NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|289803020|ref|NP_001073879|]
View 

F-box only protein 41 [Homo sapiens]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
F-box_FBXO41 cd22109
F-box domain found in F-box only protein 41 (FBXO41) and similar proteins; FBXO41, also called ...
547-593 1.59e-22

F-box domain found in F-box only protein 41 (FBXO41) and similar proteins; FBXO41, also called FBX41, is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. It acts as a novel central nervous system (CNS)-specific F-box protein that localizes to the centrosome and the cytoplasm of neurons and promotes neuronal migration. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


:

Pssm-ID: 438881  Cd Length: 47  Bit Score: 90.85  E-value: 1.59e-22
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 289803020 547 SPEILKMRAALFCIFTYLDTRTLLHAAEVCRDWRFVARHPAVWTRVL 593
Cdd:cd22109    1 SLESLRRRDALFCVFSYLDTKSLLRCAEVCREWRDVSRHPALWQRVC 47
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
202-344 1.21e-11

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 68.81  E-value: 1.21e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020 202 LARLKIRALEKLEVDRRLERLSEEVEQKIAgQVGRLQAELERKAAELETARQESARLGREKEELEERASELSRQVDVSVE 281
Cdd:COG1196  231 LLKLRELEAELEELEAELEELEAELEELEA-ELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE 309
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 289803020 282 LLASLKQDLVHKEQELSRKQQEVVQIDQFLKETAAREASAKLRLQQFIEELLERADRAERQLQ 344
Cdd:COG1196  310 RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
211-491 2.98e-06

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


:

Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 50.60  E-value: 2.98e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020 211 EKLEVDRRLERLSEEVEQKIAgQVGRLQAELERKAAELETARQE----SARLGREKEELEERASE--------------- 271
Cdd:COG3883   31 ELEAAQAELDALQAELEELNE-EYNELQAELEALQAEIDKLQAEiaeaEAEIEERREELGERARAlyrsggsvsyldvll 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020 272 --------LSRQVDVS---------VELLASLKQDLVHKEQELSRKQQEVVQIDQFLKETAAREASAKLRLQQFIEELLE 334
Cdd:COG3883  110 gsesfsdfLDRLSALSkiadadadlLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSA 189
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020 335 RADRAERQLQVISSScgstpSASLGRGGGGGGAGPNARGPGRMREHHVGPAVPNTYAVSRHGSSPSTGASSRVPAASQSS 414
Cdd:COG3883  190 EEAAAEAQLAELEAE-----LAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGA 264
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 289803020 415 GCYDSDSLELPRPEEGAPEDSGPGGLGTRAQAANGGSERSQPPRSSGLRRQAIQNWQRRPRRHSTEGEEGDVSDVGS 491
Cdd:COG3883  265 AGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAASGGSGGGSGGAGGVGSGGGAGAVVGGASAGGGGGSGGGGGSS 341
 
Name Accession Description Interval E-value
F-box_FBXO41 cd22109
F-box domain found in F-box only protein 41 (FBXO41) and similar proteins; FBXO41, also called ...
547-593 1.59e-22

F-box domain found in F-box only protein 41 (FBXO41) and similar proteins; FBXO41, also called FBX41, is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. It acts as a novel central nervous system (CNS)-specific F-box protein that localizes to the centrosome and the cytoplasm of neurons and promotes neuronal migration. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438881  Cd Length: 47  Bit Score: 90.85  E-value: 1.59e-22
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 289803020 547 SPEILKMRAALFCIFTYLDTRTLLHAAEVCRDWRFVARHPAVWTRVL 593
Cdd:cd22109    1 SLESLRRRDALFCVFSYLDTKSLLRCAEVCREWRDVSRHPALWQRVC 47
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
202-344 1.21e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 68.81  E-value: 1.21e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020 202 LARLKIRALEKLEVDRRLERLSEEVEQKIAgQVGRLQAELERKAAELETARQESARLGREKEELEERASELSRQVDVSVE 281
Cdd:COG1196  231 LLKLRELEAELEELEAELEELEAELEELEA-ELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE 309
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 289803020 282 LLASLKQDLVHKEQELSRKQQEVVQIDQFLKETAAREASAKLRLQQFIEELLERADRAERQLQ 344
Cdd:COG1196  310 RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372
F-box-like pfam12937
F-box-like; This is an F-box-like family.
557-592 1.14e-07

F-box-like; This is an F-box-like family.


Pssm-ID: 463757 [Multi-domain]  Cd Length: 45  Bit Score: 48.63  E-value: 1.14e-07
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 289803020  557 LFCIFTYLDTRTLLHAAEVCRDWRFVARHPAVWTRV 592
Cdd:pfam12937   9 LLQIFSYLDPKDLLRLALVCRRWRELASDDSLWRRL 44
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
219-332 3.40e-07

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 54.26  E-value: 3.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020  219 LERLSEEVEQKI---AGQVGRLQAELERKAAELETARQESARLGREKEELEERASELSRQVDVSVELLASLKQDLVHKEQ 295
Cdd:TIGR04523 459 LDNTRESLETQLkvlSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKES 538
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 289803020  296 ELSRKQQEVVQIDQFLKETAAREasAKLRLQQFIEEL 332
Cdd:TIGR04523 539 KISDLEDELNKDDFELKKENLEK--EIDEKNKEIEEL 573
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
211-491 2.98e-06

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 50.60  E-value: 2.98e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020 211 EKLEVDRRLERLSEEVEQKIAgQVGRLQAELERKAAELETARQE----SARLGREKEELEERASE--------------- 271
Cdd:COG3883   31 ELEAAQAELDALQAELEELNE-EYNELQAELEALQAEIDKLQAEiaeaEAEIEERREELGERARAlyrsggsvsyldvll 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020 272 --------LSRQVDVS---------VELLASLKQDLVHKEQELSRKQQEVVQIDQFLKETAAREASAKLRLQQFIEELLE 334
Cdd:COG3883  110 gsesfsdfLDRLSALSkiadadadlLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSA 189
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020 335 RADRAERQLQVISSScgstpSASLGRGGGGGGAGPNARGPGRMREHHVGPAVPNTYAVSRHGSSPSTGASSRVPAASQSS 414
Cdd:COG3883  190 EEAAAEAQLAELEAE-----LAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGA 264
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 289803020 415 GCYDSDSLELPRPEEGAPEDSGPGGLGTRAQAANGGSERSQPPRSSGLRRQAIQNWQRRPRRHSTEGEEGDVSDVGS 491
Cdd:COG3883  265 AGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAASGGSGGGSGGAGGVGSGGGAGAVVGGASAGGGGGSGGGGGSS 341
PRK12705 PRK12705
hypothetical protein; Provisional
204-346 3.05e-05

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 47.40  E-value: 3.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020 204 RLKIRALEKLEVDRRLERLSEEVEQKiagqvgRLQAELERKAAELETARQESARLGREKEEL---EERASELSRQVDVSV 280
Cdd:PRK12705  24 LLKKRQRLAKEAERILQEAQKEAEEK------LEAALLEAKELLLRERNQQRQEARREREELqreEERLVQKEEQLDARA 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020 281 ELLASLKQDLVHKEQELSRKQQEVV----QIDQFLKETA------AR-------EASAKLRLQQFIEELLERAD-RAERQ 342
Cdd:PRK12705  98 EKLDNLENQLEEREKALSARELELEelekQLDNELYRVAgltpeqARklllkllDAELEEEKAQRVKKIEEEADlEAERK 177

                 ....
gi 289803020 343 LQVI 346
Cdd:PRK12705 178 AQNI 181
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
224-318 4.58e-05

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


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 44.11  E-value: 4.58e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020   224 EEVEQKIAGQVGRLQAELERKAAELETARQEsarLGREKEEL-EERASELSRQVDVSVELLASLKQDLvhkEQELSRKQQ 302
Cdd:smart00935  17 KAAQKQLEKEFKKRQAELEKLEKELQKLKEK---LQKDAATLsEAAREKKEKELQKKVQEFQRKQQKL---QQDLQKRQQ 90
                           90       100
                   ....*....|....*....|.
gi 289803020   303 EVVQ-----IDQFLKETAARE 318
Cdd:smart00935  91 EELQkildkINKAIKEVAKKK 111
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
224-318 5.68e-05

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


Pssm-ID: 461098 [Multi-domain]  Cd Length: 140  Bit Score: 43.72  E-value: 5.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020  224 EEVEQKIAGQVGRLQAELERKAAELETARQE-SARLGREKEELEERASELSRQVDVSVELLASLKQDLVHKEQELSRKQQ 302
Cdd:pfam03938  18 KAAQAQLEKKFKKRQAELEAKQKELQKLYEElQKDGALLEEEREEKEQELQKKEQELQQLQQKAQQELQKKQQELLQPIQ 97
                          90
                  ....*....|....*.
gi 289803020  303 EvvQIDQFLKETAARE 318
Cdd:pfam03938  98 D--KINKAIKEVAKEK 111
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
347-557 1.32e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 45.93  E-value: 1.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020  347 SSSCGSTPSASLGRGGGGGGAGPNARGPGRMREHHVGPAVPntyAVSRHGSSPStGASSRVPAASQSSGCYDSDSLELPR 426
Cdd:PHA03307  182 TARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAP---APGRSAADDA-GASSSDSSSSESSGCGWGPENECPL 257
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020  427 PEEG----------APEDSGPGGLGTRAQAANGGSERSQPPRSSGLRRQAIQNwqrrPRRHSTEGEEGDVSDVGSRTTES 496
Cdd:PHA03307  258 PRPApitlptriweASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPS----SPRASSSSSSSRESSSSSTSSSS 333
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 289803020  497 EAEGPLdAPRPGPAMAGPLSSCRLSARPEGGS-GRGRRAERVSPSRSNEVISPEILKMRAAL 557
Cdd:PHA03307  334 ESSRGA-AVSPGPSPSRSPSPSRPPPPADPSSpRKRPRPSRAPSSPAASAGRPTRRRARAAV 394
FBOX smart00256
A Receptor for Ubiquitination Targets;
557-589 6.02e-03

A Receptor for Ubiquitination Targets;


Pssm-ID: 197608  Cd Length: 41  Bit Score: 35.11  E-value: 6.02e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 289803020   557 LFCIFTYLDTRTLLHAAEVCRDWRFVARHPAVW 589
Cdd:smart00256   6 LEEILSKLDPKDLLRLRKVSRKWRSLIDSHDFW 38
 
Name Accession Description Interval E-value
F-box_FBXO41 cd22109
F-box domain found in F-box only protein 41 (FBXO41) and similar proteins; FBXO41, also called ...
547-593 1.59e-22

F-box domain found in F-box only protein 41 (FBXO41) and similar proteins; FBXO41, also called FBX41, is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. It acts as a novel central nervous system (CNS)-specific F-box protein that localizes to the centrosome and the cytoplasm of neurons and promotes neuronal migration. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438881  Cd Length: 47  Bit Score: 90.85  E-value: 1.59e-22
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 289803020 547 SPEILKMRAALFCIFTYLDTRTLLHAAEVCRDWRFVARHPAVWTRVL 593
Cdd:cd22109    1 SLESLRRRDALFCVFSYLDTKSLLRCAEVCREWRDVSRHPALWQRVC 47
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
202-344 1.21e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 68.81  E-value: 1.21e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020 202 LARLKIRALEKLEVDRRLERLSEEVEQKIAgQVGRLQAELERKAAELETARQESARLGREKEELEERASELSRQVDVSVE 281
Cdd:COG1196  231 LLKLRELEAELEELEAELEELEAELEELEA-ELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE 309
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 289803020 282 LLASLKQDLVHKEQELSRKQQEVVQIDQFLKETAAREASAKLRLQQFIEELLERADRAERQLQ 344
Cdd:COG1196  310 RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
199-344 3.77e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 63.80  E-value: 3.77e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020 199 EEGLARLKIRALEKLEVDRRLERLSEEVEQKIAgQVGRLQAELERKAAELETARQESARLGREKEELEERASELSRQVDV 278
Cdd:COG1196  249 EELEAELEELEAELAELEAELEELRLELEELEL-ELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAE 327
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 289803020 279 SVELLASLKQDLVHKEQELSRKQQEVVQIDQFLKETAAREASAKLRLQQFIEELLERADRAERQLQ 344
Cdd:COG1196  328 LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
204-344 4.59e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 63.42  E-value: 4.59e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020 204 RLKIRALEKLEVDRRLERL----SEEVEQKIAGQVGRLQAELERKAAELETARQESARLGREKEELEERASELSRQVDVS 279
Cdd:COG1196  291 YELLAELARLEQDIARLEErrreLEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA 370
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 289803020 280 VELLASLKQDLVHKEQELSRKQQEVVQIDQFLKETAAREASAKLRLQQFIEELLERADRAERQLQ 344
Cdd:COG1196  371 EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEE 435
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
199-349 8.33e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 62.65  E-value: 8.33e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020 199 EEGLARLKIRALEKLEVDRRLERLSEEVEQkiagqvgrLQAELERKAAELETARQESARLGREKEELEERASELSRQVDV 278
Cdd:COG1196  221 ELKELEAELLLLKLRELEAELEELEAELEE--------LEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYE 292
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 289803020 279 SVELLASLKQDLVHKEQELSRKQQEVVQIDQFLKETAAREASAKLRLQQFIEELLERADRAERQLQVISSS 349
Cdd:COG1196  293 LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
203-348 1.07e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 62.26  E-value: 1.07e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020 203 ARLKIRALEKLEVDRRLERLSEEvEQKIAGQVGRLQAELERKAAELETARQESARLGREKEELEERASELSRQVDVSVEL 282
Cdd:COG1196  267 AELEELRLELEELELELEEAQAE-EYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEE 345
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 289803020 283 LASLKQDLVHKEQELSRKQQEVVQIDQFLKETAAREASAKLRLQQFIEELLERADRAERQLQVISS 348
Cdd:COG1196  346 LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEA 411
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
203-344 1.07e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 62.26  E-value: 1.07e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020 203 ARLKIRALEKLEVDRRLERLSEEvEQKIAGQVGRLQAELERKAAELETARQESARLGREKEELEERASELSRQVDVSVEL 282
Cdd:COG1196  302 QDIARLEERRRELEERLEELEEE-LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 289803020 283 LASLKQDLVHKEQELSRKQQEVVQID---QFLKETAAREASAKLRLQQFIEELLERADRAERQLQ 344
Cdd:COG1196  381 LEELAEELLEALRAAAELAAQLEELEeaeEALLERLERLEEELEELEEALAELEEEEEEEEEALE 445
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
197-344 1.27e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 62.26  E-value: 1.27e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020 197 AYEEGLARLKIRALEKLEVDRRLERLSEEVEQKIAG------QVGRLQAELERKAAELETARQESARLGREKEELEERAS 270
Cdd:COG1196  233 KLRELEAELEELEAELEELEAELEELEAELAELEAEleelrlELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 289803020 271 ELSRQVDVSVELLASLKQDLVHKEQELSRKQQEVVQIDQFLKETAAREASAKLRLQQFIEELLERADRAERQLQ 344
Cdd:COG1196  313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE 386
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
203-344 1.33e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 62.26  E-value: 1.33e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020 203 ARLKIRALEkLEVDRRLERLSEEVEQ--KIAGQVGRLQAELERKAAELETARQESARLGREKEELEERASELSRQVDVSV 280
Cdd:COG1196  272 LRLELEELE-LELEEAQAEEYELLAElaRLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAE 350
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 289803020 281 ELLASLKQDLVHKEQELSRKQQEVVQIDQFLKETAAREASAKLRLQQFIEELLERADRAERQLQ 344
Cdd:COG1196  351 EELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE 414
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
211-346 1.11e-08

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 57.99  E-value: 1.11e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020 211 EKLEVDRRLERLSEEVEQKIAgQVGRLQAELERKAAELETARQESARLGREKEELEERASELSRQVDVSVELLASLKQDL 290
Cdd:COG4372   74 ELEQLEEELEELNEQLQAAQA-ELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEEL 152
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 289803020 291 VHKEQELSRKQQEVVQIDQFLKETAAREASAKlrlqqfIEELLERADRAERQLQVI 346
Cdd:COG4372  153 KELEEQLESLQEELAALEQELQALSEAEAEQA------LDELLKEANRNAEKEEEL 202
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
199-344 1.93e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 58.41  E-value: 1.93e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020 199 EEGLARLKIRALEKLEVDRRLERLSEEVEQKIAGQVGRLQAELERKAAELETARQESARLGREKEELEERASELSR---Q 275
Cdd:COG1196  273 RLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEaeeE 352
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 289803020 276 VDVSVELLASLKQDLVHKEQELSRKQQEVVQIDQFLKETAAREASAKLRLQQFIEELLERADRAERQLQ 344
Cdd:COG1196  353 LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
202-346 3.97e-08

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 56.45  E-value: 3.97e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020 202 LARLKIRALEKLEVDRRLERLSEEVEQ--KIAGQVGRLQAELERKAAELETARQESARLGREKEELEERASELSRQVDVS 279
Cdd:COG4372   13 LSLFGLRPKTGILIAALSEQLRKALFEldKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAA 92
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020 280 VELLASLKQDLVHKEQELSRKQQEVVQID---QFLKETAAREASAKLRLQQFIEELLERADRAERQLQVI 346
Cdd:COG4372   93 QAELAQAQEELESLQEEAEELQEELEELQkerQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESL 162
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
218-346 4.70e-08

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 56.06  E-value: 4.70e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020 218 RLERLSEEVEQkIAGQVGRLQAELERKAAELETARQESARLGREKEELEERASELSRQVDVSVELLASLKQDLVHKEQEL 297
Cdd:COG4372   39 ELDKLQEELEQ-LREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEEL 117
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 289803020 298 SRKQQEVVQIDQFLKETAAREASAKLRL---QQFIEELLERADRAERQLQVI 346
Cdd:COG4372  118 EELQKERQDLEQQRKQLEAQIAELQSEIaerEEELKELEEQLESLQEELAAL 169
F-box-like pfam12937
F-box-like; This is an F-box-like family.
557-592 1.14e-07

F-box-like; This is an F-box-like family.


Pssm-ID: 463757 [Multi-domain]  Cd Length: 45  Bit Score: 48.63  E-value: 1.14e-07
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 289803020  557 LFCIFTYLDTRTLLHAAEVCRDWRFVARHPAVWTRV 592
Cdd:pfam12937   9 LLQIFSYLDPKDLLRLALVCRRWRELASDDSLWRRL 44
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
199-347 1.45e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 55.16  E-value: 1.45e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020 199 EEGLARLKIRALEKLEVDRRLERLSEEVEQKIAGQVGRLQaELERKAAELETARQESARLGREKEELEERASELSRQVDV 278
Cdd:COG4717  110 ELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLE-ELEERLEELRELEEELEELEAELAELQEELEELLEQLSL 188
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020 279 SVEL-LASLKQDLVHKEQELSRKQQEVVQIDQFLKEtaAREASAKLRLQQFIEELLERADRAERQLQVIS 347
Cdd:COG4717  189 ATEEeLQDLAEELEELQQRLAELEEELEEAQEELEE--LEEELEQLENELEAAALEERLKEARLLLLIAA 256
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
203-344 1.69e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 55.31  E-value: 1.69e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020  203 ARLKIRALEKL-EVDRRLERLSEEVEQKIAGqvgRLQAELERKAAELETARQESARLGREKEELEERASELSRQVD---- 277
Cdd:COG4913   247 AREQIELLEPIrELAERYAAARERLAELEYL---RAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDalre 323
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020  278 -----------VSVELLASLKQDLVHKEQELSRKQQEVVQIDQF---LKETAAREASAKLRLQQFIEELLERADRAERQL 343
Cdd:COG4913   324 eldeleaqirgNGGDRLEQLEREIERLERELEERERRRARLEALlaaLGLPLPASAEEFAALRAEAAALLEALEEELEAL 403

                  .
gi 289803020  344 Q 344
Cdd:COG4913   404 E 404
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
197-346 2.07e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.94  E-value: 2.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020 197 AYEEGLARLKIRALEKLEVDRRLERLSEEVEQKIAGQVgRLQAELERKAAELETARQESARLGREKEELEERASELSrqv 276
Cdd:COG1196  359 ELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA-ELAAQLEELEEAEEALLERLERLEEELEELEEALAELE--- 434
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020 277 dvsvELLASLKQDLVHKEQELSRKQQEVVQIDQFLKETAAREASAKLRLQQFIEELLERADRAERQLQVI 346
Cdd:COG1196  435 ----EEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAE 500
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
206-349 2.58e-07

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 52.62  E-value: 2.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020 206 KIRALEKL-EVDRRLERLsEEVEQKIAGQVGRLQAELERKAAELETARQESARLGREKEELEERASELSRQVDVS----- 279
Cdd:COG1579    5 DLRALLDLqELDSELDRL-EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYeeqlg 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020 280 --------------VELLASLKQDLVHKEQEL----SRKQQEVVQIDQFLKETAAREASAKLRLQQFIEELLERADRAER 341
Cdd:COG1579   84 nvrnnkeyealqkeIESLKRRISDLEDEILELmeriEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEA 163

                 ....*...
gi 289803020 342 QLQVISSS 349
Cdd:COG1579  164 EREELAAK 171
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
198-344 2.89e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 54.54  E-value: 2.89e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020  198 YEEGLARLKIRALEKLEVDRRLERLSEEVEQkIAGQVGRLQAELERKAAELETAR--------QESARLGREKEELEERA 269
Cdd:COG4913   276 YLRAALRLWFAQRRLELLEAELEELRAELAR-LEAELERLEARLDALREELDELEaqirgnggDRLEQLEREIERLEREL 354
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 289803020  270 SELSRQVDVSVELLASLKQDLVHKEQELSRKQQEVVQIDQFLKETAAREASAKLRLQQFIEELLERADRAERQLQ 344
Cdd:COG4913   355 EERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIA 429
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
219-332 3.40e-07

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 54.26  E-value: 3.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020  219 LERLSEEVEQKI---AGQVGRLQAELERKAAELETARQESARLGREKEELEERASELSRQVDVSVELLASLKQDLVHKEQ 295
Cdd:TIGR04523 459 LDNTRESLETQLkvlSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKES 538
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 289803020  296 ELSRKQQEVVQIDQFLKETAAREasAKLRLQQFIEEL 332
Cdd:TIGR04523 539 KISDLEDELNKDDFELKKENLEK--EIDEKNKEIEEL 573
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
197-348 3.78e-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: 3.78e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020   197 AYEEGLARLKiraLEKLEVDRRLERLSEEVEQkIAGQVGRLQAELERKAAELETARQESARLGREKEELEERASELSRQV 276
Cdd:TIGR02168  264 ELEEKLEELR---LEVSELEEEIEELQKELYA-LANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEEL 339
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020   277 DVSVELLASLKQDLVHKEQELSRKQQEVVQIDQFLKE-----TAAREASAKLRLQ--------QFIEELLER-ADRAERQ 342
Cdd:TIGR02168  340 AELEEKLEELKEELESLEAELEELEAELEELESRLEEleeqlETLRSKVAQLELQiaslnneiERLEARLERlEDRRERL 419

                   ....*.
gi 289803020   343 LQVISS 348
Cdd:TIGR02168  420 QQEIEE 425
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
213-324 3.94e-07

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: 53.23  E-value: 3.94e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020 213 LEVDRRLERLSEEVE--QKIAGQVGRLQAELERKAAELETARQESARLgreKEELEERASELSRQVDVSVELLASLKQDL 290
Cdd:COG4942  132 LDAVRRLQYLKYLAParREQAEELRADLAELAALRAELEAERAELEAL---LAELEEERAALEALKAERQKLLARLEKEL 208
                         90       100       110
                 ....*....|....*....|....*....|....
gi 289803020 291 VHKEQELSRKQQEVVQIDQFLKETAAREASAKLR 324
Cdd:COG4942  209 AELAAELAELQQEAEELEALIARLEAEAAAAAER 242
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
197-338 4.60e-07

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 51.85  E-value: 4.60e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020 197 AYEEGLARLKIrALEKLEVD-RRLERLSEEVEQKIAgqvgRLQAELE--RKAAELETARQESARLGREKEELEERASELS 273
Cdd:COG1579   42 ALEARLEAAKT-ELEDLEKEiKRLELEIEEVEARIK----KYEEQLGnvRNNKEYEALQKEIESLKRRISDLEDEILELM 116
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 289803020 274 RQVDVSVELLASLKQDLVHKEQELSRKQQEvvqIDQFLKETAAREASAKLRLQQFI----EELLERADR 338
Cdd:COG1579  117 ERIEELEEELAELEAELAELEAELEEKKAE---LDEELAELEAELEELEAEREELAakipPELLALYER 182
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
204-346 7.63e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 52.85  E-value: 7.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020 204 RLKIRALEKLEVDRRLERLSEEVEQKIAGQVGRLQAELERKAAELETARQESARLGR---------EKEELEERASELSR 274
Cdd:COG4717   67 ELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKllqllplyqELEALEAELAELPE 146
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 289803020 275 QVDV---SVELLASLKQDLVHKEQELSRKQQEVVQIDQFLKETAAREASaklRLQQFIEELLERADRAERQLQVI 346
Cdd:COG4717  147 RLEEleeRLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQ---DLAEELEELQQRLAELEEELEEA 218
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
213-348 8.76e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 53.14  E-value: 8.76e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020   213 LEVDRRLERLSEEVEQkIAGQVGRLQAELERKAAELETARQESARLGREKEELEERASELSRQVDVSVELLASLKQDLVH 292
Cdd:TIGR02168  673 LERRREIEELEEKIEE-LEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQ 751
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 289803020   293 KEQELSRKQQEVVQIDQFLKEtaarEASAKLRLQQFIEELLERADRAERQLQVISS 348
Cdd:TIGR02168  752 LSKELTELEAEIEELEERLEE----AEEELAEAEAEIEELEAQIEQLKEELKALRE 803
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
199-344 1.10e-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: 52.75  E-value: 1.10e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020   199 EEGLARLK-IRAleklEVDRRLERLSEEVEQkiAGQVGRLQAEL------------ERKAAELETARQESARLGREKEEL 265
Cdd:TIGR02168  185 RENLDRLEdILN----ELERQLKSLERQAEK--AERYKELKAELrelelallvlrlEELREELEELQEELKEAEEELEEL 258
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 289803020   266 EERASELSRQVDVSVELLASLKQDLVHKEQELSRKQQEVVQIDQFLKETAAREAsaklRLQQFIEELLERADRAERQLQ 344
Cdd:TIGR02168  259 TAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLA----NLERQLEELEAQLEELESKLD 333
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
199-347 1.25e-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: 52.37  E-value: 1.25e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020   199 EEGLARLKIRALEKLEVDRRLERLSEEVEQKIAG---QVGRLQAELERKAAELETARQESARLGREKEELEERASELSRQ 275
Cdd:TIGR02168  732 RKDLARLEAEVEQLEERIAQLSKELTELEAEIEEleeRLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAE 811
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 289803020   276 VDVSVELLASLKQDLVHKEQELSRKQQEVVQIDQFLKETAAREASAKLRlqqfIEELLERADRAERQLQVIS 347
Cdd:TIGR02168  812 LTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAE----IEELEELIEELESELEALL 879
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
211-343 1.59e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.98  E-value: 1.59e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020   211 EKLEVDRRLERLSEEVEQkIAGQVGRLQAELERKAAELETARQESARLGREKEELEERASELSRQVDVSVELLASLKQDL 290
Cdd:TIGR02168  324 QLEELESKLDELAEELAE-LEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEI 402
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 289803020   291 VHKEQELS-------RKQQEVVQIDQFLKETAAREASAKL-RLQQFIEELLERADRAERQL 343
Cdd:TIGR02168  403 ERLEARLErledrreRLQQEIEELLKKLEEAELKELQAELeELEEELEELQEELERLEEAL 463
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
204-344 1.72e-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: 51.99  E-value: 1.72e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020   204 RLKIRALEK--LEVDRRLERLSEEVEQKiAGQVGRLQAELERKAAELETARQESARLGREKEELEERASELSRQVDVSVE 281
Cdd:TIGR02169  335 LAEIEELEReiEEERKRRDKLTEEYAEL-KEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQE 413
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 289803020   282 LLASLKQDLVHKEQELSRKQQEVVQIDQFLKETAAREASAKLRLQQfIEELLERADRAERQLQ 344
Cdd:TIGR02169  414 ELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQ-LAADLSKYEQELYDLK 475
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
211-491 2.98e-06

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 50.60  E-value: 2.98e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020 211 EKLEVDRRLERLSEEVEQKIAgQVGRLQAELERKAAELETARQE----SARLGREKEELEERASE--------------- 271
Cdd:COG3883   31 ELEAAQAELDALQAELEELNE-EYNELQAELEALQAEIDKLQAEiaeaEAEIEERREELGERARAlyrsggsvsyldvll 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020 272 --------LSRQVDVS---------VELLASLKQDLVHKEQELSRKQQEVVQIDQFLKETAAREASAKLRLQQFIEELLE 334
Cdd:COG3883  110 gsesfsdfLDRLSALSkiadadadlLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSA 189
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020 335 RADRAERQLQVISSScgstpSASLGRGGGGGGAGPNARGPGRMREHHVGPAVPNTYAVSRHGSSPSTGASSRVPAASQSS 414
Cdd:COG3883  190 EEAAAEAQLAELEAE-----LAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGA 264
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 289803020 415 GCYDSDSLELPRPEEGAPEDSGPGGLGTRAQAANGGSERSQPPRSSGLRRQAIQNWQRRPRRHSTEGEEGDVSDVGS 491
Cdd:COG3883  265 AGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAASGGSGGGSGGAGGVGSGGGAGAVVGGASAGGGGGSGGGGGSS 341
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
211-331 3.10e-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: 51.22  E-value: 3.10e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020   211 EKLEVDRRLERLSEEVEQkIAGQVGRLQAELERKAAELETARQESARLGREKEELEERASELSRQVDVSVELLASLKQDL 290
Cdd:TIGR02169  386 ELKDYREKLEKLKREINE-LKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADL 464
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 289803020   291 VHKEQELSRKQQEVVQIDQFLKEtAAREASAKLRLQQFIEE 331
Cdd:TIGR02169  465 SKYEQELYDLKEEYDRVEKELSK-LQRELAEAEAQARASEE 504
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
199-344 3.58e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.09  E-value: 3.58e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020 199 EEGLARLKIRALEKLEVDRRLERLSEEVEQKIAGQVGRLQAELERKAAELETARQESARLGREKEELEERASELSRQVDV 278
Cdd:COG1196  633 EAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEA 712
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 289803020 279 SVELLASLKQDLVHKEQELSRKQQEVVQIDQFLKETAAREASAKLRLQQfIEELLERADRAERQLQ 344
Cdd:COG1196  713 EEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPD-LEELERELERLEREIE 777
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
199-346 9.49e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 49.53  E-value: 9.49e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020  199 EEGLARL--KIRALEKL--EVDRRLERLSEEVEQKIAGQVGRLQAELERKAAELETARQESARLGR-----------EKE 263
Cdd:COG4913   301 RAELARLeaELERLEARldALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEAllaalglplpaSAE 380
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020  264 ELEERASELSRQVDVSVELLASLKQDLVHKEQELSRKQQEVVQIDQFLKETAAREASAKLRLQQFIEELLERADRAERQL 343
Cdd:COG4913   381 EFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLDEAEL 460

                  ...
gi 289803020  344 QVI 346
Cdd:COG4913   461 PFV 463
F-box_FBXL14 cd22125
F-box domain found in F-box/LRR-repeat protein 14 (FBXL14) and similar proteins; FBXL14, also ...
548-589 1.12e-05

F-box domain found in F-box/LRR-repeat protein 14 (FBXL14) and similar proteins; FBXL14, also called F-box and leucine-rich repeat protein 14, is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin-protein ligase complex, which acts by mediating ubiquitination and subsequent degradation of SNAIL1. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438897  Cd Length: 41  Bit Score: 43.23  E-value: 1.12e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 289803020 548 PEILKMraalfcIFTYLDTRTLLHAAEVCRDWRFVARHPAVW 589
Cdd:cd22125    5 PEILAM------IFSYLDVRDKGRAAQVCTAWRDAAYHKSVW 40
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
204-345 1.35e-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: 48.91  E-value: 1.35e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020   204 RLKIRALEKLE-VDRRLERLSEEVEQKIAgQVGRLQAELERK------------------AAELETARQESARLGREKEE 264
Cdd:TIGR02169  170 RKKEKALEELEeVEENIERLDLIIDEKRQ-QLERLRREREKAeryqallkekreyegyelLKEKEALERQKEAIERQLAS 248
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020   265 LEERASELSRQVDVSVELLASLKQDLVHKEQELSRK-QQEVVQIDQFLKETAAREASAKlRLQQFIEELLERADRAERQL 343
Cdd:TIGR02169  249 LEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLE-RSIAEKERELEDAEERLAKL 327

                   ..
gi 289803020   344 QV 345
Cdd:TIGR02169  328 EA 329
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
209-494 1.38e-05

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 48.29  E-value: 1.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020 209 ALEKL-EVDRRLERLSEEVEQkIAGQVGRLQAELERKAAELETARQESARLgreKEELEERASE---------------- 271
Cdd:COG3883   35 AQAELdALQAELEELNEEYNE-LQAELEALQAEIDKLQAEIAEAEAEIEER---REELGERARAlyrsggsvsyldvllg 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020 272 -------LSRQVDVSV----------------ELLASLKQDLVHKEQELSRKQQEVVQIDQFLKETAAREASAKLRLQQF 328
Cdd:COG3883  111 sesfsdfLDRLSALSKiadadadlleelkadkAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAE 190
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020 329 IEELLERADRAERQLQVISSSCGSTPSASlgRGGGGGGAGPNARGPGRMREHHVGPAVPNTYAVSRHGSSPSTGASSRVP 408
Cdd:COG3883  191 EAAAEAQLAELEAELAAAEAAAAAAAAAA--AAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAA 268
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020 409 AASQSSGcyDSDSLELPRPEEGAPEDSGPGGLGTRAQAANGGSERSQPPRSSGLRRQAIQNWQRRPRRHSTEGEEGDVSD 488
Cdd:COG3883  269 AGAAGAG--AAAASAAGGGAGGAGGGGGGGGAASGGSGGGSGGAGGVGSGGGAGAVVGGASAGGGGGSGGGGGSSGGGSG 346

                 ....*.
gi 289803020 489 VGSRTT 494
Cdd:COG3883  347 GGGGGG 352
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
196-326 1.59e-05

Phage shock protein A [Transcription, Signal transduction mechanisms];


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 46.74  E-value: 1.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020 196 VAYEEGLARLKirALEKlevdrRLERLSEEVEQKIAgqvgrlqaELERKAAE-LETARQESARLG-REKEELEERASELS 273
Cdd:COG1842   40 VEARQALAQVI--ANQK-----RLERQLEELEAEAE--------KWEEKARLaLEKGREDLAREAlERKAELEAQAEALE 104
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 289803020 274 RQVDVSVELLASLKQDLVHKEQELSRKQQEvvqidqfLKETAAREASAKLRLQ 326
Cdd:COG1842  105 AQLAQLEEQVEKLKEALRQLESKLEELKAK-------KDTLKARAKAAKAQEK 150
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
203-343 1.63e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 48.76  E-value: 1.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020  203 ARLKIRALEK-LEVDRRLERLSEEvEQKIAGQVGRLqAELERKAAELETARQESARLGREKEELEERASELSRQVDVSVE 281
Cdd:COG4913   636 LEAELDALQErREALQRLAEYSWD-EIDVASAEREI-AELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKG 713
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 289803020  282 LLASLKQDLVHKEQELSRKQQEVVQI------------DQFLKETAAREASAKLR--LQQFIEELLERADRAERQL 343
Cdd:COG4913   714 EIGRLEKELEQAEEELDELQDRLEAAedlarlelrallEERFAAALGDAVERELRenLEERIDALRARLNRAEEEL 789
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
199-343 1.76e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.78  E-value: 1.76e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020 199 EEGLARLKIRALEKLEVDRRLERLSEEVEQKIAGQVGRLQAELERKAAELETARQESARLGREKEELEERASELSRQVDV 278
Cdd:COG1196  409 EEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAE 488
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 289803020 279 SVELLASLKQDL------------VHKEQELSRKQQEVVQIDQFLKE-TAAREASAKLRLQQFIEELLERADRAERQL 343
Cdd:COG1196  489 AAARLLLLLEAEadyegflegvkaALLLAGLRGLAGAVAVLIGVEAAyEAALEAALAAALQNIVVEDDEVAAAAIEYL 566
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
208-344 1.92e-05

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 47.60  E-value: 1.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020 208 RALEKLEvdRRLER--LSEEVEQKIAGQVGRLQAELERKAAELE------TARQESARLGREKEELEERASELSRQVDVS 279
Cdd:COG1340  116 KEIERLE--WRQQTevLSPEEEKELVEKIKELEKELEKAKKALEkneklkELRAELKELRKEAEEIHKKIKELAEEAQEL 193
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020 280 VELLASLKQ---------DLVHKE------------QELSRKQQEVVQIDQFLKETAAREASAKLRLQQfiEELLERADR 338
Cdd:COG1340  194 HEEMIELYKeadelrkeaDELHKEiveaqekadelhEEIIELQKELRELRKELKKLRKKQRALKREKEK--EELEEKAEE 271

                 ....*.
gi 289803020 339 AERQLQ 344
Cdd:COG1340  272 IFEKLK 277
PRK12705 PRK12705
hypothetical protein; Provisional
204-346 3.05e-05

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 47.40  E-value: 3.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020 204 RLKIRALEKLEVDRRLERLSEEVEQKiagqvgRLQAELERKAAELETARQESARLGREKEEL---EERASELSRQVDVSV 280
Cdd:PRK12705  24 LLKKRQRLAKEAERILQEAQKEAEEK------LEAALLEAKELLLRERNQQRQEARREREELqreEERLVQKEEQLDARA 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020 281 ELLASLKQDLVHKEQELSRKQQEVV----QIDQFLKETA------AR-------EASAKLRLQQFIEELLERAD-RAERQ 342
Cdd:PRK12705  98 EKLDNLENQLEEREKALSARELELEelekQLDNELYRVAgltpeqARklllkllDAELEEEKAQRVKKIEEEADlEAERK 177

                 ....
gi 289803020 343 LQVI 346
Cdd:PRK12705 178 AQNI 181
F-box_FBXO33 cd22104
F-box domain found in F-box only protein 33 (FBXO33) and similar proteins; FBXO33, also called ...
556-595 3.52e-05

F-box domain found in F-box only protein 33 (FBXO33) and similar proteins; FBXO33, also called FBX33, is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. It exerts similar functions as F-box involved in polyQ pathogenesis (FipoQ) in modulating the ubiquitination and solubility of expanded SCA3-polyQ proteins. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438876  Cd Length: 48  Bit Score: 41.86  E-value: 3.52e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 289803020 556 ALFCIFTYLDTRTLLHAAEVCRDWRFVARHPAVWTRVLLE 595
Cdd:cd22104    8 VLVHIFSYLPPRDRLRASSTCRRWREALFHPSLWRSLRLH 47
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
227-358 3.79e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.60  E-value: 3.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020  227 EQKIAgqvgRLQAELERKAAELETARQESARLGREKEELEERASELSRQVDVSVELL--ASLKQDLVHKEQELSR---KQ 301
Cdd:COG4913   609 RAKLA----ALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIdvASAEREIAELEAELERldaSS 684
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 289803020  302 QEVVQIDQFLKE-----TAAREASAKL-----RLQQFIEELLERADRAERQLQVISSSCGSTPSASL 358
Cdd:COG4913   685 DDLAALEEQLEEleaelEELEEELDELkgeigRLEKELEQAEEELDELQDRLEAAEDLARLELRALL 751
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
224-318 4.58e-05

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


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 44.11  E-value: 4.58e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020   224 EEVEQKIAGQVGRLQAELERKAAELETARQEsarLGREKEEL-EERASELSRQVDVSVELLASLKQDLvhkEQELSRKQQ 302
Cdd:smart00935  17 KAAQKQLEKEFKKRQAELEKLEKELQKLKEK---LQKDAATLsEAAREKKEKELQKKVQEFQRKQQKL---QQDLQKRQQ 90
                           90       100
                   ....*....|....*....|.
gi 289803020   303 EVVQ-----IDQFLKETAARE 318
Cdd:smart00935  91 EELQkildkINKAIKEVAKKK 111
HlpA COG2825
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ...
224-339 4.75e-05

Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442073 [Multi-domain]  Cd Length: 171  Bit Score: 44.83  E-value: 4.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020 224 EEVEQKIAGQVGRLQAELERKAAELETarqesarlgrEKEELEERASELSRqvdvsvELLASLKQDLVHKEQELSRKQQE 303
Cdd:COG2825   42 KAAQKKLEKEFKKRQAELQKLEKELQA----------LQEKLQKEAATLSE------EERQKKERELQKKQQELQRKQQE 105
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 289803020 304 vvqidqflketaaREASAKLRLQQFIEELLERADRA 339
Cdd:COG2825  106 -------------AQQDLQKRQQELLQPILEKIQKA 128
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
223-344 4.87e-05

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 47.13  E-value: 4.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020 223 SEEVEQKIAGqVGRLQAELERKAAELETARQESARLgreKEELEERASELSRQvdvsvellaslkqdlvhKEQELSRKQQ 302
Cdd:PRK00409 515 KEKLNELIAS-LEELERELEQKAEEAEALLKEAEKL---KEELEEKKEKLQEE-----------------EDKLLEEAEK 573
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 289803020 303 EVVQIDQFLKETAAREASAKLRLQQfieelLERADRAERQLQ 344
Cdd:PRK00409 574 EAQQAIKEAKKEADEIIKELRQLQK-----GGYASVKAHELI 610
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
204-333 5.45e-05

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 47.25  E-value: 5.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020  204 RLKIRALEK-LEVDRRLERLSEEVEQKIAGQV----------GRLQAELERKAAELETARQESARLGREKEELEERASEL 272
Cdd:COG3096   518 RAQLAELEQrLRQQQNAERLLEEFCQRIGQQLdaaeeleellAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKEL 597
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 289803020  273 SRQVDVSVELLASLKQDLVHKEQELSRKQqevvQIDQFLKETAARE----------ASAKLRLQQFIEELL 333
Cdd:COG3096   598 AARAPAWLAAQDALERLREQSGEALADSQ----EVTAAMQQLLEREreatverdelAARKQALESQIERLS 664
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
224-318 5.68e-05

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


Pssm-ID: 461098 [Multi-domain]  Cd Length: 140  Bit Score: 43.72  E-value: 5.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020  224 EEVEQKIAGQVGRLQAELERKAAELETARQE-SARLGREKEELEERASELSRQVDVSVELLASLKQDLVHKEQELSRKQQ 302
Cdd:pfam03938  18 KAAQAQLEKKFKKRQAELEAKQKELQKLYEElQKDGALLEEEREEKEQELQKKEQELQQLQQKAQQELQKKQQELLQPIQ 97
                          90
                  ....*....|....*.
gi 289803020  303 EvvQIDQFLKETAARE 318
Cdd:pfam03938  98 D--KINKAIKEVAKEK 111
flagell_FliJ TIGR02473
flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly ...
218-350 6.31e-05

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


Pssm-ID: 131526 [Multi-domain]  Cd Length: 141  Bit Score: 43.84  E-value: 6.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020  218 RLERLSEEVEQKIAGQVGRLQAELERKAAELEtarqesaRLGREKEELEERASELSRQVDVSVEL------LASLKQDLV 291
Cdd:TIGR02473   6 KLLDLREKEEEQAKLELAKAQAEFERLETQLQ-------QLIKYREEYEQQALEKVGAGTSALELsnyqrfIRQLDQRIQ 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020  292 HKEQELSRKQQEVVQI-DQFLKETAAREASAKLRLQQFIEELLERADRAERQLQVISSSC 350
Cdd:TIGR02473  79 QQQQELALLQQEVEAKrERLLEARRELKALEKLKEKKQKEYRAEEAKREQKEMDELATQR 138
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
238-325 6.40e-05

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 46.87  E-value: 6.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020  238 QAELERKAAELETARQESARLGREKEELEERASELSRQVDVSVELLASLKQDLVHKEQELSRKQQEVVQIDQFLKE---T 314
Cdd:PRK11448  141 ENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQERKQkrkE 220
                          90
                  ....*....|.
gi 289803020  315 AAREASAKLRL 325
Cdd:PRK11448  221 ITDQAAKRLEL 231
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
204-344 7.83e-05

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 46.39  E-value: 7.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020 204 RLKIRALEKLEVDRRLERLSEEVEQKIAGQVGRLQAELERkaaELETARQESARLGREKEELEERASELSRQvdvsvelL 283
Cdd:COG2433  367 EVKARVIRGLSIEEALEELIEKELPEEEPEAEREKEHEER---ELTEEEEEIRRLEEQVERLEAEVEELEAE-------L 436
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 289803020 284 ASLKQDLVHKEQELSRKQQEVVQIDQFLKETAAREASAKlRLQQFIEELLERADRAERQLQ 344
Cdd:COG2433  437 EEKDERIERLERELSEARSEERREIRKDREISRLDREIE-RLERELEEERERIEELKRKLE 496
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
204-334 8.02e-05

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 46.55  E-value: 8.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020  204 RLKIRALEKLEVDRRLERLSEEVEqKIAGQVgrlqAELERKAAELETARQEsarLGREKEELEERASELSRQVDVSVELL 283
Cdd:TIGR04523 413 QIKKLQQEKELLEKEIERLKETII-KNNSEI----KDLTNQDSVKELIIKN---LDNTRESLETQLKVLSRSINKIKQNL 484
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 289803020  284 ASLKQDLVHKEQELSRKQQEVVQIDQFLKETAAREASAKLRLQQFIEELLE 334
Cdd:TIGR04523 485 EQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKE 535
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
199-343 8.42e-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: 46.60  E-value: 8.42e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020   199 EEGLARLKIRALEKLEVDRRLERLSEEVEQKIAgQVGRLQAELERKAAELetARQESARLGREKEELEERASELSRQVDV 278
Cdd:TIGR02169  740 EELEEDLSSLEQEIENVKSELKELEARIEELEE-DLHKLEEALNDLEARL--SHSRIPEIQAELSKLEEEVSRIEARLRE 816
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 289803020   279 SVELLASLKQDLVHKEQELSRKQQEVVQIDQFLKETAAREASAKLRLQQFIEElLERADRAERQL 343
Cdd:TIGR02169  817 IEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEE-LEELEAALRDL 880
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
207-342 8.47e-05

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 46.02  E-value: 8.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020 207 IRALEKLEVDRRLERlsEEVEQKiaGQVGRLQAELERKAAELETARQ-ESARLGREKEELEERASELSRQVDVsvellAS 285
Cdd:COG2268  191 RRKIAEIIRDARIAE--AEAERE--TEIAIAQANREAEEAELEQEREiETARIAEAEAELAKKKAEERREAET-----AR 261
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020 286 LKQDLVHKEQElSRKQQEV---VQIDQFLKETAAREASAKLRLQQFIEELLERADrAERQ 342
Cdd:COG2268  262 AEAEAAYEIAE-ANAEREVqrqLEIAEREREIELQEKEAEREEAELEADVRKPAE-AEKQ 319
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
201-341 9.24e-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: 46.21  E-value: 9.24e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020   201 GLARLKIRALEKLEVDRRLERLSEEVEQkiagqvgrLQAELERKAAELETARQESARLGREKEELEERASELSRQVDVSV 280
Cdd:TIGR02169  658 GSRAPRGGILFSRSEPAELQRLRERLEG--------LKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLE 729
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 289803020   281 ELLASLKQDLVHKEQELSRKQQEVVQIDQFLKETAAREASAKLRLQQFIEEL--LERADRAER 341
Cdd:TIGR02169  730 QEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALndLEARLSHSR 792
F-box_FBXW5 cd22132
F-box domain found in F-box/WD repeat-containing protein 5 (FBXW5) and similar proteins; FBXW5, ...
557-593 9.99e-05

F-box domain found in F-box/WD repeat-containing protein 5 (FBXW5) and similar proteins; FBXW5, also called F-box and WD-40 domain-containing protein 5, is the substrate-recognition component of both SCF (SKP1-CUL1-F-box protein) and DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438904 [Multi-domain]  Cd Length: 46  Bit Score: 40.29  E-value: 9.99e-05
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 289803020 557 LFCIFTYLDTRTLLHAAEVCRDWRFVARHPAVWTRVL 593
Cdd:cd22132    9 LLHIFSYLSPKDLLAAGQVCKQWYRVSRDEFLWKELF 45
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
214-344 1.19e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 45.83  E-value: 1.19e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020   214 EVDRRLERLSEEVEQkIAGQVGRLQAELERKAAELEtarqesaRLGREKEELEERASELSRQVDVSVELLASLKQDLVHK 293
Cdd:TIGR02169  167 EFDRKKEKALEELEE-VEENIERLDLIIDEKRQQLE-------RLRREREKAERYQALLKEKREYEGYELLKEKEALERQ 238
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 289803020   294 ----EQELSRKQQEVVQIDQFLKETAAREASAKLRLQQFIEELLERADRAERQLQ 344
Cdd:TIGR02169  239 keaiERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVK 293
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
204-349 1.21e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 45.28  E-value: 1.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020 204 RLKIRALEKLEVDRRLERLSEEVEQKIAGQVGRLQAELERKAAELETARQESARLGREKEELEERASELSRQVDVSVELL 283
Cdd:COG4372    3 RLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL 82
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 289803020 284 ASLKQDLVHKEQELSRKQQEVVQIDQFLKETAAREAsaklRLQQFIEELLERADRAERQLQVISSS 349
Cdd:COG4372   83 EELNEQLQAAQAELAQAQEELESLQEEAEELQEELE----ELQKERQDLEQQRKQLEAQIAELQSE 144
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
203-344 1.26e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.82  E-value: 1.26e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020   203 ARLKIRALEKLEVDRRLERLSEEVEQ------KIAGQVGRLQAELERK--------------AAELETARQESARLGREK 262
Cdd:TIGR02168  225 LELALLVLRLEELREELEELQEELKEaeeeleELTAELQELEEKLEELrlevseleeeieelQKELYALANEISRLEQQK 304
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020   263 EELEERASELSRQVDVSVELLASLKQDLVHKEQELSRKQQEVVQIDQFLKETAAREASAKLRLQQF------IEELLERA 336
Cdd:TIGR02168  305 QILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELesrleeLEEQLETL 384

                   ....*...
gi 289803020   337 DRAERQLQ 344
Cdd:TIGR02168  385 RSKVAQLE 392
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
347-557 1.32e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 45.93  E-value: 1.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020  347 SSSCGSTPSASLGRGGGGGGAGPNARGPGRMREHHVGPAVPntyAVSRHGSSPStGASSRVPAASQSSGCYDSDSLELPR 426
Cdd:PHA03307  182 TARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAP---APGRSAADDA-GASSSDSSSSESSGCGWGPENECPL 257
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020  427 PEEG----------APEDSGPGGLGTRAQAANGGSERSQPPRSSGLRRQAIQNwqrrPRRHSTEGEEGDVSDVGSRTTES 496
Cdd:PHA03307  258 PRPApitlptriweASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPS----SPRASSSSSSSRESSSSSTSSSS 333
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 289803020  497 EAEGPLdAPRPGPAMAGPLSSCRLSARPEGGS-GRGRRAERVSPSRSNEVISPEILKMRAAL 557
Cdd:PHA03307  334 ESSRGA-AVSPGPSPSRSPSPSRPPPPADPSSpRKRPRPSRAPSSPAASAGRPTRRRARAAV 394
F-box_FBXL13 cd22124
F-box domain found in F-box/LRR-repeat protein 13 (FBXL13) and similar proteins; FBXL13, also ...
553-590 1.34e-04

F-box domain found in F-box/LRR-repeat protein 13 (FBXL13) and similar proteins; FBXL13, also called F-box and leucine-rich repeat protein 13, or dynein regulatory complex subunit 6, is a component of the nexin-dynein regulatory complex (N-DRC), a key regulator of ciliary/flagellar motility which maintains the alignment and integrity of the distal axoneme and regulates microtubule sliding in motile axonemes. It is also the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438896  Cd Length: 42  Bit Score: 40.01  E-value: 1.34e-04
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 289803020 553 MRAALFCIFTYLDTRTLLHAAEVCRDWRFVARHPAVWT 590
Cdd:cd22124    5 PRKAALKIFSYLDLRDLARCAQVCRSWKVITQSSSLWS 42
F-box_AtGID2-like cd22151
F-box domain found in Arabidopsis thaliana F-box protein GID2 and similar proteins; AtGID2, ...
557-589 1.40e-04

F-box domain found in Arabidopsis thaliana F-box protein GID2 and similar proteins; AtGID2, also called protein SLEEPY 1, is an essential component of the SCF-type E3 ligase complex, SCF(GID2), a complex that positively regulates the gibberellin signaling pathway. Upon gibberellin treatment, the SCF(GID2) complex mediates the ubiquitination and subsequent degradation of DELLA proteins (GAI, RGA and RGL2), some repressors of the gibberellin pathway, leading to the activation of the pathway. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438922  Cd Length: 44  Bit Score: 40.00  E-value: 1.40e-04
                         10        20        30
                 ....*....|....*....|....*....|...
gi 289803020 557 LFCIFTYLDTRTLLHAAEVCRDWRFVARHPAVW 589
Cdd:cd22151    8 LQEIFKRLDPKSLARAACVCRRWRAAARSESLW 40
mukB PRK04863
chromosome partition protein MukB;
204-338 1.44e-04

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 45.72  E-value: 1.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020  204 RLKIRALEK-LEVDRRLERLSEEVEQKIAGQV----------GRLQAELERKAAELETARQESARLGREKEELEERASEL 272
Cdd:PRK04863  519 RMRLSELEQrLRQQQRAERLLAEFCKRLGKNLddedeleqlqEELEARLESLSESVSEARERRMALRQQLEQLQARIQRL 598
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 289803020  273 SRQVDVSVELLASLKQ--DLVHKEQELSRkqqevvQIDQFLKETAAREASAKL---RLQQFIEELLERADR 338
Cdd:PRK04863  599 AARAPAWLAAQDALARlrEQSGEEFEDSQ------DVTEYMQQLLERERELTVerdELAARKQALDEEIER 663
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
204-353 1.51e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 45.83  E-value: 1.51e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020   204 RLKIRALEKLEVDRRLERLSEEVEQkIAGQVGRLQAELERKAAELETARQESARLGREKEELEERASELS--RQVDVSVE 281
Cdd:TIGR02169  217 LKEKREYEGYELLKEKEALERQKEA-IERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGeeEQLRVKEK 295
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020   282 L------LASLKQDLVHKEQELSRKQQEVVQIDQFLKETAARE-------ASAKLRLQQFIEELLERADRAE---RQLQV 345
Cdd:TIGR02169  296 IgeleaeIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIeelereiEEERKRRDKLTEEYAELKEELEdlrAELEE 375

                   ....*...
gi 289803020   346 ISSSCGST 353
Cdd:TIGR02169  376 VDKEFAET 383
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
199-349 1.85e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.31  E-value: 1.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020 199 EE--GLARLKIR---ALEKLE-VDRRLERLS---EEVEQkiagQVGRL--QAELERKAAELetarqesarlgreKEELEE 267
Cdd:COG1196  162 EEaaGISKYKERkeeAERKLEaTEENLERLEdilGELER----QLEPLerQAEKAERYREL-------------KEELKE 224
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020 268 RASELsrqvdvsvellASLKQDLVHKEQELSRKQQEVVQIDQFLKETAAREASAKL-RLQQFIEELLERADRAERQLQVI 346
Cdd:COG1196  225 LEAEL-----------LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELeELRLELEELELELEEAQAEEYEL 293

                 ...
gi 289803020 347 SSS 349
Cdd:COG1196  294 LAE 296
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
199-342 1.90e-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: 44.75  E-value: 1.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020 199 EEGLARLKIRaLEKLEvdRRLERLSEEVEQKIA-----GQVGRLQ--------AELERKAAELET---ARQESAR-LGRE 261
Cdd:COG4942   82 EAELAELEKE-IAELR--AELEAQKEELAELLRalyrlGRQPPLAlllspedfLDAVRRLQYLKYlapARREQAEeLRAD 158
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020 262 KEELEERASELSRQVDVSVELLASLKQDLVHKEQELSRKQQEVVQIDQFLKETAAREA---SAKLRLQQFIEELLERADR 338
Cdd:COG4942  159 LAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAelqQEAEELEALIARLEAEAAA 238

                 ....
gi 289803020 339 AERQ 342
Cdd:COG4942  239 AAER 242
HIP1_clath_bdg pfam16515
Clathrin-binding domain of Huntingtin-interacting protein 1; HIP1_clath_bdg is the coiled-coil ...
239-301 2.07e-04

Clathrin-binding domain of Huntingtin-interacting protein 1; HIP1_clath_bdg is the coiled-coil region of Huntington-interacting proteins 1. It carries a highly conserved HADLLRKN sequence motif at its N-terminus which effects the binding of HIP1R to clathrin light-chain EED regulatory site. this binding then stimulates clathrin lattice assembly. Huntingtin-interacting protein 1 (HIP1) is an obligate binding partner for Huntungtin, and loss of this interaction triggers the cascade of events that results in the apoptosis of neuronal cells and the onset of Hungtinton's disease. Clathrin light-chain binds to a flexible coiled-coil domain in HIP1 and induces a compact state that is refractory to actin binding.


Pssm-ID: 465154 [Multi-domain]  Cd Length: 99  Bit Score: 41.15  E-value: 2.07e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 289803020  239 AELERKAAE----LETARQESARLGREKEELE---ERAS-ELSRQVDVSVELLASLKQDLVHKEQELSRKQ 301
Cdd:pfam16515   2 ADLLRKNAEttkqLTVAQQAQEEVEREKKQLEfelERAKeEAQMKLEEQKEELERLKRELESSRAELATLQ 72
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
197-343 2.18e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 45.06  E-value: 2.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020   197 AYEEGLARLKiRALEKLEvdrrlERLSEEVEQKIAGQVGRLQAELERKAAELETARQESARLGREKEELEERASELSRQV 276
Cdd:TIGR02169  769 ELEEDLHKLE-EALNDLE-----ARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQR 842
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 289803020   277 D------VSVE-LLASLKQDLVHKEQELSRKQQEVVQIDQFLKETAA--REASAKLR-LQQFIEELLERADRAERQL 343
Cdd:TIGR02169  843 IdlkeqiKSIEkEIENLNGKKEELEEELEELEAALRDLESRLGDLKKerDELEAQLReLERKIEELEAQIEKKRKRL 919
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
204-348 2.23e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.05  E-value: 2.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020 204 RLKIRALEKLEVDRRLERLSEEvEQKIAGQVGRLQAELER---KAAELETARQESARLGREKEELEERASELSRQVDVSV 280
Cdd:PRK03918 194 LIKEKEKELEEVLREINEISSE-LPELREELEKLEKEVKEleeLKEEIEELEKELESLEGSKRKLEEKIRELEERIEELK 272
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 289803020 281 ELLASLKqDLVHKEQELSRKQQEVVQIDQFLKETAAREASAKLRLqqfiEELLERADRAERQLQVISS 348
Cdd:PRK03918 273 KEIEELE-EKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRL----SRLEEEINGIEERIKELEE 335
F-box_SF cd09917
F-box domain superfamily; This short domain is commonly found at the N-terminus of various ...
557-584 2.54e-04

F-box domain superfamily; This short domain is commonly found at the N-terminus of various proteins, and typically co-occurs with one or more other conserved domains or motifs, such as leucine rich repeats, WD40 repeats, kelch, tub, spry, and others. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression. One of the best researched roles of F-box proteins is their participation in SCF (Skp1-Cul1-F-box protein), a multi-protein complex that functions as a ubiquitin E3 ligase, where the role of the F-box protein is to recruit target substrates. Gene families containing the F-box are found greatly expanded in narrow taxonomic lineages, such as flowering plants and nematodes. In this hierarchical classification, many of the subfamilies are named according to their domain architectures.


Pssm-ID: 438852  Cd Length: 35  Bit Score: 38.96  E-value: 2.54e-04
                         10        20
                 ....*....|....*....|....*...
gi 289803020 557 LFCIFTYLDTRTLLHAAEVCRDWRFVAR 584
Cdd:cd09917    8 LLKILSYLDPRDLLRLSLVCKRWRELAS 35
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
208-343 2.57e-04

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 44.83  E-value: 2.57e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020   208 RALEKLEVDRRLERLSEEVEqKIAGQVGRLQAELERKAAELETA-----RQESARLGREKEELEERASELSRQVD---VS 279
Cdd:pfam12128  381 RSKIKEQNNRDIAGIKDKLA-KIREARDRQLAVAEDDLQALESElreqlEAGKLEFNEEEYRLKSRLGELKLRLNqatAT 459
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020   280 VELLASL--KQDLVHK---EQELSRKQQEVVQIDQFLKETAAREASAKLRL-QQFIEELLERADRAERQL 343
Cdd:pfam12128  460 PELLLQLenFDERIERareEQEAANAEVERLQSELRQARKRRDQASEALRQaSRRLEERQSALDELELQL 529
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
206-342 2.96e-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: 44.73  E-value: 2.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020  206 KIRALEKLEVDRRL--ERLSEEVE----QKIAGQ-----VGRLQAELERKAAELETARQESARLGREKEELE-ERASELS 273
Cdd:pfam17380 376 RMRELERLQMERQQknERVRQELEaarkVKILEEerqrkIQQQKVEMEQIRAEQEEARQREVRRLEEERAREmERVRLEE 455
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 289803020  274 RQVDVSVELLASLKQDLVHKEQELSRKQQEVVQIDQFLKETAAREASAklRLQQFIEE-----LLERaDRAERQ 342
Cdd:pfam17380 456 QERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEE--RKQAMIEEerkrkLLEK-EMEERQ 526
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
238-342 3.28e-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: 43.98  E-value: 3.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020 238 QAELERKAAELETARQESARLGREKEELEERASELSRQvdvsvelLASLKQDLVHKEQELSRKQQEVVQIDQFLKETAAR 317
Cdd:COG4942   19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQ-------LAALERRIAALARRIRALEQELAALEAELAELEKE 91
                         90       100
                 ....*....|....*....|....*
gi 289803020 318 EASAKLRLQQFIEELLERADRAERQ 342
Cdd:COG4942   92 IAELRAELEAQKEELAELLRALYRL 116
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
199-347 3.37e-04

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 44.58  E-value: 3.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020   199 EEGLARLKIRALEKlevdRRLERLSEEVEQKIagqvgRLQAEL-ERKAAELETARQESARLGREKEELEERASELSRQVD 277
Cdd:pfam02463  159 EEEAAGSRLKRKKK----EALKKLIEETENLA-----ELIIDLeELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYL 229
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020   278 VSVELLASLKQDLvhkeQELSRKQQEvvQIDQFLKETAAREASAKLRLQQFIEELLERADRAERQLQVIS 347
Cdd:pfam02463  230 DYLKLNEERIDLL----QELLRDEQE--EIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAK 293
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
199-346 3.68e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 44.28  E-value: 3.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020 199 EEGLARLKiRALEKL------EVDRRLERL----SEEVEQKIAGQ-VGRLQAELERKAAELETARQESARLGREKEELEE 267
Cdd:PRK03918 569 EEELAELL-KELEELgfesveELEERLKELepfyNEYLELKDAEKeLEREEKELKKLEEELDKAFEELAETEKRLEELRK 647
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 289803020 268 RASELSRQvdVSVELLASLKQDLVHKEQELSRKQQEVVQIDQFLKETAareasaklRLQQFIEELLERADRAERQLQVI 346
Cdd:PRK03918 648 ELEELEKK--YSEEEYEELREEYLELSRELAGLRAELEELEKRREEIK--------KTLEKLKEELEEREKAKKELEKL 716
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
231-348 4.11e-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: 43.60  E-value: 4.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020 231 AGQVGRLQAELERKAAELETARQESARLGREKEELEERASELSRQVDVSVELLASLKQDLVHKEQELSRKQQEVVQIDQF 310
Cdd:COG4942   19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 289803020 311 LKETAAR-----EASAKLRLQQFIEELL--ERADRAERQLQVISS 348
Cdd:COG4942   99 LEAQKEElaellRALYRLGRQPPLALLLspEDFLDAVRRLQYLKY 143
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
203-345 4.30e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.14  E-value: 4.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020  203 ARLKIRALEKlevdrRLERLSEEVEQkIAGQVGRLQAEL----ERKAA------------ELETARQESARLGREKEELE 266
Cdd:COG4913   608 NRAKLAALEA-----ELAELEEELAE-AEERLEALEAELdalqERREAlqrlaeyswdeiDVASAEREIAELEAELERLD 681
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020  267 ERASELS---RQVDVSVELLASLKQDLVHKEQELSRKQQEV----VQIDQFLKETAAREASAKLRLQQFIEELLERADRA 339
Cdd:COG4913   682 ASSDDLAaleEQLEELEAELEELEEELDELKGEIGRLEKELeqaeEELDELQDRLEAAEDLARLELRALLEERFAAALGD 761

                  ....*.
gi 289803020  340 ERQLQV 345
Cdd:COG4913   762 AVEREL 767
F-box_SpPof1-like cd22147
F-box domain found in Schizosaccharomyces pombe Skp1-binding protein 1 (SpPof1) and similar ...
548-591 5.16e-04

F-box domain found in Schizosaccharomyces pombe Skp1-binding protein 1 (SpPof1) and similar proteins; SpPof1, also called F-box/WD repeat-containing protein pof1, probably recognizes and binds to some phosphorylated proteins and promotes their ubiquitination and degradation. It is required for the inactivation of zip1 via ubiquitination. This subfamily also includes Saccharomyces cerevisiae methionine-requiring protein 30 (ScMET30, also called E3 ubiquitin ligase complex SCF(Met30) subunit MET30), Aspergillus niger sulfur controller B (AnSCONB, also called sulfur metabolite repression control protein B) and Neurospora crassa sulfur controller 2 (NcSCON2, also called sulfur metabolite repression control protein 2). ScMET30 acts as a transcriptional inhibitor that negatively regulates the expression of sulfur amino acid biosynthesis genes. It controls cell cycle function (being required for the G1/S transition and M-phase but not the S-phase), sulfur metabolism, and methionine biosynthesis as part of the E3 ubiquitin ligase complex SCF(Met30). AnSCONB and NcSCON2 are components of the SCF (sconB/scon-2) E3 ubiquitin ligase complexes involved in the regulation of sulfur metabolite repression, probably by mediating the inactivation or degradation of the metR transcription factor. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438918  Cd Length: 46  Bit Score: 38.45  E-value: 5.16e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 289803020 548 PEILKMRaalfcIFTYLDTRTLLHAAEVCRDWRFVARHPAVWTR 591
Cdd:cd22147    6 PVELSLK-----ILSYLDAKSLCRAAQVSKKWRNLADDDELWKR 44
PTZ00121 PTZ00121
MAEBL; Provisional
209-341 5.48e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.98  E-value: 5.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020  209 ALEKLEVDRRLERLSEEVEQKIAGQVGRLQAELERKAAELETARQES---ARLGREKEELEERASEL-----SRQVDVSV 280
Cdd:PTZ00121 1449 AKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAkkkADEAKKAAEAKKKADEAkkaeeAKKADEAK 1528
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 289803020  281 ELLASLKQDLVHKEQELsRKQQEVVQIDQFLKETAAREASAKLRLQQFIEELLERADRAER 341
Cdd:PTZ00121 1529 KAEEAKKADEAKKAEEK-KKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKK 1588
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
203-337 5.67e-04

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 43.32  E-value: 5.67e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020 203 ARLKIRALEKLEVDRRLERLSEEVEQKIAGQvgrlQAELERKAAE----LETARQESarlgreKEELEERASELSRQVDV 278
Cdd:COG2268  212 TEIAIAQANREAEEAELEQEREIETARIAEA----EAELAKKKAEerreAETARAEA------EAAYEIAEANAEREVQR 281
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020 279 SVELLASLKQ-DLVHKEQELSRKQQEVVQIDQFLKETAAREASAKLRLQQFIEELLERAD 337
Cdd:COG2268  282 QLEIAEREREiELQEKEAEREEAELEADVRKPAEAEKQAAEAEAEAEAEAIRAKGLAEAE 341
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
199-356 5.69e-04

Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.


Pssm-ID: 464001 [Multi-domain]  Cd Length: 200  Bit Score: 42.20  E-value: 5.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020  199 EEGLARLKIR--ALEKL--EVDRRLERLSEEVEQkiagqvgrLQAELERKAAELETARQESARLGREK---EELEERASE 271
Cdd:pfam13851  32 KEEIAELKKKeeRNEKLmsEIQQENKRLTEPLQK--------AQEEVEELRKQLENYEKDKQSLKNLKarlKVLEKELKD 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020  272 LSRQVDVSVELLASLKQDLvhkeQELSRKQQEVVQidQFLKETAAREasakLRLQQFIEELLERADRAERQLQVISSSCG 351
Cdd:pfam13851 104 LKWEHEVLEQRFEKVERER----DELYDKFEAAIQ--DVQQKTGLKN----LLLEKKLQALGETLEKKEAQLNEVLAAAN 173

                  ....*
gi 289803020  352 STPSA 356
Cdd:pfam13851 174 LDPDA 178
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
214-341 5.75e-04

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 42.91  E-value: 5.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020  214 EVDRRLERLSEEVEQKIAGQVGRLQAELERKAAELETARQESARlgREKEELEERASELSRQvdVSVELLASLKQDLVHK 293
Cdd:TIGR02794  68 ERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAA--KQAEEKQKQAEEAKAK--QAAEAKAKAEAEAERK 143
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 289803020  294 EQELSRKQQEvvqIDQFLKETAAREASAKLRLQQFIEELLERADRAER 341
Cdd:TIGR02794 144 AKEEAAKQAE---EEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAK 188
PTZ00121 PTZ00121
MAEBL; Provisional
206-341 6.07e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.98  E-value: 6.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020  206 KIRALEKLEVDRRLERLSEEVEQKIAGQVGRLQAELERKAAELETARQESAR----LGREKEELEERASELSRQVDVSVE 281
Cdd:PTZ00121 1651 ELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKkaeeLKKKEAEEKKKAEELKKAEEENKI 1730
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 289803020  282 LLASLKQdlvhKEQELSRKQQEVV-------QIDQFLKETAAREASAKLRLQQFIEELLERADRAER 341
Cdd:PTZ00121 1731 KAEEAKK----EAEEDKKKAEEAKkdeeekkKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRR 1793
PRK12704 PRK12704
phosphodiesterase; Provisional
236-348 6.17e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 43.23  E-value: 6.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020 236 RLQAELERKAAELEtARQESARLGREKE-ELEERASELSRQvdvsvellaslKQDLVHKEQELSRKQQEVVQIDQFLKET 314
Cdd:PRK12704  48 KKEAEAIKKEALLE-AKEEIHKLRNEFEkELRERRNELQKL-----------EKRLLQKEENLDRKLELLEKREEELEKK 115
                         90       100       110
                 ....*....|....*....|....*....|....
gi 289803020 315 AAREASAKLRLQQFIEELLERADRAERQLQVISS 348
Cdd:PRK12704 116 EKELEQKQQELEKKEEELEELIEEQLQELERISG 149
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
240-340 6.38e-04

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 40.29  E-value: 6.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020  240 ELERKAAELEtarqesARLGREKEELEERASELSRQVDvSVELLASLKQDLVHKEQELSRKQQEVVQIDQFLKETAAREA 319
Cdd:pfam20492   3 EAEREKQELE------ERLKQYEEETKKAQEELEESEE-TAEELEEERRQAEEEAERLEQKRQEAEEEKERLEESAEMEA 75
                          90       100
                  ....*....|....*....|.
gi 289803020  320 SAKLRLQQFIEELLERADRAE 340
Cdd:pfam20492  76 EEKEQLEAELAEAQEEIARLE 96
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
252-349 6.46e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.51  E-value: 6.46e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020   252 RQESARLGREKEELEERASELSRQVDVSVELLASLKQDLVHKEQELSRKQQEVVQIDQFLKETAAREASAKLRLQQFIEE 331
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
                           90
                   ....*....|....*...
gi 289803020   332 LLERADRAERQLQVISSS 349
Cdd:TIGR02168  756 LTELEAEIEELEERLEEA 773
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
214-344 6.86e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.22  E-value: 6.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020 214 EVDRRLERLSEEVEQ-KIAGQVGRLQAELERKAAELETARQESARLGREKEELEERASELSRQVD----VSVELLASLKQ 288
Cdd:COG4717  348 ELQELLREAEELEEElQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEellgELEELLEALDE 427
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 289803020 289 DLVhkEQELSRKQQEVVQIDQFLKETAAREASAKLRLQQF-----IEELLERADRAERQLQ 344
Cdd:COG4717  428 EEL--EEELEELEEELEELEEELEELREELAELEAELEQLeedgeLAELLQELEELKAELR 486
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
208-332 7.59e-04

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 42.96  E-value: 7.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020  208 RALEKLEVDRRLERLSEEVEQK-IAGQVGRLQAELERKAAELETARQESARLGREKEELEERASELSRQVDVSVELLASL 286
Cdd:pfam07888  55 RQREKEKERYKRDREQWERQRReLESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIREL 134
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 289803020  287 KQDL-------VHKEQELSRKQQEVVQIDQFLKETAAREASAKLRLQQFIEEL 332
Cdd:pfam07888 135 EEDIktltqrvLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEEL 187
Nuf2_DHR10-like pfam18595
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This ...
206-304 8.02e-04

Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This domain was identified as MazG related domain also designated as Designed helical repeat protein 10 (DHR10) that actually adopts a coiled-coil structure. Nuf2 is part of the Ndc80 complex, which binds to the spindle and is required for chromosome segregation and spindle checkpoint activity.


Pssm-ID: 465814 [Multi-domain]  Cd Length: 117  Bit Score: 39.88  E-value: 8.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020  206 KIRALEKLEVD-RRLERLSEEVEQKiagqvgrlQAELERKAAELETARQESARLGREKEELEERASELSRQVDVSVELLA 284
Cdd:pfam18595  24 KIDALQVVEKDlRSCIKLLEEIEAE--------LAKLEEAKKKLKELRDALEEKEIELRELERREERLQRQLENAQEKLE 95
                          90       100
                  ....*....|....*....|
gi 289803020  285 SLKQDLVHKEQELSRKQQEV 304
Cdd:pfam18595  96 RLREQAEEKREAAQARLEEL 115
F-box_ECT2L cd22173
F-box domain found in epithelial cell-transforming sequence 2 oncogene-like (ECT2L) and ...
560-590 9.71e-04

F-box domain found in epithelial cell-transforming sequence 2 oncogene-like (ECT2L) and similar proteins; ECT2L, also called lung-specific F-box and DH domain-containing protein, or putative guanine nucleotide exchange factor LFDH, may act as a guanine nucleotide exchange factor (GEF). The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438944  Cd Length: 52  Bit Score: 37.77  E-value: 9.71e-04
                         10        20        30
                 ....*....|....*....|....*....|.
gi 289803020 560 IFTYLDTRTLLHAAEVCRDWRFVARHPAVWT 590
Cdd:cd22173   14 IFSFLDPRSLCRAAQVSWHWKFLAEQDCLWM 44
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
202-349 1.02e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 42.44  E-value: 1.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020 202 LARLKIRALEKLE-VDRRLERLSEEVeQKIAGQVGRLQAELERKAAELETARQEsarLGREKEELEERASELSR------ 274
Cdd:COG4942   46 LKKEEKALLKQLAaLERRIAALARRI-RALEQELAALEAELAELEKEIAELRAE---LEAQKEELAELLRALYRlgrqpp 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020 275 -----------QVDVSVELLASLKQDLVHKEQELSRKQQEVVQIDQFLKETAAREASAKLRLQQFIEELLERADRAERQL 343
Cdd:COG4942  122 lalllspedflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLL 201

                 ....*.
gi 289803020 344 QVISSS 349
Cdd:COG4942  202 ARLEKE 207
mukB PRK04863
chromosome partition protein MukB;
203-344 1.08e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 43.02  E-value: 1.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020  203 ARLKIRALEKLE----------VDRRLERLSEEVEQ-----KIAGQVGRLQAELERKAAELETARQESARLGREKEELEE 267
Cdd:PRK04863  870 AKEGLSALNRLLprlnlladetLADRVEEIREQLDEaeeakRFVQQHGNALAQLEPIVSVLQSDPEQFEQLKQDYQQAQQ 949
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020  268 RASELSRQVDV---------------SVELLA-------SLKQDLVHKEQELSRKQQEVVQIDQFLKETAAREASAKLRL 325
Cdd:PRK04863  950 TQRDAKQQAFAltevvqrrahfsyedAAEMLAknsdlneKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSY 1029
                         170
                  ....*....|....*....
gi 289803020  326 QQFIEELLEradrAERQLQ 344
Cdd:PRK04863 1030 DAKRQMLQE----LKQELQ 1044
DUF4164 pfam13747
Domain of unknown function (DUF4164); This is a family of short, approx 100 residue-long, ...
199-281 1.10e-03

Domain of unknown function (DUF4164); This is a family of short, approx 100 residue-long, bacterial proteins of unknown function. There is several conserved LE/LD sequence pairs.


Pssm-ID: 433450 [Multi-domain]  Cd Length: 89  Bit Score: 38.84  E-value: 1.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020  199 EEGLARLKiRALEKLE--VDRRLERLSEEVEqkIAGQVGRLQAELERKAAELETARQESARLgrekeelEERASELSRQV 276
Cdd:pfam13747   7 EAALQRLE-AALDRLEaaVDRRLEADRDRDE--LEAEIEALGADRSRLAQELDQAEARANRL-------EETNREISRRL 76

                  ....*
gi 289803020  277 DVSVE 281
Cdd:pfam13747  77 DSAIE 81
F-box_FBXW4 cd20090
F-box domain found in F-box/WD repeat-containing protein 4 (FBXW4) and similar proteins; FBXW4, ...
556-591 1.14e-03

F-box domain found in F-box/WD repeat-containing protein 4 (FBXW4) and similar proteins; FBXW4, also called dactylin, or F-box and WD-40 domain-containing protein 4, probably recognizes and binds to some phosphorylated proteins and promotes their ubiquitination and degradation. It is likely to be involved in key signaling pathways crucial for normal limb development. It may participate in Wnt signaling and act as a novel tumor suppressor that regulates important cellular processes. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438853  Cd Length: 47  Bit Score: 37.58  E-value: 1.14e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 289803020 556 ALFCIFTYLDTRTLLHAAEVCRDWRFVARHPAVWTR 591
Cdd:cd20090    9 LLFLIFSYLDPASLGRLSQVCRRLYRLISRDAVWRR 44
PTZ00121 PTZ00121
MAEBL; Provisional
206-341 1.18e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.82  E-value: 1.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020  206 KIRALEKLEVDRRLERLSEEVEQKIAGQVGRLQAELERKAAE----------LETARQESARLGREKEELEERASELSRQ 275
Cdd:PTZ00121 1576 KNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEakikaeelkkAEEEKKKVEQLKKKEAEEKKKAEELKKA 1655
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 289803020  276 vdvsVELLASLKQDLVHKEQELSRKQQEVVQIDQFLK---ETAAREASAKLRLQQFIEELLERADRAER 341
Cdd:PTZ00121 1656 ----EEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKkaaEALKKEAEEAKKAEELKKKEAEEKKKAEE 1720
DUF4515 pfam14988
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ...
211-344 1.32e-03

Domain of unknown function (DUF4515); This family of proteins is found in bacteria and eukaryotes. Proteins in this family are typically between 198 and 469 amino acids in length. There are two completely conserved L residues that may be functionally important.


Pssm-ID: 405647 [Multi-domain]  Cd Length: 206  Bit Score: 40.91  E-value: 1.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020  211 EKLEVDRRLERLSEEVEQKIagqvGRLQAELERKAAELETARQESArlgrekEELEERASELSRQVDVSVELLASLKQDL 290
Cdd:pfam14988   1 ENKFFLEYLAKKTEEKQKKI----EKLWNQYVQECEEIERRRQELA------SRYTQQTAELQTQLLQKEKEQASLKKEL 70
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 289803020  291 VHKEQELSRKQQEVVQIDQFLKETAAREASAKLRLQQFIEELLERADRAERQLQ 344
Cdd:pfam14988  71 QALRPFAKLKESQEREIQDLEEEKEKVRAETAEKDREAHLQFLKEKALLEKQLQ 124
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
215-348 1.33e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 42.31  E-value: 1.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020 215 VDRRLERLSEEVEQK---IAGQVGRLQAELERKAAELETARQESarlgrekeeleeRASELSRQVDVSVELLASLKQDLV 291
Cdd:COG3206  162 LEQNLELRREEARKAlefLEEQLPELRKELEEAEAALEEFRQKN------------GLVDLSEEAKLLLQQLSELESQLA 229
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 289803020 292 HKEQELSRKQQEVVQIDQFLKETaaREASAKLRLQQFIEELLERADRAERQLQVISS 348
Cdd:COG3206  230 EARAELAEAEARLAALRAQLGSG--PDALPELLQSPVIQQLRAQLAELEAELAELSA 284
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
211-345 1.58e-03

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: 1.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020  211 EKLEVDRRLERLSEEVEQKIAgqvgrLQAELERKAA--------------ELETARQESARLGREKEELEERASELSRQV 276
Cdd:pfam17380 304 EKEEKAREVERRRKLEEAEKA-----RQAEMDRQAAiyaeqermamererELERIRQEERKRELERIRQEEIAMEISRMR 378
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020  277 D--------------VSVELLASLKQDLVHKEQELSRKQQEVVQIDQFLKETAAREASAKlRLQQFIEELLERADRA--E 340
Cdd:pfam17380 379 ElerlqmerqqknerVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVR-RLEEERAREMERVRLEeqE 457

                  ....*
gi 289803020  341 RQLQV 345
Cdd:pfam17380 458 RQQQV 462
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
197-332 1.66e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.36  E-value: 1.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020 197 AYEEgLARLKIRALEKL-EVDRRLERLSEEVEQkiagqVGRLQAELERKAAELETARQESARLGREKEELEERASELSRQ 275
Cdd:PRK03918 294 EYIK-LSEFYEEYLDELrEIEKRLSRLEEEING-----IEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEA 367
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 289803020 276 VDVSVEL------LASLKQDLVHKEQELSRKQQEVVQIDqfLKETAAREASAKLR---LQQFIEEL 332
Cdd:PRK03918 368 KAKKEELerlkkrLTGLTPEKLEKELEELEKAKEEIEEE--ISKITARIGELKKEikeLKKAIEEL 431
F-box_FBXO22 cd22097
F-box domain found in F-box only protein 22 (FBXO22) and similar proteins; FBXO22, also called ...
548-584 1.69e-03

F-box domain found in F-box only protein 22 (FBXO22) and similar proteins; FBXO22, also called FBX22, or F-box protein FBX22p44, is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. It promotes the proteasome-dependent degradation of key sarcomeric proteins, such as alpha-actinin (ACTN2) and filamin-C (FLNC), essential for maintenance of normal contractile function. FBXO22 regulates histone H3 lysine 9 and 36 methylation levels by targeting histone demethylase KDM4A for ubiquitin-mediated proteasomal degradation. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438869  Cd Length: 48  Bit Score: 36.96  E-value: 1.69e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 289803020 548 PEILKMraalfcIFTYLDTRTLLHAAEVCRDWRFVAR 584
Cdd:cd22097    5 AEIVER------ILSFLPAKALLRCARVCRLWRDCAR 35
UPF0242 pfam06785
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ...
210-317 1.89e-03

Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal transmembrane region and a C-terminal coiled-coil.


Pssm-ID: 429117 [Multi-domain]  Cd Length: 194  Bit Score: 40.57  E-value: 1.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020  210 LEKLEVDRRLERLSEEVEQKIA---GQVGRLQAELERKAAELETARQESARLGREKEELEERASELSRQVDvsvELLASL 286
Cdd:pfam06785  65 FEKSFLEEKEAKLTELDAEGFKileETLEELQSEEERLEEELSQKEEELRRLTEENQQLQIQLQQISQDFA---EFRLES 141
                          90       100       110
                  ....*....|....*....|....*....|.
gi 289803020  287 KQDLVHKEQELSRKQQEVVQIDQFLKETAAR 317
Cdd:pfam06785 142 EEQLAEKQLLINEYQQTIEEQRSVLEKRQDQ 172
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
199-344 2.04e-03

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 42.08  E-value: 2.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020   199 EEGLARLKIRALEKLEVDRRLE-RLSEEVE--QKIAGQVGRLQ---AELERKAAELETARQ------------------- 253
Cdd:pfam01576   60 EEMRARLAARKQELEEILHELEsRLEEEEErsQQLQNEKKKMQqhiQDLEEQLDEEEAARQklqlekvtteakikkleed 139
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020   254 ------ESARLGREKEELEERASELSRQVDVSVELLASL-----KQDLVHKEQELSRKQ-----QEVVQIDQFLKETAAR 317
Cdd:pfam01576  140 illledQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLsklknKHEAMISDLEERLKKeekgrQELEKAKRKLEGESTD 219
                          170       180
                   ....*....|....*....|....*..
gi 289803020   318 EASAKLRLQQFIEELLERADRAERQLQ 344
Cdd:pfam01576  220 LQEQIAELQAQIAELRAQLAKKEEELQ 246
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
205-340 2.14e-03

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


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 41.16  E-value: 2.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020   205 LKIRALEKLE-VDRRLERLSEEVEQ--KIAGQVGRLQAELERKAAELETARQE-----SARLGREKEELeeraSELSRQV 276
Cdd:smart00787 145 LKEGLDENLEgLKEDYKLLMKELELlnSIKPKLRDRKDALEEELRQLKQLEDEledcdPTELDRAKEKL----KKLLQEI 220
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 289803020   277 DVSVELLASLKQDLVHKEQELsrkQQEVVQIDQFLKETAAREaSAKLRLQQF----IEELLERADRAE 340
Cdd:smart00787 221 MIKVKKLEELEEELQELESKI---EDLTNKKSELNTEIAEAE-KKLEQCRGFtfkeIEKLKEQLKLLQ 284
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
199-341 2.19e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.97  E-value: 2.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020 199 EEGLARLKIRALEKL--EVDRRLERLSEEVEqKIAGQVGRLQaELERKAAELETARQESARLGREKEELEERASELSRQV 276
Cdd:PRK03918 246 ELESLEGSKRKLEEKirELEERIEELKKEIE-ELEEKVKELK-ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEI 323
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 289803020 277 DVSVELLaslkqdlvhkeQELSRKQQEVVQIDQFLKETAAREASAKLRLQQFiEELLERADRAER 341
Cdd:PRK03918 324 NGIEERI-----------KELEEKEERLEELKKKLKELEKRLEELEERHELY-EEAKAKKEELER 376
APG6_N pfam17675
Apg6 coiled-coil region; In yeast, 15 Apg proteins coordinate the formation of autophagosomes. ...
217-297 2.32e-03

Apg6 coiled-coil region; In yeast, 15 Apg proteins coordinate the formation of autophagosomes. Autophagy is a bulk degradation process induced by starvation in eukaryotic cells. Apg6/Vps30p has two distinct functions in the autophagic process, either associated with the membrane or in a retrieval step of the carboxypeptidase Y sorting pathway.


Pssm-ID: 465452 [Multi-domain]  Cd Length: 127  Bit Score: 38.73  E-value: 2.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020  217 RRLERLSEEVEQKIAGQVGRLQAELERKAAELETARQESARLGREKEELEERASELSRQVDVSVELLASLKQDLVHKEQE 296
Cdd:pfam17675  33 KKLEKETPEELEELEKELEKLEKEEEELLQELEELEKEREELDAELEALEEELEALDEEEEEFWREYNALQLQLLEFQDE 112

                  .
gi 289803020  297 L 297
Cdd:pfam17675 113 R 113
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
203-344 2.34e-03

Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.


Pssm-ID: 464768 [Multi-domain]  Cd Length: 374  Bit Score: 41.18  E-value: 2.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020  203 ARLKIRALEKLEVDRRLERLSEEVEQkiagqvgRLQAELERKAAELETARQESARLGREKEELEERASELSRQVDVSVEL 282
Cdd:pfam15558  80 RRADRREKQVIEKESRWREQAEDQEN-------QRQEKLERARQEAEQRKQCQEQRLKEKEEELQALREQNSLQLQERLE 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020  283 LASLKQDLvhKEQELSRKQQEV------------VQID-QFLKETAAREASAKLRLQQFIE-----------ELLERADR 338
Cdd:pfam15558 153 EACHKRQL--KEREEQKKVQENnlsellnhqarkVLVDcQAKAEELLRRLSLEQSLQRSQEnyeqlveerhrELREKAQK 230

                  ....*.
gi 289803020  339 AERQLQ 344
Cdd:pfam15558 231 EEEQFQ 236
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
209-344 2.36e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 41.29  E-value: 2.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020 209 ALEKLEVDRRLERLSEEVEQKIAgQVGRLQAELERKAAELETARQESARLGREKEELEERASELSRQVDVSVELLASLKQ 288
Cdd:COG4942   19 ADAAAEAEAELEQLQQEIAELEK-ELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 289803020 289 DLVHKEQELSR------KQQEVVQIDQFLKETAAREASAKLR-LQQFIEELLERADRAERQLQ 344
Cdd:COG4942   98 ELEAQKEELAEllralyRLGRQPPLALLLSPEDFLDAVRRLQyLKYLAPARREQAEELRADLA 160
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
199-346 2.56e-03

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


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 41.57  E-value: 2.56e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020   199 EEGLARLKIRALEKLEVDRRLERLSEEVEQKIAGQV-------GRLQAELERKAA----ELETARQESARLGREKEELEE 267
Cdd:TIGR00606  268 DNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLndlyhnhQRTVREKERELVdcqrELEKLNKERRLLNQEKTELLV 347
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020   268 RASELSRQVDVSVEllASLKQDLVHKEQE-------LSRKQQEVVQIDQFLKETAAREASAKLRLQQFIEELLERADRAE 340
Cdd:TIGR00606  348 EQGRLQLQADRHQE--HIRARDSLIQSLAtrleldgFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQ 425

                   ....*.
gi 289803020   341 RQLQVI 346
Cdd:TIGR00606  426 EQADEI 431
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
213-332 2.57e-03

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 41.75  E-value: 2.57e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020   213 LEVDRRLERLSEeVEQKIAgqvgRLQAELERKAAELETARQESARLGREKEELEERASELSRQVDVSVELLASLKQDLVH 292
Cdd:pfam12128  807 QRRPRLATQLSN-IERAIS----ELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATLKEDANS 881
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 289803020   293 KEQELSRKQQeVVQIDQFLKetaaREASAKLRLQQFIEEL 332
Cdd:pfam12128  882 EQAQGSIGER-LAQLEDLKL----KRDYLSESVKKYVEHF 916
HIP1_clath_bdg pfam16515
Clathrin-binding domain of Huntingtin-interacting protein 1; HIP1_clath_bdg is the coiled-coil ...
209-270 2.85e-03

Clathrin-binding domain of Huntingtin-interacting protein 1; HIP1_clath_bdg is the coiled-coil region of Huntington-interacting proteins 1. It carries a highly conserved HADLLRKN sequence motif at its N-terminus which effects the binding of HIP1R to clathrin light-chain EED regulatory site. this binding then stimulates clathrin lattice assembly. Huntingtin-interacting protein 1 (HIP1) is an obligate binding partner for Huntungtin, and loss of this interaction triggers the cascade of events that results in the apoptosis of neuronal cells and the onset of Hungtinton's disease. Clathrin light-chain binds to a flexible coiled-coil domain in HIP1 and induces a compact state that is refractory to actin binding.


Pssm-ID: 465154 [Multi-domain]  Cd Length: 99  Bit Score: 38.07  E-value: 2.85e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 289803020  209 ALEKLEVDRRLERLSEEVEQKIAGQ---VGRLQAELERKAAELETAR-------QESARLGREKEELE-ERAS 270
Cdd:pfam16515  26 EREKKQLEFELERAKEEAQMKLEEQkeeLERLKRELESSRAELATLQstlqsseQSGSQLSSQLAALQaEKEG 98
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
233-304 3.43e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.58  E-value: 3.43e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 289803020 233 QVGRLQAELERKAAELETARQESARLGREKEELEERASELSRQVDVSVELLASLKQDLVHKEQELSRKQQEV 304
Cdd:COG3883   17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL 88
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
219-344 3.45e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 3.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020 219 LERLSEEVEQ--KIAGQVGRLQ-AELERKAAELETARQESARLgrekEELEERASELSRQVDVSVELLASLKQDLVHKEQ 295
Cdd:COG4717   48 LERLEKEADElfKPQGRKPELNlKELKELEEELKEAEEKEEEY----AELQEELEELEEELEELEAELEELREELEKLEK 123
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 289803020 296 ELSRKQ--QEVVQIDQFLKETAAREASAKLRLQQfIEELLERADRAERQLQ 344
Cdd:COG4717  124 LLQLLPlyQELEALEAELAELPERLEELEERLEE-LRELEEELEELEAELA 173
F-box_FBXO48 cd22113
F-box domain found in F-box only protein 48 (FBXO48) and similar proteins; FBXO48, also called ...
560-589 3.59e-03

F-box domain found in F-box only protein 48 (FBXO48) and similar proteins; FBXO48, also called FBX48, is one of the paralogs of the F-box only protein 7 (FBXO7), which is the causative gene for PARK15 (also known as Parkinsonian-pyramidal disease, PPD). The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438885  Cd Length: 46  Bit Score: 36.14  E-value: 3.59e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 289803020 560 IFTYLDTRTLLHAAEVCRDWR-FVARHPAVW 589
Cdd:cd22113   12 IFSQLDVQSLCRASQTCKTWNdLIENSDYLW 42
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
195-346 3.79e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 3.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020 195 DVAYEEGLARLKIRALEKLEVDRRLERLSEEVEQK---------------IAGQVGRLQAELERKAAELETARQESARLG 259
Cdd:COG4717  380 GVEDEEELRAALEQAEEYQELKEELEELEEQLEELlgeleellealdeeeLEEELEELEEELEELEEELEELREELAELE 459
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020 260 REKEELEEraselsrqvdvsvellaslKQDLVHKEQELSRKQQEvvqidqfLKETAAREASAKLrLQQFIEELLERAdRA 339
Cdd:COG4717  460 AELEQLEE-------------------DGELAELLQELEELKAE-------LRELAEEWAALKL-ALELLEEAREEY-RE 511

                 ....*..
gi 289803020 340 ERQLQVI 346
Cdd:COG4717  512 ERLPPVL 518
F-box_FBXL7 cd22120
F-box domain found in F-box/LRR-repeat protein 7 (FBXL7) and similar proteins; FBXL7, also ...
560-592 3.82e-03

F-box domain found in F-box/LRR-repeat protein 7 (FBXL7) and similar proteins; FBXL7, also called F-box and leucine-rich repeat protein 7, or F-box protein FBL6/FBL7, is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of Aurora kinase A (AURKA) during mitosis, causing mitotic arrest. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438892  Cd Length: 44  Bit Score: 35.82  E-value: 3.82e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 289803020 560 IFTYLDTRTLLHAAEVCRDWRFVARHPAVWTRV 592
Cdd:cd22120   12 IFSHLPTNQLCRCARVCRRWYNLAWDPRLWTTI 44
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
217-346 4.08e-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: 4.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020  217 RRLERLSEEVEQKIA--GQVGRLQAELERKAAELETARQESARL-----GREKEELEERASELSRQVDVSVELLASLKQD 289
Cdd:COG4913   238 ERAHEALEDAREQIEllEPIRELAERYAAARERLAELEYLRAALrlwfaQRRLELLEAELEELRAELARLEAELERLEAR 317
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 289803020  290 LVHKEQELSRKQQEVVQIDQFLKETAAREASaklRLQQFIEELLERADRAERQLQVI 346
Cdd:COG4913   318 LDALREELDELEAQIRGNGGDRLEQLEREIE---RLERELEERERRRARLEALLAAL 371
F-box_FBXW12 cd22137
F-box domain found in F-box/WD repeat-containing protein 12 (FBXW12) and similar proteins; ...
556-591 4.15e-03

F-box domain found in F-box/WD repeat-containing protein 12 (FBXW12) and similar proteins; FBXW12, also called F-box and WD-40 domain-containing protein 12, or F-box only protein 35 (FBXO35), is the substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex that mediates the ubiquitination and subsequent proteasomal degradation of target proteins. It functions as an epithelial growth suppressor. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438909  Cd Length: 44  Bit Score: 35.82  E-value: 4.15e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 289803020 556 ALFCIFTYLDTRTLLHAAEVCRDWRFVARHPAVWTR 591
Cdd:cd22137    7 PMLRIFSFLDAFSLLQAAQVNKQWNKVADSDYLWRN 42
PRK12704 PRK12704
phosphodiesterase; Provisional
203-338 4.60e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.53  E-value: 4.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020 203 ARLKIRALEK---LEVDRRLERLSEEVEQKIAGQVGRLQAELERKAAELETARQESARLGREKEELEERASELSRQvdvs 279
Cdd:PRK12704  47 AKKEAEAIKKealLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQK---- 122
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 289803020 280 vellaslKQDLVHKEQELSRKQQEVVQ-----------------IDQfLKETAAREASAKLRlqQFIEELLERADR 338
Cdd:PRK12704 123 -------QQELEKKEEELEELIEEQLQelerisgltaeeakeilLEK-VEEEARHEAAVLIK--EIEEEAKEEADK 188
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
248-344 4.65e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 40.58  E-value: 4.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020 248 LETARQ--------ESAR--LGREKEELEE---RASELSRQVDVSVELLASLKQDLVHKEQELSRKQQEVVQIDQFLKET 314
Cdd:PRK00409 491 FEIAKRlglpeniiEEAKklIGEDKEKLNEliaSLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEE 570
                         90       100       110
                 ....*....|....*....|....*....|
gi 289803020 315 AAREAsaklrlQQFIEELLERADRAERQLQ 344
Cdd:PRK00409 571 AEKEA------QQAIKEAKKEADEIIKELR 594
F-box_FBXO16-like cd22094
F-box domain found in F-box only protein 16 (FBXO16), epithelial cell-transforming sequence 2 ...
560-589 4.88e-03

F-box domain found in F-box only protein 16 (FBXO16), epithelial cell-transforming sequence 2 oncogene-like (ECT2L) and similar proteins; This family includes FBXO16 and ECT2L. FBXO16, also called FBX16, is part of an SCF (SKP1-cullin-F-box) protein ligase complex. It probably recognizes and binds to some phosphorylated proteins and promotes their ubiquitination and degradation. It functions as a tumor suppressor by attenuating nuclear beta-catenin function. ECT2L, also called lung-specific F-box and DH domain-containing protein, or putative guanine nucleotide exchange factor LFDH, may act as a guanine nucleotide exchange factor (GEF). The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438866  Cd Length: 49  Bit Score: 35.89  E-value: 4.88e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 289803020 560 IFTYLDTRTLLHAAEVCRDWRFVARHPAVW 589
Cdd:cd22094   14 IFSYLDPRSLCRAAQVSWYWKFLCESDELW 43
GOLGA2L5 pfam15070
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein ...
224-332 5.28e-03

Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein family remains unknown. This family of proteins is thought to be found in the Golgi apparatus of eukaryotes.


Pssm-ID: 464485 [Multi-domain]  Cd Length: 521  Bit Score: 40.43  E-value: 5.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020  224 EEVEQKIAGQVGRLQAELERKAAELETARQESARLGREKEELEERASELSRQVDvsvellaslkqdlVHKEQELSRKQQ- 302
Cdd:pfam15070  81 SEEEQRLQEEAEQLQKELEALAGQLQAQVQDNEQLSRLNQEQEQRLLELERAAE-------------RWGEQAEDRKQIl 147
                          90       100       110
                  ....*....|....*....|....*....|
gi 289803020  303 EVVQIDqflKETAAREASAKLRLQQFIEEL 332
Cdd:pfam15070 148 EDMQSD---RATISRALSQNRELKEQLAEL 174
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
210-341 5.29e-03

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 40.54  E-value: 5.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020   210 LEKLEvdRRLERLSEEVEQKIA---GQVGRLQAELERKAAELETA----------RQESARLGREKE----ELEE----- 267
Cdd:pfam01576  206 LEKAK--RKLEGESTDLQEQIAelqAQIAELRAQLAKKEEELQAAlarleeetaqKNNALKKIRELEaqisELQEdlese 283
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020   268 ---RASELSRQVDVSVELLAsLK------QDLVHKEQEL-SRKQQEVVQIDQFLK-ETAAREAS-AKLRLQQF--IEELL 333
Cdd:pfam01576  284 raaRNKAEKQRRDLGEELEA-LKteledtLDTTAAQQELrSKREQEVTELKKALEeETRSHEAQlQEMRQKHTqaLEELT 362

                   ....*...
gi 289803020   334 ERADRAER 341
Cdd:pfam01576  363 EQLEQAKR 370
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
214-344 5.78e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.41  E-value: 5.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020 214 EVDRRLERLSEEVEQK----------IAGQVGRLQaELERKAAELETARQESARLGREKEELEERASELSRQV------- 276
Cdd:PRK02224 217 ELDEEIERYEEQREQAretrdeadevLEEHEERRE-ELETLEAEIEDLRETIAETEREREELAEEVRDLRERLeeleeer 295
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 289803020 277 ----------DVSVELLASLKQDLVHKEQELSRKQQEVVQIDQFLKETAAREASAKLRLQQFIEELLERADRAERQLQ 344
Cdd:PRK02224 296 ddllaeagldDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELE 373
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
208-345 5.90e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.89  E-value: 5.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020 208 RALEKLE-VDRRLERLSEEVEQkIAGQVGRLQAELERKAAELETARQESARLGREKEELEERASELSRQVDVSVELLASL 286
Cdd:COG4372   98 QAQEELEsLQEEAEELQEELEE-LQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQAL 176
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 289803020 287 KQDlvHKEQELSRKQQEVVQIDQFLKETAAREASAKLRLQQFIEELLERADRAERQLQV 345
Cdd:COG4372  177 SEA--EAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGL 233
FBOX smart00256
A Receptor for Ubiquitination Targets;
557-589 6.02e-03

A Receptor for Ubiquitination Targets;


Pssm-ID: 197608  Cd Length: 41  Bit Score: 35.11  E-value: 6.02e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 289803020   557 LFCIFTYLDTRTLLHAAEVCRDWRFVARHPAVW 589
Cdd:smart00256   6 LEEILSKLDPKDLLRLRKVSRKWRSLIDSHDFW 38
F-box_FBXO11 cd22091
F-box domain found in F-box only protein 11 (FBXO11) and similar proteins; FBXO11, also called ...
557-591 6.11e-03

F-box domain found in F-box only protein 11 (FBXO11) and similar proteins; FBXO11, also called FBX11, protein arginine N-methyltransferase 9 (PRMT9), or vitiligo-associated protein 1 (VIT-1), is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins, such as DTL/CDT2, BCL6 and PRDM1/BLIMP1. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438863  Cd Length: 45  Bit Score: 35.48  E-value: 6.11e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 289803020 557 LFCIFTYLDTRTLLHAAEVCRDWRFVARHPAVWTR 591
Cdd:cd22091    9 LLKIFSYLLEQDLCRAAQVCKRFNTLANDPELWKR 43
ARGLU pfam15346
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ...
199-305 7.23e-03

Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is required for the oestrogen-dependent expression of ESR1 target genes. It functions in cooperation with MED1. The family of proteins is found in eukaryotes.


Pssm-ID: 405931 [Multi-domain]  Cd Length: 151  Bit Score: 38.11  E-value: 7.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020  199 EEGLARLKIRALEKlEVDRRLERLSEEVEQKIAGQVGRLQAELERK-AAELETARQESARLGREKEE--------LEERA 269
Cdd:pfam15346   9 EEETARRVEEAVAK-RVEEELEKRKDEIEAEVERRVEEARKIMEKQvLEELEREREAELEEERRKEEeerkkreeLERIL 87
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 289803020  270 SELSRQVDVSVELLASL--------------KQDLVHKEQELSRKQQEVV 305
Cdd:pfam15346  88 EENNRKIEEAQRKEAEErlamleeqrrmkeeRQRREKEEEEREKREQQKI 137
fliH PRK06669
flagellar assembly protein H; Validated
214-337 8.63e-03

flagellar assembly protein H; Validated


Pssm-ID: 235850 [Multi-domain]  Cd Length: 281  Bit Score: 39.23  E-value: 8.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020 214 EVDRRLERLSEEVEQKIAgqvgRLQAELE--------RKAAELETARQESARLGREK--EELEERASELSRQVDVSVELL 283
Cdd:PRK06669  78 EAKEELLKKTDEASSIIE----KLQMQIEreqeeweeELERLIEEAKAEGYEEGYEKgrEEGLEEVRELIEQLNKIIEKL 153
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 289803020 284 ASLKQDLVHK-EQELSrkqQEVVQI-DQFLKETAAREASAKLRL-QQFIEELLERAD 337
Cdd:PRK06669 154 IKKREEILESsEEEIV---ELALDIaKKVIKEISENSKEIALALvKELLKEVKDATD 207
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
236-339 8.64e-03

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


Pssm-ID: 461098 [Multi-domain]  Cd Length: 140  Bit Score: 37.56  E-value: 8.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803020  236 RLQAELERKAAELEtarqesARLGREKEELEERASELSRQVDVSVELLASLKQDLVHKEQELSRKQQEvvqidqFLKETA 315
Cdd:pfam03938  19 AAQAQLEKKFKKRQ------AELEAKQKELQKLYEELQKDGALLEEEREEKEQELQKKEQELQQLQQK------AQQELQ 86
                          90       100
                  ....*....|....*....|....
gi 289803020  316 AREasaklrlQQFIEELLERADRA 339
Cdd:pfam03938  87 KKQ-------QELLQPIQDKINKA 103
F-box pfam00646
F-box domain; This domain is approximately 50 amino acids long, and is usually found in the ...
556-591 9.34e-03

F-box domain; This domain is approximately 50 amino acids long, and is usually found in the N-terminal half of a variety of proteins. Two motifs that are commonly found associated with the F-box domain are the leucine rich repeats (LRRs; pfam00560 and pfam07723) and the WD repeat (pfam00400). The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 425796  Cd Length: 43  Bit Score: 34.82  E-value: 9.34e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 289803020  556 ALFCIFTYLDTRTLLHAAEVCRDWRFVARHPAVWTR 591
Cdd:pfam00646   8 LLLEILSRLDPKDLLRLSLVSKRWRSLVDSLKLWKK 43
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH