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Conserved domains on  [gi|2462509871|ref|XP_054192905|]
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protein Hook homolog 1 isoform X4 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
HOOK super family cl38191
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
186-414 4.40e-107

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.


The actual alignment was detected with superfamily member pfam05622:

Pssm-ID: 461694 [Multi-domain]  Cd Length: 528  Bit Score: 327.03  E-value: 4.40e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871 186 ELQEALAEKEELRQRCEELDMQVTTLQDEKNSLVSENEMMNEKLDQLDgSFDDPNTVVAKKYFHAQLQLEQLQEENFRLE 265
Cdd:pfam05622   1 DLSEAQEEKDELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQLE-SGDDSGTPGGKKYLLLQKQLEQLQEENFRLE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871 266 AAKDDYRVHCEELEKQLIEFQHRNDELTSLAEETRALKDEIDVLRATSDKANKLESTVEIYRQKLQDLNDLRKQVKTLQE 345
Cdd:pfam05622  80 TARDDYRIKCEELEKEVLELQHRNEELTSLAEEAQALKDEMDILRESSDKVKKLEATVETYKKKLEDLGDLRRQVKLLEE 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462509871 346 TNMMYMHNTVSLEEELKKANAARTQLETYKRQVQDLHVKLSSESKRADTLAFEMKRLEEKHEALLKEKE 414
Cdd:pfam05622 160 RNAEYMQRTLQLEEELKKANALRGQLETYKRQVQELHGKLSEESKKADKLEFEYKKLEEKLEALQKEKE 228
HkD_Hook1 cd22225
Hook domain found in protein Hook 1 (Hook1) and similar proteins; Hook1 is a ...
15-163 1.97e-102

Hook domain found in protein Hook 1 (Hook1) and similar proteins; Hook1 is a microtubule-binding protein required for spermatid differentiation. It is a component of the FTS/Hook/FHIP complex (FHF complex), which may function to promote vesicle trafficking and/or fusion via the homotypic vesicular protein sorting (HOPS) complex.


:

Pssm-ID: 411796  Cd Length: 150  Bit Score: 301.77  E-value: 1.97e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871  15 CDSLMIWLQTFNTASPCQDVKQLTSGVAMAQVLHQIDAAWFNESWLSRIKEDVGDNWRIKASNVKKVLQGIMSYYHEFLG 94
Cdd:cd22225     2 CDSLIIWLQTFNTAAPCQTVQDLTSGVAMAQVLHQIDSSWFDESWLSRIKEDVGDNWRIKMSNLKKILQGIVDYYHEFLD 81
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462509871  95 QQISEALIPDLNQITECSDPVELGRLLQLILGCAINCEKKQEHIQNIMTLEESVQHVVMTAIQELMSKE 163
Cdd:cd22225    82 QQISEFLLPDLNRIAEHSDPVELGRLLQLILGCAVNCEKKQEHIQNIMTLEESVQHVVMTAIQELMSKE 150
 
Name Accession Description Interval E-value
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
186-414 4.40e-107

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: 327.03  E-value: 4.40e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871 186 ELQEALAEKEELRQRCEELDMQVTTLQDEKNSLVSENEMMNEKLDQLDgSFDDPNTVVAKKYFHAQLQLEQLQEENFRLE 265
Cdd:pfam05622   1 DLSEAQEEKDELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQLE-SGDDSGTPGGKKYLLLQKQLEQLQEENFRLE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871 266 AAKDDYRVHCEELEKQLIEFQHRNDELTSLAEETRALKDEIDVLRATSDKANKLESTVEIYRQKLQDLNDLRKQVKTLQE 345
Cdd:pfam05622  80 TARDDYRIKCEELEKEVLELQHRNEELTSLAEEAQALKDEMDILRESSDKVKKLEATVETYKKKLEDLGDLRRQVKLLEE 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462509871 346 TNMMYMHNTVSLEEELKKANAARTQLETYKRQVQDLHVKLSSESKRADTLAFEMKRLEEKHEALLKEKE 414
Cdd:pfam05622 160 RNAEYMQRTLQLEEELKKANALRGQLETYKRQVQELHGKLSEESKKADKLEFEYKKLEEKLEALQKEKE 228
HkD_Hook1 cd22225
Hook domain found in protein Hook 1 (Hook1) and similar proteins; Hook1 is a ...
15-163 1.97e-102

Hook domain found in protein Hook 1 (Hook1) and similar proteins; Hook1 is a microtubule-binding protein required for spermatid differentiation. It is a component of the FTS/Hook/FHIP complex (FHF complex), which may function to promote vesicle trafficking and/or fusion via the homotypic vesicular protein sorting (HOPS) complex.


Pssm-ID: 411796  Cd Length: 150  Bit Score: 301.77  E-value: 1.97e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871  15 CDSLMIWLQTFNTASPCQDVKQLTSGVAMAQVLHQIDAAWFNESWLSRIKEDVGDNWRIKASNVKKVLQGIMSYYHEFLG 94
Cdd:cd22225     2 CDSLIIWLQTFNTAAPCQTVQDLTSGVAMAQVLHQIDSSWFDESWLSRIKEDVGDNWRIKMSNLKKILQGIVDYYHEFLD 81
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462509871  95 QQISEALIPDLNQITECSDPVELGRLLQLILGCAINCEKKQEHIQNIMTLEESVQHVVMTAIQELMSKE 163
Cdd:cd22225    82 QQISEFLLPDLNRIAEHSDPVELGRLLQLILGCAVNCEKKQEHIQNIMTLEESVQHVVMTAIQELMSKE 150
HOOK_N pfam19047
HOOK domain; This domain is found at the N-terminus of HOOK proteins.
15-163 2.17e-93

HOOK domain; This domain is found at the N-terminus of HOOK proteins.


Pssm-ID: 465958  Cd Length: 151  Bit Score: 278.52  E-value: 2.17e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871  15 CDSLMIWLQTFNTASPCQDVKQLTSGVAMAQVLHQIDAAWFNESWLSRIKEDVGDNWRIKASNVKKVLQGIMSYYHEFLG 94
Cdd:pfam19047   3 CDSLLTWLQTFNVPAPCATVEDLTDGVAMAQVLHQIDPSWFTEAWLSRIKEDVGDNWRLKVSNLKKILQSVVDYYQDVLG 82
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462509871  95 QQISEALIPDLNQITECSDPVELGRLLQLILGCAINCEKKQEHIQNIMTLEESVQHVVMTAIQELMSKE 163
Cdd:pfam19047  83 QQISDFLLPDVNLIGEHSDPAELGRLLQLILGCAVNCEKKQEYIQQIMTLEESVQHVVMTAIQELMSKD 151
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
175-414 8.36e-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: 54.68  E-value: 8.36e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871  175 ELEQQLKRALEELQEALAEKEELRQRCEELDMQVTTLQDEKNSLVSENEMMNEKLDQLDGSfddpntvvakkyfhAQLQL 254
Cdd:TIGR02168  681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAE--------------VEQLE 746
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871  255 EQLQEENFRLEAAKDDYRVHCEELEKQLIEFQHRNDELTSLAEETRALKDEIDVLRATSDKANKLESTVEI-YRQKLQDL 333
Cdd:TIGR02168  747 ERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEeAANLRERL 826
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871  334 NDLRKQVKTLQETNMMYMHNTVSLEEELKKANAARTQLETYKRQVQDLHVKLSSESKRADTLAFEMKRLEEKHEALLKEK 413
Cdd:TIGR02168  827 ESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELREL 906

                   .
gi 2462509871  414 E 414
Cdd:TIGR02168  907 E 907
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
175-414 3.22e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.02  E-value: 3.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871 175 ELEQQLKRALEELQEALAEKEELRQRCEELDMQVTTLQDEKNSLVSENEMMNEKLDqldgsfddpntvvakkyfHAQLQL 254
Cdd:COG1196   250 ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIA------------------RLEERR 311
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871 255 EQLQEENFRLEAAKDDYRVHCEELEKQLIEFQHRNDELTSLAEETRALKDEID--VLRATSDKANKLESTVEIYRQKLQD 332
Cdd:COG1196   312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEeaLLEAEAELAEAEEELEELAEELLEA 391
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871 333 LNDLRKQVKTLQETNMMYMHNTVSLEEELKKANAARTQLETYKRQVQDLHVKLSSESKRADTLAFEMKRLEEKHEALLKE 412
Cdd:COG1196   392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE 471

                  ..
gi 2462509871 413 KE 414
Cdd:COG1196   472 AA 473
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
177-414 2.36e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.49  E-value: 2.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871 177 EQQLKRALEELQEALAEKEELRQRCEELDMQVTTLQDEKNSLVSENEMMNEKLDQLDGSFDDPNTVVAKKyfhaqlqleq 256
Cdd:PRK02224  201 EKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAET---------- 270
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871 257 lqeenfrlEAAKDDYRVHCEELEKQLIEFQHRNDELTSLAEETRALKDEIDVLRAT-SDKANKLESTVEIYRQKLQDLND 335
Cdd:PRK02224  271 --------EREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREElEDRDEELRDRLEECRVAAQAHNE 342
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871 336 ----LRKQVKTLQETNMMYMHNTVSLEEELKkanAARTQLETYKRQVQDLHVKLSSESKRADTLAFEMKRLEEKHEALLK 411
Cdd:PRK02224  343 eaesLREDADDLEERAEELREEAAELESELE---EAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELRE 419

                  ...
gi 2462509871 412 EKE 414
Cdd:PRK02224  420 ERD 422
 
Name Accession Description Interval E-value
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
186-414 4.40e-107

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: 327.03  E-value: 4.40e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871 186 ELQEALAEKEELRQRCEELDMQVTTLQDEKNSLVSENEMMNEKLDQLDgSFDDPNTVVAKKYFHAQLQLEQLQEENFRLE 265
Cdd:pfam05622   1 DLSEAQEEKDELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQLE-SGDDSGTPGGKKYLLLQKQLEQLQEENFRLE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871 266 AAKDDYRVHCEELEKQLIEFQHRNDELTSLAEETRALKDEIDVLRATSDKANKLESTVEIYRQKLQDLNDLRKQVKTLQE 345
Cdd:pfam05622  80 TARDDYRIKCEELEKEVLELQHRNEELTSLAEEAQALKDEMDILRESSDKVKKLEATVETYKKKLEDLGDLRRQVKLLEE 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462509871 346 TNMMYMHNTVSLEEELKKANAARTQLETYKRQVQDLHVKLSSESKRADTLAFEMKRLEEKHEALLKEKE 414
Cdd:pfam05622 160 RNAEYMQRTLQLEEELKKANALRGQLETYKRQVQELHGKLSEESKKADKLEFEYKKLEEKLEALQKEKE 228
HkD_Hook1 cd22225
Hook domain found in protein Hook 1 (Hook1) and similar proteins; Hook1 is a ...
15-163 1.97e-102

Hook domain found in protein Hook 1 (Hook1) and similar proteins; Hook1 is a microtubule-binding protein required for spermatid differentiation. It is a component of the FTS/Hook/FHIP complex (FHF complex), which may function to promote vesicle trafficking and/or fusion via the homotypic vesicular protein sorting (HOPS) complex.


Pssm-ID: 411796  Cd Length: 150  Bit Score: 301.77  E-value: 1.97e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871  15 CDSLMIWLQTFNTASPCQDVKQLTSGVAMAQVLHQIDAAWFNESWLSRIKEDVGDNWRIKASNVKKVLQGIMSYYHEFLG 94
Cdd:cd22225     2 CDSLIIWLQTFNTAAPCQTVQDLTSGVAMAQVLHQIDSSWFDESWLSRIKEDVGDNWRIKMSNLKKILQGIVDYYHEFLD 81
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462509871  95 QQISEALIPDLNQITECSDPVELGRLLQLILGCAINCEKKQEHIQNIMTLEESVQHVVMTAIQELMSKE 163
Cdd:cd22225    82 QQISEFLLPDLNRIAEHSDPVELGRLLQLILGCAVNCEKKQEHIQNIMTLEESVQHVVMTAIQELMSKE 150
HOOK_N pfam19047
HOOK domain; This domain is found at the N-terminus of HOOK proteins.
15-163 2.17e-93

HOOK domain; This domain is found at the N-terminus of HOOK proteins.


Pssm-ID: 465958  Cd Length: 151  Bit Score: 278.52  E-value: 2.17e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871  15 CDSLMIWLQTFNTASPCQDVKQLTSGVAMAQVLHQIDAAWFNESWLSRIKEDVGDNWRIKASNVKKVLQGIMSYYHEFLG 94
Cdd:pfam19047   3 CDSLLTWLQTFNVPAPCATVEDLTDGVAMAQVLHQIDPSWFTEAWLSRIKEDVGDNWRLKVSNLKKILQSVVDYYQDVLG 82
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462509871  95 QQISEALIPDLNQITECSDPVELGRLLQLILGCAINCEKKQEHIQNIMTLEESVQHVVMTAIQELMSKE 163
Cdd:pfam19047  83 QQISDFLLPDVNLIGEHSDPAELGRLLQLILGCAVNCEKKQEYIQQIMTLEESVQHVVMTAIQELMSKD 151
HkD_Hook cd22222
Hook domain found in Hook family of microtubule-binding proteins; The Hook family includes ...
15-161 2.41e-88

Hook domain found in Hook family of microtubule-binding proteins; The Hook family includes Hook1-3. Hook1 is a microtubule-binding protein required for spermatid differentiation. Hook2, also a microtubule-binding protein, contributes to the establishment and maintenance of centrosome function. It may function in the positioning or formation of aggresomes, which are pericentriolar accumulations of misfolded proteins, proteasomes and chaperones. Hook3 is an adaptor protein for microtubule-dependent intracellular vesicle and protein trafficking. It is involved in Golgi and endosome transport. It acts as a scaffold for the opposite-polarity microtubule-based motors cytoplasmic dynein-1 and the kinesin KIF1C. It may participate in the turnover of the endocytosed scavenger receptor. Hook proteins are components of the FTS/Hook/FHIP complex (FHF complex), which may function to promote vesicle trafficking and/or fusion via the homotypic vesicular protein sorting (HOPS) complex. Hook adaptor proteins share an N-terminal conserved globular Hook domain, which folds as a variant of the helical calponin homology (CH) domain, and contacts the helix alpha1 of dynein light intermediate chain 1 (LIC1) in a hydrophobic groove.


Pssm-ID: 411793  Cd Length: 147  Bit Score: 265.65  E-value: 2.41e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871  15 CDSLMIWLQTFNTASPCQDVKQLTSGVAMAQVLHQIDAAWFNESWLSRIKEDVGDNWRIKASNVKKVLQGIMSYYHEFLG 94
Cdd:cd22222     1 CDSLLQWLQTFNLIAPHATAEDLSDGVAIAQVLNQIDPEYFSDSWLSKIKPDVGDNWRLKVSNLKKILKGIVDYYSEVLG 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462509871  95 QQISEALIPDLNQITECSDPVELGRLLQLILGCAINCEKKQEHIQNIMTLEESVQHVVMTAIQELMS 161
Cdd:cd22222    81 QQISGFTMPDVNAIAEKEDPKELGRLLQLVLGCAVNCERKEEYIQAIMGLEESVQHVVMEAIQELMS 147
HkD_Hook2 cd22227
Hook domain found in protein Hook 2 (Hook2) and similar proteins; Hook2 is a ...
15-162 7.61e-75

Hook domain found in protein Hook 2 (Hook2) and similar proteins; Hook2 is a microtubule-binding protein that contributes to the establishment and maintenance of centrosome function. It may function in the positioning or formation of aggresomes, which are pericentriolar accumulations of misfolded proteins, proteasomes and chaperones. Hook2 is a component of the FTS/Hook/FHIP complex (FHF complex), which may function to promote vesicle trafficking and/or fusion via the homotypic vesicular protein sorting (HOPS) complex.


Pssm-ID: 411798  Cd Length: 150  Bit Score: 231.30  E-value: 7.61e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871  15 CDSLMIWLQTFNTASPCQDVKQLTSGVAMAQVLHQIDAAWFNESWLSRIKEDVGDNWRIKASNVKKVLQGIMSYYHEFLG 94
Cdd:cd22227     3 CDSLLTWLQTFQVPSPCSSYQDLTSGVAIAQVLNRIDPSWFNEAWLGRIKEDTGDNWRLKVSNLKKILQSLLEYYQDVLG 82
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462509871  95 QQISEALIPDLNQITECSDPVELGRLLQLILGCAINCEKKQEHIQNIMTLEESVQHVVMTAIQELMSK 162
Cdd:cd22227    83 HQVSEDHLPDVNLIGEFSDDTELGKLLQLVLGCAISCEKKQEHIQQIMTLEESVQHVVMEAIQELLTK 150
HkD_Hook3 cd22226
Hook domain found in protein Hook 3 (Hook3) and similar proteins; Hook3 is an adaptor protein ...
15-162 9.57e-75

Hook domain found in protein Hook 3 (Hook3) and similar proteins; Hook3 is an adaptor protein for microtubule-dependent intracellular vesicle and protein trafficking. It is involved in Golgi and endosome transport. It acts as a scaffold for the opposite-polarity microtubule-based motors cytoplasmic dynein-1 and the kinesin KIF1C. It may participate in the turnover of the endocytosed scavenger receptor. Hook3 is a component of the FTS/Hook/FHIP complex (FHF complex), which may function to promote vesicle trafficking and/or fusion via the homotypic vesicular protein sorting (HOPS) complex.


Pssm-ID: 411797  Cd Length: 153  Bit Score: 231.01  E-value: 9.57e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871  15 CDSLMIWLQTFNTASPCQDVKQLTSGVAMAQVLHQIDAAWFNESWLSRIKEDVGDNWRIKASNVKKVLQGIMSYYHEFLG 94
Cdd:cd22226     6 CESLLTWIQTFNVDAPCQTVEDLTSGVVMAQVLQKIDPAYFDENWLNRIKTEVGDNWRLKISNLKKILKGILDYNHEILG 85
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462509871  95 QQISEALIPDLNQITECSDPVELGRLLQLILGCAINCEKKQEHIQNIMTLEESVQHVVMTAIQELMSK 162
Cdd:cd22226    86 QQINDFTLPDVNLIGEHSDAAELGRMLQLILGCAVNCEQKQEYIQTIMMMEESVQHVVMTAIQELMSK 153
HkD_SF cd22211
Hook domain-containing proteins superfamily; The Hook domain superfamily includes Hook adaptor ...
16-161 7.13e-50

Hook domain-containing proteins superfamily; The Hook domain superfamily includes Hook adaptor proteins, Hook-related proteins and nuclear mitotic apparatus protein (NuMA). They share an N-terminal conserved globular Hook domain, which folds as a variant of the helical calponin homology (CH) domain with an extended alpha-helix. The Hook domain is responsible for the binding of microtubule. The Hook family includes microtubule-binding proteins, Hook1-3. Hook1 is required for spermatid differentiation. Hook2 contributes to the establishment and maintenance of centrosome function. Hook3 is an adaptor protein for microtubule-dependent intracellular vesicle and protein trafficking, and is involved in Golgi and endosome transport. Hook proteins are components of the FTS/Hook/FHIP complex (FHF complex), which may function to promote vesicle trafficking and/or fusion via the homotypic vesicular protein sorting (HOPS) complex. The Hook-related protein (HkRP) family includes Daple, Girdin and Gipie. Daple, also called Dvl-associating protein with a high frequency of leucine residues, or coiled-coil domain-containing protein 88C(CCDC88C), or Hook-related protein 2 (HkRP2), is a novel non-receptor nucleotide exchange factor (GEF) required for activation of guanine nucleotide-binding proteins (G-proteins) during non-canonical Wnt signaling. Girdin, also called Akt phosphorylation enhancer (APE), or coiled-coil domain-containing protein 88A (CCDC88A), or G alpha-interacting vesicle-associated protein (GIV), or Girders of actin filament, or Hook-related protein 1 (HkRP1), is a bifunctional modulator of guanine nucleotide-binding proteins (G proteins). Gipie, also called GRP78-interacting protein induced by ER stress, or coiled-coil domain-containing protein 88B(CCDC88B), or brain leucine zipper domain-containing protein, or Hook-related protein 3 (HkRP3), is a novel actin cytoskeleton-binding protein and Akt substrate that regulates cell migratory responses in various biological contexts. NuMA, also called nuclear mitotic apparatus protein 1, or nuclear matrix protein-22 (NMP-22), or SP-H antigen, is a microtubule (MT)-binding protein that plays a role in the formation and maintenance of the spindle poles and the alignment and the segregation of chromosomes during mitotic cell division.


Pssm-ID: 411792  Cd Length: 145  Bit Score: 166.30  E-value: 7.13e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871  16 DSLMIWLQTFNTASPCQDVKQLTSGVAMAQVLHQIDAAWFNESWLSriKEDVGDNWRIKASNVKKVLQGIMSYYHEFLGQ 95
Cdd:cd22211     2 AALLAWINTFPLSSPVESLDDLSDGVVLAEILSQIDPSYFDSEWLE--SRDSSDNWVLKLNNLKKLYRSLSKYYREVLGQ 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462509871  96 QISEALIPDLNQITECSDPVELGRLLQLILGCAINCEKKQEHIQNIMTLEESVQHVVMTAIQELMS 161
Cdd:cd22211    80 QLSDLPLPDLSAIARDGDEEEIVKLLELVLGAAVQCENKEEYIARIQQLDESTQAELMLIIQEVLE 145
HkD_HkRP cd22223
Hook domain found in the Hook-related protein (HkRP) family; The HkRP family includes Daple, ...
17-159 1.92e-22

Hook domain found in the Hook-related protein (HkRP) family; The HkRP family includes Daple, Girdin and Gipie. Daple, also called Dvl-associating protein with a high frequency of leucine residues, or coiled-coil domain-containing protein 88C (CCDC88C), or Hook-related protein 2 (HkRP2), is a novel non-receptor nucleotide exchange factor (GEF) required for activation of guanine nucleotide-binding proteins (G-proteins) during non-canonical Wnt signaling. Girdin, also called Akt phosphorylation enhancer (APE), or coiled-coil domain-containing protein 88A (CCDC88A), or G alpha-interacting vesicle-associated protein (GIV), or Girders of actin filament, or Hook-related protein 1 (HkRP1), is a bifunctional modulator of guanine nucleotide-binding proteins (G proteins). It acts as a non-receptor guanine nucleotide exchange factor which binds to and activates guanine nucleotide-binding protein G(i) alpha subunits. It also acts as a guanine nucleotide dissociation inhibitor for guanine nucleotide-binding protein G(s) subunit alpha GNAS. In addition, Girdin plays an essential role in cell migration. Gipie, also called GRP78-interacting protein induced by ER stress, or coiled-coil domain-containing protein 88B (CCDC88B), or brain leucine zipper domain-containing protein, or Hook-related protein 3 (HkRP3), is a novel actin cytoskeleton-binding protein and Akt substrate that regulates cell migratory responses in various biological contexts. It acts as a positive regulator of T-cell maturation and inflammatory function. As a microtubule-binding protein, Gipie regulates lytic granule clustering and NK cell killing. All family members contain a conserved globular Hook domain which folds as a variant of the helical calponin homology (CH) domain.


Pssm-ID: 411794  Cd Length: 149  Bit Score: 93.04  E-value: 1.92e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871  17 SLMIWLQTFNTASPCQ-DVKQLTSGVAMAQVLHQIDAAWFNESWLSRIKEDVgdNWRIKasNVKKVLQGIMSYYHEFLGQ 95
Cdd:cd22223     5 PLVTWAKTFADDGSAElSYTDLVDGVFLNNVMLQIDPRPFSEVSNRNVDDDV--NARIQ--NLDLLLRNIKSFYQEVLQQ 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871  96 QISEALiPDLNQIteCSDP------VELGRLLQLILGCAINCEKKQEHIQNIMTLEESVQHVVMTAIQEL 159
Cdd:cd22223    81 LIVMKL-PDILTI--GREPeseqslEELEKLLLLLLGCAVQCERKEEFIERIKNLDLEVQHALVACIQEV 147
HkD_Daple cd22228
Hook domain found in Daple (Dvl-associating protein with a high frequency of leucine residues) ...
18-159 4.66e-13

Hook domain found in Daple (Dvl-associating protein with a high frequency of leucine residues) and similar proteins; Protein Daple, also called coiled-coil domain-containing protein 88C (CCDC88C), or Hook-related protein 2 (HkRP2), is a novel non-receptor nucleotide exchange factor (GEF) required for activation of guanine nucleotide-binding proteins (G-proteins) during non-canonical Wnt signaling.


Pssm-ID: 411799  Cd Length: 153  Bit Score: 66.49  E-value: 4.66e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871  18 LMIWLQTFNTASPCQDVK-----QLTSGVAMAQVLHQIDAAWFNEswlsRIKEDVGDNWRIKASNVKKVLQGIMSYYHEF 92
Cdd:cd22228     6 LVTWVKTFGPLGFGSEDKlsmymDLVDGVFLNKIMLQIDPRPTNQ----RVNKHVNNDVNLRIQNLTILVRHIKTYYQEV 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462509871  93 LGQQISEALiPDLNQITEcsDPV------ELGRLLQLILGCAINCEKKQEHIQNIMTLEESVQHVVMTAIQEL 159
Cdd:cd22228    82 LQQLIVMNL-PNVLMIGK--DPLsgksmeEIKKMLLLVLGCAVQCERKEEFIERIKQLDIETQAAIVSHIQEV 151
HkD_Girdin cd22229
Hook domain found in Girdin and similar proteins; Girdin, also called Akt phosphorylation ...
18-159 8.84e-11

Hook domain found in Girdin and similar proteins; Girdin, also called Akt phosphorylation enhancer (APE), or coiled-coil domain-containing protein 88A (CCDC88A), or G alpha-interacting vesicle-associated protein (GIV), or Girders of actin filament, or Hook-related protein 1 (HkRP1), is a bifunctional modulator of guanine nucleotide-binding proteins (G proteins). It acts as a non-receptor guanine nucleotide exchange factor which binds to and activates guanine nucleotide-binding protein G(i) alpha subunits. It also acts as a guanine nucleotide dissociation inhibitor for guanine nucleotide-binding protein G(s) subunit alpha GNAS. In addition, Girdin plays an essential role in cell migration.


Pssm-ID: 411800  Cd Length: 156  Bit Score: 60.19  E-value: 8.84e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871  18 LMIWLQTF-----NTASPCQDVKQLTSGVAMAQVLHQIDAAWFNEswlsRIKEDVGDNWRIKASNVKKVLQGIMSYYHEF 92
Cdd:cd22229     9 LVTWVKTFgplatGNGTPLDEYVALVDGVFLNEVMLQINPKSSNQ----RVNKKVNNDASLRIQNLSILVKQIKLYYQET 84
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462509871  93 LGQQISEALiPDL-----NQITEcSDPVELGRLLQLILGCAINCEKKQEHIQNIMTLEESVQHVVMTAIQEL 159
Cdd:cd22229    85 LQQLIMMSL-PNVlvlgrNPLSE-QGTEEMKKLLLLLLGCAVQCERKEEFIERIQTLDFDTKAAVAAHIQEV 154
HkD_Gipie cd22230
Hook domain found in Gipie (GRP78-interacting protein induced by ER stress) and similar ...
36-159 2.30e-08

Hook domain found in Gipie (GRP78-interacting protein induced by ER stress) and similar proteins; Gipie, also called coiled-coil domain-containing protein 88B (CCDC88B), or brain leucine zipper domain-containing protein, or Hook-related protein 3 (HkRP3), is a novel actin cytoskeleton-binding protein and Akt substrate that regulates cell migratory responses in various biological contexts. It acts as a positive regulator of T-cell maturation and inflammatory function. As a microtubule-binding protein, Gipie regulates lytic granule clustering and NK cell killing.


Pssm-ID: 411801  Cd Length: 170  Bit Score: 53.30  E-value: 2.30e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871  36 QLTSGVAMAQVLHQIDAawfNESWLSRIKEDVGDN-WRIKasNVKKVLQGIMSYYHEFLGQQISEALiPDL-----NQIT 109
Cdd:cd22230    46 RLSNGDLLNRVMGIIDP---SPRGGPRMRGDDGPAaHRVQ--NLHILWGRLRDFYQEELQQLILSPP-PDLqvmgrDPFT 119
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2462509871 110 ECSdPVELGRLLQLILGCAINCEKKQEHIQNIMTLEESVQHVVMTAIQEL 159
Cdd:cd22230   120 EEA-VQELEKLLRLLLGAAVQCERRELFIRHIQGLDLDVQAELAEAIQEV 168
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
175-414 8.36e-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: 54.68  E-value: 8.36e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871  175 ELEQQLKRALEELQEALAEKEELRQRCEELDMQVTTLQDEKNSLVSENEMMNEKLDQLDGSfddpntvvakkyfhAQLQL 254
Cdd:TIGR02168  681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAE--------------VEQLE 746
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871  255 EQLQEENFRLEAAKDDYRVHCEELEKQLIEFQHRNDELTSLAEETRALKDEIDVLRATSDKANKLESTVEI-YRQKLQDL 333
Cdd:TIGR02168  747 ERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEeAANLRERL 826
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871  334 NDLRKQVKTLQETNMMYMHNTVSLEEELKKANAARTQLETYKRQVQDLHVKLSSESKRADTLAFEMKRLEEKHEALLKEK 413
Cdd:TIGR02168  827 ESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELREL 906

                   .
gi 2462509871  414 E 414
Cdd:TIGR02168  907 E 907
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
171-404 1.09e-07

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 54.35  E-value: 1.09e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871  171 DAVGELEQQLKRALEELQEALAEKEELRQRCEELDMQVT-------------TLQDEKNSLVSENEMMNE-KLDQLDGSF 236
Cdd:pfam15921  342 DKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQklladlhkrekelSLEKEQNKRLWDRDTGNSiTIDHLRREL 421
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871  237 DDPNTVVAkkyfhaqlqleqlqeenfRLEAAKDDYRVHCE-ELEKQLIEFQHRNDELTSLAEETRALKDEIDVLRATSDK 315
Cdd:pfam15921  422 DDRNMEVQ------------------RLEALLKAMKSECQgQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEE 483
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871  316 ANKLESTVEIYRQKLQDLN-DLRKQVKTLQETN--MMYMHNTVSLE-EELKKANAARTQLETYKRQVQDLHVKLSSESKR 391
Cdd:pfam15921  484 LTAKKMTLESSERTVSDLTaSLQEKERAIEATNaeITKLRSRVDLKlQELQHLKNEGDHLRNVQTECEALKLQMAEKDKV 563
                          250
                   ....*....|...
gi 2462509871  392 ADTLAFEMKRLEE 404
Cdd:pfam15921  564 IEILRQQIENMTQ 576
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
179-425 1.39e-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: 54.29  E-value: 1.39e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871  179 QLKRALEELQEALAEKEELRQRCEELDMQVTTLQDEKNSLVSENEMMNEKLDQLDGSFDDPNTVVAKKyfhaqlqLEQLQ 258
Cdd:TIGR02168  233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRL-------EQQKQ 305
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871  259 EENFRLEAAKDDYrvhcEELEKQLIEFQHRNDEltsLAEETRALKDEIDVLRATSD-KANKLESTVEIYRQKLQDLNDLR 337
Cdd:TIGR02168  306 ILRERLANLERQL----EELEAQLEELESKLDE---LAEELAELEEKLEELKEELEsLEAELEELEAELEELESRLEELE 378
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871  338 KQVKTLQEtnmmymhNTVSLEEELKKANAARTQLETYKRQVQDLHVKLSSESKRADTLAFEMKRLEEKHEALLKEKEIFA 417
Cdd:TIGR02168  379 EQLETLRS-------KVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEE 451

                   ....*...
gi 2462509871  418 LPLAFSSL 425
Cdd:TIGR02168  452 LQEELERL 459
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
175-414 3.22e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.02  E-value: 3.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871 175 ELEQQLKRALEELQEALAEKEELRQRCEELDMQVTTLQDEKNSLVSENEMMNEKLDqldgsfddpntvvakkyfHAQLQL 254
Cdd:COG1196   250 ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIA------------------RLEERR 311
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871 255 EQLQEENFRLEAAKDDYRVHCEELEKQLIEFQHRNDELTSLAEETRALKDEID--VLRATSDKANKLESTVEIYRQKLQD 332
Cdd:COG1196   312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEeaLLEAEAELAEAEEELEELAEELLEA 391
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871 333 LNDLRKQVKTLQETNMMYMHNTVSLEEELKKANAARTQLETYKRQVQDLHVKLSSESKRADTLAFEMKRLEEKHEALLKE 412
Cdd:COG1196   392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE 471

                  ..
gi 2462509871 413 KE 414
Cdd:COG1196   472 AA 473
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
170-414 9.91e-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: 51.21  E-value: 9.91e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871  170 NDAVGELEQQLKRALEELQEALAEKEELRQRCEELDMQVTTLQDEKNSLVSENEMMNEKLDQLDGSFDDPNTVVAKKYFH 249
Cdd:TIGR02168  753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERR 832
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871  250 AQLQLEQLQEENFRLEAAK----------DDYRVHCEELEKQLIEFQhrnDELTSLAEETRALKDEIDVLRATsdkANKL 319
Cdd:TIGR02168  833 IAATERRLEDLEEQIEELSedieslaaeiEELEELIEELESELEALL---NERASLEEALALLRSELEELSEE---LREL 906
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871  320 ESTVEIYRQKLQDLNDLRKQVKT-LQETNMMYMHNT--------VSLEEELKKANAARTQLETYKRQVQDLHVKLsSESK 390
Cdd:TIGR02168  907 ESKRSELRRELEELREKLAQLELrLEGLEVRIDNLQerlseeysLTLEEAEALENKIEDDEEEARRRLKRLENKI-KELG 985
                          250       260
                   ....*....|....*....|....*
gi 2462509871  391 RADTLAF-EMKRLEEKHEALLKEKE 414
Cdd:TIGR02168  986 PVNLAAIeEYEELKERYDFLTAQKE 1010
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
173-414 3.09e-06

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: 3.09e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871  173 VGELEQQLKRALEELQEALAEKEELRQRCEELDMQVTTLQDEKNSLVSENEMMNEKLDQldgsfddPNTVVAKKYFHAQL 252
Cdd:TIGR02169  165 VAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREY-------EGYELLKEKEALER 237
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871  253 QLEQLQEENFRLEAAKDDYRVHCEELEKQLIEfqhRNDELTSLAEETRALKDE--IDVLRATSDKANKLESTVEIYRQKL 330
Cdd:TIGR02169  238 QKEAIERQLASLEEELEKLTEEISELEKRLEE---IEQLLEELNKKIKDLGEEeqLRVKEKIGELEAEIASLERSIAEKE 314
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871  331 QDLNDLRKQVKTLQETNMMYMHNTVSLEEELKKANAARTQLET----YKRQVQDLHVKLSSESKRADTLAFEMKRLEEKH 406
Cdd:TIGR02169  315 RELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEeyaeLKEELEDLRAELEEVDKEFAETRDELKDYREKL 394

                   ....*...
gi 2462509871  407 EALLKEKE 414
Cdd:TIGR02169  395 EKLKREIN 402
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
170-407 3.32e-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: 49.67  E-value: 3.32e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871  170 NDAVGELEQQLKRALEELQEALAEKEELRQRCEELDMQVTTLQDEKNSLVSE-------NEMMNEKLDQLDGSFDDPNTV 242
Cdd:TIGR02168  245 QEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEisrleqqKQILRERLANLERQLEELEAQ 324
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871  243 VAKKYFHAQLQLEQLQeenfRLEAAKDDYRVHCEELEKQLIEFQHRNDELTS----LAEETRALKDEIDVLRAtsdKANK 318
Cdd:TIGR02168  325 LEELESKLDELAEELA----ELEEKLEELKEELESLEAELEELEAELEELESrleeLEEQLETLRSKVAQLEL---QIAS 397
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871  319 LESTVEIYRQKLQDLNDLRKQVKTLQETNMMYMHNT----------------VSLEEELKKANAARTQLETYKRQVQDLH 382
Cdd:TIGR02168  398 LNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAelkelqaeleeleeelEELQEELERLEEALEELREELEEAEQAL 477
                          250       260
                   ....*....|....*....|....*
gi 2462509871  383 VKLSSESKRADTLAFEMKRLEEKHE 407
Cdd:TIGR02168  478 DAAERELAQLQARLDSLERLQENLE 502
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
170-414 9.46e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.01  E-value: 9.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871 170 NDAVGELEQQLK----------RALE--------ELQEALAEKEELRQRCEELDMQVTTLQDEKNSLVSENEMMNEKLDQ 231
Cdd:COG1196   192 EDILGELERQLEplerqaekaeRYRElkeelkelEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEE 271
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871 232 LDGSFDDpntvvakkyfhaqlqleqlqeENFRLEAAKDDYRVHCEELEKQLIEFQHRNDELTSLAEETRALKDEIDVLRA 311
Cdd:COG1196   272 LRLELEE---------------------LELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEE 330
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871 312 TSDKANKLESTVEiyRQKLQDLNDLRKQVKTLQETNMMYMHNTVSLEEELKKANAARTQLETYKRQVQDLHVKLSSESKR 391
Cdd:COG1196   331 ELEELEEELEELE--EELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEA 408
                         250       260
                  ....*....|....*....|...
gi 2462509871 392 ADTLAFEMKRLEEKHEALLKEKE 414
Cdd:COG1196   409 EEALLERLERLEEELEELEEALA 431
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
104-414 1.05e-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: 48.14  E-value: 1.05e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871  104 DLNQITECSdPVELGRLLQLILGCAINCEKKQEHIQNIMTLEES---VQHVVMTAIQELmskEILSSPPNDAvgELEQQL 180
Cdd:TIGR02169  143 DVTDFISMS-PVERRKIIDEIAGVAEFDRKKEKALEELEEVEENierLDLIIDEKRQQL---ERLRREREKA--ERYQAL 216
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871  181 KRALEELQ--EALAEKEELRQRCEELDMQVTTLQDEKNSLVSENEMMNEKLDQLDGSFDDPNTVVAKK----YFHAQLQL 254
Cdd:TIGR02169  217 LKEKREYEgyELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgeeeQLRVKEKI 296
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871  255 EQLQEENFRLEAAKDDYRVHCEELEKQLIEFQhrnDELTSLAEETRALKDEIDvlratsDKANKLESTVEIYRQKLQDLN 334
Cdd:TIGR02169  297 GELEAEIASLERSIAEKERELEDAEERLAKLE---AEIDKLLAEIEELEREIE------EERKRRDKLTEEYAELKEELE 367
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871  335 DLRKQVKTLQETNMMYMHNTVSLEEELKKANAARTQLETYKRQVQDLHVKLSSESKRADTlafEMKRLEEKHEALLKEKE 414
Cdd:TIGR02169  368 DLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNA---AIAGIEAKINELEEEKE 444
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
172-420 1.17e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.01  E-value: 1.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871 172 AVGELEQQLKRALEELQEALAEKEELRQRCEELDMQVTTLQDEKNSLVSENEMMNEKLDQLDGSfddpntvvakkyfhaq 251
Cdd:COG1196   296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE---------------- 359
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871 252 lqleqlqeenfRLEAAKDDYRVHCEELEKQLIEFQHRNDELTSLAEETRALKDEIDVLRATSDKANKLESTVEIYRQKLQ 331
Cdd:COG1196   360 -----------LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEE 428
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871 332 DLNDLRKQVKTLQETNMMYMHNTVSLEEELKKAN----AARTQLETYKRQVQDLHVKLSSESKRADTLAFEMKRLEEKHE 407
Cdd:COG1196   429 ALAELEEEEEEEEEALEEAAEEEAELEEEEEALLellaELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLE 508
                         250
                  ....*....|...
gi 2462509871 408 ALLKEKEIFALPL 420
Cdd:COG1196   509 GVKAALLLAGLRG 521
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
177-412 4.84e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.06  E-value: 4.84e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871  177 EQQLKRALEELQEALAEKEELRQRCEELDMQVTTLQDEKNSLvsenemmnEKLDQLDGSFDDpntvvakkyfhaqlqleq 256
Cdd:COG4913    609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREAL--------QRLAEYSWDEID------------------ 662
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871  257 lqeenfrLEAAKDDYRvhceELEKQLIEFQHRNDELTSLAEETRALKDEIDVLRATSDKANKLESTVEiyrQKLQDLNDL 336
Cdd:COG4913    663 -------VASAEREIA----ELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLE---KELEQAEEE 728
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462509871  337 RKQVKTLQETnmMYMHNTVSLEEELKKANAARTQLETYKRQVQDLHVKLSSESKRADTLAfemKRLEEKHEALLKE 412
Cdd:COG4913    729 LDELQDRLEA--AEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAE---EELERAMRAFNRE 799
Macoilin pfam09726
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ...
165-393 5.62e-05

Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 trasnmembrane helices, followed by a C-terminal coiled-coil region. Macoilin is a highly conserved protein present in eukaryotes. Macoilin appears to be found in the ER and be involved in the function of neurons.


Pssm-ID: 462859 [Multi-domain]  Cd Length: 670  Bit Score: 45.61  E-value: 5.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871 165 LSSPpnDAVGELEQQLKRALEELQEALAEKEELRQRCEELDMQVTTLQDEKNSLVSENEMMNEKLDqldgsfddpNTVVA 244
Cdd:pfam09726 391 LSKP--DALVRLEQDIKKLKAELQASRQTEQELRSQISSLTSLERSLKSELGQLRQENDLLQTKLH---------NAVSA 459
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871 245 KKyfhaqlqleqlqeenfrleaaKDDYRVhcEELEKQLIEFQ-HRNDELTSLAEETRALKDEIDVL-RATSDKANKLEST 322
Cdd:pfam09726 460 KQ---------------------KDKQTV--QQLEKRLKAEQeARASAEKQLAEEKKRKKEEEATAaRAVALAAASRGEC 516
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462509871 323 VEIYRQKLQdlnDLRKQVKTLQetnmmymHNTVSLEEELKKANAARTQLETYKRQVQDLHVKLSSESKRAD 393
Cdd:pfam09726 517 TESLKQRKR---ELESEIKKLT-------HDIKLKEEQIRELEIKVQELRKYKESEKDTEVLMSALSAMQD 577
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
177-414 2.36e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.49  E-value: 2.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871 177 EQQLKRALEELQEALAEKEELRQRCEELDMQVTTLQDEKNSLVSENEMMNEKLDQLDGSFDDPNTVVAKKyfhaqlqleq 256
Cdd:PRK02224  201 EKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAET---------- 270
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871 257 lqeenfrlEAAKDDYRVHCEELEKQLIEFQHRNDELTSLAEETRALKDEIDVLRAT-SDKANKLESTVEIYRQKLQDLND 335
Cdd:PRK02224  271 --------EREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREElEDRDEELRDRLEECRVAAQAHNE 342
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871 336 ----LRKQVKTLQETNMMYMHNTVSLEEELKkanAARTQLETYKRQVQDLHVKLSSESKRADTLAFEMKRLEEKHEALLK 411
Cdd:PRK02224  343 eaesLREDADDLEERAEELREEAAELESELE---EAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELRE 419

                  ...
gi 2462509871 412 EKE 414
Cdd:PRK02224  420 ERD 422
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
178-380 5.01e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 42.72  E-value: 5.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871 178 QQLKRALEELQEALA----EKEELRQRCEELDMQVTTLQDEKNSLVSENEMMNEKLDQLDGSFDDpntvvakkyfhaqlq 253
Cdd:PRK02224  254 ETLEAEIEDLRETIAeterEREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREE--------------- 318
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871 254 leqlqeenfrLEAAKDDYRvhcEELEKQLIEFQHRNDELTSLAEETRALKDEIDVLRatsDKANKLESTVEIYRQKLQD- 332
Cdd:PRK02224  319 ----------LEDRDEELR---DRLEECRVAAQAHNEEAESLREDADDLEERAEELR---EEAAELESELEEAREAVEDr 382
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871 333 ---LNDLRKQVKTLQET---------NMMYMHNtvSLEEELKKANAARTQLETYKRQVQD 380
Cdd:PRK02224  383 reeIEELEEEIEELRERfgdapvdlgNAEDFLE--ELREERDELREREAELEATLRTARE 440
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
170-414 5.50e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.12  E-value: 5.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871 170 NDAVGELEQQLKRALEELQEALAEKEELRQRCEELDMQVTTLQDEKNSLVSENEMMNEKLDQLDgsfddpntvvakkyfh 249
Cdd:COG3883    22 QKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERR---------------- 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871 250 aqlqleqlqeenfrleaakddyrvhcEELEKQLIEFQhRNDELTSLAEEtralkdeidVLRATS-----DKANKLESTVE 324
Cdd:COG3883    86 --------------------------EELGERARALY-RSGGSVSYLDV---------LLGSESfsdflDRLSALSKIAD 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871 325 IYRQKLQDLNDLRKQVKTLQEtnmmymhntvSLEEELKKANAARTQLETYKRQVQDlhvKLSSESKRADTLAFEMKRLEE 404
Cdd:COG3883   130 ADADLLEELKADKAELEAKKA----------ELEAKLAELEALKAELEAAKAELEA---QQAEQEALLAQLSAEEAAAEA 196
                         250
                  ....*....|
gi 2462509871 405 KHEALLKEKE 414
Cdd:COG3883   197 QLAELEAELA 206
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
176-414 6.54e-04

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 42.03  E-value: 6.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871 176 LEQQLKRALEELQEALAEKEELRQRCEELDMQVTTLQdEKNSLVSENEMMNEKLDQ-LDGS------------FDDPNTV 242
Cdd:pfam17380 342 MAMERERELERIRQEERKRELERIRQEEIAMEISRMR-ELERLQMERQQKNERVRQeLEAArkvkileeerqrKIQQQKV 420
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871 243 VAKKYFHAQLQLEQLQEENFRLEAAKDDYRVHCEELEKQLIEFQHRNDELTSLAEETRALKDEIDVLRATSDKANKLEST 322
Cdd:pfam17380 421 EMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKE 500
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871 323 VEIYRQKLQDLNDLRKQVktlqETNMMYMHNTVSLEEELKKANAA-RTQLET-YKRQVQDLHVKLSSESKRADTLAFEMK 400
Cdd:pfam17380 501 LEERKQAMIEEERKRKLL----EKEMEERQKAIYEEERRREAEEErRKQQEMeERRRIQEQMRKATEERSRLEAMERERE 576
                         250
                  ....*....|....
gi 2462509871 401 RLEEKHEALLKEKE 414
Cdd:pfam17380 577 MMRQIVESEKARAE 590
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
170-414 6.83e-04

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: 42.34  E-value: 6.83e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871  170 NDAVGELEQQLKRALEELQEALAEKEELRQRCEELDMQVTTLQDEKNSLVSENEMMNEKLDQLdgsfddpNTVVAKKYFH 249
Cdd:TIGR00606  694 QEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKV-------NRDIQRLKND 766
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871  250 AQLQLEQLQEENFRLEAAKD---DYRVhCEELEKQLIEFQHRNDELTSLAEETRALKDEIDVLRATSDKANKLESTVEIY 326
Cdd:TIGR00606  767 IEEQETLLGTIMPEEESAKVcltDVTI-MERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKI 845
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871  327 RQKLQDLNDLRKQVKTLQETNMMYMHNTVSLEEELKKANAARTQLETYKRQVQDLHVKLSSESKRADTLAFEMKRLEEKH 406
Cdd:TIGR00606  846 ELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEK 925

                   ....*...
gi 2462509871  407 EALLKEKE 414
Cdd:TIGR00606  926 EELISSKE 933
Med21 pfam11221
Subunit 21 of Mediator complex; Med21 has been known as Srb7 in yeasts, hSrb7 in humans and ...
173-210 7.52e-04

Subunit 21 of Mediator complex; Med21 has been known as Srb7 in yeasts, hSrb7 in humans and Trap 19 in Drosophila. The heterodimer of the two subunits Med7 and Med21 appears to act as a hinge between the middle and the tail regions of Mediator.


Pssm-ID: 463241  Cd Length: 134  Bit Score: 39.50  E-value: 7.52e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2462509871 173 VGELEQQLKRALEELQEALAEKEELRQRCEELDMQVTT 210
Cdd:pfam11221  97 IKELEEELREAEEERQEAVKEKEELLKKLDELIRSVAR 134
PRK10361 PRK10361
DNA recombination protein RmuC; Provisional
280-412 7.82e-04

DNA recombination protein RmuC; Provisional


Pssm-ID: 182409 [Multi-domain]  Cd Length: 475  Bit Score: 41.89  E-value: 7.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871 280 KQLIEFQHRNDELTSLAEETRALKD-----EIDVLRATSdkanKLESTV----EIYRQKLQDLNDLRKQVKTLqeTNMMY 350
Cdd:PRK10361   50 QQITQSEHWRAECELLNNEVRSLQSintslEADLREVTT----RMEAAQqhadDKIRQMINSEQRLSEQFENL--ANRIF 123
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462509871 351 MHNTVSLEEELKKA-----NAARTQLETYKRQVQDlhvKLSSESKRADTLAFEMKRLEEKHEALLKE 412
Cdd:PRK10361  124 EHSNRRVDEQNRQSlnsllSPLREQLDGFRRQVQD---SFGKEAQERHTLAHEIRNLQQLNAQMAQE 187
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
164-414 9.02e-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: 41.29  E-value: 9.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871 164 ILSSPPNDAVGELEQQLKRALEELQEALAEKEELRQRceeldmqvttLQDEKNSLVSENEMMNEKLDQLdgsfddpntvv 243
Cdd:COG4942     9 LLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAA----------LKKEEKALLKQLAALERRIAAL----------- 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871 244 akkyfhaqlqleqlqeeNFRLEAAKDDYRvhceELEKQLIEFQHRNDEL-TSLAEETRALKDEIDVLRAT---------- 312
Cdd:COG4942    68 -----------------ARRIRALEQELA----ALEAELAELEKEIAELrAELEAQKEELAELLRALYRLgrqpplalll 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871 313 -SDKANKLESTVEIYRQKLQD----LNDLRKQVKTLQETNMMYMHNTVSLEEELKKANAARTQLETYKRQVQDLHVKLSS 387
Cdd:COG4942   127 sPEDFLDAVRRLQYLKYLAPArreqAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEK 206
                         250       260       270
                  ....*....|....*....|....*....|.
gi 2462509871 388 E----SKRADTLAFEMKRLEEKHEALLKEKE 414
Cdd:COG4942   207 ElaelAAELAELQQEAEELEALIARLEAEAA 237
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
170-389 9.83e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.54  E-value: 9.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871 170 NDAVGELEQQLKRALEELQEALAEKEELRQRCEELDM---------QVTTLQDEKNSLVSENEMMNEKLDQLDGSFDDPN 240
Cdd:COG3206   174 RKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLseeaklllqQLSELESQLAEARAELAEAEARLAALRAQLGSGP 253
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871 241 TVVAkkyfhaqlqleqLQEENFRLEAAKDDYRvhceELEKQLIE----FQHRNDELTSLAEETRALKDEIDvlRATSDKA 316
Cdd:COG3206   254 DALP------------ELLQSPVIQQLRAQLA----ELEAELAElsarYTPNHPDVIALRAQIAALRAQLQ--QEAQRIL 315
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462509871 317 NKLESTVEIYRQKLQDLN----DLRKQVKTLQETNMMYMhntvSLEEElkkANAARTQLETYKRQVQDLHVKLSSES 389
Cdd:COG3206   316 ASLEAELEALQAREASLQaqlaQLEARLAELPELEAELR----RLERE---VEVARELYESLLQRLEEARLAEALTV 385
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
170-412 1.12e-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: 41.59  E-value: 1.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871  170 NDAVGELEQQLKRALEELQEALAEKEELRQRCEELDMQVTTLQDEKNSLVSENEMMNEKLDQLdgsfddpntvvAKKYFH 249
Cdd:TIGR02169  680 RERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEEL-----------EEDLSS 748
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871  250 AQLQLEQLQEENFRLEAAKDDYRVHCEELEKQL--IEFQHRNDELTSLAEETRALKDEI----DVLRATSDKANKLESTV 323
Cdd:TIGR02169  749 LEQEIENVKSELKELEARIEELEEDLHKLEEALndLEARLSHSRIPEIQAELSKLEEEVsrieARLREIEQKLNRLTLEK 828
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871  324 EIYRQKLQDL----NDLRKQVKTLQETNMMYMHNTVSLEEELKKANAARTQLET----YKRQVQDLHVKLSSESKRADTL 395
Cdd:TIGR02169  829 EYLEKEIQELqeqrIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESrlgdLKKERDELEAQLRELERKIEEL 908
                          250       260
                   ....*....|....*....|....
gi 2462509871  396 AFE-------MKRLEEKHEALLKE 412
Cdd:TIGR02169  909 EAQiekkrkrLSELKAKLEALEEE 932
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
175-381 1.25e-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: 41.58  E-value: 1.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871  175 ELEQQLKRALEELQEALAEKEELRQRCEELDMQVTTLQDEKNSLVSENEMMNEKLDQLDGSFDDPNTVVAKKYFHAQlql 254
Cdd:TIGR02168  842 DLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELE--- 918
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871  255 eqlqeenfRLEAAKDDYRVHCEELEKQLIEFQHRndeltsLAEETRALKDEIDvlratsdkanKLESTVEIYRQKLQD-L 333
Cdd:TIGR02168  919 --------ELREKLAQLELRLEGLEVRIDNLQER------LSEEYSLTLEEAE----------ALENKIEDDEEEARRrL 974
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 2462509871  334 NDLRKQVKTLQETNMMYMhntvsleEELKKANaarTQLETYKRQVQDL 381
Cdd:TIGR02168  975 KRLENKIKELGPVNLAAI-------EEYEELK---ERYDFLTAQKEDL 1012
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
276-414 1.39e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.05  E-value: 1.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871  276 EELEKQLIEFQhrnDELTSLAEETRALKDEIDVLRATSDKANKLESTVEiyrqklqDLNDLRKQVKTLQEtnmmymhntv 355
Cdd:COG4913    613 AALEAELAELE---EELAEAEERLEALEAELDALQERREALQRLAEYSW-------DEIDVASAEREIAE---------- 672
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462509871  356 sLEEELKKANAARTQLETYKRQVQDLHVKLSSESKRADTLAFEMKRLEEKHEALLKEKE 414
Cdd:COG4913    673 -LEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELD 730
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
177-376 2.10e-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: 40.82  E-value: 2.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871  177 EQQLKRA--LEELQEALAEKEELRQRCEELDMQVTTLQDEKNSLVSENEMMNEKLDQLDGSFDdpntvvakkyfhaqlql 254
Cdd:TIGR02169  347 EERKRRDklTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELD----------------- 409
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871  255 eQLQEENFRLEAAKDDYRVHCEELEKQLIEFQhrnDELTSLAEETRALKDEIDVLRATSDKANKlestvEIYRQKlQDLN 334
Cdd:TIGR02169  410 -RLQEELQRLSEELADLNAAIAGIEAKINELE---EEKEDKALEIKKQEWKLEQLAADLSKYEQ-----ELYDLK-EEYD 479
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 2462509871  335 DLRKQVKtlqetnmmymhntvSLEEELKKANAARTQLETYKR 376
Cdd:TIGR02169  480 RVEKELS--------------KLQRELAEAEAQARASEERVR 507
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
183-414 2.54e-03

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 40.19  E-value: 2.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871 183 ALEELQEALAEKEELRQRC-EELDMQVTTLQDEKNSLVSENEMMNEKLDQLDGSFDDPNTVVAKKYFHAQLQLEQLQEEN 261
Cdd:pfam10174 437 ALTTLEEALSEKERIIERLkEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKD 516
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871 262 FR---LEAAKDDYRVHCEELEKQLIEFQHRNDELTS---LAEETRALKDEIDVLRATSDKAN-KLESTVEIYRQKLQDLN 334
Cdd:pfam10174 517 SKlksLEIAVEQKKEECSKLENQLKKAHNAEEAVRTnpeINDRIRLLEQEVARYKEESGKAQaEVERLLGILREVENEKN 596
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871 335 DLRKQVKTLQETNMMYMHntvslEEELKKANAARTQLETYKRQVQDLHVKLSSESKRADTLAfeMKRLEEKHEALLKEKE 414
Cdd:pfam10174 597 DKDKKIAELESLTLRQMK-----EQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQ--QLQLEELMGALEKTRQ 669
COG4026 COG4026
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ...
175-238 3.27e-03

Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];


Pssm-ID: 443204 [Multi-domain]  Cd Length: 287  Bit Score: 39.33  E-value: 3.27e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462509871 175 ELEQQLKRALEELQEALAEKEELRQRCEELDMQVTTLQDEKNSLVSENEMMNEKLDQLDGSFDD 238
Cdd:COG4026   132 ELREELLELKEKIDEIAKEKEKLTKENEELESELEELREEYKKLREENSILEEEFDNIKSEYSD 195
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
173-414 3.37e-03

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 39.12  E-value: 3.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871 173 VGELEQQLKRALEELQEALAEKEELRQRCEELDMQVTTLQDEKNSLVSENEMMNEKLDQLDGSFDDPNTVVAKKYFHAQL 252
Cdd:COG1340    17 IEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDE 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871 253 QLEQLQEENfRLEAAKDDYRVHCEELEKQLIEFQHRNDELTSLAEETRALKDEIDVLRATSDKANKLESTVEIYRQKLQD 332
Cdd:COG1340    97 LRKELAELN-KAGGSIDKLRKEIERLEWRQQTEVLSPEEEKELVEKIKELEKELEKAKKALEKNEKLKELRAELKELRKE 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871 333 LNDLRKQVKTLQEtNMMYMHNtvSLEEELKKANAARTQLETYKRQVQDLHVKLSSESKRADTLAFEMKRLEEKHEALLKE 412
Cdd:COG1340   176 AEEIHKKIKELAE-EAQELHE--EMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKK 252

                  ..
gi 2462509871 413 KE 414
Cdd:COG1340   253 QR 254
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
107-342 3.66e-03

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 39.91  E-value: 3.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871 107 QITECSDPVE---LGRLLQLilgcAINCEKKQEHIQNIMTLEESVQHVVMTaIQELMSKEILSSPpNDAVGELEQQLKRA 183
Cdd:PRK05771   32 HIEDLKEELSnerLRKLRSL----LTKLSEALDKLRSYLPKLNPLREEKKK-VSVKSLEELIKDV-EEELEKIEKEIKEL 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871 184 LEELQEALAEKEELRQRCEEL------DMQVTTLQDEKNSLVSENEMMNEKLDQLDGSFDDPNTVVAKKYfhaqlqleqL 257
Cdd:PRK05771  106 EEEISELENEIKELEQEIERLepwgnfDLDLSLLLGFKYVSVFVGTVPEDKLEELKLESDVENVEYISTD---------K 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871 258 QEENFRLEAAKDDYRVHCEELEK---QLIEFQHR---NDELTSLAEETRALKDEIDVLRAT-SDKANKLE----STVEIY 326
Cdd:PRK05771  177 GYVYVVVVVLKELSDEVEEELKKlgfERLELEEEgtpSELIREIKEELEEIEKERESLLEElKELAKKYLeellALYEYL 256
                         250
                  ....*....|....*.
gi 2462509871 327 RQKLQDLNDLRKQVKT 342
Cdd:PRK05771  257 EIELERAEALSKFLKT 272
PLN02939 PLN02939
transferase, transferring glycosyl groups
176-391 3.94e-03

transferase, transferring glycosyl groups


Pssm-ID: 215507 [Multi-domain]  Cd Length: 977  Bit Score: 39.89  E-value: 3.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871 176 LEQQLKRALEELQEALAEKEELRQRCEELDMQVTTlQDEKNSLVSEN----EMMNEKLDQLDGSFDDPNTVVAKKYFHAQ 251
Cdd:PLN02939  147 LNQARLQALEDLEKILTEKEALQGKINILEMRLSE-TDARIKLAAQEkihvEILEEQLEKLRNELLIRGATEGLCVHSLS 225
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871 252 LQLEQLQEENFRL------------EAAKDDYRVHCEELEKQLIEFQHRNDELTSLAEETRALK----------DEIDVL 309
Cdd:PLN02939  226 KELDVLKEENMLLkddiqflkaeliEVAETEERVFKLEKERSLLDASLRELESKFIVAQEDVSKlsplqydcwwEKVENL 305
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871 310 RATSDKANKlesTVEIYRQKLQDLNDLRKQV----KTLQETNM---------MYMHNTVSLEEELKKANAA-RTQLETYK 375
Cdd:PLN02939  306 QDLLDRATN---QVEKAALVLDQNQDLRDKVdkleASLKEANVskfssykveLLQQKLKLLEERLQASDHEiHSYIQLYQ 382
                         250
                  ....*....|....*....
gi 2462509871 376 RQVQDLHVKLSS---ESKR 391
Cdd:PLN02939  383 ESIKEFQDTLSKlkeESKK 401
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
131-414 5.31e-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: 39.28  E-value: 5.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871  131 CEKKQEHIQNIMTLEESVQHVVMTAIQELMSK-EILSSPPNDAVGELEQqLKRALEELQEALA----EKEELRQRCEELD 205
Cdd:TIGR02169  693 LQSELRRIENRLDELSQELSDASRKIGEIEKEiEQLEQEEEKLKERLEE-LEEDLSSLEQEIEnvksELKELEARIEELE 771
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871  206 MQVTTLQDEKNSLvsENEMMNEKLDQLDGSFDDPNTVVAKKYFHAQLQLEQLQEENFRLEAAKD------DYRVHCE--- 276
Cdd:TIGR02169  772 EDLHKLEEALNDL--EARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKeiqelqEQRIDLKeqi 849
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871  277 -ELEKQLIEFQHRNDELTSLAEETRA-----------LKDEID----VLRATSDKANKLESTVEIYRQKLqdlNDLRKQV 340
Cdd:TIGR02169  850 kSIEKEIENLNGKKEELEEELEELEAalrdlesrlgdLKKERDeleaQLRELERKIEELEAQIEKKRKRL---SELKAKL 926
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462509871  341 KTLQETNMMYMHNTVSLEEELKKANAARTQLETYKRQVQDLH----VKLSSESKRADTLAfEMKRLEEKHEALLKEKE 414
Cdd:TIGR02169  927 EALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRalepVNMLAIQEYEEVLK-RLDELKEKRAKLEEERK 1003
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
174-414 5.60e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.28  E-value: 5.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871 174 GELEQQLKRALEELQEALAEKEELRQRCEELDMQVTTLQDEKNSLVSENEMMNEKLDQLDGSFDDPNTVvaKKYFHAQLQ 253
Cdd:PRK03918  168 GEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEEL--KEEIEELEK 245
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871 254 LEQLQEENFR-LEAAKDDYRVHCEELEKQLIEFQHRNDELTSLAEETRALKDEIDVLRATSDKANKLESTVEIYRQKlqd 332
Cdd:PRK03918  246 ELESLEGSKRkLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEE--- 322
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871 333 LNDLRKQVKTLQETNmmymHNTVSLEEELKKANAARTQLETYKRQVQDLHVKLSS-ESKRADTLAFEMKRLEEKHEALLK 411
Cdd:PRK03918  323 INGIEERIKELEEKE----ERLEELKKKLKELEKRLEELEERHELYEEAKAKKEElERLKKRLTGLTPEKLEKELEELEK 398

                  ...
gi 2462509871 412 EKE 414
Cdd:PRK03918  399 AKE 401
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
170-414 6.24e-03

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


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 38.95  E-value: 6.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871 170 NDAVGELEQQLKRALEELQEALAEKEELRQRCEELD---MQVTTLQDEKNSLVSENEMMNEKLDQLDgsfddpntvvakk 246
Cdd:pfam05557 110 KNELSELRRQIQRAELELQSTNSELEELQERLDLLKakaSEAEQLRQNLEKQQSSLAEAEQRIKELE------------- 176
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871 247 YFHAQLQLEQLQEENFRLEAAKddyrvhCEELEKQLIEFQHRNDELTSLAEETRALKDEIDVLRA-------TSDKANKL 319
Cdd:pfam05557 177 FEIQSQEQDSEIVKNSKSELAR------IPELEKELERLREHNKHLNENIENKLLLKEEVEDLKRklereekYREEAATL 250
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871 320 ESTVEIYRQKLQ-----------DLN---DLRKQVKTLQETNMMYMHNTVSLEEELKKANAARTQLETYKRQVQDLHVKL 385
Cdd:pfam05557 251 ELEKEKLEQELQswvklaqdtglNLRspeDLSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDL 330
                         250       260
                  ....*....|....*....|....*....
gi 2462509871 386 SSESKRADTLAfemKRLEEKHEALLKEKE 414
Cdd:pfam05557 331 NKKLKRHKALV---RRLQRRVLLLTKERD 356
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
169-284 7.18e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 38.74  E-value: 7.18e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871  169 PNDAVGELEQQLKRALEELQEALAEKEELRQRCEELDMQVTTLQDEKNSLvsenemmNEKLDQLDGSFDDPNTVVAKKYF 248
Cdd:COG4913    683 SSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDEL-------QDRLEAAEDLARLELRALLEERF 755
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 2462509871  249 HAQLQLEQLQEENFRLEAAKDDYRVHCEELEKQLIE 284
Cdd:COG4913    756 AAALGDAVERELRENLEERIDALRARLNRAEEELER 791
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
167-409 8.53e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 38.48  E-value: 8.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871 167 SPPNDAVGELEQQLKRALEELQEALAEKEELRQRCEELDmQVTTLQDEKNSLVSENEMMNEKLDQLDGSFDDPNTVVAKK 246
Cdd:PRK02224  464 SPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAE-DLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEEL 542
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871 247 YFHAQLqleqlqeenfrLEAAKDDYRvhcEELEKQLIEFQHRNDELTSLAEETRALKDEIDVLRATSDKANKLE---STV 323
Cdd:PRK02224  543 RERAAE-----------LEAEAEEKR---EAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIAdaeDEI 608
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871 324 EIYRQKLQDLNDLRKQVK-TLQETNmmymHNTVSLEEE-----LKKANAARTQLETYKRQVQDLHVKLS----------- 386
Cdd:PRK02224  609 ERLREKREALAELNDERReRLAEKR----ERKRELEAEfdearIEEAREDKERAEEYLEQVEEKLDELReerddlqaeig 684
                         250       260
                  ....*....|....*....|....*.
gi 2462509871 387 ---SESKRADTLAFEMKRLEEKHEAL 409
Cdd:PRK02224  685 aveNELEELEELRERREALENRVEAL 710
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
263-413 9.38e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 38.74  E-value: 9.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509871  263 RLEAAKDDYRVHCEELEkQLIEFQHRNDELTSLAEETRALKDEIDVLRATSDKANKLESTVEIYRQKLQDLNDLRKQVKt 342
Cdd:COG4913    635 ALEAELDALQERREALQ-RLAEYSWDEIDVASAEREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELK- 712
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462509871  343 lqetnmmymhntvsleeelKKANAARTQLETYKRQVQDLHVKLSSESKRADTLAFEmkRLEEKHEALLKEK 413
Cdd:COG4913    713 -------------------GEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRA--LLEERFAAALGDA 762
 
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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