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Conserved domains on  [gi|47564092|ref|NP_001001160|]
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F-box only protein 41 [Mus musculus]

Protein Classification

Graphical summary

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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 ...
545-591 1.51e-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: 91.24  E-value: 1.51e-22
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 47564092 545 SPEILKMRAALFCIFTYLDTRTLLHAAEVCRDWRFVARHPAVWTRVL 591
Cdd:cd22109   1 SLESLRRRDALFCVFSYLDTKSLLRCAEVCREWRDVSRHPALWQRVC 47
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
200-342 1.02e-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: 1.02e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092 200 LARLKIRALEKLEVDRRLERLSEEVEQKIAgQVGRLQAELERKAAELETARQESARLGREKEELEERASELSRQVDVSVE 279
Cdd:COG1196 231 LLKLRELEAELEELEAELEELEAELEELEA-ELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE 309
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 47564092 280 LLASLKQDLVHKEQELSRKQQEVVQIDQFLKETAAREASAKLRLQQFIEELLERADRAERQLQ 342
Cdd:COG1196 310 RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
209-512 1.48e-06

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


:

Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 51.37  E-value: 1.48e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092 209 EKLEVDRRLERLSEEVEQKIAgQVGRLQAELERKAAELETARQE----SARLGREKEELEERASE--------------- 269
Cdd:COG3883  31 ELEAAQAELDALQAELEELNE-EYNELQAELEALQAEIDKLQAEiaeaEAEIEERREELGERARAlyrsggsvsyldvll 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092 270 --------LSRQVDVS---------VELLASLKQDLVHKEQELSRKQQEVVQIDQFLKETAAREASAKLRLQQFIEELLE 332
Cdd:COG3883 110 gsesfsdfLDRLSALSkiadadadlLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSA 189
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092 333 RADRAERQLQVISSSCGSTPSASLGRGGGGSASGPGVRGPGrmrehhAGSAVPSTYAVSRHGSSPSTGASSRVPAASQSS 412
Cdd:COG3883 190 EEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA------AAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAG 263
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092 413 GCYDSDSLELPRPEEGPSEDSGPGGLGSRAQATNGGSERSQAPRSSGLRRQAIQNWQRRPRRHSTEGEEGDVSDVGSRTT 492
Cdd:COG3883 264 AAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAASGGSGGGSGGAGGVGSGGGAGAVVGGASAGGGGGSGGGGGSSGG 343
                       330       340
                ....*....|....*....|
gi 47564092 493 ESEAEGPSDVPRPGPAVAGP 512
Cdd:COG3883 344 GSGGGGGGGGGGGGSSSGGG 363
 
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 ...
545-591 1.51e-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: 91.24  E-value: 1.51e-22
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 47564092 545 SPEILKMRAALFCIFTYLDTRTLLHAAEVCRDWRFVARHPAVWTRVL 591
Cdd:cd22109   1 SLESLRRRDALFCVFSYLDTKSLLRCAEVCREWRDVSRHPALWQRVC 47
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
200-342 1.02e-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: 1.02e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092 200 LARLKIRALEKLEVDRRLERLSEEVEQKIAgQVGRLQAELERKAAELETARQESARLGREKEELEERASELSRQVDVSVE 279
Cdd:COG1196 231 LLKLRELEAELEELEAELEELEAELEELEA-ELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE 309
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 47564092 280 LLASLKQDLVHKEQELSRKQQEVVQIDQFLKETAAREASAKLRLQQFIEELLERADRAERQLQ 342
Cdd:COG1196 310 RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372
F-box-like pfam12937
F-box-like; This is an F-box-like family.
555-590 1.07e-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: 1.07e-07
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 47564092   555 LFCIFTYLDTRTLLHAAEVCRDWRFVARHPAVWTRV 590
Cdd:pfam12937   9 LLQIFSYLDPKDLLRLALVCRRWRELASDDSLWRRL 44
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
217-330 3.39e-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: 3.39e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092   217 LERLSEEVEQKI---AGQVGRLQAELERKAAELETARQESARLGREKEELEERASELSRQVDVSVELLASLKQDLVHKEQ 293
Cdd:TIGR04523 459 LDNTRESLETQLkvlSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKES 538
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 47564092   294 ELSRKQQEVVQIDQFLKETAAREasAKLRLQQFIEEL 330
Cdd:TIGR04523 539 KISDLEDELNKDDFELKKENLEK--EIDEKNKEIEEL 573
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
209-512 1.48e-06

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 51.37  E-value: 1.48e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092 209 EKLEVDRRLERLSEEVEQKIAgQVGRLQAELERKAAELETARQE----SARLGREKEELEERASE--------------- 269
Cdd:COG3883  31 ELEAAQAELDALQAELEELNE-EYNELQAELEALQAEIDKLQAEiaeaEAEIEERREELGERARAlyrsggsvsyldvll 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092 270 --------LSRQVDVS---------VELLASLKQDLVHKEQELSRKQQEVVQIDQFLKETAAREASAKLRLQQFIEELLE 332
Cdd:COG3883 110 gsesfsdfLDRLSALSkiadadadlLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSA 189
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092 333 RADRAERQLQVISSSCGSTPSASLGRGGGGSASGPGVRGPGrmrehhAGSAVPSTYAVSRHGSSPSTGASSRVPAASQSS 412
Cdd:COG3883 190 EEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA------AAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAG 263
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092 413 GCYDSDSLELPRPEEGPSEDSGPGGLGSRAQATNGGSERSQAPRSSGLRRQAIQNWQRRPRRHSTEGEEGDVSDVGSRTT 492
Cdd:COG3883 264 AAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAASGGSGGGSGGAGGVGSGGGAGAVVGGASAGGGGGSGGGGGSSGG 343
                       330       340
                ....*....|....*....|
gi 47564092 493 ESEAEGPSDVPRPGPAVAGP 512
Cdd:COG3883 344 GSGGGGGGGGGGGGSSSGGG 363
PRK12705 PRK12705
hypothetical protein; Provisional
202-344 3.04e-05

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 47.40  E-value: 3.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092  202 RLKIRALEKLEVDRRLERLSEEVEQKiagqvgRLQAELERKAAELETARQESARLGREKEEL---EERASELSRQVDVSV 278
Cdd:PRK12705  24 LLKKRQRLAKEAERILQEAQKEAEEK------LEAALLEAKELLLRERNQQRQEARREREELqreEERLVQKEEQLDARA 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092  279 ELLASLKQDLVHKEQELSRKQQEVV----QIDQFLKETA------AR-------EASAKLRLQQFIEELLERAD-RAERQ 340
Cdd:PRK12705  98 EKLDNLENQLEEREKALSARELELEelekQLDNELYRVAgltpeqARklllkllDAELEEEKAQRVKKIEEEADlEAERK 177

                 ....
gi 47564092  341 LQVI 344
Cdd:PRK12705 178 AQNI 181
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
222-316 4.57e-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: 4.57e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092    222 EEVEQKIAGQVGRLQAELERKAAELETARQEsarLGREKEEL-EERASELSRQVDVSVELLASLKQDLvhkEQELSRKQQ 300
Cdd:smart00935  17 KAAQKQLEKEFKKRQAELEKLEKELQKLKEK---LQKDAATLsEAAREKKEKELQKKVQEFQRKQQKL---QQDLQKRQQ 90
                           90       100
                   ....*....|....*....|.
gi 47564092    301 EVVQ-----IDQFLKETAARE 316
Cdd:smart00935  91 EELQkildkINKAIKEVAKKK 111
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
222-316 5.20e-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: 44.10  E-value: 5.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092   222 EEVEQKIAGQVGRLQAELERKAAELETARQE-SARLGREKEELEERASELSRQVDVSVELLASLKQDLVHKEQELSRKQQ 300
Cdd:pfam03938  18 KAAQAQLEKKFKKRQAELEAKQKELQKLYEElQKDGALLEEEREEKEQELQKKEQELQQLQQKAQQELQKKQQELLQPIQ 97
                          90
                  ....*....|....*.
gi 47564092   301 EvvQIDQFLKETAARE 316
Cdd:pfam03938  98 D--KINKAIKEVAKEK 111
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
345-555 3.11e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 44.78  E-value: 3.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092   345 SSSCGSTPSASLGRGGGGSASGPGVRGPGRMREHHAGSAVPSTyavSRHGSSPStGASSRVPAASQSSGCYDSDSLELPR 424
Cdd:PHA03307  182 TARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAP---GRSAADDA-GASSSDSSSSESSGCGWGPENECPL 257
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092   425 PEEGPSEDSGPGGLGSRAqatNGGSERSQAPRSSGLRRQAIQNWQR-------RPRRHSTEGEEGDVSDVGSRTTESEAE 497
Cdd:PHA03307  258 PRPAPITLPTRIWEASGW---NGPSSRPGPASSSSSPRERSPSPSPsspgsgpAPSSPRASSSSSSSRESSSSSTSSSSE 334
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092   498 GPSD-VPRPGPAVAGPLNSCRLSARPEGGS-GRGRRVERGSPSRSNEVISPEILKMRAAL 555
Cdd:PHA03307  335 SSRGaAVSPGPSPSRSPSPSRPPPPADPSSpRKRPRPSRAPSSPAASAGRPTRRRARAAV 394
FBOX smart00256
A Receptor for Ubiquitination Targets;
555-587 6.01e-03

A Receptor for Ubiquitination Targets;


Pssm-ID: 197608  Cd Length: 41  Bit Score: 35.11  E-value: 6.01e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 47564092    555 LFCIFTYLDTRTLLHAAEVCRDWRFVARHPAVW 587
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 ...
545-591 1.51e-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: 91.24  E-value: 1.51e-22
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 47564092 545 SPEILKMRAALFCIFTYLDTRTLLHAAEVCRDWRFVARHPAVWTRVL 591
Cdd:cd22109   1 SLESLRRRDALFCVFSYLDTKSLLRCAEVCREWRDVSRHPALWQRVC 47
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
200-342 1.02e-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: 1.02e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092 200 LARLKIRALEKLEVDRRLERLSEEVEQKIAgQVGRLQAELERKAAELETARQESARLGREKEELEERASELSRQVDVSVE 279
Cdd:COG1196 231 LLKLRELEAELEELEAELEELEAELEELEA-ELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE 309
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 47564092 280 LLASLKQDLVHKEQELSRKQQEVVQIDQFLKETAAREASAKLRLQQFIEELLERADRAERQLQ 342
Cdd:COG1196 310 RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
197-342 3.36e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 64.19  E-value: 3.36e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092 197 EEGLARLKIRALEKLEVDRRLERLSEEVEQKIAgQVGRLQAELERKAAELETARQESARLGREKEELEERASELSRQVDV 276
Cdd:COG1196 249 EELEAELEELEAELAELEAELEELRLELEELEL-ELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAE 327
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 47564092 277 SVELLASLKQDLVHKEQELSRKQQEVVQIDQFLKETAAREASAKLRLQQFIEELLERADRAERQLQ 342
Cdd:COG1196 328 LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
202-342 4.38e-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: 4.38e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092 202 RLKIRALEKLEVDRRLERL----SEEVEQKIAGQVGRLQAELERKAAELETARQESARLGREKEELEERASELSRQVDVS 277
Cdd:COG1196 291 YELLAELARLEQDIARLEErrreLEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA 370
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 47564092 278 VELLASLKQDLVHKEQELSRKQQEVVQIDQFLKETAAREASAKLRLQQFIEELLERADRAERQLQ 342
Cdd:COG1196 371 EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEE 435
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
197-347 7.24e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 63.03  E-value: 7.24e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092 197 EEGLARLKIRALEKLEVDRRLERLSEEVEQkiagqvgrLQAELERKAAELETARQESARLGREKEELEERASELSRQVDV 276
Cdd:COG1196 221 ELKELEAELLLLKLRELEAELEELEAELEE--------LEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYE 292
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 47564092 277 SVELLASLKQDLVHKEQELSRKQQEVVQIDQFLKETAAREASAKLRLQQFIEELLERADRAERQLQVISSS 347
Cdd:COG1196 293 LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
201-346 9.27e-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: 9.27e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092 201 ARLKIRALEKLEVDRRLERLSEEvEQKIAGQVGRLQAELERKAAELETARQESARLGREKEELEERASELSRQVDVSVEL 280
Cdd:COG1196 267 AELEELRLELEELELELEEAQAE-EYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEE 345
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 47564092 281 LASLKQDLVHKEQELSRKQQEVVQIDQFLKETAAREASAKLRLQQFIEELLERADRAERQLQVISS 346
Cdd:COG1196 346 LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEA 411
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
201-342 9.76e-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: 9.76e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092 201 ARLKIRALEKLEVDRRLERLSEEvEQKIAGQVGRLQAELERKAAELETARQESARLGREKEELEERASELSRQVDVSVEL 280
Cdd:COG1196 302 QDIARLEERRRELEERLEELEEE-LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 47564092 281 LASLKQDLVHKEQELSRKQQEVVQIDQFLKETAAREA---SAKLRLQQFIEELLERADRAERQLQ 342
Cdd:COG1196 381 LEELAEELLEALRAAAELAAQLEELEEAEEALLERLErleEELEELEEALAELEEEEEEEEEALE 445
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
195-342 1.13e-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: 1.13e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092 195 AYEEGLARLKIRALEKLEVDRRLERLSEEVEQKIAG------QVGRLQAELERKAAELETARQESARLGREKEELEERAS 268
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAEleelrlELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 47564092 269 ELSRQVDVSVELLASLKQDLVHKEQELSRKQQEVVQIDQFLKETAAREASAKLRLQQFIEELLERADRAERQLQ 342
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE 386
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
201-342 1.13e-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: 1.13e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092 201 ARLKIRALEkLEVDRRLERLSEEVEQ--KIAGQVGRLQAELERKAAELETARQESARLGREKEELEERASELSRQVDVSV 278
Cdd:COG1196 272 LRLELEELE-LELEEAQAEEYELLAElaRLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAE 350
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 47564092 279 ELLASLKQDLVHKEQELSRKQQEVVQIDQFLKETAAREASAKLRLQQFIEELLERADRAERQLQ 342
Cdd:COG1196 351 EELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE 414
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
209-344 9.84e-09

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 58.38  E-value: 9.84e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092 209 EKLEVDRRLERLSEEVEQKIAgQVGRLQAELERKAAELETARQESARLGREKEELEERASELSRQVDVSVELLASLKQDL 288
Cdd:COG4372  74 ELEQLEEELEELNEQLQAAQA-ELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEEL 152
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 47564092 289 VHKEQELSRKQQEVVQIDQFLKETAAREASAKlrlqqfIEELLERADRAERQLQVI 344
Cdd:COG4372 153 KELEEQLESLQEELAALEQELQALSEAEAEQA------LDELLKEANRNAEKEEEL 202
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
197-342 1.81e-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: 1.81e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092 197 EEGLARLKIRALEKLEVDRRLERLSEEVEQKIAGQVGRLQAELERKAAELETARQESARLGREKEELEERASELSR---Q 273
Cdd:COG1196 273 RLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEaeeE 352
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 47564092 274 VDVSVELLASLKQDLVHKEQELSRKQQEVVQIDQFLKETAAREASAKLRLQQFIEELLERADRAERQLQ 342
Cdd:COG1196 353 LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
200-344 3.38e-08

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 56.45  E-value: 3.38e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092 200 LARLKIRALEKLEVDRRLERLSEEVEQ--KIAGQVGRLQAELERKAAELETARQESARLGREKEELEERASELSRQVDVS 277
Cdd:COG4372  13 LSLFGLRPKTGILIAALSEQLRKALFEldKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAA 92
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092 278 VELLASLKQDLVHKEQELSRKQQEVVQID---QFLKETAAREASAKLRLQQFIEELLERADRAERQLQVI 344
Cdd:COG4372  93 QAELAQAQEELESLQEEAEELQEELEELQkerQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESL 162
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
216-344 3.96e-08

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 56.45  E-value: 3.96e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092 216 RLERLSEEVEQkIAGQVGRLQAELERKAAELETARQESARLGREKEELEERASELSRQVDVSVELLASLKQDLVHKEQEL 295
Cdd:COG4372  39 ELDKLQEELEQ-LREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEEL 117
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 47564092 296 SRKQQEVVQIDQFLKETAAREASAKLRL---QQFIEELLERADRAERQLQVI 344
Cdd:COG4372 118 EELQKERQDLEQQRKQLEAQIAELQSEIaerEEELKELEEQLESLQEELAAL 169
F-box-like pfam12937
F-box-like; This is an F-box-like family.
555-590 1.07e-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: 1.07e-07
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 47564092   555 LFCIFTYLDTRTLLHAAEVCRDWRFVARHPAVWTRV 590
Cdd:pfam12937   9 LLQIFSYLDPKDLLRLALVCRRWRELASDDSLWRRL 44
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
197-345 1.13e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 55.54  E-value: 1.13e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092 197 EEGLARLKIRALEKLEVDRRLERLSEEVEQKIAGQVGRLQaELERKAAELETARQESARLGREKEELEERASELSRQVDV 276
Cdd:COG4717 110 ELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLE-ELEERLEELRELEEELEELEAELAELQEELEELLEQLSL 188
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092 277 SVEL-LASLKQDLVHKEQELSRKQQEVVQIDQFLKEtaAREASAKLRLQQFIEELLERADRAERQLQVIS 345
Cdd:COG4717 189 ATEEeLQDLAEELEELQQRLAELEEELEEAQEELEE--LEEELEQLENELEAAALEERLKEARLLLLIAA 256
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
201-342 1.64e-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: 1.64e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092  201 ARLKIRALEKL-EVDRRLERLSEEVEQKIAGqvgRLQAELERKAAELETARQESARLGREKEELEERASELSRQVD---- 275
Cdd:COG4913  247 AREQIELLEPIrELAERYAAARERLAELEYL---RAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDalre 323
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092  276 -----------VSVELLASLKQDLVHKEQELSRKQQEVVQIDQF---LKETAAREASAKLRLQQFIEELLERADRAERQL 341
Cdd:COG4913  324 eldeleaqirgNGGDRLEQLEREIERLERELEERERRRARLEALlaaLGLPLPASAEEFAALRAEAAALLEALEEELEAL 403

                 .
gi 47564092  342 Q 342
Cdd:COG4913  404 E 404
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
195-344 1.91e-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: 1.91e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092 195 AYEEGLARLKIRALEKLEVDRRLERLSEEVEQKIAGQVgRLQAELERKAAELETARQESARLGREKEELEERASELSrqv 274
Cdd:COG1196 359 ELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA-ELAAQLEELEEAEEALLERLERLEEELEELEEALAELE--- 434
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092 275 dvsvELLASLKQDLVHKEQELSRKQQEVVQIDQFLKETAAREASAKLRLQQFIEELLERADRAERQLQVI 344
Cdd:COG1196 435 ----EEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAE 500
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
204-347 2.04e-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: 53.00  E-value: 2.04e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092 204 KIRALEKL-EVDRRLERLsEEVEQKIAGQVGRLQAELERKAAELETARQESARLGREKEELEERASELSRQVDVS----- 277
Cdd:COG1579   5 DLRALLDLqELDSELDRL-EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYeeqlg 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092 278 --------------VELLASLKQDLVHKEQEL----SRKQQEVVQIDQFLKETAAREASAKLRLQQFIEELLERADRAER 339
Cdd:COG1579  84 nvrnnkeyealqkeIESLKRRISDLEDEILELmeriEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEA 163

                ....*...
gi 47564092 340 QLQVISSS 347
Cdd:COG1579 164 EREELAAK 171
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
196-342 2.81e-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: 2.81e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092  196 YEEGLARLKIRALEKLEVDRRLERLSEEVEQkIAGQVGRLQAELERKAAELETAR--------QESARLGREKEELEERA 267
Cdd:COG4913  276 YLRAALRLWFAQRRLELLEAELEELRAELAR-LEAELERLEARLDALREELDELEaqirgnggDRLEQLEREIERLEREL 354
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 47564092  268 SELSRQVDVSVELLASLKQDLVHKEQELSRKQQEVVQIDQFLKETAAREASAKLRLQQFIEELLERADRAERQLQ 342
Cdd:COG4913  355 EERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIA 429
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
217-330 3.39e-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: 3.39e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092   217 LERLSEEVEQKI---AGQVGRLQAELERKAAELETARQESARLGREKEELEERASELSRQVDVSVELLASLKQDLVHKEQ 293
Cdd:TIGR04523 459 LDNTRESLETQLkvlSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKES 538
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 47564092   294 ELSRKQQEVVQIDQFLKETAAREasAKLRLQQFIEEL 330
Cdd:TIGR04523 539 KISDLEDELNKDDFELKKENLEK--EIDEKNKEIEEL 573
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
195-346 3.43e-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: 3.43e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092    195 AYEEGLARLKiraLEKLEVDRRLERLSEEVEQkIAGQVGRLQAELERKAAELETARQESARLGREKEELEERASELSRQV 274
Cdd:TIGR02168  264 ELEEKLEELR---LEVSELEEEIEELQKELYA-LANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEEL 339
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092    275 DVSVELLASLKQDLVHKEQELSRKQQEVVQIDQFLKE-----TAAREASAKLRLQ--------QFIEELLER-ADRAERQ 340
Cdd:TIGR02168  340 AELEEKLEELKEELESLEAELEELEAELEELESRLEEleeqlETLRSKVAQLELQiaslnneiERLEARLERlEDRRERL 419

                   ....*.
gi 47564092    341 LQVISS 346
Cdd:TIGR02168  420 QQEIEE 425
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
195-336 3.45e-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: 52.23  E-value: 3.45e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092 195 AYEEGLARLKIrALEKLEVD-RRLERLSEEVEQKIAgqvgRLQAELE--RKAAELETARQESARLGREKEELEERASELS 271
Cdd:COG1579  42 ALEARLEAAKT-ELEDLEKEiKRLELEIEEVEARIK----KYEEQLGnvRNNKEYEALQKEIESLKRRISDLEDEILELM 116
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 47564092 272 RQVDVSVELLASLKQDLVHKEQELSRKQQEvvqIDQFLKETAAREASAKLRLQQFI----EELLERADR 336
Cdd:COG1579 117 ERIEELEEELAELEAELAELEAELEEKKAE---LDEELAELEAELEELEAEREELAakipPELLALYER 182
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
211-322 3.83e-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: 3.83e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092 211 LEVDRRLERLSEEVE--QKIAGQVGRLQAELERKAAELETARQESARLgreKEELEERASELSRQVDVSVELLASLKQDL 288
Cdd:COG4942 132 LDAVRRLQYLKYLAParREQAEELRADLAELAALRAELEAERAELEAL---LAELEEERAALEALKAERQKLLARLEKEL 208
                        90       100       110
                ....*....|....*....|....*....|....
gi 47564092 289 VHKEQELSRKQQEVVQIDQFLKETAAREASAKLR 322
Cdd:COG4942 209 AELAAELAELQQEAEELEALIARLEAEAAAAAER 242
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
202-344 6.04e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 53.23  E-value: 6.04e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092 202 RLKIRALEKLEVDRRLERLSEEVEQKIAGQVGRLQAELERKAAELETARQESARLGR---------EKEELEERASELSR 272
Cdd:COG4717  67 ELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKllqllplyqELEALEAELAELPE 146
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 47564092 273 QVDV---SVELLASLKQDLVHKEQELSRKQQEVVQIDQFLKETAAREASaklRLQQFIEELLERADRAERQLQVI 344
Cdd:COG4717 147 RLEEleeRLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQ---DLAEELEELQQRLAELEEELEEA 218
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
211-346 8.30e-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: 8.30e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092    211 LEVDRRLERLSEEVEQkIAGQVGRLQAELERKAAELETARQESARLGREKEELEERASELSRQVDVSVELLASLKQDLVH 290
Cdd:TIGR02168  673 LERRREIEELEEKIEE-LEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQ 751
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 47564092    291 KEQELSRKQQEVVQIDQFLKEtaarEASAKLRLQQFIEELLERADRAERQLQVISS 346
Cdd:TIGR02168  752 LSKELTELEAEIEELEERLEE----AEEELAEAEAEIEELEAQIEQLKEELKALRE 803
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
197-342 1.05e-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: 1.05e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092    197 EEGLARLK-IRAleklEVDRRLERLSEEVEQkiAGQVGRLQAEL------------ERKAAELETARQESARLGREKEEL 263
Cdd:TIGR02168  185 RENLDRLEdILN----ELERQLKSLERQAEK--AERYKELKAELrelelallvlrlEELREELEELQEELKEAEEELEEL 258
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 47564092    264 EERASELSRQVDVSVELLASLKQDLVHKEQELSRKQQEVVQIDQFLKETAAREAsaklRLQQFIEELLERADRAERQLQ 342
Cdd:TIGR02168  259 TAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLA----NLERQLEELEAQLEELESKLD 333
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
197-345 1.19e-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: 1.19e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092    197 EEGLARLKIRALEKLEVDRRLERLSEEVEQKIAG---QVGRLQAELERKAAELETARQESARLGREKEELEERASELSRQ 273
Cdd:TIGR02168  732 RKDLARLEAEVEQLEERIAQLSKELTELEAEIEEleeRLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAE 811
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 47564092    274 VDVSVELLASLKQDLVHKEQELSRKQQEVVQIDQFLKETAAREASAKLRlqqfIEELLERADRAERQLQVIS 345
Cdd:TIGR02168  812 LTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAE----IEELEELIEELESELEALL 879
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
209-341 1.47e-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: 1.47e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092    209 EKLEVDRRLERLSEEVEQkIAGQVGRLQAELERKAAELETARQESARLGREKEELEERASELSRQVDVSVELLASLKQDL 288
Cdd:TIGR02168  324 QLEELESKLDELAEELAE-LEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEI 402
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 47564092    289 VHKEQELS-------RKQQEVVQIDQFLKETAAREASAKL-RLQQFIEELLERADRAERQL 341
Cdd:TIGR02168  403 ERLEARLErledrreRLQQEIEELLKKLEEAELKELQAELeELEEELEELQEELERLEEAL 463
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
209-512 1.48e-06

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 51.37  E-value: 1.48e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092 209 EKLEVDRRLERLSEEVEQKIAgQVGRLQAELERKAAELETARQE----SARLGREKEELEERASE--------------- 269
Cdd:COG3883  31 ELEAAQAELDALQAELEELNE-EYNELQAELEALQAEIDKLQAEiaeaEAEIEERREELGERARAlyrsggsvsyldvll 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092 270 --------LSRQVDVS---------VELLASLKQDLVHKEQELSRKQQEVVQIDQFLKETAAREASAKLRLQQFIEELLE 332
Cdd:COG3883 110 gsesfsdfLDRLSALSkiadadadlLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSA 189
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092 333 RADRAERQLQVISSSCGSTPSASLGRGGGGSASGPGVRGPGrmrehhAGSAVPSTYAVSRHGSSPSTGASSRVPAASQSS 412
Cdd:COG3883 190 EEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA------AAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAG 263
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092 413 GCYDSDSLELPRPEEGPSEDSGPGGLGSRAQATNGGSERSQAPRSSGLRRQAIQNWQRRPRRHSTEGEEGDVSDVGSRTT 492
Cdd:COG3883 264 AAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAASGGSGGGSGGAGGVGSGGGAGAVVGGASAGGGGGSGGGGGSSGG 343
                       330       340
                ....*....|....*....|
gi 47564092 493 ESEAEGPSDVPRPGPAVAGP 512
Cdd:COG3883 344 GSGGGGGGGGGGGGSSSGGG 363
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
202-342 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 47564092    202 RLKIRALEK--LEVDRRLERLSEEVEQKiAGQVGRLQAELERKAAELETARQESARLGREKEELEERASELSRQVDVSVE 279
Cdd:TIGR02169  335 LAEIEELEReiEEERKRRDKLTEEYAEL-KEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQE 413
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 47564092    280 LLASLKQDLVHKEQELSRKQQEVVQIDQFLKETAAREASAKLRLQQfIEELLERADRAERQLQ 342
Cdd:TIGR02169  414 ELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQ-LAADLSKYEQELYDLK 475
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
209-329 3.09e-06

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 51.22  E-value: 3.09e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092    209 EKLEVDRRLERLSEEVEQkIAGQVGRLQAELERKAAELETARQESARLGREKEELEERASELSRQVDVSVELLASLKQDL 288
Cdd:TIGR02169  386 ELKDYREKLEKLKREINE-LKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADL 464
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 47564092    289 VHKEQELSRKQQEVVQIDQFLKEtAAREASAKLRLQQFIEE 329
Cdd:TIGR02169  465 SKYEQELYDLKEEYDRVEKELSK-LQRELAEAEAQARASEE 504
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
197-342 3.23e-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: 3.23e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092 197 EEGLARLKIRALEKLEVDRRLERLSEEVEQKIAGQVGRLQAELERKAAELETARQESARLGREKEELEERASELSRQVDV 276
Cdd:COG1196 633 EAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEA 712
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 47564092 277 SVELLASLKQDLVHKEQELSRKQQEVVQIDQFLKETAAREASAKLRLQQfIEELLERADRAERQLQ 342
Cdd:COG1196 713 EEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPD-LEELERELERLEREIE 777
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
197-344 8.91e-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: 8.91e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092  197 EEGLARL--KIRALEKL--EVDRRLERLSEEVEQKIAGQVGRLQAELERKAAELETARQESARLGR-----------EKE 261
Cdd:COG4913  301 RAELARLeaELERLEARldALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEAllaalglplpaSAE 380
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092  262 ELEERASELSRQVDVSVELLASLKQDLVHKEQELSRKQQEVVQIDQFLKETAAREASAKLRLQQFIEELLERADRAERQL 341
Cdd:COG4913  381 EFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLDEAEL 460

                 ...
gi 47564092  342 QVI 344
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 ...
546-587 1.06e-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: 1.06e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 47564092 546 PEILKMraalfcIFTYLDTRTLLHAAEVCRDWRFVARHPAVW 587
Cdd:cd22125   5 PEILAM------IFSYLDVRDKGRAAQVCTAWRDAAYHKSVW 40
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
194-324 1.10e-05

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


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 47.51  E-value: 1.10e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092 194 VAYEEGLARLKirALEKlevdrRLERLSEEVEQKIAgqvgrlqaELERKAAE-LETARQESARLG-REKEELEERASELS 271
Cdd:COG1842  40 VEARQALAQVI--ANQK-----RLERQLEELEAEAE--------KWEEKARLaLEKGREDLAREAlERKAELEAQAEALE 104
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 47564092 272 RQVDVSVELLASLKQDLVHKEQELSRKQQEvvqidqfLKETAAREASAKLRLQ 324
Cdd:COG1842 105 AQLAQLEEQVEKLKEALRQLESKLEELKAK-------KDTLKARAKAAKAQEK 150
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
202-343 1.34e-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: 1.34e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092    202 RLKIRALEKLE-VDRRLERLSEEVEQKIAgQVGRLQAELERK------------------AAELETARQESARLGREKEE 262
Cdd:TIGR02169  170 RKKEKALEELEeVEENIERLDLIIDEKRQ-QLERLRREREKAeryqallkekreyegyelLKEKEALERQKEAIERQLAS 248
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092    263 LEERASELSRQVDVSVELLASLKQDLVHKEQELSRK-QQEVVQIDQFLKETAAREASAKlRLQQFIEELLERADRAERQL 341
Cdd:TIGR02169  249 LEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLE-RSIAEKERELEDAEERLAKL 327

                   ..
gi 47564092    342 QV 343
Cdd:TIGR02169  328 EA 329
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
201-341 1.55e-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: 1.55e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092  201 ARLKIRALEK-LEVDRRLERLSEEvEQKIAGQVGRLqAELERKAAELETARQESARLGREKEELEERASELSRQVDVSVE 279
Cdd:COG4913  636 LEAELDALQErREALQRLAEYSWD-EIDVASAEREI-AELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKG 713
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 47564092  280 LLASLKQDLVHKEQELSRKQQEVVQI------------DQFLKETAAREASAKLR--LQQFIEELLERADRAERQL 341
Cdd:COG4913  714 EIGRLEKELEQAEEELDELQDRLEAAedlarlelrallEERFAAALGDAVERELRenLEERIDALRARLNRAEEEL 789
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
206-342 1.64e-05

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 47.60  E-value: 1.64e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092 206 RALEKLEvdRRLER--LSEEVEQKIAGQVGRLQAELERKAAELE------TARQESARLGREKEELEERASELSRQVDVS 277
Cdd:COG1340 116 KEIERLE--WRQQTevLSPEEEKELVEKIKELEKELEKAKKALEkneklkELRAELKELRKEAEEIHKKIKELAEEAQEL 193
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092 278 VELLASLKQ---------DLVHKE------------QELSRKQQEVVQIDQFLKETAAREASAKLRLQQfiEELLERADR 336
Cdd:COG1340 194 HEEMIELYKeadelrkeaDELHKEiveaqekadelhEEIIELQKELRELRKELKKLRKKQRALKREKEK--EELEEKAEE 271

                ....*.
gi 47564092 337 AERQLQ 342
Cdd:COG1340 272 IFEKLK 277
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
197-341 1.69e-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: 1.69e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092 197 EEGLARLKIRALEKLEVDRRLERLSEEVEQKIAGQVGRLQAELERKAAELETARQESARLGREKEELEERASELSRQVDV 276
Cdd:COG1196 409 EEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAE 488
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 47564092 277 SVELLASLKQDL------------VHKEQELSRKQQEVVQIDQFLKE-TAAREASAKLRLQQFIEELLERADRAERQL 341
Cdd:COG1196 489 AAARLLLLLEAEadyegflegvkaALLLAGLRGLAGAVAVLIGVEAAyEAALEAALAAALQNIVVEDDEVAAAAIEYL 566
PRK12705 PRK12705
hypothetical protein; Provisional
202-344 3.04e-05

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 47.40  E-value: 3.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092  202 RLKIRALEKLEVDRRLERLSEEVEQKiagqvgRLQAELERKAAELETARQESARLGREKEEL---EERASELSRQVDVSV 278
Cdd:PRK12705  24 LLKKRQRLAKEAERILQEAQKEAEEK------LEAALLEAKELLLRERNQQRQEARREREELqreEERLVQKEEQLDARA 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092  279 ELLASLKQDLVHKEQELSRKQQEVV----QIDQFLKETA------AR-------EASAKLRLQQFIEELLERAD-RAERQ 340
Cdd:PRK12705  98 EKLDNLENQLEEREKALSARELELEelekQLDNELYRVAgltpeqARklllkllDAELEEEKAQRVKKIEEEADlEAERK 177

                 ....
gi 47564092  341 LQVI 344
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 ...
554-593 3.38e-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: 3.38e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 47564092 554 ALFCIFTYLDTRTLLHAAEVCRDWRFVARHPAVWTRVLLE 593
Cdd:cd22104   8 VLVHIFSYLPPRDRLRASSTCRRWREALFHPSLWRSLRLH 47
HlpA COG2825
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ...
222-337 3.60e-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: 45.21  E-value: 3.60e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092 222 EEVEQKIAGQVGRLQAELERKAAELETarqesarlgrEKEELEERASELSRqvdvsvELLASLKQDLVHKEQELSRKQQE 301
Cdd:COG2825  42 KAAQKKLEKEFKKRQAELQKLEKELQA----------LQEKLQKEAATLSE------EERQKKERELQKKQQELQRKQQE 105
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 47564092 302 vvqidqflketaaREASAKLRLQQFIEELLERADRA 337
Cdd:COG2825 106 -------------AQQDLQKRQQELLQPILEKIQKA 128
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
225-351 4.04e-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: 4.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092  225 EQKIAgqvgRLQAELERKAAELETARQESARLGREKEELEERASELSRQVDVSVELLaslkqDLVHKEQELSRKQQEVVQ 304
Cdd:COG4913  609 RAKLA----ALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEI-----DVASAEREIAELEAELER 679
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 47564092  305 IDqflketaarEASAKLR-LQQFIEELLERADRAERQLQVISSSCGST 351
Cdd:COG4913  680 LD---------ASSDDLAaLEEQLEELEAELEELEEELDELKGEIGRL 718
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
222-316 4.57e-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: 4.57e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092    222 EEVEQKIAGQVGRLQAELERKAAELETARQEsarLGREKEEL-EERASELSRQVDVSVELLASLKQDLvhkEQELSRKQQ 300
Cdd:smart00935  17 KAAQKQLEKEFKKRQAELEKLEKELQKLKEK---LQKDAATLsEAAREKKEKELQKKVQEFQRKQQKL---QQDLQKRQQ 90
                           90       100
                   ....*....|....*....|.
gi 47564092    301 EVVQ-----IDQFLKETAARE 316
Cdd:smart00935  91 EELQkildkINKAIKEVAKKK 111
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
221-342 4.85e-05

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 47.13  E-value: 4.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092  221 SEEVEQKIAGqVGRLQAELERKAAELETARQESARLgreKEELEERASELSRQvdvsvellaslkqdlvhKEQELSRKQQ 300
Cdd:PRK00409 515 KEKLNELIAS-LEELERELEQKAEEAEALLKEAEKL---KEELEEKKEKLQEE-----------------EDKLLEEAEK 573
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 47564092  301 EVVQIDQFLKETAAREASAKLRLQQfieelLERADRAERQLQ 342
Cdd:PRK00409 574 EAQQAIKEAKKEADEIIKELRQLQK-----GGYASVKAHELI 610
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
202-331 5.04e-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: 5.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092  202 RLKIRALEK-LEVDRRLERLSEEVEQKIAGQV----------GRLQAELERKAAELETARQESARLGREKEELEERASEL 270
Cdd:COG3096  518 RAQLAELEQrLRQQQNAERLLEEFCQRIGQQLdaaeeleellAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKEL 597
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 47564092  271 SRQVDVSVELLASLKQDLVHKEQELSRKQqevvQIDQFLKETAARE----------ASAKLRLQQFIEELL 331
Cdd:COG3096  598 AARAPAWLAAQDALERLREQSGEALADSQ----EVTAAMQQLLEREreatverdelAARKQALESQIERLS 664
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
222-316 5.20e-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: 44.10  E-value: 5.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092   222 EEVEQKIAGQVGRLQAELERKAAELETARQE-SARLGREKEELEERASELSRQVDVSVELLASLKQDLVHKEQELSRKQQ 300
Cdd:pfam03938  18 KAAQAQLEKKFKKRQAELEAKQKELQKLYEElQKDGALLEEEREEKEQELQKKEQELQQLQQKAQQELQKKQQELLQPIQ 97
                          90
                  ....*....|....*.
gi 47564092   301 EvvQIDQFLKETAARE 316
Cdd:pfam03938  98 D--KINKAIKEVAKEK 111
flagell_FliJ TIGR02473
flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly ...
216-348 5.56e-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: 5.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092   216 RLERLSEEVEQKIAGQVGRLQAELERKAAELEtarqesaRLGREKEELEERASELSRQVDVSVEL------LASLKQDLV 289
Cdd:TIGR02473   6 KLLDLREKEEEQAKLELAKAQAEFERLETQLQ-------QLIKYREEYEQQALEKVGAGTSALELsnyqrfIRQLDQRIQ 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092   290 HKEQELSRKQQEVVQI-DQFLKETAAREASAKLRLQQFIEELLERADRAERQLQVISSSC 348
Cdd:TIGR02473  79 QQQQELALLQQEVEAKrERLLEARRELKALEKLKEKKQKEYRAEEAKREQKEMDELATQR 138
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
236-323 6.38e-05

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 46.87  E-value: 6.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092   236 QAELERKAAELETARQESARLGREKEELEERASELSRQVDVSVELLASLKQDLVHKEQELSRKQQEVVQIDQFLKE---T 312
Cdd:PRK11448  141 ENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQERKQkrkE 220
                          90
                  ....*....|.
gi 47564092   313 AAREASAKLRL 323
Cdd:PRK11448  221 ITDQAAKRLEL 231
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
205-340 6.74e-05

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 46.40  E-value: 6.74e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092 205 IRALEKLEVDRRLERlsEEVEQKiaGQVGRLQAELERKAAELETARQ-ESARLGREKEELEERASELSRQVDVsvellAS 283
Cdd:COG2268 191 RRKIAEIIRDARIAE--AEAERE--TEIAIAQANREAEEAELEQEREiETARIAEAEAELAKKKAEERREAET-----AR 261
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092 284 LKQDLVHKEQElSRKQQEV---VQIDQFLKETAAREASAKLRLQQFIEELLERADrAERQ 340
Cdd:COG2268 262 AEAEAAYEIAE-ANAEREVqrqLEIAEREREIELQEKEAEREEAELEADVRKPAE-AEKQ 319
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
202-332 8.00e-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: 8.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092   202 RLKIRALEKLEVDRRLERLSEEVEqKIAGQVgrlqAELERKAAELETARQEsarLGREKEELEERASELSRQVDVSVELL 281
Cdd:TIGR04523 413 QIKKLQQEKELLEKEIERLKETII-KNNSEI----KDLTNQDSVKELIIKN---LDNTRESLETQLKVLSRSINKIKQNL 484
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 47564092   282 ASLKQDLVHKEQELSRKQQEVVQIDQFLKETAAREASAKLRLQQFIEELLE 332
Cdd:TIGR04523 485 EQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKE 535
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
197-341 8.39e-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: 8.39e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092    197 EEGLARLKIRALEKLEVDRRLERLSEEVEQKIAgQVGRLQAELERKAAELetARQESARLGREKEELEERASELSRQVDV 276
Cdd:TIGR02169  740 EELEEDLSSLEQEIENVKSELKELEARIEELEE-DLHKLEEALNDLEARL--SHSRIPEIQAELSKLEEEVSRIEARLRE 816
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 47564092    277 SVELLASLKQDLVHKEQELSRKQQEVVQIDQFLKETAAREASAKLRLQQFIEElLERADRAERQL 341
Cdd:TIGR02169  817 IEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEE-LEELEAALRDL 880
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
202-342 8.66e-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: 8.66e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092 202 RLKIRALEKLEVDRRLERLSEEVEQKIAGQVGRLQAELERkaaELETARQESARLGREKEELEERASELSRQvdvsvelL 281
Cdd:COG2433 367 EVKARVIRGLSIEEALEELIEKELPEEEPEAEREKEHEER---ELTEEEEEIRRLEEQVERLEAEVEELEAE-------L 436
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 47564092 282 ASLKQDLVHKEQELSRKQQEVVQIDQFLKETAAREASAKlRLQQFIEELLERADRAERQLQ 342
Cdd:COG2433 437 EEKDERIERLERELSEARSEERREIRKDREISRLDREIE-RLERELEEERERIEELKRKLE 496
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
199-339 9.22e-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: 9.22e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092    199 GLARLKIRALEKLEVDRRLERLSEEVEQkiagqvgrLQAELERKAAELETARQESARLGREKEELEERASELSRQVDVSV 278
Cdd:TIGR02169  658 GSRAPRGGILFSRSEPAELQRLRERLEG--------LKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLE 729
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 47564092    279 ELLASLKQDLVHKEQELSRKQQEVVQIDQFLKETAAREASAKLRLQQFIEEL--LERADRAER 339
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, ...
555-591 9.97e-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: 9.97e-05
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 47564092 555 LFCIFTYLDTRTLLHAAEVCRDWRFVARHPAVWTRVL 591
Cdd:cd22132   9 LLHIFSYLSPKDLLAAGQVCKQWYRVSRDEFLWKELF 45
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
202-347 1.08e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 45.66  E-value: 1.08e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092 202 RLKIRALEKLEVDRRLERLSEEVEQKIAGQVGRLQAELERKAAELETARQESARLGREKEELEERASELSRQVDVSVELL 281
Cdd:COG4372   3 RLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL 82
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 47564092 282 ASLKQDLVHKEQELSRKQQEVVQIDQFLKETAAREAsaklRLQQFIEELLERADRAERQLQVISSS 347
Cdd:COG4372  83 EELNEQLQAAQAELAQAQEELESLQEEAEELQEELE----ELQKERQDLEQQRKQLEAQIAELQSE 144
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
201-342 1.16e-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: 46.20  E-value: 1.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092    201 ARLKIRALEKLEVDRRLERLSEEVEQ------KIAGQVGRLQAELERK--------------AAELETARQESARLGREK 260
Cdd:TIGR02168  225 LELALLVLRLEELREELEELQEELKEaeeeleELTAELQELEEKLEELrlevseleeeieelQKELYALANEISRLEQQK 304
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092    261 EELEERASELSRQVDVSVELLASLKQDLVHKEQELSRKQQEVVQIDQFLKETAAREASAKLRLQQF------IEELLERA 334
Cdd:TIGR02168  305 QILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELesrleeLEEQLETL 384

                   ....*...
gi 47564092    335 DRAERQLQ 342
Cdd:TIGR02168  385 RSKVAQLE 392
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
212-342 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 47564092    212 EVDRRLERLSEEVEQkIAGQVGRLQAELERKAAELEtarqesaRLGREKEELEERASELSRQVDVSVELLASLKQDLVHK 291
Cdd:TIGR02169  167 EFDRKKEKALEELEE-VEENIERLDLIIDEKRQQLE-------RLRREREKAERYQALLKEKREYEGYELLKEKEALERQ 238
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 47564092    292 ----EQELSRKQQEVVQIDQFLKETAAREASAKLRLQQFIEELLERADRAERQLQ 342
Cdd:TIGR02169  239 keaiERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVK 293
F-box_AtGID2-like cd22151
F-box domain found in Arabidopsis thaliana F-box protein GID2 and similar proteins; AtGID2, ...
555-587 1.24e-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: 1.24e-04
                        10        20        30
                ....*....|....*....|....*....|...
gi 47564092 555 LFCIFTYLDTRTLLHAAEVCRDWRFVARHPAVW 587
Cdd:cd22151   8 LQEIFKRLDPKSLARAACVCRRWRAAARSESLW 40
F-box_FBXL13 cd22124
F-box domain found in F-box/LRR-repeat protein 13 (FBXL13) and similar proteins; FBXL13, also ...
551-588 1.30e-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: 1.30e-04
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 47564092 551 MRAALFCIFTYLDTRTLLHAAEVCRDWRFVARHPAVWT 588
Cdd:cd22124   5 PRKAALKIFSYLDLRDLARCAQVCRSWKVITQSSSLWS 42
mukB PRK04863
chromosome partition protein MukB;
202-336 1.36e-04

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 45.72  E-value: 1.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092   202 RLKIRALEK-LEVDRRLERLSEEVEQKIAGQV----------GRLQAELERKAAELETARQESARLGREKEELEERASEL 270
Cdd:PRK04863  519 RMRLSELEQrLRQQQRAERLLAEFCKRLGKNLddedeleqlqEELEARLESLSESVSEARERRMALRQQLEQLQARIQRL 598
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 47564092   271 SRQVDVSVELLASLKQ--DLVHKEQELSRkqqevvQIDQFLKETAAREASAKL---RLQQFIEELLERADR 336
Cdd:PRK04863  599 AARAPAWLAAQDALARlrEQSGEEFEDSQ------DVTEYMQQLLERERELTVerdELAARKQALDEEIER 663
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
202-351 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 47564092    202 RLKIRALEKLEVDRRLERLSEEVEQkIAGQVGRLQAELERKAAELETARQESARLGREKEELEERASELS--RQVDVSVE 279
Cdd:TIGR02169  217 LKEKREYEGYELLKEKEALERQKEA-IERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGeeEQLRVKEK 295
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092    280 L------LASLKQDLVHKEQELSRKQQEVVQIDQFLKETAARE-------ASAKLRLQQFIEELLERADRAE---RQLQV 343
Cdd:TIGR02169  296 IgeleaeIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIeelereiEEERKRRDKLTEEYAELKEELEdlrAELEE 375

                   ....*...
gi 47564092    344 ISSSCGST 351
Cdd:TIGR02169  376 VDKEFAET 383
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
197-347 1.57e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.70  E-value: 1.57e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092 197 EE--GLARLKIR---ALEKLE-VDRRLERLS---EEVEQkiagQVGRL--QAELERKAAELetarqesarlgreKEELEE 265
Cdd:COG1196 162 EEaaGISKYKERkeeAERKLEaTEENLERLEdilGELER----QLEPLerQAEKAERYREL-------------KEELKE 224
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092 266 RASELsrqvdvsvellASLKQDLVHKEQELSRKQQEVVQIDQFLKETAAREASAKL-RLQQFIEELLERADRAERQLQVI 344
Cdd:COG1196 225 LEAEL-----------LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELeELRLELEELELELEEAQAEEYEL 293

                ...
gi 47564092 345 SSS 347
Cdd:COG1196 294 LAE 296
HIP1_clath_bdg pfam16515
Clathrin-binding domain of Huntingtin-interacting protein 1; HIP1_clath_bdg is the coiled-coil ...
237-299 1.77e-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: 41.53  E-value: 1.77e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 47564092   237 AELERKAAE----LETARQESARLGREKEELE---ERAS-ELSRQVDVSVELLASLKQDLVHKEQELSRKQ 299
Cdd:pfam16515   2 ADLLRKNAEttkqLTVAQQAQEEVEREKKQLEfelERAKeEAQMKLEEQKEELERLKRELESSRAELATLQ 72
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
197-340 1.87e-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: 1.87e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092 197 EEGLARLKIRaLEKLEvdRRLERLSEEVEQKIA-----GQVGRLQ--------AELERKAAELET---ARQESAR-LGRE 259
Cdd:COG4942  82 EAELAELEKE-IAELR--AELEAQKEELAELLRalyrlGRQPPLAlllspedfLDAVRRLQYLKYlapARREQAEeLRAD 158
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092 260 KEELEERASELSRQVDVSVELLASLKQDLVHKEQELSRKQQEVVQIDQFLKETAAREA---SAKLRLQQFIEELLERADR 336
Cdd:COG4942 159 LAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAelqQEAEELEALIARLEAEAAA 238

                ....
gi 47564092 337 AERQ 340
Cdd:COG4942 239 AAER 242
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
195-341 2.17e-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: 2.17e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092    195 AYEEGLARLKiRALEKLEvdrrlERLSEEVEQKIAGQVGRLQAELERKAAELETARQESARLGREKEELEERASELSRQV 274
Cdd:TIGR02169  769 ELEEDLHKLE-EALNDLE-----ARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQR 842
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 47564092    275 D------VSVE-LLASLKQDLVHKEQELSRKQQEVVQIDQFLKETAA--REASAKLR-LQQFIEELLERADRAERQL 341
Cdd:TIGR02169  843 IdlkeqiKSIEkEIENLNGKKEELEEELEELEAALRDLESRLGDLKKerDELEAQLReLERKIEELEAQIEKKRKRL 919
F-box_SF cd09917
F-box domain superfamily; This short domain is commonly found at the N-terminus of various ...
555-582 2.25e-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: 2.25e-04
                        10        20
                ....*....|....*....|....*...
gi 47564092 555 LFCIFTYLDTRTLLHAAEVCRDWRFVAR 582
Cdd:cd09917   8 LLKILSYLDPRDLLRLSLVCKRWRELAS 35
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
202-346 2.26e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.05  E-value: 2.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092  202 RLKIRALEKLEVDRRLERLSEEvEQKIAGQVGRLQAELER---KAAELETARQESARLGREKEELEERASELSRQVDVSV 278
Cdd:PRK03918 194 LIKEKEKELEEVLREINEISSE-LPELREELEKLEKEVKEleeLKEEIEELEKELESLEGSKRKLEEKIRELEERIEELK 272
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 47564092  279 ELLASLKqDLVHKEQELSRKQQEVVQIDQFLKETAAREASAKLRLqqfiEELLERADRAERQLQVISS 346
Cdd:PRK03918 273 KEIEELE-EKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRL----SRLEEEINGIEERIKELEE 335
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
206-341 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 47564092    206 RALEKLEVDRRLERLSEEVEqKIAGQVGRLQAELERKAAELETA-----RQESARLGREKEELEERASELSRQVD---VS 277
Cdd:pfam12128  381 RSKIKEQNNRDIAGIKDKLA-KIREARDRQLAVAEDDLQALESElreqlEAGKLEFNEEEYRLKSRLGELKLRLNqatAT 459
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092    278 VELLASL--KQDLVHK---EQELSRKQQEVVQIDQFLKETAAREASAKLRL-QQFIEELLERADRAERQL 341
Cdd:pfam12128  460 PELLLQLenFDERIERareEQEAANAEVERLQSELRQARKRRDQASEALRQaSRRLEERQSALDELELQL 529
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
204-340 2.93e-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: 2.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092   204 KIRALEKLEVDRRL--ERLSEEVE----QKIAGQ-----VGRLQAELERKAAELETARQESARLGREKEELE-ERASELS 271
Cdd:pfam17380 376 RMRELERLQMERQQknERVRQELEaarkVKILEEerqrkIQQQKVEMEQIRAEQEEARQREVRRLEEERAREmERVRLEE 455
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 47564092   272 RQVDVSVELLASLKQDLVHKEQELSRKQQEVVQIDQFLKETAAREASAklRLQQFIEE-----LLERaDRAERQ 340
Cdd:pfam17380 456 QERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEE--RKQAMIEEerkrkLLEK-EMEERQ 526
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
345-555 3.11e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 44.78  E-value: 3.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092   345 SSSCGSTPSASLGRGGGGSASGPGVRGPGRMREHHAGSAVPSTyavSRHGSSPStGASSRVPAASQSSGCYDSDSLELPR 424
Cdd:PHA03307  182 TARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAP---GRSAADDA-GASSSDSSSSESSGCGWGPENECPL 257
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092   425 PEEGPSEDSGPGGLGSRAqatNGGSERSQAPRSSGLRRQAIQNWQR-------RPRRHSTEGEEGDVSDVGSRTTESEAE 497
Cdd:PHA03307  258 PRPAPITLPTRIWEASGW---NGPSSRPGPASSSSSPRERSPSPSPsspgsgpAPSSPRASSSSSSSRESSSSSTSSSSE 334
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092   498 GPSD-VPRPGPAVAGPLNSCRLSARPEGGS-GRGRRVERGSPSRSNEVISPEILKMRAAL 555
Cdd:PHA03307  335 SSRGaAVSPGPSPSRSPSPSRPPPPADPSSpRKRPRPSRAPSSPAASAGRPTRRRARAAV 394
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
197-345 3.19e-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: 3.19e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092    197 EEGLARLKIRALEKlevdRRLERLSEEVEQKIagqvgRLQAEL-ERKAAELETARQESARLGREKEELEERASELSRQVD 275
Cdd:pfam02463  159 EEEAAGSRLKRKKK----EALKKLIEETENLA-----ELIIDLeELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYL 229
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092    276 VSVELLASLKQDLvhkeQELSRKQQEvvQIDQFLKETAAREASAKLRLQQFIEELLERADRAERQLQVIS 345
Cdd:pfam02463  230 DYLKLNEERIDLL----QELLRDEQE--EIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAK 293
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
236-340 3.24e-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: 3.24e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092 236 QAELERKAAELETARQESARLGREKEELEERASELSRQvdvsvelLASLKQDLVHKEQELSRKQQEVVQIDQFLKETAAR 315
Cdd:COG4942  19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQ-------LAALERRIAALARRIRALEQELAALEAELAELEKE 91
                        90       100
                ....*....|....*....|....*
gi 47564092 316 EASAKLRLQQFIEELLERADRAERQ 340
Cdd:COG4942  92 IAELRAELEAQKEELAELLRALYRL 116
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
212-339 3.83e-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: 43.68  E-value: 3.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092   212 EVDRRLERLSEEVEQKIAGQVGRLQAELERKAAELETARQESARlgREKEELEERASELSRQvdVSVELLASLKQDLVHK 291
Cdd:TIGR02794  68 ERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAA--KQAEEKQKQAEEAKAK--QAAEAKAKAEAEAERK 143
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 47564092   292 EQELSRKQQEvvqIDQFLKETAAREASAKLRLQQFIEELLERADRAER 339
Cdd:TIGR02794 144 AKEEAAKQAE---EEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAK 188
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
197-344 3.86e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 44.28  E-value: 3.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092  197 EEGLARLKiRALEKL------EVDRRLERL----SEEVEQKIAGQ-VGRLQAELERKAAELETARQESARLGREKEELEE 265
Cdd:PRK03918 569 EEELAELL-KELEELgfesveELEERLKELepfyNEYLELKDAEKeLEREEKELKKLEEELDKAFEELAETEKRLEELRK 647
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 47564092  266 RASELSRQvdVSVELLASLKQDLVHKEQELSRKQQEVVQIDQFLKETAareasaklRLQQFIEELLERADRAERQLQVI 344
Cdd:PRK03918 648 ELEELEKK--YSEEEYEELREEYLELSRELAGLRAELEELEKRREEIK--------KTLEKLKEELEEREKAKKELEKL 716
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
229-346 3.99e-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: 3.99e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092 229 AGQVGRLQAELERKAAELETARQESARLGREKEELEERASELSRQVDVSVELLASLKQDLVHKEQELSRKQQEVVQIDQF 308
Cdd:COG4942  19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 47564092 309 LKETAAR-----EASAKLRLQQFIEELL--ERADRAERQLQVISS 346
Cdd:COG4942  99 LEAQKEElaellRALYRLGRQPPLALLLspEDFLDAVRRLQYLKY 143
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
201-343 4.14e-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: 4.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092  201 ARLKIRALEKlevdrRLERLSEEVEQkIAGQVGRLQAEL----ERKAA------------ELETARQESARLGREKEELE 264
Cdd:COG4913  608 NRAKLAALEA-----ELAELEEELAE-AEERLEALEAELdalqERREAlqrlaeyswdeiDVASAEREIAELEAELERLD 681
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092  265 ERASELS---RQVDVSVELLASLKQDLVHKEQELSRKQQEV----VQIDQFLKETAAREASAKLRLQQFIEELLERADRA 337
Cdd:COG4913  682 ASSDDLAaleEQLEELEAELEELEEELDELKGEIGRLEKELeqaeEELDELQDRLEAAEDLARLELRALLEERFAAALGD 761

                 ....*.
gi 47564092  338 ERQLQV 343
Cdd:COG4913  762 AVEREL 767
F-box_SpPof1-like cd22147
F-box domain found in Schizosaccharomyces pombe Skp1-binding protein 1 (SpPof1) and similar ...
546-589 4.53e-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: 4.53e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 47564092 546 PEILKMRaalfcIFTYLDTRTLLHAAEVCRDWRFVARHPAVWTR 589
Cdd:cd22147   6 PVELSLK-----ILSYLDAKSLCRAAQVSKKWRNLADDDELWKR 44
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
238-338 4.63e-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: 40.67  E-value: 4.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092   238 ELERKAAELEtarqesARLGREKEELEERASELSRQVDvSVELLASLKQDLVHKEQELSRKQQEVVQIDQFLKETAAREA 317
Cdd:pfam20492   3 EAEREKQELE------ERLKQYEEETKKAQEELEESEE-TAEELEEERRQAEEEAERLEQKRQEAEEEKERLEESAEMEA 75
                          90       100
                  ....*....|....*....|.
gi 47564092   318 SAKLRLQQFIEELLERADRAE 338
Cdd:pfam20492  76 EEKEQLEAELAEAQEEIARLE 96
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
201-335 4.92e-04

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 43.71  E-value: 4.92e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092 201 ARLKIRALEKLEVDRRLERLSEEVEQKIAGQvgrlQAELERKAAE----LETARQESarlgreKEELEERASELSRQVDV 276
Cdd:COG2268 212 TEIAIAQANREAEEAELEQEREIETARIAEA----EAELAKKKAEerreAETARAEA------EAAYEIAEANAEREVQR 281
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092 277 SVELLASLKQ-DLVHKEQELSRKQQEVVQIDQFLKETAAREASAKLRLQQFIEELLERAD 335
Cdd:COG2268 282 QLEIAEREREiELQEKEAEREEAELEADVRKPAEAEKQAAEAEAEAEAEAIRAKGLAEAE 341
PTZ00121 PTZ00121
MAEBL; Provisional
207-339 5.47e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.98  E-value: 5.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092   207 ALEKLEVDRRLERLSEEVEQKIAGQVGRLQAELERKAAELETARQES---ARLGREKEELEERASEL-----SRQVDVSV 278
Cdd:PTZ00121 1449 AKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAkkkADEAKKAAEAKKKADEAkkaeeAKKADEAK 1528
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 47564092   279 ELLASLKQDLVHKEQELsRKQQEVVQIDQFLKETAAREASAKLRLQQFIEELLERADRAER 339
Cdd:PTZ00121 1529 KAEEAKKADEAKKAEEK-KKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKK 1588
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
212-342 5.82e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.60  E-value: 5.82e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092 212 EVDRRLERLSEEVEQ-KIAGQVGRLQAELERKAAELETARQESARLGREKEELEERASELSRQVD----VSVELLASLKQ 286
Cdd:COG4717 348 ELQELLREAEELEEElQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEellgELEELLEALDE 427
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 47564092 287 DLVhkEQELSRKQQEVVQIDQFLKETAAREASAKLRLQQF-----IEELLERADRAERQLQ 342
Cdd:COG4717 428 EEL--EEELEELEEELEELEEELEELREELAELEAELEQLeedgeLAELLQELEELKAELR 486
PTZ00121 PTZ00121
MAEBL; Provisional
204-339 6.05e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.98  E-value: 6.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092   204 KIRALEKLEVDRRLERLSEEVEQKIAGQVGRLQAELERKAAELETARQESAR----LGREKEELEERASELSRQVDVSVE 279
Cdd:PTZ00121 1651 ELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKkaeeLKKKEAEEKKKAEELKKAEEENKI 1730
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 47564092   280 LLASLKQdlvhKEQELSRKQQEVV-------QIDQFLKETAAREASAKLRLQQFIEELLERADRAER 339
Cdd:PTZ00121 1731 KAEEAKK----EAEEDKKKAEEAKkdeeekkKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRR 1793
PRK12704 PRK12704
phosphodiesterase; Provisional
234-346 6.05e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 43.23  E-value: 6.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092  234 RLQAELERKAAELEtARQESARLGREKE-ELEERASELSRQvdvsvellaslKQDLVHKEQELSRKQQEVVQIDQFLKET 312
Cdd:PRK12704  48 KKEAEAIKKEALLE-AKEEIHKLRNEFEkELRERRNELQKL-----------EKRLLQKEENLDRKLELLEKREEELEKK 115
                         90       100       110
                 ....*....|....*....|....*....|....
gi 47564092  313 AAREASAKLRLQQFIEELLERADRAERQLQVISS 346
Cdd:PRK12704 116 EKELEQKQQELEKKEEELEELIEEQLQELERISG 149
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
250-347 6.23e-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: 6.23e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092    250 RQESARLGREKEELEERASELSRQVDVSVELLASLKQDLVHKEQELSRKQQEVVQIDQFLKETAAREASAKLRLQQFIEE 329
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
                           90
                   ....*....|....*...
gi 47564092    330 LLERADRAERQLQVISSS 347
Cdd:TIGR02168  756 LTELEAEIEELEERLEEA 773
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
197-347 6.28e-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: 41.82  E-value: 6.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092   197 EEGLARLKIR--ALEKL--EVDRRLERLSEEVEQkiagqvgrLQAELERKAAELETARQESARLGREK---EELEERASE 269
Cdd:pfam13851  32 KEEIAELKKKeeRNEKLmsEIQQENKRLTEPLQK--------AQEEVEELRKQLENYEKDKQSLKNLKarlKVLEKELKD 103
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 47564092   270 LSRQVDVSVELLASLKQDLvhkeQELSRKQQEVVQidQFLKETAAREasakLRLQQFIEELLERADRAERQL-QVISSS 347
Cdd:pfam13851 104 LKWEHEVLEQRFEKVERER----DELYDKFEAAIQ--DVQQKTGLKN----LLLEKKLQALGETLEKKEAQLnEVLAAA 172
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
206-330 6.65e-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: 43.35  E-value: 6.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092   206 RALEKLEVDRRLERLSEEVEQK-IAGQVGRLQAELERKAAELETARQESARLGREKEELEERASELSRQVDVSVELLASL 284
Cdd:pfam07888  55 RQREKEKERYKRDREQWERQRReLESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIREL 134
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 47564092   285 KQDL-------VHKEQELSRKQQEVVQIDQFLKETAAREASAKLRLQQFIEEL 330
Cdd:pfam07888 135 EEDIktltqrvLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEEL 187
PRK12678 PRK12678
transcription termination factor Rho; Provisional
369-541 6.85e-04

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 43.35  E-value: 6.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092  369 VRGPGRMR---------EHHAGSAVPSTYAVSRHGSSPSTGASSRVPAASQSSGCYDSDSLELPRPEEGPSEDSGPGGLG 439
Cdd:PRK12678  40 IKGTSGMRkgeliaaikEARGGGAAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAA 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092  440 SRAQATnGGSERSQAPRSSGLRRQAIQNwqRRPRRHSTEGEEGDVSDVGSRTTESEAEGPSDVPRPGPAVAGPLNSCRLS 519
Cdd:PRK12678 120 SAPEAA-QARERRERGEAARRGAARKAG--EGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREER 196
                        170       180
                 ....*....|....*....|..
gi 47564092  520 ARPEGGSGRGRRVERGSPSRSN 541
Cdd:PRK12678 197 GRDGDDRDRRDRREQGDRREER 218
Nuf2_DHR10-like pfam18595
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This ...
204-302 6.99e-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: 40.26  E-value: 6.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092   204 KIRALEKLEVD-RRLERLSEEVEQKiagqvgrlQAELERKAAELETARQESARLGREKEELEERASELSRQVDVSVELLA 282
Cdd:pfam18595  24 KIDALQVVEKDlRSCIKLLEEIEAE--------LAKLEEAKKKLKELRDALEEKEIELRELERREERLQRQLENAQEKLE 95
                          90       100
                  ....*....|....*....|
gi 47564092   283 SLKQDLVHKEQELSRKQQEV 302
Cdd:pfam18595  96 RLREQAEEKREAAQARLEEL 115
F-box_ECT2L cd22173
F-box domain found in epithelial cell-transforming sequence 2 oncogene-like (ECT2L) and ...
558-588 9.68e-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: 9.68e-04
                        10        20        30
                ....*....|....*....|....*....|.
gi 47564092 558 IFTYLDTRTLLHAAEVCRDWRFVARHPAVWT 588
Cdd:cd22173  14 IFSFLDPRSLCRAAQVSWHWKFLAEQDCLWM 44
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
200-347 9.78e-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: 42.44  E-value: 9.78e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092 200 LARLKIRALEKLE-VDRRLERLSEEVeQKIAGQVGRLQAELERKAAELETARQEsarLGREKEELEERASELSR------ 272
Cdd:COG4942  46 LKKEEKALLKQLAaLERRIAALARRI-RALEQELAALEAELAELEKEIAELRAE---LEAQKEELAELLRALYRlgrqpp 121
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092 273 -----------QVDVSVELLASLKQDLVHKEQELSRKQQEVVQIDQFLKETAAREASAKLRLQQFIEELLERADRAERQL 341
Cdd:COG4942 122 lalllspedflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLL 201

                ....*.
gi 47564092 342 QVISSS 347
Cdd:COG4942 202 ARLEKE 207
DUF4164 pfam13747
Domain of unknown function (DUF4164); This is a family of short, approx 100 residue-long, ...
197-279 9.95e-04

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: 9.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092   197 EEGLARLKiRALEKLE--VDRRLERLSEEVEqkIAGQVGRLQAELERKAAELETARQESARLgrekeelEERASELSRQV 274
Cdd:pfam13747   7 EAALQRLE-AALDRLEaaVDRRLEADRDRDE--LEAEIEALGADRSRLAQELDQAEARANRL-------EETNREISRRL 76

                  ....*
gi 47564092   275 DVSVE 279
Cdd:pfam13747  77 DSAIE 81
mukB PRK04863
chromosome partition protein MukB;
201-342 1.03e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 43.02  E-value: 1.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092   201 ARLKIRALEKLE----------VDRRLERLSEEVEQ-----KIAGQVGRLQAELERKAAELETARQESARLGREKEELEE 265
Cdd:PRK04863  870 AKEGLSALNRLLprlnlladetLADRVEEIREQLDEaeeakRFVQQHGNALAQLEPIVSVLQSDPEQFEQLKQDYQQAQQ 949
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092   266 RASELSRQVDV---------------SVELLA-------SLKQDLVHKEQELSRKQQEVVQIDQFLKETAAREASAKLRL 323
Cdd:PRK04863  950 TQRDAKQQAFAltevvqrrahfsyedAAEMLAknsdlneKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSY 1029
                         170
                  ....*....|....*....
gi 47564092   324 QQFIEELLEradrAERQLQ 342
Cdd:PRK04863 1030 DAKRQMLQE----LKQELQ 1044
F-box_FBXW4 cd20090
F-box domain found in F-box/WD repeat-containing protein 4 (FBXW4) and similar proteins; FBXW4, ...
554-589 1.08e-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: 1.08e-03
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 47564092 554 ALFCIFTYLDTRTLLHAAEVCRDWRFVARHPAVWTR 589
Cdd:cd20090   9 LLFLIFSYLDPASLGRLSQVCRRLYRLISRDAVWRR 44
DUF4515 pfam14988
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ...
209-342 1.12e-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: 41.29  E-value: 1.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092   209 EKLEVDRRLERLSEEVEQKIagqvGRLQAELERKAAELETARQESArlgrekEELEERASELSRQVDVSVELLASLKQDL 288
Cdd:pfam14988   1 ENKFFLEYLAKKTEEKQKKI----EKLWNQYVQECEEIERRRQELA------SRYTQQTAELQTQLLQKEKEQASLKKEL 70
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 47564092   289 VHKEQELSRKQQEVVQIDQFLKETAAREASAKLRLQQFIEELLERADRAERQLQ 342
Cdd:pfam14988  71 QALRPFAKLKESQEREIQDLEEEKEKVRAETAEKDREAHLQFLKEKALLEKQLQ 124
PTZ00121 PTZ00121
MAEBL; Provisional
204-339 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 47564092   204 KIRALEKLEVDRRLERLSEEVEQKIAGQVGRLQAELERKAAE----------LETARQESARLGREKEELEERASELSRQ 273
Cdd:PTZ00121 1576 KNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEakikaeelkkAEEEKKKVEQLKKKEAEEKKKAEELKKA 1655
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 47564092   274 vdvsVELLASLKQDLVHKEQELSRKQQEVVQIDQFLK---ETAAREASAKLRLQQFIEELLERADRAER 339
Cdd:PTZ00121 1656 ----EEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKkaaEALKKEAEEAKKAEELKKKEAEEKKKAEE 1720
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
213-346 1.22e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 42.70  E-value: 1.22e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092 213 VDRRLERLSEEVEQK---IAGQVGRLQAELERKAAELETARQESarlgrekeeleeRASELSRQVDVSVELLASLKQDLV 289
Cdd:COG3206 162 LEQNLELRREEARKAlefLEEQLPELRKELEEAEAALEEFRQKN------------GLVDLSEEAKLLLQQLSELESQLA 229
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 47564092 290 HKEQELSRKQQEVVQIDQFLKETaaREASAKLRLQQFIEELLERADRAERQLQVISS 346
Cdd:COG3206 230 EARAELAEAEARLAALRAQLGSG--PDALPELLQSPVIQQLRAQLAELEAELAELSA 284
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
209-343 1.51e-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: 42.42  E-value: 1.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092   209 EKLEVDRRLERLSEEVEQKIAgqvgrLQAELERKAA--------------ELETARQESARLGREKEELEERASELSRQV 274
Cdd:pfam17380 304 EKEEKAREVERRRKLEEAEKA-----RQAEMDRQAAiyaeqermamererELERIRQEERKRELERIRQEEIAMEISRMR 378
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092   275 D--------------VSVELLASLKQDLVHKEQELSRKQQEVVQIDQFLKETAAREASAKlRLQQFIEELLERADRA--E 338
Cdd:pfam17380 379 ElerlqmerqqknerVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVR-RLEEERAREMERVRLEeqE 457

                  ....*
gi 47564092   339 RQLQV 343
Cdd:pfam17380 458 RQQQV 462
UPF0242 pfam06785
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ...
208-315 1.64e-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: 1.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092   208 LEKLEVDRRLERLSEEVEQKIA---GQVGRLQAELERKAAELETARQESARLGREKEELEERASELSRQVDvsvELLASL 284
Cdd:pfam06785  65 FEKSFLEEKEAKLTELDAEGFKileETLEELQSEEERLEEELSQKEEELRRLTEENQQLQIQLQQISQDFA---EFRLES 141
                          90       100       110
                  ....*....|....*....|....*....|.
gi 47564092   285 KQDLVHKEQELSRKQQEVVQIDQFLKETAAR 315
Cdd:pfam06785 142 EEQLAEKQLLINEYQQTIEEQRSVLEKRQDQ 172
F-box_FBXO22 cd22097
F-box domain found in F-box only protein 22 (FBXO22) and similar proteins; FBXO22, also called ...
546-582 1.65e-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: 1.65e-03
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 47564092 546 PEILKMraalfcIFTYLDTRTLLHAAEVCRDWRFVAR 582
Cdd:cd22097   5 AEIVER------ILSFLPAKALLRCARVCRLWRDCAR 35
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
195-330 1.67e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.36  E-value: 1.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092  195 AYEEgLARLKIRALEKL-EVDRRLERLSEEVEQkiagqVGRLQAELERKAAELETARQESARLGREKEELEERASELSRQ 273
Cdd:PRK03918 294 EYIK-LSEFYEEYLDELrEIEKRLSRLEEEING-----IEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEA 367
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 47564092  274 VDVSVEL------LASLKQDLVHKEQELSRKQQEVVQIDqfLKETAAREASAKLR---LQQFIEEL 330
Cdd:PRK03918 368 KAKKEELerlkkrLTGLTPEKLEKELEELEKAKEEIEEE--ISKITARIGELKKEikeLKKAIEEL 431
APG6_N pfam17675
Apg6 coiled-coil region; In yeast, 15 Apg proteins coordinate the formation of autophagosomes. ...
215-295 1.84e-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: 39.12  E-value: 1.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092   215 RRLERLSEEVEQKIAGQVGRLQAELERKAAELETARQESARLGREKEELEERASELSRQVDVSVELLASLKQDLVHKEQE 294
Cdd:pfam17675  33 KKLEKETPEELEELEKELEKLEKEEEELLQELEELEKEREELDAELEALEEELEALDEEEEEFWREYNALQLQLLEFQDE 112

                  .
gi 47564092   295 L 295
Cdd:pfam17675 113 R 113
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
197-342 1.84e-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: 1.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092    197 EEGLARLKIRALEKLEVDRRLE-RLSEEVE--QKIAGQVGRLQ---AELERKAAELETARQ------------------- 251
Cdd:pfam01576   60 EEMRARLAARKQELEEILHELEsRLEEEEErsQQLQNEKKKMQqhiQDLEEQLDEEEAARQklqlekvtteakikkleed 139
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092    252 ------ESARLGREKEELEERASELSRQVDVSVELLASL-----KQDLVHKEQELSRKQ-----QEVVQIDQFLKETAAR 315
Cdd:pfam01576  140 illledQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLsklknKHEAMISDLEERLKKeekgrQELEKAKRKLEGESTD 219
                          170       180
                   ....*....|....*....|....*..
gi 47564092    316 EASAKLRLQQFIEELLERADRAERQLQ 342
Cdd:pfam01576  220 LQEQIAELQAQIAELRAQLAKKEEELQ 246
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
203-338 2.13e-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: 2.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092    203 LKIRALEKLE-VDRRLERLSEEVEQ--KIAGQVGRLQAELERKAAELETARQE-----SARLGREKEELeeraSELSRQV 274
Cdd:smart00787 145 LKEGLDENLEgLKEDYKLLMKELELlnSIKPKLRDRKDALEEELRQLKQLEDEledcdPTELDRAKEKL----KKLLQEI 220
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 47564092    275 DVSVELLASLKQDLVHKEQELsrkQQEVVQIDQFLKETAAREaSAKLRLQQF----IEELLERADRAE 338
Cdd:smart00787 221 MIKVKKLEELEEELQELESKI---EDLTNKKSELNTEIAEAE-KKLEQCRGFtfkeIEKLKEQLKLLQ 284
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
197-339 2.17e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.97  E-value: 2.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092  197 EEGLARLKIRALEKL--EVDRRLERLSEEVEqKIAGQVGRLQaELERKAAELETARQESARLGREKEELEERASELSRQV 274
Cdd:PRK03918 246 ELESLEGSKRKLEEKirELEERIEELKKEIE-ELEEKVKELK-ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEI 323
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 47564092  275 DVSVELLaslkqdlvhkeQELSRKQQEVVQIDQFLKETAAREASAKLRLQQFiEELLERADRAER 339
Cdd:PRK03918 324 NGIEERI-----------KELEEKEERLEELKKKLKELEKRLEELEERHELY-EEAKAKKEELER 376
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
201-342 2.18e-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: 2.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092   201 ARLKIRALEKLEVDRRLERLSEEVEQkiagqvgRLQAELERKAAELETARQESARLGREKEELEERASELSRQVDVSVEL 280
Cdd:pfam15558  80 RRADRREKQVIEKESRWREQAEDQEN-------QRQEKLERARQEAEQRKQCQEQRLKEKEEELQALREQNSLQLQERLE 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092   281 LASLKQDLvhKEQELSRKQQEV------------VQID-QFLKETAAREASAKLRLQQFIE-----------ELLERADR 336
Cdd:pfam15558 153 EACHKRQL--KEREEQKKVQENnlsellnhqarkVLVDcQAKAEELLRRLSLEQSLQRSQEnyeqlveerhrELREKAQK 230

                  ....*.
gi 47564092   337 AERQLQ 342
Cdd:pfam15558 231 EEEQFQ 236
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
207-342 2.33e-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: 2.33e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092 207 ALEKLEVDRRLERLSEEVEQKIAgQVGRLQAELERKAAELETARQESARLGREKEELEERASELSRQVDVSVELLASLKQ 286
Cdd:COG4942  19 ADAAAEAEAELEQLQQEIAELEK-ELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 47564092 287 DLVHKEQELSR------KQQEVVQIDQFLKETAAREASAKLR-LQQFIEELLERADRAERQLQ 342
Cdd:COG4942  98 ELEAQKEELAEllralyRLGRQPPLALLLSPEDFLDAVRRLQyLKYLAPARREQAEELRADLA 160
HIP1_clath_bdg pfam16515
Clathrin-binding domain of Huntingtin-interacting protein 1; HIP1_clath_bdg is the coiled-coil ...
207-268 2.50e-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: 2.50e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 47564092   207 ALEKLEVDRRLERLSEEVEQKIAGQ---VGRLQAELERKAAELETAR-------QESARLGREKEELE-ERAS 268
Cdd:pfam16515  26 EREKKQLEFELERAKEEAQMKLEEQkeeLERLKRELESSRAELATLQstlqsseQSGSQLSSQLAALQaEKEG 98
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
211-330 2.52e-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: 2.52e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092    211 LEVDRRLERLSEeVEQKIAgqvgRLQAELERKAAELETARQESARLGREKEELEERASELSRQVDVSVELLASLKQDLVH 290
Cdd:pfam12128  807 QRRPRLATQLSN-IERAIS----ELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATLKEDANS 881
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 47564092    291 KEQELSRKQQeVVQIDQFLKetaaREASAKLRLQQFIEEL 330
Cdd:pfam12128  882 EQAQGSIGER-LAQLEDLKL----KRDYLSESVKKYVEHF 916
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
197-344 2.57e-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: 2.57e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092    197 EEGLARLKIRALEKLEVDRRLERLSEEVEQKIAGQV-------GRLQAELERKAA----ELETARQESARLGREKEELEE 265
Cdd:TIGR00606  268 DNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLndlyhnhQRTVREKERELVdcqrELEKLNKERRLLNQEKTELLV 347
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092    266 RASELSRQVDVSVEllASLKQDLVHKEQE-------LSRKQQEVVQIDQFLKETAAREASAKLRLQQFIEELLERADRAE 338
Cdd:TIGR00606  348 EQGRLQLQADRHQE--HIRARDSLIQSLAtrleldgFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQ 425

                   ....*.
gi 47564092    339 RQLQVI 344
Cdd:TIGR00606  426 EQADEI 431
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
217-342 2.78e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.29  E-value: 2.78e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092 217 LERLSEEVEQ--KIAGQVGRLQ-AELERKAAELETARQESARLgrekEELEERASELSRQVDVSVELLASLKQDLVHKEQ 293
Cdd:COG4717  48 LERLEKEADElfKPQGRKPELNlKELKELEEELKEAEEKEEEY----AELQEELEELEEELEELEAELEELREELEKLEK 123
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 47564092 294 ELSRKQ--QEVVQIDQFLKETAAREASAKLRLQQfIEELLERADRAERQLQ 342
Cdd:COG4717 124 LLQLLPlyQELEALEAELAELPERLEELEERLEE-LRELEEELEELEAELA 173
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
193-344 3.11e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.29  E-value: 3.11e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092 193 DVAYEEGLARLKIRALEKLEVDRRLERLSEEVEQK---------------IAGQVGRLQAELERKAAELETARQESARLG 257
Cdd:COG4717 380 GVEDEEELRAALEQAEEYQELKEELEELEEQLEELlgeleellealdeeeLEEELEELEEELEELEEELEELREELAELE 459
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092 258 REKEELEEraselsrqvdvsvellaslKQDLVHKEQELSRKQQEvvqidqfLKETAAREASAKLrLQQFIEELLERAdRA 337
Cdd:COG4717 460 AELEQLEE-------------------DGELAELLQELEELKAE-------LRELAEEWAALKL-ALELLEEAREEY-RE 511

                ....*..
gi 47564092 338 ERQLQVI 344
Cdd:COG4717 512 ERLPPVL 518
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
231-302 3.17e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.97  E-value: 3.17e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 47564092 231 QVGRLQAELERKAAELETARQESARLGREKEELEERASELSRQVDVSVELLASLKQDLVHKEQELSRKQQEV 302
Cdd:COG3883  17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL 88
F-box_FBXO48 cd22113
F-box domain found in F-box only protein 48 (FBXO48) and similar proteins; FBXO48, also called ...
558-587 3.37e-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: 3.37e-03
                        10        20        30
                ....*....|....*....|....*....|.
gi 47564092 558 IFTYLDTRTLLHAAEVCRDWR-FVARHPAVW 587
Cdd:cd22113  12 IFSQLDVQSLCRASQTCKTWNdLIENSDYLW 42
F-box_FBXL7 cd22120
F-box domain found in F-box/LRR-repeat protein 7 (FBXL7) and similar proteins; FBXL7, also ...
558-590 3.73e-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: 3.73e-03
                        10        20        30
                ....*....|....*....|....*....|...
gi 47564092 558 IFTYLDTRTLLHAAEVCRDWRFVARHPAVWTRV 590
Cdd:cd22120  12 IFSHLPTNQLCRCARVCRRWYNLAWDPRLWTTI 44
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
215-344 3.83e-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: 3.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092  215 RRLERLSEEVEQKIA--GQVGRLQAELERKAAELETARQESARL-----GREKEELEERASELSRQVDVSVELLASLKQD 287
Cdd:COG4913  238 ERAHEALEDAREQIEllEPIRELAERYAAARERLAELEYLRAALrlwfaQRRLELLEAELEELRAELARLEAELERLEAR 317
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 47564092  288 LVHKEQELSRKQQEVVQIDQFLKETAAREASaklRLQQFIEELLERADRAERQLQVI 344
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; ...
554-589 4.14e-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: 4.14e-03
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 47564092 554 ALFCIFTYLDTRTLLHAAEVCRDWRFVARHPAVWTR 589
Cdd:cd22137   7 PMLRIFSFLDAFSLLQAAQVNKQWNKVADSDYLWRN 42
PRK12704 PRK12704
phosphodiesterase; Provisional
201-336 4.40e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.53  E-value: 4.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092  201 ARLKIRALEK---LEVDRRLERLSEEVEQKIAGQVGRLQAELERKAAELETARQESARLGREKEELEERASELSRQvdvs 277
Cdd:PRK12704  47 AKKEAEAIKKealLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQK---- 122
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 47564092  278 vellaslKQDLVHKEQELSRKQQEVVQ-----------------IDQfLKETAAREASAKLRlqQFIEELLERADR 336
Cdd:PRK12704 123 -------QQELEKKEEELEELIEEQLQelerisgltaeeakeilLEK-VEEEARHEAAVLIK--EIEEEAKEEADK 188
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
208-339 4.41e-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: 40.93  E-value: 4.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092    208 LEKLEvdRRLERLSEEVEQKIA---GQVGRLQAELERKAAELETA----------RQESARLGREKE----ELEE----- 265
Cdd:pfam01576  206 LEKAK--RKLEGESTDLQEQIAelqAQIAELRAQLAKKEEELQAAlarleeetaqKNNALKKIRELEaqisELQEdlese 283
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092    266 ---RASELSRQVDVSVELLAsLK------QDLVHKEQEL-SRKQQEVVQIDQFLK-ETAAREAS-AKLRLQQF--IEELL 331
Cdd:pfam01576  284 raaRNKAEKQRRDLGEELEA-LKteledtLDTTAAQQELrSKREQEVTELKKALEeETRSHEAQlQEMRQKHTqaLEELT 362

                   ....*...
gi 47564092    332 ERADRAER 339
Cdd:pfam01576  363 EQLEQAKR 370
F-box_FBXO16-like cd22094
F-box domain found in F-box only protein 16 (FBXO16), epithelial cell-transforming sequence 2 ...
558-587 4.46e-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: 4.46e-03
                        10        20        30
                ....*....|....*....|....*....|
gi 47564092 558 IFTYLDTRTLLHAAEVCRDWRFVARHPAVW 587
Cdd:cd22094  14 IFSYLDPRSLCRAAQVSWYWKFLCESDELW 43
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
246-342 4.63e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 40.58  E-value: 4.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092  246 LETARQ--------ESAR--LGREKEELEE---RASELSRQVDVSVELLASLKQDLVHKEQELSRKQQEVVQIDQFLKET 312
Cdd:PRK00409 491 FEIAKRlglpeniiEEAKklIGEDKEKLNEliaSLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEE 570
                         90       100       110
                 ....*....|....*....|....*....|
gi 47564092  313 AAREAsaklrlQQFIEELLERADRAERQLQ 342
Cdd:PRK00409 571 AEKEA------QQAIKEAKKEADEIIKELR 594
GOLGA2L5 pfam15070
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein ...
222-330 4.67e-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: 4.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092   222 EEVEQKIAGQVGRLQAELERKAAELETARQESARLGREKEELEERASELSRQVDvsvellaslkqdlVHKEQELSRKQQ- 300
Cdd:pfam15070  81 SEEEQRLQEEAEQLQKELEALAGQLQAQVQDNEQLSRLNQEQEQRLLELERAAE-------------RWGEQAEDRKQIl 147
                          90       100       110
                  ....*....|....*....|....*....|
gi 47564092   301 EVVQIDqflKETAAREASAKLRLQQFIEEL 330
Cdd:pfam15070 148 EDMQSD---RATISRALSQNRELKEQLAEL 174
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
206-343 4.99e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.27  E-value: 4.99e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092 206 RALEKLE-VDRRLERLSEEVEQkIAGQVGRLQAELERKAAELETARQESARLGREKEELEERASELSRQVDVSVELLASL 284
Cdd:COG4372  98 QAQEELEsLQEEAEELQEELEE-LQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQAL 176
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 47564092 285 KQDlvHKEQELSRKQQEVVQIDQFLKETAAREASAKLRLQQFIEELLERADRAERQLQV 343
Cdd:COG4372 177 SEA--EAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGL 233
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
212-342 5.53e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.41  E-value: 5.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092  212 EVDRRLERLSEEVEQK----------IAGQVGRLQaELERKAAELETARQESARLGREKEELEERASELSRQV------- 274
Cdd:PRK02224 217 ELDEEIERYEEQREQAretrdeadevLEEHEERRE-ELETLEAEIEDLRETIAETEREREELAEEVRDLRERLeeleeer 295
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 47564092  275 ----------DVSVELLASLKQDLVHKEQELSRKQQEVVQIDQFLKETAAREASAKLRLQQFIEELLERADRAERQLQ 342
Cdd:PRK02224 296 ddllaeagldDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELE 373
F-box_FBXO11 cd22091
F-box domain found in F-box only protein 11 (FBXO11) and similar proteins; FBXO11, also called ...
555-589 5.86e-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: 5.86e-03
                        10        20        30
                ....*....|....*....|....*....|....*
gi 47564092 555 LFCIFTYLDTRTLLHAAEVCRDWRFVARHPAVWTR 589
Cdd:cd22091   9 LLKIFSYLLEQDLCRAAQVCKRFNTLANDPELWKR 43
FBOX smart00256
A Receptor for Ubiquitination Targets;
555-587 6.01e-03

A Receptor for Ubiquitination Targets;


Pssm-ID: 197608  Cd Length: 41  Bit Score: 35.11  E-value: 6.01e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 47564092    555 LFCIFTYLDTRTLLHAAEVCRDWRFVARHPAVW 587
Cdd:smart00256   6 LEEILSKLDPKDLLRLRKVSRKWRSLIDSHDFW 38
ARGLU pfam15346
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ...
197-303 6.20e-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: 6.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092   197 EEGLARLKIRALEKlEVDRRLERLSEEVEQKIAGQVGRLQAELERK-AAELETARQESARLGREKEE--------LEERA 267
Cdd:pfam15346   9 EEETARRVEEAVAK-RVEEELEKRKDEIEAEVERRVEEARKIMEKQvLEELEREREAELEEERRKEEeerkkreeLERIL 87
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 47564092   268 SELSRQVDVSVELLASL--------------KQDLVHKEQELSRKQQEVV 303
Cdd:pfam15346  88 EENNRKIEEAQRKEAEErlamleeqrrmkeeRQRREKEEEEREKREQQKI 137
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
234-337 7.84e-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: 7.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092   234 RLQAELERKAAELEtarqesARLGREKEELEERASELSRQVDVSVELLASLKQDLVHKEQELSRKQQEvvqidqFLKETA 313
Cdd:pfam03938  19 AAQAQLEKKFKKRQ------AELEAKQKELQKLYEELQKDGALLEEEREEKEQELQKKEQELQQLQQK------AQQELQ 86
                          90       100
                  ....*....|....*....|....
gi 47564092   314 AREasaklrlQQFIEELLERADRA 337
Cdd:pfam03938  87 KKQ-------QELLQPIQDKINKA 103
fliH PRK06669
flagellar assembly protein H; Validated
212-335 8.16e-03

flagellar assembly protein H; Validated


Pssm-ID: 235850 [Multi-domain]  Cd Length: 281  Bit Score: 39.23  E-value: 8.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092  212 EVDRRLERLSEEVEQKIAgqvgRLQAELE--------RKAAELETARQESARLGREK--EELEERASELSRQVDVSVELL 281
Cdd:PRK06669  78 EAKEELLKKTDEASSIIE----KLQMQIEreqeeweeELERLIEEAKAEGYEEGYEKgrEEGLEEVRELIEQLNKIIEKL 153
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 47564092  282 ASLKQDLVHK-EQELSrkqQEVVQI-DQFLKETAAREASAKLRL-QQFIEELLERAD 335
Cdd:PRK06669 154 IKKREEILESsEEEIV---ELALDIaKKVIKEISENSKEIALALvKELLKEVKDATD 207
F-box pfam00646
F-box domain; This domain is approximately 50 amino acids long, and is usually found in the ...
554-589 9.05e-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: 9.05e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 47564092   554 ALFCIFTYLDTRTLLHAAEVCRDWRFVARHPAVWTR 589
Cdd:pfam00646   8 LLLEILSRLDPKDLLRLSLVSKRWRSLVDSLKLWKK 43
PRK10698 PRK10698
phage shock protein PspA; Provisional
200-324 9.42e-03

phage shock protein PspA; Provisional


Pssm-ID: 182657 [Multi-domain]  Cd Length: 222  Bit Score: 38.60  E-value: 9.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092  200 LARLKIRALEKLEVDRRLERLSEEVEQKiagQVGRLQAELERKAAELetarQESARLG--REKEELEeRASELSRQVdvS 277
Cdd:PRK10698  28 LVRLMIQEMEDTLVEVRSTSARALAEKK---QLTRRIEQAEAQQVEW----QEKAELAlrKEKEDLA-RAALIEKQK--L 97
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 47564092  278 VELLASLKQDLVHKEQELSRKQQEVVQIDQFLKETAAREASAKLRLQ 324
Cdd:PRK10698  98 TDLIATLEHEVTLVDETLARMKKEIGELENKLSETRARQQALMLRHQ 144
F-box_FBXL5 cd22118
F-box domain found in F-box/LRR-repeat protein 5 (FBXL5) and similar proteins; FBXL5, also ...
541-587 9.73e-03

F-box domain found in F-box/LRR-repeat protein 5 (FBXL5) and similar proteins; FBXL5, also called F-box and leucine-rich repeat protein 5, F-box protein FBL4/FBL5, or p45SKP2-like protein, is the substrate-recognition component of an SCF (SKP1-cullin-F-box) protein ligase complex that plays a central role in iron homeostasis by promoting the ubiquitination and subsequent degradation of IREB2/IRP2. 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: 438890  Cd Length: 41  Bit Score: 34.62  E-value: 9.73e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 47564092 541 NEVISPEILkmraalFCIFTYLDTRTLLHAAEVCRDWRFVARHPAVW 587
Cdd:cd22118   1 ISSLPPEIM------LKIFSYLNPQDLCRCAQVCTKWSQLARDGSLW 41
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
212-333 9.86e-03

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 39.12  E-value: 9.86e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47564092 212 EVDRRLERLSEEVEQkIAGQVGRLQAELERKAAELETARQESARLGREKEELEERASELSRQVDVSVELLASLKQDLVHK 291
Cdd:COG1340   5 ELSSSLEELEEKIEE-LREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDEL 83
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 47564092 292 EQELSRKQQEVVQIDQFLKETAAREASAKlRLQQFIEELLER 333
Cdd:COG1340  84 NEKLNELREELDELRKELAELNKAGGSID-KLRKEIERLEWR 124
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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