NEA--EKQKGLQEVQIT-LAARLGEAEEKI 145
Cdd:pfam05622  241 NEELRCAQLQQAELSQADALLSPSSDPGDNLAAEIMPaeirEKLirLQHeNKMlrLGQEGSYRERLTeLQQLLEDANRRK 320

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1647818745  146 KVLHSALKATQAELLELRRKYDE------EAASKADEVGLIMTNLEKANQRAEAAQREVESLREQLASVNSSIrlaccsp 219
Cdd:pfam05622  321 NELETQNRLANQRILELQQQVEElqkalqEQGSKAEDSSLLKQKLEEHLEKLHEAQSELQKKKEQIEELEPKQ------- 393

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1647818745  220 QGPSGDKVNftlcsgpRLEAALASKDREIL----RLLKDVQHLQSSLQELE----EASANQIADLERQLTAKSEAIEKLE 291
Cdd:pfam05622  394 DSNLAQKID-------ELQEALRKKDEDMKameeRYKKYVEKAKSVIKTLDpkqnPASPPEIQALKNQLLEKDKKIEHLE 466

                          250
                   ....*....|....
gi 1647818745  292 ---EKLQAQSDYEE 302
Cdd:pfam05622  467 rdfEKSKLQREQEE 480
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
120-313 1.39e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 49.68  E-value: 1.39e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1647818745  120 EAEKQKGLQEVQITLAARLGEAEEKIKVLHSALKA---TQAELLELRRKYDEEAASKADEVGLIMTNLEKANQRAEAAQR 196
Cdd:PRK03918   547 ELEKLEELKKKLAELEKKLDELEEELAELLKELEElgfESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEE 626

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1647818745  197 EVESLREQLASVNSSIRLAccsPQGPSGDKVNFTLCSGPRLEAALASKDREILRLLKDVQHLQSSLQELEEAsanqIADL 276
Cdd:PRK03918   627 ELDKAFEELAETEKRLEEL---RKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKT----LEKL 699

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1647818745  277 ERQLTAKSEAIEKLEEKLQAQSDYEEIKTELSILKAM 313
Cdd:PRK03918   700 KEELEEREKAKKELEKLEKALERVEELREKVKKYKAL 736
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 157-316 2.85e-03

Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 41.59  E-value: 2.85e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1647818745  157 AELLELRRKYDEEAASKADE---------VGLIMTNLEKANQRAEAAQREVESLREQLASVNSSIrlaccspqgpSGDKv 227
Cdd:cd22656     94 AEILELIDDLADATDDEELEeakktikalLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTAL----------ETLE- 162

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1647818745  228 nftlcsgPRLEAALASKDREILRllKDVQHLQsslQELEEASANQIADLERQLTAKSEAIEKLEEKLQA----QSDYEEI 303
Cdd:cd22656    163 -------KALKDLLTDEGGAIAR--KEIKDLQ---KELEKLNEEYAAKLKAKIDELKALIADDEAKLAAalrlIADLTAA 230

                          170
                   ....*....|....
gi 1647818745  304 KTEL-SILKAMKLA 316
Cdd:cd22656    231 DTDLdNLLALIGPA 244
COG5576 COG5576
Homeodomain-containing transcription factor [Transcription];
1107-1174 3.29e-03

Homeodomain-containing transcription factor [Transcription];


Pssm-ID: 227863 [Multi-domain]  Cd Length: 156  Bit Score: 39.73  E-value: 3.29e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1647818745 1107 KKPRVVLAPEEKEALRKAYQLEPYPSQQTIELLSFQLNLKTNTVINWFHNYRSRMRREMLVEGTQDEP 1174
Cdd:COG5576     52 KSKRRRTTDEQLMVLEREFEINPYPSSITRIKLSLLLNMPPKSVQIWFQNKRAKEKKKRSGKVEQRPG 119
 
Name Accession Description Interval E-value
CUT pfam02376
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in ...
 981-1057 1.60e-31

CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in cooperation with the homeodomain, often found downstream of the CUT domain. Multiple copies of the CUT domain can exist in one protein.


Pssm-ID: 460543  Cd Length: 78  Bit Score: 118.46  E-value: 1.60e-31
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1647818745  981 MSPELDTYSITKRVKEVLTDNNLGQRLFGESILGLTQGSVSDLLSRPKPWHKLSLKGREpFVRMQLWLNDPHNVEKL 1057
Cdd:pfam02376    1 DSEELDTKDIADRIKEELKRHKISQAVFAEKVLNRSQGTLSDLLRKPKPWEKLKSGGRT-FIRMYNWLSLPEDERME 76
CUT pfam02376
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in ...
 830-903 2.88e-29

CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in cooperation with the homeodomain, often found downstream of the CUT domain. Multiple copies of the CUT domain can exist in one protein.


Pssm-ID: 460543  Cd Length: 78  Bit Score: 111.92  E-value: 2.88e-29
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1647818745  830 MYREVDTLELTRQVKEKLAKNGICQRIFGEKVLGLSQGSVSDMLSRPKPWSKLTQKGREpFIRMQLWLSDQLGQ 903
Cdd:pfam02376    1 DSEELDTKDIADRIKEELKRHKISQAVFAEKVLNRSQGTLSDLLRKPKPWEKLKSGGRT-FIRMYNWLSLPEDE 73
CUT pfam02376
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in ...
 491-563 2.65e-26

CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in cooperation with the homeodomain, often found downstream of the CUT domain. Multiple copies of the CUT domain can exist in one protein.


Pssm-ID: 460543  Cd Length: 78  Bit Score: 103.44  E-value: 2.65e-26
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1647818745  491 LDTAEIAFQVKEQLLKHNIGQRVFGHYVLGLSQGSVSEILARPKPWRKLTVKGKEpFIKMKQFLSDEQNVLAL 563
Cdd:pfam02376    5 LDTKDIADRIKEELKRHKISQAVFAEKVLNRSQGTLSDLLRKPKPWEKLKSGGRT-FIRMYNWLSLPEDERME 76
Homeodomain pfam00046
Homeodomain;
1107-1163 1.26e-14

Homeodomain;


Pssm-ID: 459649 [Multi-domain]  Cd Length: 57  Bit Score: 69.45  E-value: 1.26e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1647818745 1107 KKPRVVLAPEEKEALRKAYQLEPYPSQQTIELLSFQLNLKTNTVINWFHNYRSRMRR 1163
Cdd:pfam00046    1 RRKRTTFTPEQLEELEKEFQENPYPSAEEREELAAQLGLTERQVKVWFQNRRAKWKR 57
homeodomain cd00086
Homeodomain; DNA binding domains involved in the transcriptional regulation of key eukaryotic ...
 1107-1165 1.20e-11

Homeodomain; DNA binding domains involved in the transcriptional regulation of key eukaryotic developmental processes; may bind to DNA as monomers or as homo- and/or heterodimers, in a sequence-specific manner.


Pssm-ID: 238039 [Multi-domain]  Cd Length: 59  Bit Score: 61.11  E-value: 1.20e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1647818745 1107 KKPRVVLAPEEKEALRKAYQLEPYPSQQTIELLSFQLNLKTNTVINWFHNYRSRMRREM 1165
Cdd:cd00086      1 RRKRTRFTPEQLEELEKEFEKNPYPSREEREELAKELGLTERQVKIWFQNRRAKLKRSE 59
HOX smart00389
Homeodomain; DNA-binding factors that are involved in the transcriptional regulation of key ...
 1107-1162 9.32e-11

Homeodomain; DNA-binding factors that are involved in the transcriptional regulation of key developmental processes


Pssm-ID: 197696 [Multi-domain]  Cd Length: 57  Bit Score: 58.42  E-value: 9.32e-11
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 1647818745  1107 KKPRVVLAPEEKEALRKAYQLEPYPSQQTIELLSFQLNLKTNTVINWFHNYRSRMR 1162
Cdd:smart00389    2 RRKRTSFTPEQLEELEKEFQKNPYPSREEREELAKKLGLSERQVKVWFQNRRAKWK 57
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 117-317 7.80e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 60.34  E-value: 7.80e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1647818745  117 QRNEAEK----QKGLQEVQITLAA-RLGEAEEKIKVLHSALKATQAELLELRRKYDEEAASkadevglimtnLEKANQRA 191
Cdd:COG1196    208 QAEKAERyrelKEELKELEAELLLlKLRELEAELEELEAELEELEAELEELEAELAELEAE-----------LEELRLEL 276

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1647818745  192 EAAQREVESLREQLASVNSSIRlaccspqgpsgdkvnftlcsgpRLEAALASKDREILRLLKDVQHLQSSLQELEEASAN 271
Cdd:COG1196    277 EELELELEEAQAEEYELLAELA----------------------RLEQDIARLEERRRELEERLEELEEELAELEEELEE 334

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1647818745  272 QIADLERQLTAKSEAIEKLEEKLQAQSDYEEIKTELSILKAMKLAS 317
Cdd:COG1196    335 LEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 111-308 2.50e-08

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: 58.91  E-value: 2.50e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1647818745  111 LTETLLQRNEAEKQKGLQEVQI-TLAARLGEAEEKIKVLHSALKATQAELLELRrkydEEAASKADEVGLIMTNLEKANQ 189
Cdd:TIGR02168  763 IEELEERLEEAEEELAEAEAEIeELEAQIEQLKEELKALREALDELRAELTLLN----EEAANLRERLESLERRIAATER 838

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1647818745  190 RAEAAQREVESLREQLASVNSSIrlaccSPQGPSGDKVNFTLCSgprLEAALASKDREILRLLKDVQHLQSSLQELEEas 269
Cdd:TIGR02168  839 RLEDLEEQIEELSEDIESLAAEI-----EELEELIEELESELEA---LLNERASLEEALALLRSELEELSEELRELES-- 908

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1647818745  270 anQIADLERQLTAKSEAIEKLEEKLQ-AQSDYEEIKTELS 308
Cdd:TIGR02168  909 --KRSELRRELEELREKLAQLELRLEgLEVRIDNLQERLS 946
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 108-321 2.87e-08

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: 56.09  E-value: 2.87e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1647818745  108 KALLTetlLQRNEAEKQKgLQEVQITLAARLGEAEEKIKVLHSALKATQAELLELRRKYDEeaasKADEVGLIMTNLEKA 187
Cdd:COG1579      7 RALLD---LQELDSELDR-LEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKR----LELEIEEVEARIKKY 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1647818745  188 NQR---------AEAAQREVESLREQLASVNSSIRlaccspqgpsgdkvnftlcsgpRLEAALASKDREILRLLKDVQHL 258
Cdd:COG1579     79 EEQlgnvrnnkeYEALQKEIESLKRRISDLEDEIL----------------------ELMERIEELEEELAELEAELAEL 136

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1647818745  259 QSSLQELEEASANQIADLERQLTAKSEAIEKLEEKLQAQ--SDYEEIKTELSILKAMKLASSTCS 321
Cdd:COG1579    137 EAELEEKKAELDEELAELEAELEELEAEREELAAKIPPEllALYERIRKRKNGLAVVPVEGGACG 201
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 113-312 3.13e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 58.41  E-value: 3.13e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1647818745  113 ETLLQRNEAEKQKGLQEVQITLAARLGEAEEKIKVLHSALKATQAELLELRRKYDEEAASKADEVGLIMTNLEKANQRAE 192
Cdd:COG1196    307 LEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE 386

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1647818745  193 AAQREVESLREQLASVNssirlaccspqgpsgdkvnftlcsgpRLEAALASKDREILRLLKDVQHLQSSLQELEEAsanQ 272
Cdd:COG1196    387 ELLEALRAAAELAAQLE--------------------------ELEEAEEALLERLERLEEELEELEEALAELEEE---E 437

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1647818745  273 IADLERQLTAKSEAIEKLEEKLQAQSDYEEIKTELSILKA 312
Cdd:COG1196    438 EEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEA 477
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 109-317 7.88e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 57.25  E-value: 7.88e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1647818745  109 ALLTETLLQRNEAEKQ-KGLQEVQITLAARLGEAEEKIKVLHSALKATQAELLELRRKYDEEAASKADEVglimTNLEKA 187
Cdd:COG1196    267 AELEELRLELEELELElEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELE----EELEEL 342

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1647818745  188 NQRAEAAQREVESLREQLASVNSSIRlaccspqgpsgdkvnftlcsgpRLEAALASKDREILRLLKDVQHLQSSLQELEe 267
Cdd:COG1196    343 EEELEEAEEELEEAEAELAEAEEALL----------------------EAEAELAEAEEELEELAEELLEALRAAAELA- 399

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1647818745  268 asaNQIADLERQLTAKSEAIEKLEEKLQAQSDYEEIKTELSILKAMKLAS 317
Cdd:COG1196    400 ---AQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEE 446
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
127-309 8.74e-08

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 57.23  E-value: 8.74e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1647818745  127 LQEVQITLAARLGEAEEKIKVLHSALKATQAELLELRRKYDEEAASKADEvglimtnLEKANQRAEAAQREVESLREQLA 206
Cdd:COG4913    293 LEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQ-------LEREIERLERELEERERRRARLE 365

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1647818745  207 svnssirlaccspqgpsgdkvnfTLCSgpRLEAALASKDREILRLLKDVQHLQSSLQELEEASANQIADLERQLTAKSEA 286
Cdd:COG4913    366 -----------------------ALLA--ALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRE 420

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1647818745  287 IEKLEEKLQA----QSDY--------EEIKTELSI 309
Cdd:COG4913    421 LRELEAEIASlerrKSNIparllalrDALAEALGL 455
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 115-312 1.85e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 56.10  E-value: 1.85e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1647818745  115 LLQRNEAEKQKGLQEVQIT--------LAARLGEAEEKIKVLHSALKATQAELLELRRKYDEEAASKADEVGlimtNLEK 186
Cdd:COG1196    231 LLKLRELEAELEELEAELEeleaeleeLEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQ----DIAR 306

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1647818745  187 ANQRAEAAQREVESLREQLASVNSSIRLAccspqgpsgdkvnftlcsGPRLEAALASKDREILRLLKDVQHLQSSLQELE 266
Cdd:COG1196    307 LEERRRELEERLEELEEELAELEEELEEL------------------EEELEELEEELEEAEEELEEAEAELAEAEEALL 368

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1647818745  267 EASANQIADLERQLTAKSEAIEKLEEKLQAQSDYEEIKTELSILKA 312
Cdd:COG1196    369 EAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE 414
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
111-310 2.18e-07

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 55.41  E-value: 2.18e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1647818745  111 LTETLLQRNEAEKQKGLQEVQITLAARLGEAEEKikvlhsaLKATQAELLELRRKYDEEAASkaDEVGLIMTNLEKANQR 190
Cdd:COG3206    157 LAEAYLEQNLELRREEARKALEFLEEQLPELRKE-------LEEAEAALEEFRQKNGLVDLS--EEAKLLLQQLSELESQ 227

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1647818745  191 AEAAQREVESLREQLASVNSSIRLACCSPQGPSGDKVNftlcsgPRLEAALASKDREILRLLK-------DVQHLQSSLQ 263
Cdd:COG3206    228 LAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVI------QQLRAQLAELEAELAELSArytpnhpDVIALRAQIA 301

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1647818745  264 ELEEASANQIADLERQLTAKSEAIEKLEEKLQAQsdYEEIKTELSIL 310
Cdd:COG3206    302 ALRAQLQQEAQRILASLEAELEALQAREASLQAQ--LAQLEARLAEL 346
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 134-314 4.27e-07

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 54.07  E-value: 4.27e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1647818745  134 LAARLGEAEEKIKVLHSALKATQAELLELRRKYDEeaasKADEVGLIMTNLEKANQRAEAAQREVESLREQLASVNSSIR 213
Cdd:COG3883     21 KQKELSELQAELEAAQAELDALQAELEELNEEYNE----LQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALY 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1647818745  214 LaccspQGPSGDKVNFTLCSGP------RLEA--ALASKDREILRLLKDvqhLQSSLQELEEASANQIADLERQLTAKSE 285
Cdd:COG3883     97 R-----SGGSVSYLDVLLGSESfsdfldRLSAlsKIADADADLLEELKA---DKAELEAKKAELEAKLAELEALKAELEA 168

                          170       180       190
                   ....*....|....*....|....*....|
gi 1647818745  286 AIEKLEEKL-QAQSDYEEIKTELSILKAMK 314
Cdd:COG3883    169 AKAELEAQQaEQEALLAQLSAEEAAAEAQL 198
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 108-299 7.86e-07

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: 53.91  E-value: 7.86e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1647818745  108 KALLTETLLQRNEAEKQkGLQEVQITLAARLGEAEEKIKVLHSALKATQAELLELRRKYDE---EAASKADEVGLIMTNL 184
Cdd:TIGR02168  331 KLDELAEELAELEEKLE-ELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQlelQIASLNNEIERLEARL 409

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1647818745  185 EKANQRAEAAQREVESLREQLASVnssiRLACCSPQGPSGDKVNFTLCSG-PRLEAALASKDREILRLLKDVQHLQSSLQ 263
Cdd:TIGR02168  410 ERLEDRRERLQQEIEELLKKLEEA----ELKELQAELEELEEELEELQEElERLEEALEELREELEEAEQALDAAERELA 485

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1647818745  264 ELeeasANQIADLERQLTAKSEAIEKLEEKLQAQSD 299
Cdd:TIGR02168  486 QL----QARLDSLERLQENLEGFSEGVKALLKNQSG 517
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 116-358 1.01e-06

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: 53.52  E-value: 1.01e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1647818745  116 LQRNEAEKQKGLQEVQI---TLAARLGEAEEKIKVLHSALKATQAEL--LELR-RKYDEEAASKADEVGLIMTNLEKANQ 189
Cdd:TIGR02168  251 AEEELEELTAELQELEEkleELRLEVSELEEEIEELQKELYALANEIsrLEQQkQILRERLANLERQLEELEAQLEELES 330

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1647818745  190 RAEAAQREVESLREQLASVNssIRLACCSPQGPSGDKVNFTLCSGPR-LEAALASKDREILRLLKDVQHLQSSLQELEEa 268
Cdd:TIGR02168  331 KLDELAEELAELEEKLEELK--EELESLEAELEELEAELEELESRLEeLEEQLETLRSKVAQLELQIASLNNEIERLEA- 407

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1647818745  269 sanQIADLERQLTAKSEAIEKLEEKLQAQsDYEEIKTELSILKAM--KLASSTCSLPQGMAKPEDSLLIAKEAFFPTQKF 346
Cdd:TIGR02168  408 ---RLERLEDRRERLQQEIEELLKKLEEA-ELKELQAELEELEEEleELQEELERLEEALEELREELEEAEQALDAAERE 483

                          250
                   ....*....|..
gi 1647818745  347 LLEKPSLLASPE 358
Cdd:TIGR02168  484 LAQLQARLDSLE 495
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
117-313 1.66e-06

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 52.46  E-value: 1.66e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1647818745  117 QRNEAEKQKG----LQEVQITLAARLGEAEEKIKVL--HSALKATQAELLELRRKYdEEAASKADEVGLIMTNLEKANQR 190
Cdd:COG4717     79 ELKEAEEKEEeyaeLQEELEELEEELEELEAELEELreELEKLEKLLQLLPLYQEL-EALEAELAELPERLEELEERLEE 157

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1647818745  191 AEAAQREVESLREQLASVNSSIRLAccspqgpsgdkvnftlcsgprLEAALASKDREILRLLKDVQHLQSSLQELEEasa 270
Cdd:COG4717    158 LRELEEELEELEAELAELQEELEEL---------------------LEQLSLATEEELQDLAEELEELQQRLAELEE--- 213

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1647818745  271 nQIADLERQLTAKSEAIEKLEEKLQAQSDYEEIKTELSILKAM 313
Cdd:COG4717    214 -ELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIA 255
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
120-314 3.00e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 52.22  E-value: 3.00e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1647818745  120 EAEKQ-KGLQEVQiTLAARLGEAEEKIKVLHSALKATQAELLELR-RKYDEEAASKADEVGLIMTNLEKANQRAEAAQRE 197
Cdd:COG4913    246 DAREQiELLEPIR-ELAERYAAARERLAELEYLRAALRLWFAQRRlELLEAELEELRAELARLEAELERLEARLDALREE 324

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1647818745  198 VESLREQLASvNSSIRLAccspqgpsgdkvnftlcsgpRLEAALASKDREILRLLKDVQHLQSSLQELE---EASANQIA 274
Cdd:COG4913    325 LDELEAQIRG-NGGDRLE--------------------QLEREIERLERELEERERRRARLEALLAALGlplPASAEEFA 383

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1647818745  275 DLERQLTAKSEAIEKLEEKLQ------------AQSDYEEIKTELSILKAMK 314
Cdd:COG4913    384 ALRAEAAALLEALEEELEALEealaeaeaalrdLRRELRELEAEIASLERRK 435
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
 76-302 3.46e-06

HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.


Pssm-ID: 461694 [Multi-domain]  Cd Length: 528  Bit Score: 51.61  E-value: 3.46e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1647818745   76 NPELLSPKEQREGTSPAGPTLTEGSRLPGIPGKALLT----ETL--LQR-NEA--EKQKGLQEVQIT-LAARLGEAEEKI 145
Cdd:pfam05622  241 NEELRCAQLQQAELSQADALLSPSSDPGDNLAAEIMPaeirEKLirLQHeNKMlrLGQEGSYRERLTeLQQLLEDANRRK 320

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1647818745  146 KVLHSALKATQAELLELRRKYDE------EAASKADEVGLIMTNLEKANQRAEAAQREVESLREQLASVNSSIrlaccsp 219
Cdd:pfam05622  321 NELETQNRLANQRILELQQQVEElqkalqEQGSKAEDSSLLKQKLEEHLEKLHEAQSELQKKKEQIEELEPKQ------- 393

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1647818745  220 QGPSGDKVNftlcsgpRLEAALASKDREIL----RLLKDVQHLQSSLQELE----EASANQIADLERQLTAKSEAIEKLE 291
Cdd:pfam05622  394 DSNLAQKID-------ELQEALRKKDEDMKameeRYKKYVEKAKSVIKTLDpkqnPASPPEIQALKNQLLEKDKKIEHLE 466

                          250
                   ....*....|....
gi 1647818745  292 ---EKLQAQSDYEE 302
Cdd:pfam05622  467 rdfEKSKLQREQEE 480
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 122-314 5.36e-06

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: 51.21  E-value: 5.36e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1647818745  122 EKQKGLQEVQITLAA-RLGEAEEKIKVLHSALKATQAELLELRRKYDEeAASKADEVGLIMTNLEKanqRAEAAQREVES 200
Cdd:TIGR02168  217 ELKAELRELELALLVlRLEELREELEELQEELKEAEEELEELTAELQE-LEEKLEELRLEVSELEE---EIEELQKELYA 292

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1647818745  201 LREQLASVNSSIRLAccspqgpsGDKVNFTLCSGPRLEAALASKDREILRLLKDVQHLQSSLQELE---EASANQIADLE 277
Cdd:TIGR02168  293 LANEISRLEQQKQIL--------RERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKeelESLEAELEELE 364

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1647818745  278 RQLTAKSEAIEKLEEKLQAQSDyEEIKTELSILKAMK 314
Cdd:TIGR02168  365 AELEELESRLEELEEQLETLRS-KVAQLELQIASLNN 400
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
107-368 5.57e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 50.29  E-value: 5.57e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1647818745  107 GKALLTETLLQRNEAEKQKGLQEVQITLAARLGEAEEKIKVLHSALKATQAELLELRrkydEEAASKADEVGLIMTNLEK 186
Cdd:COG4372      9 GKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLE----EELEQARSELEQLEEELEE 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1647818745  187 ANQRAEAAQREVESLREQLASVNSSIRlaccspqgpsgdkvnftlcsgpRLEAALASKDREILRLLKDVQHLQSSLQELE 266
Cdd:COG4372     85 LNEQLQAAQAELAQAQEELESLQEEAE----------------------ELQEELEELQKERQDLEQQRKQLEAQIAELQ 142

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1647818745  267 EASAN---QIADLERQLTAKSEAIEKLEEKLQAQSDyEEIKTELSILK--AMKLASSTCSLPQGMAKPEDSLLIAKEAFF 341
Cdd:COG4372    143 SEIAEreeELKELEEQLESLQEELAALEQELQALSE-AEAEQALDELLkeANRNAEKEEELAEAEKLIESLPRELAEELL 221

                          250       260
                   ....*....|....*....|....*..
gi 1647818745  342 PTQKFLLEKPSLLASPEEDPSEDDSIK 368
Cdd:COG4372    222 EAKDSLEAKLGLALSALLDALELEEDK 248
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
120-313 1.39e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 49.68  E-value: 1.39e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1647818745  120 EAEKQKGLQEVQITLAARLGEAEEKIKVLHSALKA---TQAELLELRRKYDEEAASKADEVGLIMTNLEKANQRAEAAQR 196
Cdd:PRK03918   547 ELEKLEELKKKLAELEKKLDELEEELAELLKELEElgfESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEE 626

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1647818745  197 EVESLREQLASVNSSIRLAccsPQGPSGDKVNFTLCSGPRLEAALASKDREILRLLKDVQHLQSSLQELEEAsanqIADL 276
Cdd:PRK03918   627 ELDKAFEELAETEKRLEEL---RKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKT----LEKL 699

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1647818745  277 ERQLTAKSEAIEKLEEKLQAQSDYEEIKTELSILKAM 313
Cdd:PRK03918   700 KEELEEREKAKKELEKLEKALERVEELREKVKKYKAL 736
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 121-312 2.47e-05

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: 48.22  E-value: 2.47e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1647818745  121 AEKQKGLQEVQITLAA---RLGEAEEKIKVLHSALKATQAELLELRRKYDEeaasKADEVGLIMTNLEKANQRAEAAQRE 197
Cdd:COG4942     23 AEAEAELEQLQQEIAElekELAALKKEEKALLKQLAALERRIAALARRIRA----LEQELAALEAELAELEKEIAELRAE 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1647818745  198 VESLREQLASVnssIRLACCSPQGPsgdKVNFTLCSGPRLEAA-----LASKDREILRLLKDVQHLQSSLQELEEASANQ 272
Cdd:COG4942     99 LEAQKEELAEL---LRALYRLGRQP---PLALLLSPEDFLDAVrrlqyLKYLAPARREQAEELRADLAELAALRAELEAE 172

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1647818745  273 IADLERQLTAKSEAIEKLEEKLQAQ--------SDYEEIKTELSILKA 312
Cdd:COG4942    173 RAELEALLAELEEERAALEALKAERqkllarleKELAELAAELAELQQ 220
PRK12704 PRK12704
phosphodiesterase; Provisional
 138-302 2.65e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 48.62  E-value: 2.65e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1647818745  138 LGEAEEKIKVL-HSALKATQAELLELRRKYDEEAASKADEVglimTNLEKANQraeaaQREvESLREQLASVNssirlac 216
Cdd:PRK12704    44 LEEAKKEAEAIkKEALLEAKEEIHKLRNEFEKELRERRNEL----QKLEKRLL-----QKE-ENLDRKLELLE------- 106

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1647818745  217 cspqgpsgdkvnftlcsgpRLEAALASKDREILRLLKDVQHLQsslQELEEASANQIADLER--QLT---AKSEAIEKLE 291
Cdd:PRK12704   107 -------------------KREEELEKKEKELEQKQQELEKKE---EELEELIEEQLQELERisGLTaeeAKEILLEKVE 164

                          170
                   ....*....|....*.
gi 1647818745  292 EKLQAQS-----DYEE 302
Cdd:PRK12704   165 EEARHEAavlikEIEE 180
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
141-308 3.58e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 48.37  E-value: 3.58e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1647818745  141 AEEKIKVLhsalkatQAELLELRRKydeeaaskadevglimtnLEKANQRAEAAQREVESLREQLASVNssiRLAccspq 220
Cdd:COG4913    608 NRAKLAAL-------EAELAELEEE------------------LAEAEERLEALEAELDALQERREALQ---RLA----- 654

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1647818745  221 gpsgdKVNFTLCSGPRLEAALASKDREILRLLK---DVQHLQSSLQELEEasanQIADLERQLTAKSEAIEKLEEKL-QA 296
Cdd:COG4913    655 -----EYSWDEIDVASAEREIAELEAELERLDAssdDLAALEEQLEELEA----ELEELEEELDELKGEIGRLEKELeQA 725

                          170
                   ....*....|..
gi 1647818745  297 QSDYEEIKTELS 308
Cdd:COG4913    726 EEELDELQDRLE 737
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 121-299 6.88e-05

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: 47.74  E-value: 6.88e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1647818745  121 AEKQKGLQEVQITLAarlgEAEEKIKVLHSALKATQAELLELRRKYDEeaaskadevglIMTNLEKANQRAEAAQREVES 200
Cdd:TIGR02168  666 AKTNSSILERRREIE----ELEEKIEELEEKIAELEKALAELRKELEE-----------LEEELEQLRKELEELSRQISA 730

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1647818745  201 LREQLASVNSSIRLACCSPQgpsgdkvnftlcsgpRLEAALASKDREILRLLKDVQHLQSSLQELEEASAN---QIADLE 277
Cdd:TIGR02168  731 LRKDLARLEAEVEQLEERIA---------------QLSKELTELEAEIEELEERLEEAEEELAEAEAEIEEleaQIEQLK 795

                          170       180
                   ....*....|....*....|..
gi 1647818745  278 RQLTAKSEAIEKLEEKLQAQSD 299
Cdd:TIGR02168  796 EELKALREALDELRAELTLLNE 817
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
116-208 9.46e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.22  E-value: 9.46e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1647818745  116 LQRNEAEKQKGLQEVQitlaARLGEAEEKIKVLHSALKATQAELLELRRKYDEEAASKADEVGLIMTNLEKANQRAEAAQ 195
Cdd:COG4913    343 LEREIERLERELEERE----RRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLR 418

                           90
                   ....*....|...
gi 1647818745  196 REVESLREQLASV 208
Cdd:COG4913    419 RELRELEAEIASL 431
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
121-300 1.15e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.83  E-value: 1.15e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1647818745  121 AEKQKGLQEVQITLAARLGEAEEKIKVLHSALKATQAELLELRR------------KYDEEAASKADEVGLIMTN---LE 185
Cdd:COG4913    609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRlaeyswdeidvaSAEREIAELEAELERLDASsddLA 688

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1647818745  186 KANQRAEAAQREVESLREQLASVNSSIRlaccspqgpsgdkvnftlcsgpRLEAALASKDREILRLLKDVQHLQSS---- 261
Cdd:COG4913    689 ALEEQLEELEAELEELEEELDELKGEIG----------------------RLEKELEQAEEELDELQDRLEAAEDLarle 746

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1647818745  262 ---------LQELEEASANQI-ADLERQLTAKSEAIEKLEEKL-QAQSDY 300
Cdd:COG4913    747 lralleerfAAALGDAVERELrENLEERIDALRARLNRAEEELeRAMRAF 796
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 120-311 2.22e-04

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: 45.83  E-value: 2.22e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1647818745  120 EAEKQKGLQEvqitlaarLGEAEEKIKVLHSALKATQAELLELRR------KYDEEAASKAD-EVGLIMTNLEKANQRAE 192
Cdd:TIGR02169  169 DRKKEKALEE--------LEEVEENIERLDLIIDEKRQQLERLRRerekaeRYQALLKEKREyEGYELLKEKEALERQKE 240

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1647818745  193 AAQREVESLREQLASVNSSIrlaccspqgpsgDKVNFTLcsgPRLEAALASKDREILRLLKDVQ-HLQSSLQELEeasaN 271
Cdd:TIGR02169  241 AIERQLASLEEELEKLTEEI------------SELEKRL---EEIEQLLEELNKKIKDLGEEEQlRVKEKIGELE----A 301

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1647818745  272 QIADLERQLTAKSEAIEKLEEKL-QAQSDYEEIKTELSILK 311
Cdd:TIGR02169  302 EIASLERSIAEKERELEDAEERLaKLEAEIDKLLAEIEELE 342
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 127-369 2.22e-04

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: 45.83  E-value: 2.22e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1647818745  127 LQEVQITLAARLGEAEEKIKVLHSALKATQAELLELRRKYDEEAASKAdEVGLIMTNLEK--ANQRAEAAQREVESLREQ 204
Cdd:TIGR02169  728 LEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLH-KLEEALNDLEArlSHSRIPEIQAELSKLEEE 806

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1647818745  205 LASVNSSIRlaccspqgpsgdkvnftlcsgpRLEAALASKDREILRLLKDVQHLQSSLQELEEasanQIADLERQ---LT 281
Cdd:TIGR02169  807 VSRIEARLR----------------------EIEQKLNRLTLEKEYLEKEIQELQEQRIDLKE----QIKSIEKEienLN 860

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1647818745  282 AKSEAIEKLEEKLQAQ-----SDYEEIKTELSILKA----MKLASSTCSLPQGMAKPEDSLLIAKEAFFPTQKFLLEKPs 352
Cdd:TIGR02169  861 GKKEELEEELEELEAAlrdleSRLGDLKKERDELEAqlreLERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDP- 939

                          250
                   ....*....|....*..
gi 1647818745  353 lLASPEEDPSEDDSIKD 369
Cdd:TIGR02169  940 -KGEDEEIPEEELSLED 955
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 116-310 2.68e-04

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: 45.83  E-value: 2.68e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1647818745  116 LQRNEAEKQKGLQEVQITLA---ARLGEAEEKIKVLH--------------SALKATQAELLELRRKYDEEAASKA---D 175
Cdd:TIGR02169  306 LERSIAEKERELEDAEERLAkleAEIDKLLAEIEELEreieeerkrrdkltEEYAELKEELEDLRAELEEVDKEFAetrD 385

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1647818745  176 EVGLIMTNLEKANQRAEAAQREVESLREQLasVNSSIRLAccspqgpsgdkvnftlcsgpRLEAALASKDREILRLLKDV 255
Cdd:TIGR02169  386 ELKDYREKLEKLKREINELKRELDRLQEEL--QRLSEELA--------------------DLNAAIAGIEAKINELEEEK 443

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1647818745  256 QHLQSSLQELE---EASANQIADLERQLTAKSEAIEKLEEKL-QAQSDYEEIKTELSIL 310
Cdd:TIGR02169  444 EDKALEIKKQEwklEQLAADLSKYEQELYDLKEEYDRVEKELsKLQRELAEAEAQARAS 502
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
100-314 4.42e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.05  E-value: 4.42e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1647818745  100 SRLPGIPGKALLTETLLQRNEAEKQKgLQEVQITLAARLGEA---EEKIKVLHSALKATQAELLELRRKYDE--EAASKA 174
Cdd:PRK03918   214 SELPELREELEKLEKEVKELEELKEE-IEELEKELESLEGSKrklEEKIRELEERIEELKKEIEELEEKVKElkELKEKA 292

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1647818745  175 DEVGLIMTNLEKANQRAEAAQREVESLREQLASVNSSIRlaccspqgpsgdkvnftlcSGPRLEAALASKDREILRLLKD 254
Cdd:PRK03918   293 EEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIK-------------------ELEEKEERLEELKKKLKELEKR 353

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1647818745  255 VQHLQSSLQELEEASA--NQIADLERQLTAKSeaIEKLEEKLQ-AQSDYEEIKTELSILKAMK 314
Cdd:PRK03918   354 LEELEERHELYEEAKAkkEELERLKKRLTGLT--PEKLEKELEeLEKAKEEIEEEISKITARI 414
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
118-311 5.33e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 44.65  E-value: 5.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1647818745  118 RNEAEkqkGLQEVQITLAARLGEAEEKIKVLHSALKATQAELLELRRK---YDEEAASKADEVGLIMTNLEKANQRAEAA 194
Cdd:PRK02224   341 NEEAE---SLREDADDLEERAEELREEAAELESELEEAREAVEDRREEieeLEEEIEELRERFGDAPVDLGNAEDFLEEL 417

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1647818745  195 QREVESLREQLASVNSSIRlaccspqgpsgdKVNFTLCSGPRLEAalASKDREILRLLKDVQHLqSSLQELEEasanQIA 274
Cdd:PRK02224   418 REERDELREREAELEATLR------------TARERVEEAEALLE--AGKCPECGQPVEGSPHV-ETIEEDRE----RVE 478

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1647818745  275 DLERQLTAKSEAIEKLEEKLQAQSDYEEIKTELSILK 311
Cdd:PRK02224   479 ELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLE 515
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
108-312 8.20e-04

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.99  E-value: 8.20e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1647818745  108 KALLTETLLQRNEAEKQKGLQEVQIT-LAARLG--------EAEEKIKVLhSALKATQAELLELRRKYDEEAASKADEVG 178
Cdd:COG4717    297 KASLGKEAEELQALPALEELEEEELEeLLAALGlppdlspeELLELLDRI-EELQELLREAEELEEELQLEELEQEIAAL 375

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1647818745  179 LI---MTNLEKANQRAEAAQREVEsLREQLASVNSSIRLAccspqgpsgdkvnftlcsGPRLEAALASKDREilRLLKDV 255
Cdd:COG4717    376 LAeagVEDEEELRAALEQAEEYQE-LKEELEELEEQLEEL------------------LGELEELLEALDEE--ELEEEL 434

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1647818745  256 QHLQSSLQELEEasanQIADLERQLTAKSEAIEKLEEklqaQSDYEEIKTELSILKA 312
Cdd:COG4717    435 EELEEELEELEE----ELEELREELAELEAELEQLEE----DGELAELLQELEELKA 483
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 108-293 1.12e-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: 43.21  E-value: 1.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1647818745  108 KALLTETLLQRNEAEKQKGLQEVQI-TLAARLGEAEEKIKVLHSALKATQAELLELRRKYDEEAA------------SKA 174
Cdd:COG4942     40 EKELAALKKEEKALLKQLAALERRIaALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEelaellralyrlGRQ 119

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1647818745  175 DEVGLIM--TNLEKANQRAEAAQREVESLREQLASVNSSIRlaccspqgpsgdkvnftlcsgpRLEAALASKDREILRLL 252
Cdd:COG4942    120 PPLALLLspEDFLDAVRRLQYLKYLAPARREQAEELRADLA----------------------ELAALRAELEAERAELE 177

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1647818745  253 KDVQHLQSSLQELEEASANQ---IADLERQLTAKSEAIEKLEEK 293
Cdd:COG4942    178 ALLAELEEERAALEALKAERqklLARLEKELAELAAELAELQQE 221
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 127-297 1.77e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.51  E-value: 1.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1647818745  127 LQEVQITLAARLGEAEEKIKVLHSALKATQAELLELRRKYDEEAAS------KADEVGLIM--TNLEKANQRAEAAQREV 198
Cdd:COG3883     49 LNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARAlyrsggSVSYLDVLLgsESFSDFLDRLSALSKIA 128

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1647818745  199 ESLREQLASVNSSIRLAccspqgpsgdkvnftlcsgPRLEAALASKDREILRLLKDVQHLQSSLQELEEASANQIADLER 278
Cdd:COG3883    129 DADADLLEELKADKAEL-------------------EAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSA 189

                          170
                   ....*....|....*....
gi 1647818745  279 QLTAKSEAIEKLEEKLQAQ 297
Cdd:COG3883    190 EEAAAEAQLAELEAELAAA 208
MscS_porin pfam12795
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ...
 117-296 2.12e-03

Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.


Pssm-ID: 432790 [Multi-domain]  Cd Length: 238  Bit Score: 41.52  E-value: 2.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1647818745  117 QRNEAEKQKGLQEVQITLA--ARLGEAEEKIKVLHSALKATQAELLELRRKYDEEAASKADEVGLIMTNL--EKANQRAE 192
Cdd:pfam12795    9 KLDEAAKKKLLQDLQQALSllDKIDASKQRAAAYQKALDDAPAELRELRQELAALQAKAEAAPKEILASLslEELEQRLL 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1647818745  193 AAQREVESLREQLASVNSSIRLACCSPQGPSG---------DKVNFTLCSGPRLEAALASKDREILRLLKDVQHLQSSLQ 263
Cdd:pfam12795   89 QTSAQLQELQNQLAQLNSQLIELQTRPERAQQqlsearqrlQQIRNRLNGPAPPGEPLSEAQRWALQAELAALKAQIDML 168

                          170       180       190
                   ....*....|....*....|....*....|....
gi 1647818745  264 ELEEASANQIADLER-QLTAKSEAIEKLEEKLQA 296
Cdd:pfam12795  169 EQELLSNNNRQDLLKaRRDLLTLRIQRLEQQLQA 202
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 157-316 2.85e-03

Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 41.59  E-value: 2.85e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1647818745  157 AELLELRRKYDEEAASKADE---------VGLIMTNLEKANQRAEAAQREVESLREQLASVNSSIrlaccspqgpSGDKv 227
Cdd:cd22656     94 AEILELIDDLADATDDEELEeakktikalLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTAL----------ETLE- 162

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1647818745  228 nftlcsgPRLEAALASKDREILRllKDVQHLQsslQELEEASANQIADLERQLTAKSEAIEKLEEKLQA----QSDYEEI 303
Cdd:cd22656    163 -------KALKDLLTDEGGAIAR--KEIKDLQ---KELEKLNEEYAAKLKAKIDELKALIADDEAKLAAalrlIADLTAA 230

                          170
                   ....*....|....
gi 1647818745  304 KTEL-SILKAMKLA 316
Cdd:cd22656    231 DTDLdNLLALIGPA 244
COG5576 COG5576
Homeodomain-containing transcription factor [Transcription];
1107-1174 3.29e-03

Homeodomain-containing transcription factor [Transcription];


Pssm-ID: 227863 [Multi-domain]  Cd Length: 156  Bit Score: 39.73  E-value: 3.29e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1647818745 1107 KKPRVVLAPEEKEALRKAYQLEPYPSQQTIELLSFQLNLKTNTVINWFHNYRSRMRREMLVEGTQDEP 1174
Cdd:COG5576     52 KSKRRRTTDEQLMVLEREFEINPYPSSITRIKLSLLLNMPPKSVQIWFQNKRAKEKKKRSGKVEQRPG 119
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 245-312 3.71e-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: 40.68  E-value: 3.71e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1647818745  245 DREILRLLKDVQHLQSSLQELEEASAN---QIADLERQLTAKSEAIEKLEEKL-QAQSDYEEIKTELSILKA 312
Cdd:COG1579      2 MPEDLRALLDLQELDSELDRLEHRLKElpaELAELEDELAALEARLEAAKTELeDLEKEIKRLELEIEEVEA 73
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 113-207 5.79e-03

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 41.31  E-value: 5.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1647818745  113 ETLLQRNEAEKQKGLQEVQITLAARLGEAEEKIKVLHSALKATQAELLELRRKYDEEAASkadevgliMTNLEKANQRae 192
Cdd:pfam01576  480 ETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGT--------LEALEEGKKR-- 549

                           90
                   ....*....|....*
gi 1647818745  193 aAQREVESLREQLAS 207
Cdd:pfam01576  550 -LQRELEALTQQLEE 563
flagell_FliJ TIGR02473
flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly ...
 159-306 6.28e-03

flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly every case, in the midst of other flagellar biosynthesis genes in bacgterial genomes. Typically the fliJ gene is found adjacent to the gene for the flagellum-specific ATPase FliI. Sequence scoring in the gray zone between trusted and noise cutoffs include both probable FliJ proteins and components of bacterial type III secretion systems.


Pssm-ID: 131526 [Multi-domain]  Cd Length: 141  Bit Score: 38.45  E-value: 6.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1647818745  159 LLELRRKYDEEAAskadevglimTNLEKANQRAEAAQREVESLREQL----ASVNSSIRlaccspQGPSGdkvnftlcsg 234
Cdd:TIGR02473    7 LLDLREKEEEQAK----------LELAKAQAEFERLETQLQQLIKYReeyeQQALEKVG------AGTSA---------- 60

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1647818745  235 prleAALASKDREILRLLKDVQHLQSSLQELEeasaNQIADLERQLTAKS---EAIEKLEEKLQAQSDYEEIKTE 306
Cdd:TIGR02473   61 ----LELSNYQRFIRQLDQRIQQQQQELALLQ----QEVEAKRERLLEARrelKALEKLKEKKQKEYRAEEAKRE 127
 
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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