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Conserved domains on  [gi|254540204|ref|NP_001156922.1|]
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C-Jun-amino-terminal kinase-interacting protein 3 isoform e [Mus musculus]

Protein Classification

Jnk-SapK_ap_N and JIP_LZII domain-containing protein (domain architecture ID 12101541)

protein containing domains Jnk-SapK_ap_N, SMC_N, JIP_LZII, and Auto_anti-p27

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Jnk-SapK_ap_N pfam09744
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins ...
30-183 7.37e-77

JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins conserved from yeasts to humans. Most of the proteins in this entry have an RhoGEF pfam00621 domain at their C-terminal end.


:

Pssm-ID: 313040  Cd Length: 154  Bit Score: 252.52  E-value: 7.37e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204    30 SGLAGSIYREFERLIHCYDEEVVKELMPLVVNVLENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRKQAEEKFI 109
Cdd:pfam09744    1 YDIASSIYKEFERLIDRYGEDVVKGLMPKVVNVLELLESLASRNQEHEVELEELREDNEQLETQYEREKELRKRAEEELL 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 254540204   110 EFEDALEQEKKELQIQVEHYEFQTRQLELKAKNYADQISRLEERESEMKKEYNALHQRHTEMIQTYVEHIERSK 183
Cdd:pfam09744   81 ELEDQWEGERKDLQSKVEQLEEENRQLELKAKNYADQVSRLEEKEAELKKEYSKLHERENELLKKLKELVERQR 154
JIP_LZII pfam16471
JNK-interacting protein leucine zipper II; This is the second leucine zipper domain (LZII) of ...
386-454 4.19e-30

JNK-interacting protein leucine zipper II; This is the second leucine zipper domain (LZII) of several JNK-interacting proteins (JIP). It interacts with the small GTP-binding protein ARF6.


:

Pssm-ID: 318633  Cd Length: 69  Bit Score: 116.94  E-value: 4.19e-30
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 254540204   386 MGKEVGNLLLENSQLLETKNALNVVKNDLIAKVDQLSGEQEVLKGELEAAKQAKVKLENRIKELEEELK 454
Cdd:pfam16471    1 MGKEVENLIKENTELLETKNALNVVKDDLIARVEELTNEREALKEELESLQESKTRLESRLKELEEELK 69
SMC_N super family cl25732
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
49-517 3.67e-08

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


The actual alignment was detected with superfamily member COG0419:

Pssm-ID: 330553  Cd Length: 908  Bit Score: 57.85  E-value: 3.67e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204   49 EEVVKELMPLVVNvLENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRKQAEEKFIEFEDALEQEKKELQIQVEH 128
Cdd:COG0419   294 EELEREIEELEEE-LEGLRALLEELEELLEKLKSLEERLEKLEEKLEKLESELEELAEEKNELAKLLEERLKELEERLEE 372
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204  129 YEFQTRQLELKAKNYADQISRLEERESEMKKEYNALHQRHTEMIQTYVEhIERSKMQQVGGSGQTESSLpgRSRKERPTS 208
Cdd:COG0419   373 LEKELEKALERLKQLEEAIQELKEELAELSAALEEIQEELEELEKELEE-LERELEELEEEIKKLEEQI--NQLESKELM 449
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204  209 LNVFPLADGMCPNdemsesgqssaaatpsttgtksntptssvpsaavtpLNESLQPLGDYVSVTKNNKQAREKRNSRNME 288
Cdd:COG0419   450 IAELAGAGEKCPV------------------------------------CGQELPEEHEKELLELYELELEELEEELSRE 493
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204  289 VQVtQEMRNVsigmgssdewsdVQDIIDSTPELDVCPETRLErtgssptqgivnkafginTDSLYHELSTAGSEVIGDVD 368
Cdd:COG0419   494 KEE-AELREE------------IEELEKELRELEEELIELLE------------------LEEALKEELEEKLEKLENLL 542
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204  369 EGADLLGEFSVRDDFFGMGKEVGNLLLENSQLLETKNALNVVKNDL----------IAKVDQLSGEQEVLKGELEA--AK 436
Cdd:COG0419   543 EELEELKEKLQLQQLKEELRQLEDRLQELKELLEELRLLRTRKEELeelrerlkelKKKLKELEERLSQLEELLQSleLS 622
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204  437 QAKVKLENRIKELEEELKRVKSEAVTARREP------REEVEDVSSYLCTELDKIPMAQRRRFTRVEMARVLMERNQYKE 510
Cdd:COG0419   623 EAENELEEAEEELESELEKLNLQAELEELLQaaleelEEKVEELEAEIRRELQRIENEEQLEEKLEELEQLEEELEQLRE 702

                  ....*..
gi 254540204  511 RLMELQE 517
Cdd:COG0419   703 ELEELLK 709
Auto_anti-p27 super family cl00713
Sjogren's syndrome/scleroderma autoantigen 1 (Autoantigen p27); This family consists of ...
834-940 7.91e-04

Sjogren's syndrome/scleroderma autoantigen 1 (Autoantigen p27); This family consists of several Sjogren's syndrome/scleroderma autoantigen 1 (Autoantigen p27) sequences. It is thought that the potential association of anti-p27 with anti-centromere antibodies suggests that autoantigen p27 might play a role in mitosis.


The actual alignment was detected with superfamily member PRK12495:

Pssm-ID: 321126  Cd Length: 226  Bit Score: 42.55  E-value: 7.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204  834 SRGDTPVLDKGQG-DVATTANGKVNPSQSTEEATEATEVPDPGPSESEA-------TTVRPGPLTEHVFTDPAPTPSssT 905
Cdd:PRK12495   69 TEDGAAGDDAGDGaEATAPSDAGSQASPDDDAQPAAEAEAADQSAPPEAsstsatdEAATDPPATAAARDGPTPDPT--A 146
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 254540204  906 QPASENGSESNGTIVQPQVEPSGElSTTTSSAAPT 940
Cdd:PRK12495  147 QPATPDERRSPRQRPPVSGEPPTP-STPDAHVAGT 180
 
Name Accession Description Interval E-value
Jnk-SapK_ap_N pfam09744
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins ...
30-183 7.37e-77

JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins conserved from yeasts to humans. Most of the proteins in this entry have an RhoGEF pfam00621 domain at their C-terminal end.


Pssm-ID: 313040  Cd Length: 154  Bit Score: 252.52  E-value: 7.37e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204    30 SGLAGSIYREFERLIHCYDEEVVKELMPLVVNVLENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRKQAEEKFI 109
Cdd:pfam09744    1 YDIASSIYKEFERLIDRYGEDVVKGLMPKVVNVLELLESLASRNQEHEVELEELREDNEQLETQYEREKELRKRAEEELL 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 254540204   110 EFEDALEQEKKELQIQVEHYEFQTRQLELKAKNYADQISRLEERESEMKKEYNALHQRHTEMIQTYVEHIERSK 183
Cdd:pfam09744   81 ELEDQWEGERKDLQSKVEQLEEENRQLELKAKNYADQVSRLEEKEAELKKEYSKLHERENELLKKLKELVERQR 154
JIP_LZII pfam16471
JNK-interacting protein leucine zipper II; This is the second leucine zipper domain (LZII) of ...
386-454 4.19e-30

JNK-interacting protein leucine zipper II; This is the second leucine zipper domain (LZII) of several JNK-interacting proteins (JIP). It interacts with the small GTP-binding protein ARF6.


Pssm-ID: 318633  Cd Length: 69  Bit Score: 116.94  E-value: 4.19e-30
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 254540204   386 MGKEVGNLLLENSQLLETKNALNVVKNDLIAKVDQLSGEQEVLKGELEAAKQAKVKLENRIKELEEELK 454
Cdd:pfam16471    1 MGKEVENLIKENTELLETKNALNVVKDDLIARVEELTNEREALKEELESLQESKTRLESRLKELEEELK 69
RILP-like cd14445
Rab interacting lysosomal protein-like 1 and 2 (Rilpl1 and Rilpl2); This domain is found in ...
32-103 2.95e-11

Rab interacting lysosomal protein-like 1 and 2 (Rilpl1 and Rilpl2); This domain is found in Rab interacting lysosomal protein-like 1 and 2, and appears to be conserved in Bilateria. The Rilp-like proteins regulate the concentration of ciliary membrane proteins in the primary cilium. Rilpl2 interacts with myosin-Va and has been linked to the regulation of cellular morphology in neurons; it forms a complex with Rac1 and activates Rac1-Pak signaling, dependent on myosin-Va.


Pssm-ID: 271220  Cd Length: 89  Bit Score: 63.00  E-value: 2.95e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 254540204   32 LAGSIYREFERLIHCYDEEVVKELMPLVVNVLENLDSVLSENQEHEVELELLREDNEQLltqyEREKALRKQ 103
Cdd:cd14445    21 IASAIGKEFERLIDRYGPEAVAGLMPKVVRVLELLEALASRNERENLEIEELRLEVDRL----ELEKRERAQ 88
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
49-517 3.67e-08

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 223496  Cd Length: 908  Bit Score: 57.85  E-value: 3.67e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204   49 EEVVKELMPLVVNvLENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRKQAEEKFIEFEDALEQEKKELQIQVEH 128
Cdd:COG0419   294 EELEREIEELEEE-LEGLRALLEELEELLEKLKSLEERLEKLEEKLEKLESELEELAEEKNELAKLLEERLKELEERLEE 372
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204  129 YEFQTRQLELKAKNYADQISRLEERESEMKKEYNALHQRHTEMIQTYVEhIERSKMQQVGGSGQTESSLpgRSRKERPTS 208
Cdd:COG0419   373 LEKELEKALERLKQLEEAIQELKEELAELSAALEEIQEELEELEKELEE-LERELEELEEEIKKLEEQI--NQLESKELM 449
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204  209 LNVFPLADGMCPNdemsesgqssaaatpsttgtksntptssvpsaavtpLNESLQPLGDYVSVTKNNKQAREKRNSRNME 288
Cdd:COG0419   450 IAELAGAGEKCPV------------------------------------CGQELPEEHEKELLELYELELEELEEELSRE 493
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204  289 VQVtQEMRNVsigmgssdewsdVQDIIDSTPELDVCPETRLErtgssptqgivnkafginTDSLYHELSTAGSEVIGDVD 368
Cdd:COG0419   494 KEE-AELREE------------IEELEKELRELEEELIELLE------------------LEEALKEELEEKLEKLENLL 542
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204  369 EGADLLGEFSVRDDFFGMGKEVGNLLLENSQLLETKNALNVVKNDL----------IAKVDQLSGEQEVLKGELEA--AK 436
Cdd:COG0419   543 EELEELKEKLQLQQLKEELRQLEDRLQELKELLEELRLLRTRKEELeelrerlkelKKKLKELEERLSQLEELLQSleLS 622
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204  437 QAKVKLENRIKELEEELKRVKSEAVTARREP------REEVEDVSSYLCTELDKIPMAQRRRFTRVEMARVLMERNQYKE 510
Cdd:COG0419   623 EAENELEEAEEELESELEKLNLQAELEELLQaaleelEEKVEELEAEIRRELQRIENEEQLEEKLEELEQLEEELEQLRE 702

                  ....*..
gi 254540204  511 RLMELQE 517
Cdd:COG0419   703 ELEELLK 709
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
27-181 6.82e-06

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 223496  Cd Length: 908  Bit Score: 50.53  E-value: 6.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204   27 ERVSGLAGSIYREFERLIhcydEEVVKELMPLvvnvLENLDSVLSENQEHEVELELLREDNEQLltQYEREKALRKQAEE 106
Cdd:COG0419   170 EKLSELLKEVIKEAKAKI----EELEGQLSEL----LEDIEDLLEALEEELKELKKLEEIQEEQ--EEEELEQEIEALEE 239
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204  107 KFIEFEDALEQ-EKKELQIQ---------VEHYEFQTRQLELKAKNYADQISRLEERESEMKKEYNAL--HQRHTEMIQT 174
Cdd:COG0419   240 RLAELEEEKERlEELKARLLeiesleleaLKIREEELRELERLLEELEEKIERLEELEREIEELEEELegLRALLEELEE 319

                  ....*..
gi 254540204  175 YVEHIER 181
Cdd:COG0419   320 LLEKLKS 326
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
63-182 7.35e-06

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  Cd Length: 745  Bit Score: 50.40  E-value: 7.35e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204    63 LENLDSVLSENQ----EHEVELELLREDNEQLLTQYERekaLRKQAEEKFIEFEDAlEQEKKELQIQVEHYEFQTRQLE- 137
Cdd:TIGR04523  351 LTNSESENSEKQreleEKQNEIEKLKKENQSYKQEIKN---LESQINDLESKIQNQ-EKLNQQKDEQIKKLQQEKELLEk 426
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 254540204   138 ----LKAKNY--ADQISRLEERESEMKKEYNALHQRhTEMIQTYVEHIERS 182
Cdd:TIGR04523  427 eierLKETIIknNSEIKDLTNQDSVKELIIKNLDNT-RESLETQLKVLSRS 476
PRK03918 PRK03918
chromosome segregation protein; Provisional
74-540 6.17e-05

chromosome segregation protein; Provisional


Pssm-ID: 235175  Cd Length: 880  Bit Score: 47.37  E-value: 6.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204   74 QEHEVELELLREDNEQLLTQYEREKALRKQAEE--KFIEFEDALEQEKKELQIQVEHYEFQTRQLELKAKNYADQISRLE 151
Cdd:PRK03918  262 RELEERIEELKKEIEELEEKVKELKELKEKAEEyiKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLE 341
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204  152 E---RESEMKKEYNALHQRHT--EMIQTYVEHIERSKMQQVGGS-------------------------GQTESSLPGRs 201
Cdd:PRK03918  342 ElkkKLKELEKRLEELEERHElyEEAKAKKEELERLKKRLTGLTpeklekeleelekakeeieeeiskiTARIGELKKE- 420
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204  202 RKERPTSLNVFPLADGMCP--NDEMSEsgqssaaatpsttgtksntptssvpsaavtplNESLQPLGDYvsvtknnkqar 279
Cdd:PRK03918  421 IKELKKAIEELKKAKGKCPvcGRELTE--------------------------------EHRKELLEEY----------- 457
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204  280 ekrnsrnmevqvTQEMRNVSigmgssdewSDVQDIIDSTPELDVcPETRLERTGSSPTQGIVNKAFGINTDSLYHELSTA 359
Cdd:PRK03918  458 ------------TAELKRIE---------KELKEIEEKERKLRK-ELRELEKVLKKESELIKLKELAEQLKELEEKLKKY 515
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204  360 GSEvigDVDEGADLLGEfsVRDDFFGMGKEVGNLLLEnsqlLETKNALNVVKNDLIAKVDQLSGEQEVLKGELEAAKQAK 439
Cdd:PRK03918  516 NLE---ELEKKAEEYEK--LKEKLIKLKGEIKSLKKE----LEKLEELKKKLAELEKKLDELEEELAELLKELEELGFES 586
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204  440 VK-LENRIKELEEELKRVkSEAVTARREPREEVEDVSSyLCTELDKIPMAQRRRFTRVEMARVLME---RNQYKERLMEL 515
Cdd:PRK03918  587 VEeLEERLKELEPFYNEY-LELKDAEKELEREEKELKK-LEEELDKAFEELAETEKRLEELRKELEeleKKYSEEEYEEL 664
                         490       500
                  ....*....|....*....|....*
gi 254540204  516 QEavrwtEMIRASREHPSVQEKKKS 540
Cdd:PRK03918  665 RE-----EYLELSRELAGLRAELEE 684
PRK03918 PRK03918
chromosome segregation protein; Provisional
33-164 8.37e-05

chromosome segregation protein; Provisional


Pssm-ID: 235175  Cd Length: 880  Bit Score: 46.98  E-value: 8.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204   33 AGSIYREFERLIHCYDEEVVKE--LMPLVVNVLENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRKQAEEKFIE 110
Cdd:PRK03918  167 LGEVIKEIKRRIERLEKFIKRTenIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKE 246
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 254540204  111 FEdALEQEKKELQIQVEHYEFQTRQLELKAKNYADQISRLEEREsEMKKEYNAL 164
Cdd:PRK03918  247 LE-SLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELK-EKAEEYIKL 298
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
397-523 2.12e-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  Cd Length: 1179  Bit Score: 45.82  E-value: 2.12e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204   397 NSQLLETKNALNVVK---NDLIAKVDQLSGEQEVLKGELEAAKQAKVKLENRIKELEEELKRVKSEAVTARRE------- 466
Cdd:TIGR02168  322 EAQLEELESKLDELAeelAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQiaslnne 401
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204   467 ---PREEVEDVSSYLcTELDKIPMAQRRRFTRVEMARVLMERNQYKERLMELQEAVRWTE 523
Cdd:TIGR02168  402 ierLEARLERLEDRR-ERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLE 460
Filament pfam00038
Intermediate filament protein;
393-530 3.46e-04

Intermediate filament protein;


Pssm-ID: 306535  Cd Length: 313  Bit Score: 44.14  E-value: 3.46e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204   393 LLLENSQL-LETKNALNVVKnDLIAKV-DQLSGEQEV------LKGELEAAKQAKVKLENRIKELEEE---LKRVKSEAV 461
Cdd:pfam00038   66 LTVERARLqLEIDNLRLAAE-DFRQKYeDELNLRQSAeadlvgLRKDLDEATLARVDLEMKVESLQEElafLKKNHEEEV 144
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 254540204   462 tarREPREEVED------VSSYLCTELDKIpMAQRRRFTRVEMARVLME-RNQYKERLMELQEAV-RWTEMIRASRE 530
Cdd:pfam00038  145 ---RELQSQVQDtqvnveMDAARKLDLTSA-LAEIRAQYEEIAAKNREEaEEWYQSKLEELQQAAaRNGDALRSAKE 217
PRK12495 PRK12495
hypothetical protein; Provisional
834-940 7.91e-04

hypothetical protein; Provisional


Pssm-ID: 183558  Cd Length: 226  Bit Score: 42.55  E-value: 7.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204  834 SRGDTPVLDKGQG-DVATTANGKVNPSQSTEEATEATEVPDPGPSESEA-------TTVRPGPLTEHVFTDPAPTPSssT 905
Cdd:PRK12495   69 TEDGAAGDDAGDGaEATAPSDAGSQASPDDDAQPAAEAEAADQSAPPEAsstsatdEAATDPPATAAARDGPTPDPT--A 146
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 254540204  906 QPASENGSESNGTIVQPQVEPSGElSTTTSSAAPT 940
Cdd:PRK12495  147 QPATPDERRSPRQRPPVSGEPPTP-STPDAHVAGT 180
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
86-181 3.42e-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: 214922  Cd Length: 140  Bit Score: 39.10  E-value: 3.42e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204     86 DNEQLLTQYEREKALRKQAEEKFIEFEDALEQEKKELQIQVEhyEFQTRQLELKAKNYADQISRLEERESEMKKEYNA-- 163
Cdd:smart00935    5 DVQKILQESPAGKAAQKQLEKEFKKRQAELEKLEKELQKLKE--KLQKDAATLSEAAREKKEKELQKKVQEFQRKQQKlq 82
                            90       100
                    ....*....|....*....|
gi 254540204    164 --LHQRHTEMIQTYVEHIER 181
Cdd:smart00935   83 qdLQKRQQEELQKILDKINK 102
SH3_and_anchor TIGR04211
SH3 domain protein; Members of this protein family have a signal peptide, a strongly conserved ...
388-466 3.76e-03

SH3 domain protein; Members of this protein family have a signal peptide, a strongly conserved SH3 domain, a variable region, and then a C-terminal hydrophobic transmembrane alpha helix region.


Pssm-ID: 275056  Cd Length: 198  Bit Score: 39.99  E-value: 3.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204   388 KEVGNLLLENSQLLETKNALNVVKNDLIAKVDQLSGEQEVLKGELEAAKQAK---VKLENRIKELEEELKRVKSEAVTAR 464
Cdd:TIGR04211   73 QELAELQEELAELQEQLAELRQENQELKQQLSTLEAELEELQKELERIKQISanaIELDEENRELREELAELKQENEALE 152

                   ..
gi 254540204   465 RE 466
Cdd:TIGR04211  153 AE 154
 
Name Accession Description Interval E-value
Jnk-SapK_ap_N pfam09744
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins ...
30-183 7.37e-77

JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins conserved from yeasts to humans. Most of the proteins in this entry have an RhoGEF pfam00621 domain at their C-terminal end.


Pssm-ID: 313040  Cd Length: 154  Bit Score: 252.52  E-value: 7.37e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204    30 SGLAGSIYREFERLIHCYDEEVVKELMPLVVNVLENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRKQAEEKFI 109
Cdd:pfam09744    1 YDIASSIYKEFERLIDRYGEDVVKGLMPKVVNVLELLESLASRNQEHEVELEELREDNEQLETQYEREKELRKRAEEELL 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 254540204   110 EFEDALEQEKKELQIQVEHYEFQTRQLELKAKNYADQISRLEERESEMKKEYNALHQRHTEMIQTYVEHIERSK 183
Cdd:pfam09744   81 ELEDQWEGERKDLQSKVEQLEEENRQLELKAKNYADQVSRLEEKEAELKKEYSKLHERENELLKKLKELVERQR 154
JIP_LZII pfam16471
JNK-interacting protein leucine zipper II; This is the second leucine zipper domain (LZII) of ...
386-454 4.19e-30

JNK-interacting protein leucine zipper II; This is the second leucine zipper domain (LZII) of several JNK-interacting proteins (JIP). It interacts with the small GTP-binding protein ARF6.


Pssm-ID: 318633  Cd Length: 69  Bit Score: 116.94  E-value: 4.19e-30
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 254540204   386 MGKEVGNLLLENSQLLETKNALNVVKNDLIAKVDQLSGEQEVLKGELEAAKQAKVKLENRIKELEEELK 454
Cdd:pfam16471    1 MGKEVENLIKENTELLETKNALNVVKDDLIARVEELTNEREALKEELESLQESKTRLESRLKELEEELK 69
RILP-like cd14445
Rab interacting lysosomal protein-like 1 and 2 (Rilpl1 and Rilpl2); This domain is found in ...
32-103 2.95e-11

Rab interacting lysosomal protein-like 1 and 2 (Rilpl1 and Rilpl2); This domain is found in Rab interacting lysosomal protein-like 1 and 2, and appears to be conserved in Bilateria. The Rilp-like proteins regulate the concentration of ciliary membrane proteins in the primary cilium. Rilpl2 interacts with myosin-Va and has been linked to the regulation of cellular morphology in neurons; it forms a complex with Rac1 and activates Rac1-Pak signaling, dependent on myosin-Va.


Pssm-ID: 271220  Cd Length: 89  Bit Score: 63.00  E-value: 2.95e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 254540204   32 LAGSIYREFERLIHCYDEEVVKELMPLVVNVLENLDSVLSENQEHEVELELLREDNEQLltqyEREKALRKQ 103
Cdd:cd14445    21 IASAIGKEFERLIDRYGPEAVAGLMPKVVRVLELLEALASRNERENLEIEELRLEVDRL----ELEKRERAQ 88
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
49-517 3.67e-08

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 223496  Cd Length: 908  Bit Score: 57.85  E-value: 3.67e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204   49 EEVVKELMPLVVNvLENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRKQAEEKFIEFEDALEQEKKELQIQVEH 128
Cdd:COG0419   294 EELEREIEELEEE-LEGLRALLEELEELLEKLKSLEERLEKLEEKLEKLESELEELAEEKNELAKLLEERLKELEERLEE 372
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204  129 YEFQTRQLELKAKNYADQISRLEERESEMKKEYNALHQRHTEMIQTYVEhIERSKMQQVGGSGQTESSLpgRSRKERPTS 208
Cdd:COG0419   373 LEKELEKALERLKQLEEAIQELKEELAELSAALEEIQEELEELEKELEE-LERELEELEEEIKKLEEQI--NQLESKELM 449
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204  209 LNVFPLADGMCPNdemsesgqssaaatpsttgtksntptssvpsaavtpLNESLQPLGDYVSVTKNNKQAREKRNSRNME 288
Cdd:COG0419   450 IAELAGAGEKCPV------------------------------------CGQELPEEHEKELLELYELELEELEEELSRE 493
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204  289 VQVtQEMRNVsigmgssdewsdVQDIIDSTPELDVCPETRLErtgssptqgivnkafginTDSLYHELSTAGSEVIGDVD 368
Cdd:COG0419   494 KEE-AELREE------------IEELEKELRELEEELIELLE------------------LEEALKEELEEKLEKLENLL 542
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204  369 EGADLLGEFSVRDDFFGMGKEVGNLLLENSQLLETKNALNVVKNDL----------IAKVDQLSGEQEVLKGELEA--AK 436
Cdd:COG0419   543 EELEELKEKLQLQQLKEELRQLEDRLQELKELLEELRLLRTRKEELeelrerlkelKKKLKELEERLSQLEELLQSleLS 622
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204  437 QAKVKLENRIKELEEELKRVKSEAVTARREP------REEVEDVSSYLCTELDKIPMAQRRRFTRVEMARVLMERNQYKE 510
Cdd:COG0419   623 EAENELEEAEEELESELEKLNLQAELEELLQaaleelEEKVEELEAEIRRELQRIENEEQLEEKLEELEQLEEELEQLRE 702

                  ....*..
gi 254540204  511 RLMELQE 517
Cdd:COG0419   703 ELEELLK 709
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
65-180 9.13e-07

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: 316375  Cd Length: 200  Bit Score: 50.68  E-value: 9.13e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204    65 NLDSVLSENQEHEVELELLREDNEQL---LTQYEREKALRKQAEEKFIEfedaLEQEKKELQIQVEhyefqtrqlelkak 141
Cdd:pfam13851   48 LMSEIAQENKRLTEPLKKAQEEVEELrkqLKNYEKDKQSLKNLKARLKV----LEKELKDLKWEHE-------------- 109
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 254540204   142 nyadqisRLEERESEMKKEYNALHQRHTEMIQTYVEHIE 180
Cdd:pfam13851  110 -------VLEQRFEKVERERDELYKKFEDAIQDVQQKTG 141
COG5665 COG5665
CCR4-NOT transcriptional regulation complex, NOT5 subunit [Transcription];
98-337 2.38e-06

CCR4-NOT transcriptional regulation complex, NOT5 subunit [Transcription];


Pssm-ID: 227952  Cd Length: 548  Bit Score: 51.60  E-value: 2.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204   98 KALRKQAEEKFI-----EFEDALEQ-EKKELQIQVEHYEFQTRQLELKAKNYAD-QIS-------------RLEERESEM 157
Cdd:COG5665   106 KELKKRDQVLFIhdcldELQKQLEQyEAQENEEQTERHEFHIANLENILKKLQNnEMDpepveefqddikyYVENNDDPD 185
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204  158 KKEYNALHQRHTEMIQTYVEHIERSKmqqVGGSGQTESSLPGRSRKERPTSL-----NVFPLADGMCPNDEMSESGQSSA 232
Cdd:COG5665   186 FIEYDTIYEDMGCEIQPSSSNNEAPK---EGNNQTSLSSIRSSKKQERSPKKkapqrDVSISDRATTPIAPGVESASQSI 262
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204  233 AATPSTTGTKsnTPTSSVPSAAVTPLNESLQPLGDYVSVTKNNKQA---------REKRNSRNMEVQVTQEMRNVSIGMG 303
Cdd:COG5665   263 SSTPTPVSTD--TPLHTVKDDSIKFDNSTLGTPTTHVSMKKKESENdseqqlnfpKDSTDEIRKTIQHDVETNAAFQNPL 340
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 254540204  304 SSDE--WSDVQDIIDSTPELDVCPETRLERTGSSPT 337
Cdd:COG5665   341 FNDElkWWLASKRYLTQPLQEMSPSMVSTLENSLLN 376
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
39-519 5.06e-06

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


Pssm-ID: 224117  Cd Length: 1163  Bit Score: 50.87  E-value: 5.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204   39 EFERLIHCYDEEVvKELMPLVVNVLENLDSVLSENQ----EHEVELELLREDNEQLLTQYEREKALRKQAEEKFIEFEDA 114
Cdd:COG1196   362 ELEEKLSALLEEL-EELFEALREELAELEAELAEIRneleELKREIESLEERLERLSERLEDLKEELKELEAELEELQTE 440
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204  115 LEQEKKELQIQVEHYEFQTRQLELKAKNYA---DQISRLEERESEMKKEYNALHQRHTEMiqTYVEHIERSKMQQVGGS- 190
Cdd:COG1196   441 LEELNEELEELEEQLEELRDRLKELERELAelqEELQRLEKELSSLEARLDRLEAEQRAS--QGVRAVLEALESGLPGVy 518
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204  191 GQTESSLPGRSRKER------PTSLNVF----PLADGMCPNdEMSESGQSSAAATPSTTgTKSNTPTSSVPSAAVTPL-- 258
Cdd:COG1196   519 GPVAELIKVKEKYETaleaalGNRLQAVvvenEEVAKKAIE-FLKENKAGRATFLPLDR-IKPLRSLKSDAAPGFLGLas 596
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204  259 -----NESLQPLGDYV--------SVTKNNKQAREKRNSRNMeVQVTQE-----------MRNVSIGMGSSDEWSDVQDI 314
Cdd:COG1196   597 dlidfDPKYEPAVRFVlgdtlvvdDLEQARRLARKLRIKYRI-VTLDGDlvepsgsitggSRNKRSSLAQKRELKELEEE 675
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204  315 IDSTpeldvcpETRLERTGSSptqgivNKAFGINTDSLYHELSTAGSEVigdvdEGADLLGEFSvrddffgmGKEVGNLL 394
Cdd:COG1196   676 LAEL-------EAQLEKLEEE------LKSLKNELRSLEDLLEELRRQL-----EELERQLEEL--------KRELAALE 729
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204  395 LENSQLLETKNALNVVKNDLIAKVDQLSGEQEVLKGELEAAKQAKVKLENRIKELEEELKRVKsEAVTARREPREEVEDV 474
Cdd:COG1196   730 EELEQLQSRLEELEEELEELEEELEELQERLEELEEELESLEEALAKLKEEIEELEEKRQALQ-EELEELEEELEEAERR 808
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*
gi 254540204  475 SSYLCTELDKIpmAQRRRFTRVEMARVLMERNQYKERLMELQEAV 519
Cdd:COG1196   809 LDALERELESL--EQRRERLEQEIEELEEEIEELEEKLDELEEEL 851
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
60-181 5.14e-06

Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation.


Pssm-ID: 310624  Cd Length: 542  Bit Score: 50.60  E-value: 5.14e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204    60 VNVLENLDSV---LSENQEHEVELEL--LREDNEQLLTQY-------EREKALRKQAEEKFIEFEDAL---EQEKKELQI 124
Cdd:pfam06160  233 LNIEYEIEELekkIEEILALLKVLELedAEEELKTIEDYIdslyddfEKEVEAKKYVEKNLKELKDKLehaEKQNKELKE 312
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 254540204   125 QVEH----YEFQTRQLElKAKNYADQIsrleereSEMKKEYNALHQRHTEMIQTYVEHIER 181
Cdd:pfam06160  313 ELDRlkqsYDLNEDELE-RLRELEKEL-------KELEKDYDELVERLANKKFAYSELQEE 365
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
63-520 5.80e-06

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


Pssm-ID: 224117  Cd Length: 1163  Bit Score: 50.87  E-value: 5.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204   63 LENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRKQAEEKFIEfedALEQEKKELQIQVEHYEFQTRQLELKAKN 142
Cdd:COG1196   332 IEALKEELEERETLLEELEQLLAELEEAKEELEEKLSALLEELEELFE---ALREELAELEAELAEIRNELEELKREIES 408
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204  143 YADQISRLEERESEMKKEYNALH------QRHTEMIQTYVEHIERSKMQQVGGSGQTESSLPGRSRKERPTslnvfplad 216
Cdd:COG1196   409 LEERLERLSERLEDLKEELKELEaeleelQTELEELNEELEELEEQLEELRDRLKELERELAELQEELQRL--------- 479
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204  217 gmcpNDEMSESGQSSAAATpstTGTKSNTPTSSVPSAAVTPLNESLQPLGDYVSVTKNNKQArekrnsrnmevqvtqemr 296
Cdd:COG1196   480 ----EKELSSLEARLDRLE---AEQRASQGVRAVLEALESGLPGVYGPVAELIKVKEKYETA------------------ 534
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204  297 nVSIGMGSSDEWSDVQDIIDSTPELDVCPETRLERT---------GSSPTQGIVNKAFGINTDSLY---HELSTAGSEVI 364
Cdd:COG1196   535 -LEAALGNRLQAVVVENEEVAKKAIEFLKENKAGRAtflpldrikPLRSLKSDAAPGFLGLASDLIdfdPKYEPAVRFVL 613
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204  365 GDV------DEGADLLGEFSVR--------DDFFGMGKEVGNLLLENSQLLETKNAlnvvkNDLIAKVDQLSGEQEVLKG 430
Cdd:COG1196   614 GDTlvvddlEQARRLARKLRIKyrivtldgDLVEPSGSITGGSRNKRSSLAQKREL-----KELEEELAELEAQLEKLEE 688
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204  431 ELEAAKQAKVKLENRIKELE---EELKRVKSEAVTARREPREEVEDVSSYLcTELDKipmaqrrrftrvEMARVLMERNQ 507
Cdd:COG1196   689 ELKSLKNELRSLEDLLEELRrqlEELERQLEELKRELAALEEELEQLQSRL-EELEE------------ELEELEEELEE 755
                         490
                  ....*....|...
gi 254540204  508 YKERLMELQEAVR 520
Cdd:COG1196   756 LQERLEELEEELE 768
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
27-181 6.82e-06

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 223496  Cd Length: 908  Bit Score: 50.53  E-value: 6.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204   27 ERVSGLAGSIYREFERLIhcydEEVVKELMPLvvnvLENLDSVLSENQEHEVELELLREDNEQLltQYEREKALRKQAEE 106
Cdd:COG0419   170 EKLSELLKEVIKEAKAKI----EELEGQLSEL----LEDIEDLLEALEEELKELKKLEEIQEEQ--EEEELEQEIEALEE 239
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204  107 KFIEFEDALEQ-EKKELQIQ---------VEHYEFQTRQLELKAKNYADQISRLEERESEMKKEYNAL--HQRHTEMIQT 174
Cdd:COG0419   240 RLAELEEEKERlEELKARLLeiesleleaLKIREEELRELERLLEELEEKIERLEELEREIEELEEELegLRALLEELEE 319

                  ....*..
gi 254540204  175 YVEHIER 181
Cdd:COG0419   320 LLEKLKS 326
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
63-182 7.35e-06

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  Cd Length: 745  Bit Score: 50.40  E-value: 7.35e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204    63 LENLDSVLSENQ----EHEVELELLREDNEQLLTQYERekaLRKQAEEKFIEFEDAlEQEKKELQIQVEHYEFQTRQLE- 137
Cdd:TIGR04523  351 LTNSESENSEKQreleEKQNEIEKLKKENQSYKQEIKN---LESQINDLESKIQNQ-EKLNQQKDEQIKKLQQEKELLEk 426
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 254540204   138 ----LKAKNY--ADQISRLEERESEMKKEYNALHQRhTEMIQTYVEHIERS 182
Cdd:TIGR04523  427 eierLKETIIknNSEIKDLTNQDSVKELIIKNLDNT-RESLETQLKVLSRS 476
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
48-187 7.47e-06

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


Pssm-ID: 224117  Cd Length: 1163  Bit Score: 50.48  E-value: 7.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204   48 DEEVVKELMPLVVNVLENLDSVLSENQEH----EVELELLREDNEQLLTQYEREKALRKQAEEKFIEFEDAL---EQEKK 120
Cdd:COG1196   780 EIEELEEKRQALQEELEELEEELEEAERRldalERELESLEQRRERLEQEIEELEEEIEELEEKLDELEEELeelEKELE 859
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 254540204  121 ELQIQVEHYEFQTRQLElkaknyaDQISRLEERESEMKKEYNALHQRHTEM---IQTYVEHIER--SKMQQV 187
Cdd:COG1196   860 ELKEELEELEAEKEELE-------DELKELEEEKEELEEELRELESELAELkeeIEKLRERLEEleAKLERL 924
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
63-185 2.13e-05

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


Pssm-ID: 224117  Cd Length: 1163  Bit Score: 48.94  E-value: 2.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204   63 LENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRKQAEEKFIEFEDALEQEKKELQIQVEHYEFQTRQLELKAKN 142
Cdd:COG1196   739 LEELEEELEELEEELEELQERLEELEEELESLEEALAKLKEEIEELEEKRQALQEELEELEEELEEAERRLDALERELES 818
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 254540204  143 YADQISRLEERESEMKKEYNALHQRhtemIQTYVEHIERSKMQ 185
Cdd:COG1196   819 LEQRRERLEQEIEELEEEIEELEEK----LDELEEELEELEKE 857
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
32-167 4.67e-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  Cd Length: 1164  Bit Score: 47.76  E-value: 4.67e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204    32 LAGSIYREFERLIHCYDEEVVKelmplVVNVLENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRKQAEEKFIEF 111
Cdd:TIGR02169  788 LSHSRIPEIQAELSKLEEEVSR-----IEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGK 862
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 254540204   112 EDALEQEKKELQIQVEHYEFQTRQLELKAKNYADQISRLEERESEMKKEYNALHQR 167
Cdd:TIGR02169  863 KEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKR 918
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
66-182 5.53e-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  Cd Length: 1164  Bit Score: 47.37  E-value: 5.53e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204    66 LDSVLSENQEHEVELELLREDNEQLLTQYEREKALRKQAEEKFIEFEDALEQEKKELQiqveHYEFQTRQLELKAKNYAD 145
Cdd:TIGR02169  704 LDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELK----ELEARIEELEEDLHKLEE 779
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 254540204   146 QISRLEERES-----EMKKEYNALHQRHTEmIQTYVEHIERS 182
Cdd:TIGR02169  780 ALNDLEARLShsripEIQAELSKLEEEVSR-IEARLREIEQK 820
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
86-173 5.67e-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: 309164  Cd Length: 155  Bit Score: 44.48  E-value: 5.67e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204    86 DNEQLLTQYEREKALRKQAEEKFIEFEDALEQEKKELQIQVEHYEFQTRQLELKAKNYADQISRLEERESEMKKEYNALH 165
Cdd:pfam03938   22 DVQKILQESPEGKAAQAQLEKEFKKRQAELEAKEKELQKLYEELQKDGATLEEEREEKEQELQKKEQELQQLQQKAQELQ 101

                   ....*...
gi 254540204   166 QRHTEMIQ 173
Cdd:pfam03938  102 KKQQELLQ 109
PRK03918 PRK03918
chromosome segregation protein; Provisional
74-540 6.17e-05

chromosome segregation protein; Provisional


Pssm-ID: 235175  Cd Length: 880  Bit Score: 47.37  E-value: 6.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204   74 QEHEVELELLREDNEQLLTQYEREKALRKQAEE--KFIEFEDALEQEKKELQIQVEHYEFQTRQLELKAKNYADQISRLE 151
Cdd:PRK03918  262 RELEERIEELKKEIEELEEKVKELKELKEKAEEyiKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLE 341
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204  152 E---RESEMKKEYNALHQRHT--EMIQTYVEHIERSKMQQVGGS-------------------------GQTESSLPGRs 201
Cdd:PRK03918  342 ElkkKLKELEKRLEELEERHElyEEAKAKKEELERLKKRLTGLTpeklekeleelekakeeieeeiskiTARIGELKKE- 420
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204  202 RKERPTSLNVFPLADGMCP--NDEMSEsgqssaaatpsttgtksntptssvpsaavtplNESLQPLGDYvsvtknnkqar 279
Cdd:PRK03918  421 IKELKKAIEELKKAKGKCPvcGRELTE--------------------------------EHRKELLEEY----------- 457
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204  280 ekrnsrnmevqvTQEMRNVSigmgssdewSDVQDIIDSTPELDVcPETRLERTGSSPTQGIVNKAFGINTDSLYHELSTA 359
Cdd:PRK03918  458 ------------TAELKRIE---------KELKEIEEKERKLRK-ELRELEKVLKKESELIKLKELAEQLKELEEKLKKY 515
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204  360 GSEvigDVDEGADLLGEfsVRDDFFGMGKEVGNLLLEnsqlLETKNALNVVKNDLIAKVDQLSGEQEVLKGELEAAKQAK 439
Cdd:PRK03918  516 NLE---ELEKKAEEYEK--LKEKLIKLKGEIKSLKKE----LEKLEELKKKLAELEKKLDELEEELAELLKELEELGFES 586
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204  440 VK-LENRIKELEEELKRVkSEAVTARREPREEVEDVSSyLCTELDKIPMAQRRRFTRVEMARVLME---RNQYKERLMEL 515
Cdd:PRK03918  587 VEeLEERLKELEPFYNEY-LELKDAEKELEREEKELKK-LEEELDKAFEELAETEKRLEELRKELEeleKKYSEEEYEEL 664
                         490       500
                  ....*....|....*....|....*
gi 254540204  516 QEavrwtEMIRASREHPSVQEKKKS 540
Cdd:PRK03918  665 RE-----EYLELSRELAGLRAELEE 684
PRK03918 PRK03918
chromosome segregation protein; Provisional
33-164 8.37e-05

chromosome segregation protein; Provisional


Pssm-ID: 235175  Cd Length: 880  Bit Score: 46.98  E-value: 8.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204   33 AGSIYREFERLIHCYDEEVVKE--LMPLVVNVLENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRKQAEEKFIE 110
Cdd:PRK03918  167 LGEVIKEIKRRIERLEKFIKRTenIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKE 246
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 254540204  111 FEdALEQEKKELQIQVEHYEFQTRQLELKAKNYADQISRLEEREsEMKKEYNAL 164
Cdd:PRK03918  247 LE-SLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELK-EKAEEYIKL 298
PRK12704 PRK12704
phosphodiesterase; Provisional
72-224 9.75e-05

phosphodiesterase; Provisional


Pssm-ID: 237177  Cd Length: 520  Bit Score: 46.31  E-value: 9.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204   72 ENQEHEVELELlREDNEQLLTQYEREKALR----KQAEEKFIEFE-------DALEQEKKELQIQVEHYEFQTRQLELKA 140
Cdd:PRK12704   52 EAIKKEALLEA-KEEIHKLRNEFEKELRERrnelQKLEKRLLQKEenldrklELLEKREEELEKKEKELEQKQQELEKKE 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204  141 KNY----ADQISRLEE---------RE---SEMKKEynALHQRhTEMIQTYVEHIE-----RSK------MQQVGGSGQT 193
Cdd:PRK12704  131 EELeeliEEQLQELERisgltaeeaKEillEKVEEE--ARHEA-AVLIKEIEEEAKeeadkKAKeilaqaIQRCAADHVA 207
                         170       180       190
                  ....*....|....*....|....*....|.
gi 254540204  194 EsslpgrsrkerpTSLNVFPLadgmcPNDEM 224
Cdd:PRK12704  208 E------------TTVSVVNL-----PNDEM 221
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
25-186 1.08e-04

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 223496  Cd Length: 908  Bit Score: 46.68  E-value: 1.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204   25 MSERVSGLAGSIYREFERLIHCYD--EEVVKELMPLV----VNVLENLDSVLSENQEHEVELELLREDNEQLLTQYEREK 98
Cdd:COG0419   183 AKAKIEELEGQLSELLEDIEDLLEalEEELKELKKLEeiqeEQEEEELEQEIEALEERLAELEEEKERLEELKARLLEIE 262
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204   99 AL-------RKQAEEKFIEFEDALEQEKKEL-QIQVEHYEFQTRQLELKAK-----NYADQISRLEERESEMKKEYNALh 165
Cdd:COG0419   263 SLelealkiREEELRELERLLEELEEKIERLeELEREIEELEEELEGLRALleeleELLEKLKSLEERLEKLEEKLEKL- 341
                         170       180
                  ....*....|....*....|.
gi 254540204  166 QRHTEMIQTYVEhiERSKMQQ 186
Cdd:COG0419   342 ESELEELAEEKN--ELAKLLE 360
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
70-186 1.66e-04

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


Pssm-ID: 224117  Cd Length: 1163  Bit Score: 45.86  E-value: 1.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204   70 LSENQEHEVELELLREDneqLLTQYERekaLRKQAEeKFIEFEDaLEQEKKELQIQVEHYEFQTRQLELKA--------- 140
Cdd:COG1196   181 LERTEENLERLEDLLEE---LEKQLEK---LERQAE-KAERYQE-LKAELRELELALLLAKLKELRKELEEleeelsrle 252
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 254540204  141 ----------KNYADQISRLEERESEMKKEYNALHQRH---TEMIQTYVEHIERSKMQQ 186
Cdd:COG1196   253 eeleelqeelEEAEKEIEELKSELEELREELEELQEELlelKEEIEELEGEISLLRERL 311
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
397-523 2.12e-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  Cd Length: 1179  Bit Score: 45.82  E-value: 2.12e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204   397 NSQLLETKNALNVVK---NDLIAKVDQLSGEQEVLKGELEAAKQAKVKLENRIKELEEELKRVKSEAVTARRE------- 466
Cdd:TIGR02168  322 EAQLEELESKLDELAeelAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQiaslnne 401
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204   467 ---PREEVEDVSSYLcTELDKIPMAQRRRFTRVEMARVLMERNQYKERLMELQEAVRWTE 523
Cdd:TIGR02168  402 ierLEARLERLEDRR-ERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLE 460
TPR_MLP1_2 pfam07926
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ...
64-167 2.14e-04

TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerisation of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.


Pssm-ID: 311742  Cd Length: 124  Bit Score: 42.59  E-value: 2.14e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204    64 ENLDSVLSENQEHEVELELLREDNE---QLLTQ----YERE--------KALRK------QAEEKFIEFEDALEQEKKEL 122
Cdd:pfam07926    3 SEIKRLKEEIEEYEAQLQSLQEDLEsqaEIAKEaqqkYERElvlhaediKALQAlreelnELKQEIAELKAEAESAKAEL 82
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 254540204   123 QIQVEHYEFQTRQLElkaknyaDQISRLEERESEMKKEYNALHQR 167
Cdd:pfam07926   83 EESEESWEEQKKELE-------KELSELEKRIEDLNEQNKLLHDQ 120
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
64-160 2.36e-04

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  Cd Length: 745  Bit Score: 45.40  E-value: 2.36e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204    64 ENLDSVLSENQEHEVELELLREDNEQ--------------LLTQYEREKALRKQAEEKFIEFEDA-------LEQEKKEL 122
Cdd:TIGR04523  412 EQIKKLQQEKELLEKEIERLKETIIKnnseikdltnqdsvKELIIKNLDNTRESLETQLKVLSRSinkikqnLEQKQKEL 491
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 254540204   123 QIQV-EHYEF--QTRQLELKAKNYADQISRLEERESEMKKE 160
Cdd:TIGR04523  492 KSKEkELKKLneEKKELEEKVKDLTKKISSLKEKIEKLESE 532
Taxilin pfam09728
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ...
66-186 2.64e-04

Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain in its C-terminal half and is ubiquitously expressed. It is a novel binding partner of several syntaxin family members and is possibly involved in Ca2+-dependent exocytosis in neuroendocrine cells. Gamma-taxilin, described as leucine zipper protein Factor Inhibiting ATF4-mediated Transcription (FIAT), localizes to the nucleus in osteoblasts and dimerizes with ATF4 to form inactive dimers, thus inhibiting ATF4-mediated transcription.


Pssm-ID: 313024  Cd Length: 302  Bit Score: 44.55  E-value: 2.64e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204    66 LDSVLSENQEHEVELELLR--EDNEQLLTQYEREKALRKQAE---EKFIEFEDALEQEKKElqiqvehyeFQTRQLELKA 140
Cdd:pfam09728  172 LQQANEEQEKKAQEKELLKlrELQAQVQTLSETEKELREQLNvyvEKFKEFQDTLNKSNEL---------FLTFKKEMEK 242
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 254540204   141 KNyaDQISRLEERESEMKKEYNALHQRHTEMIQTYVEHIERSKMQQ 186
Cdd:pfam09728  243 MS--KKTKKLEKENLTWKRKHEKTNKALLEMAEERQKLKEELEKLK 286
APG6 pfam04111
Autophagy protein Apg6; In yeast, 15 Apg proteins coordinate the formation of autophagosomes. ...
61-170 2.70e-04

Autophagy protein Apg6; 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: 309295  Cd Length: 308  Bit Score: 44.48  E-value: 2.70e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204    61 NVLENLDSVLSENQ-EHEVELELLREDNEQLLTQYEREKALR-----KQAEEKFIEFEDALEQEKKELQIQVEHYEFQTR 134
Cdd:pfam04111    9 LLLEELDKELEQLEkERDAYQEFLKKLEKEKPSDEEIEALEKeleklEKEEEELLQELEELEKEREELDAELEKLEEELE 88
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 254540204   135 QlelkaknyadqisrLEERESEMKKEYNALHQRHTE 170
Cdd:pfam04111   89 E--------------LDEEEEEYWREYNAFQLELLE 110
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
350-541 3.41e-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  Cd Length: 1179  Bit Score: 45.05  E-value: 3.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204   350 DSLYHELSTAGSEVIGDVDEGADLLGEFS-VRDDFFGMGKEVGNLLLENSQLLETKNALNVVKNDLIAKVDQLSG----- 423
Cdd:TIGR02168  701 AELRKELEELEEELEQLRKELEELSRQISaLRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEelaea 780
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204   424 --EQEVLKGELEAAKQAKVKLENRIKELEEELKRVKSEAVTARREpREEVEDVSSYLCTELDKIpmAQRRRFTRVEMARV 501
Cdd:TIGR02168  781 eaEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER-LESLERRIAATERRLEDL--EEQIEELSEDIESL 857
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 254540204   502 LMERNQYKERLMELQEAV-RWTEMIRASREHPSVQEKKKST 541
Cdd:TIGR02168  858 AAEIEELEELIEELESELeALLNERASLEEALALLRSELEE 898
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
66-183 3.41e-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: 308206  Cd Length: 1162  Bit Score: 44.96  E-value: 3.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204    66 LDSVLSENQEHEVELELLREDNEQLLtqyEREKALRKQAEEKFIEFEDALEQEKKELQIQVEHYEFQTRQLELKAKNYAD 145
Cdd:pfam02463  229 YLDYLKLNEERIDLLQELLRDEQEEI---ESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLK 305
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 254540204   146 ---QISRLEERESEMKKEyNALHQRHTEMIQTYVEHIERSK 183
Cdd:pfam02463  306 lerRKVDDEEKLKESEKE-KKKAEKELKKEKEEIEELEKEL 345
Filament pfam00038
Intermediate filament protein;
393-530 3.46e-04

Intermediate filament protein;


Pssm-ID: 306535  Cd Length: 313  Bit Score: 44.14  E-value: 3.46e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204   393 LLLENSQL-LETKNALNVVKnDLIAKV-DQLSGEQEV------LKGELEAAKQAKVKLENRIKELEEE---LKRVKSEAV 461
Cdd:pfam00038   66 LTVERARLqLEIDNLRLAAE-DFRQKYeDELNLRQSAeadlvgLRKDLDEATLARVDLEMKVESLQEElafLKKNHEEEV 144
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 254540204   462 tarREPREEVED------VSSYLCTELDKIpMAQRRRFTRVEMARVLME-RNQYKERLMELQEAV-RWTEMIRASRE 530
Cdd:pfam00038  145 ---RELQSQVQDtqvnveMDAARKLDLTSA-LAEIRAQYEEIAAKNREEaEEWYQSKLEELQQAAaRNGDALRSAKE 217
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
41-540 4.24e-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  Cd Length: 1164  Bit Score: 44.67  E-value: 4.24e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204    41 ERLIHCYDEEVvKELMPLVVNVLENLDSVLSENQEHEVELELLREDNEQLLTQY----EREKALRKQAEE---KFIEFED 113
Cdd:TIGR02169  307 ERSIAEKEREL-EDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYaelkEELEDLRAELEEvdkEFAETRD 385
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204   114 ALEQEKKEL-QIQVEHYEFQTRQLELKaknyaDQISRLEERESEMKKEYNALHQRHTEM------IQTYVEHIERSKMQQ 186
Cdd:TIGR02169  386 ELKDYREKLeKLKREINELKRELDRLQ-----EELQRLSEELADLNAAIAGIEAKINELeeekedKALEIKKQEWKLEQL 460
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204   187 VGGSGQTESSLpgRSRKERPTSLNvfpladgmcpnDEMSESgQSSAAATPSTTGTKSNTPTSSvpSAAVTPLNESLQ--- 263
Cdd:TIGR02169  461 AADLSKYEQEL--YDLKEEYDRVE-----------KELSKL-QRELAEAEAQARASEERVRGG--RAVEEVLKASIQgvh 524
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204   264 -PLGDYVSVtknnkqarEKRNSRNMEVQVTQEMRNVSIgmgssDEWSDVQDIIDSTPELDVCPET-----RLERTGSSPT 337
Cdd:TIGR02169  525 gTVAQLGSV--------GERYATAIEVAAGNRLNNVVV-----EDDAVAKEAIELLKRRKAGRATflplnKMRDERRDLS 591
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204   338 QGIVNKAFGINTDSLYHE--LSTAGSEVIGD------VDEGADLLGEFSvrddFFGMGKEvgnlLLENSQLL----ETKN 405
Cdd:TIGR02169  592 ILSEDGVIGFAVDLVEFDpkYEPAFKYVFGDtlvvedIEAARRLMGKYR----MVTLEGE----LFEKSGAMtggsRAPR 663
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204   406 ALNVVKNDLIAKVDQLSGEQEVLKGELEAAKQAKVKLENRIKELEEELKRVKSEAVTARRE----------PREEVEDVS 475
Cdd:TIGR02169  664 GGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEieqleqeeekLKERLEELE 743
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 254540204   476 SYLcTELDkipmaQRRRFTRVEMARVLMERNQYKERLMELQEAVrwtEMIRASREHPSVQEKKKS 540
Cdd:TIGR02169  744 EDL-SSLE-----QEIENVKSELKELEARIEELEEDLHKLEEAL---NDLEARLSHSRIPEIQAE 799
COG4372 COG4372
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];
415-516 4.54e-04

Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 226809  Cd Length: 499  Bit Score: 44.25  E-value: 4.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204  415 IAKVDQLSGEQEVLKGELEAAKQAKvklenriKELEEELKRVKSEAVTARREpREEVEDVSSYLCTELDKIPMAQRR--- 491
Cdd:COG4372    73 VFQLDDIRPQLRALRTELGTAQGEK-------RAAETEREAARSELQKARQE-REAVRQELAAARQNLAKAQQELARltk 144
                          90       100
                  ....*....|....*....|....*..
gi 254540204  492 --RFTRVEMARVLMERNQYKERLMELQ 516
Cdd:COG4372   145 qaQDLQTRLKTLAEQRRQLEAQAQSLQ 171
Lebercilin pfam15619
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ...
39-167 4.57e-04

Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.


Pssm-ID: 317931  Cd Length: 180  Bit Score: 42.58  E-value: 4.57e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204    39 EFERLIHCYDEEVvkelmplvvnvlENLDSVLSENQEHEVELEL-LREDNEQLLTQYEREKALRKQAEEKFI----EFED 113
Cdd:pfam15619   50 ELPQLLARHNEEV------------RVLRERLRRSQEKERDLERkLKEKEAELLRLQDKLKKLKKLSEDKNLpereELQK 117
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 254540204   114 ALEQEKKELQIQVEhyEFQT--RQLELKAKNYADQISRLEERESEMKKEYNALHQR 167
Cdd:pfam15619  118 KLEALEAKLEEKER--KIKEleRQLELLEKNFRRQLAAEKKKTKEAQEEVKALQEE 171
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
61-174 4.61e-04

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  Cd Length: 745  Bit Score: 44.24  E-value: 4.61e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204    61 NVLENLDSVLSENQEHEVELELLREDNEQLLTQYEREK-ALRKQAEEKFIEFEDaLEQEKKELQIQVEHYEFQTRQLELK 139
Cdd:TIGR04523  321 KKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENsEKQRELEEKQNEIEK-LKKENQSYKQEIKNLESQINDLESK 399
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 254540204   140 AKNYADQISRLEERESEMKKEYNALHQRHTEMIQT 174
Cdd:TIGR04523  400 IQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKET 434
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
379-518 5.00e-04

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


Pssm-ID: 224117  Cd Length: 1163  Bit Score: 44.32  E-value: 5.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204  379 VRDDFFGMGKEVGNLLLENSQLLETKNALNVVKNDLIAKVDQLSGEQEVLKGELEAAKQAKVKLENRIKELEEELKRVKS 458
Cdd:COG1196   805 AERRLDALERELESLEQRRERLEQEIEELEEEIEELEEKLDELEEELEELEKELEELKEELEELEAEKEELEDELKELEE 884
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204  459 EAVTARREPREevedvssyLCTELDKIpmAQRRRFTRVEMARVLMERNQYKERLMELQEA 518
Cdd:COG1196   885 EKEELEEELRE--------LESELAEL--KEEIEKLRERLEELEAKLERLEVELPELEEE 934
RNase_Y TIGR03319
ribonuclease Y; Members of this family are RNase Y, an endoribonuclease. The member from ...
74-194 5.38e-04

ribonuclease Y; Members of this family are RNase Y, an endoribonuclease. The member from Bacillus subtilis, YmdA, has been shown to be involved in turnover of yitJ riboswitch. [Transcription, Degradation of RNA]


Pssm-ID: 188306  Cd Length: 514  Bit Score: 44.15  E-value: 5.38e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204    74 QEHEVELELLREDNEQLLTQYERE-KALRKQA-----EEKFI---EFEDALEQEKKELQIQVEHYEFQTRQLELKAKNYA 144
Cdd:TIGR03319   21 RIAEKKLGSAEELAKRIIEEAKKEaETLKKEAlleakEEVHKlraELERELKERRNELQRLERRLLQREETLDRKMESLD 100
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 254540204   145 DQISRLEERESEMKKEYNALHQRHTEMIQTYVEhiERSKMQQVGGSGQTE 194
Cdd:TIGR03319  101 KKEENLEKKEKELSNKEKNLDEKEEELEELIAE--QREELERISGLTQEE 148
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
64-530 5.38e-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  Cd Length: 1179  Bit Score: 44.28  E-value: 5.38e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204    64 ENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRKQAEEKFIEFEDALEQEKKELQIQVEHYEFQTRQLELKAKNY 143
Cdd:TIGR02168  309 ERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKV 388
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204   144 AD----------QISRLEERESEMKKEYNALHQRHTEMIQTYVEHIERSKMQQVGGSGQTESSLPGR-SRKERPTSLNVF 212
Cdd:TIGR02168  389 AQlelqiaslnnEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEElERLEEALEELRE 468
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204   213 PLADGMCPNDEMSESGQSSAAATPSTTGTKSNtpTSSVPSAAVTPLNESLQ------PLGDYVSVTKNNKQAREKRNSRN 286
Cdd:TIGR02168  469 ELEEAEQALDAAERELAQLQARLDSLERLQEN--LEGFSEGVKALLKNQSGlsgilgVLSELISVDEGYEAAIEAALGGR 546
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204   287 MEVQVtqeMRNVSIGMG--SSDEWSDVQDIidSTPELDVCPETRLE-RTGSSPTQGIVNKAFGINTDSLYHELSTA---- 359
Cdd:TIGR02168  547 LQAVV---VENLNAAKKaiAFLKQNELGRV--TFLPLDSIKGTEIQgNDREILKNIEGFLGVAKDLVKFDPKLRKAlsyl 621
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204   360 --GSEVIGDVDEGADLLGE-------FSVRDDFFGM-GKEVGNLLLENSQLLETKNALNVVKND---LIAKVDQLSGEQE 426
Cdd:TIGR02168  622 lgGVLVVDDLDNALELAKKlrpgyriVTLDGDLVRPgGVITGGSAKTNSSILERRREIEELEEKieeLEEKIAELEKALA 701
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204   427 VLKGELEAAKQAKVKLENRIKELEEELKRVKSEAVTARREPREEVEDVS--SYLCTELDKIPMAQRRRF--TRVEMARVL 502
Cdd:TIGR02168  702 ELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAqlSKELTELEAEIEELEERLeeAEEELAEAE 781
                          490       500
                   ....*....|....*....|....*....
gi 254540204   503 MERNQYKERLMELQEAVR-WTEMIRASRE 530
Cdd:TIGR02168  782 AEIEELEAQIEQLKEELKaLREALDELRA 810
Spc7 pfam08317
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
385-522 5.80e-04

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


Pssm-ID: 311978  Cd Length: 311  Bit Score: 43.37  E-value: 5.80e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204   385 GMGKEVGNLLLENSQLLETKNALNVVKNDLIAKVDQLSGEQEVL-----------KGELEAAKQ----AKVKLENR---I 446
Cdd:pfam08317  144 GLEENLEGLEEDKAVLEKQEELLDELLPELVKEYAELEEELELLqeraeelencdKDELEELREelaeQDAEIEEKkreL 223
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 254540204   447 KELEEELKRV--KSEAVTARRepREEVEDVSsylctELDKIPMAQrRRFTRVEMARvlmernqYKERLMELQEAVRWT 522
Cdd:pfam08317  224 AELQEQLEELeeKIEELKEQK--QELLEEIA-----EAERVREEC-RGWTESEVSR-------LKARVDALENLTGWR 286
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
70-167 6.63e-04

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 316391  Cd Length: 352  Bit Score: 43.35  E-value: 6.63e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204    70 LSENQEHEVELELLREDNEQLLTQYEREKALRKQAEEKFIEfedaLEQEKKELQIQVEHYEFQTRQLELKAKNYADQISR 149
Cdd:pfam13868  237 LKQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDERIE----QEEAEKRREKRLEHRRELEKQIEERERQREAEREE 312
                           90
                   ....*....|....*...
gi 254540204   150 LEERESEMKKEYNALHQR 167
Cdd:pfam13868  313 EFEEGEALREEEAERRER 330
Filament pfam00038
Intermediate filament protein;
66-185 6.80e-04

Intermediate filament protein;


Pssm-ID: 306535  Cd Length: 313  Bit Score: 42.98  E-value: 6.80e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204    66 LDSVLSENQEHEVELELLREDNEQLLTQYEREKALRKQAEEKFIEFE---DALEQEKKELQIQVEHYefqTRQLELKAKN 142
Cdd:pfam00038   63 LDQLTVERARLQLEIDNLRLAAEDFRQKYEDELNLRQSAEADLVGLRkdlDEATLARVDLEMKVESL---QEELAFLKKN 139
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 254540204   143 YADQISRLEERES------EMKkeyNALHQRHT----EMIQTYVEHIERSKMQ 185
Cdd:pfam00038  140 HEEEVRELQSQVQdtqvnvEMD---AARKLDLTsalaEIRAQYEEIAAKNREE 189
Taxilin pfam09728
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ...
63-162 6.98e-04

Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain in its C-terminal half and is ubiquitously expressed. It is a novel binding partner of several syntaxin family members and is possibly involved in Ca2+-dependent exocytosis in neuroendocrine cells. Gamma-taxilin, described as leucine zipper protein Factor Inhibiting ATF4-mediated Transcription (FIAT), localizes to the nucleus in osteoblasts and dimerizes with ATF4 to form inactive dimers, thus inhibiting ATF4-mediated transcription.


Pssm-ID: 313024  Cd Length: 302  Bit Score: 43.01  E-value: 6.98e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204    63 LENLDSVLSENQEHEVELellREDNEQL-------LTQYE-REKALRKQAEEKfiEFEDALeQEKKELQIQVEHYEFQTR 134
Cdd:pfam09728  112 LKDIQDKMEENSEPNEKL---REENEELreklkslIEQYElRELHFEKLLKTK--ELEVQL-AEAKLQQANEEQEKKAQE 185
                           90       100
                   ....*....|....*....|....*...
gi 254540204   135 QLELKAKNYADQISRLEERESEMKKEYN 162
Cdd:pfam09728  186 KELLKLRELQAQVQTLSETEKELREQLN 213
COG1579 COG1579
Predicted nucleic acid-binding protein, contains Zn-ribbon domain [General function ...
386-523 7.03e-04

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


Pssm-ID: 224495  Cd Length: 239  Bit Score: 42.74  E-value: 7.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204  386 MGKEVGNLLLENSQLLETKNALNVVKNDLIAKVDQLSGEQEVLKGELEAAKQAKVKLENRIKELEEELK---------RV 456
Cdd:COG1579     1 MMNNNLKSLLAIQKLDLEKDRLEPRIKEIRKALKKAKAELEALNKALEALEIELEDLENQVSQLESEIQeirerikraEE 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 254540204  457 KSEAVTARREPREevedvssyLCTELDKipmAQRRRFT-RVEMARVLMERNQYKERLMELQEAVRWTE 523
Cdd:COG1579    81 KLSAVKDERELRA--------LNIEIQI---AKERINSlEDELAELMEEIEKLEKEIEDLKERLERLE 137
Taxilin pfam09728
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ...
394-472 7.17e-04

Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain in its C-terminal half and is ubiquitously expressed. It is a novel binding partner of several syntaxin family members and is possibly involved in Ca2+-dependent exocytosis in neuroendocrine cells. Gamma-taxilin, described as leucine zipper protein Factor Inhibiting ATF4-mediated Transcription (FIAT), localizes to the nucleus in osteoblasts and dimerizes with ATF4 to form inactive dimers, thus inhibiting ATF4-mediated transcription.


Pssm-ID: 313024  Cd Length: 302  Bit Score: 43.01  E-value: 7.17e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 254540204   394 LLENSQLLETKNALNVVKNDLIAKvdqlsgEQEVLKGELEAAKQAKVKLENRIKELEEELKRVKSEavtARREPREEVE 472
Cdd:pfam09728   30 LLEEMKRLEKDLKKLKKRADQLQK------EKDQLQSELSKAILAKSKLEKLCRELQKQNKKIKEE---SKKLAKEEEE 99
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
41-198 7.28e-04

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


Pssm-ID: 224755  Cd Length: 225  Bit Score: 42.30  E-value: 7.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204   41 ERLIHCYDEEVVKELmplvVNVLENLDSVLSENQEHEVELELLREDNEQLltqYER-EKALRKqAEEKFIEFedALEqEK 119
Cdd:COG1842    26 EKMLEQAIRDMESEL----AKARQALAQAIARQKQLERKLEEAQARAEKL---EEKaELALQA-GNEDLARE--ALE-EK 94
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 254540204  120 KELQIQVEHYEFQTRQLELKAKNYADQISRLEERESEMKKEYNALHQRHTeMIQTyvehieRSKMQQVGGSGQTESSLP 198
Cdd:COG1842    95 QSLEDLAKALEAELQQAEEQVEKLKKQLAALEQKIAELRAKKEALKARKA-AAKA------QEKVNRSLGGGSSSSAMA 166
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
48-170 7.37e-04

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


Pssm-ID: 224117  Cd Length: 1163  Bit Score: 43.93  E-value: 7.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204   48 DEEVVKELMPLVVNVLENLDSVLSENQEHEVELE----LLREDNEQLLTQYEREKALRKQAEEKFIEFEDA--------- 114
Cdd:COG1196   738 RLEELEEELEELEEELEELQERLEELEEELESLEealaKLKEEIEELEEKRQALQEELEELEEELEEAERRldalerele 817
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 254540204  115 --------LEQEKKELQIQVEHYEFQTRQLELKAKNYADQISRLEERESEMKKEYNALHQRHTE 170
Cdd:COG1196   818 sleqrrerLEQEIEELEEEIEELEEKLDELEEELEELEKELEELKEELEELEAEKEELEDELKE 881
PRK12495 PRK12495
hypothetical protein; Provisional
834-940 7.91e-04

hypothetical protein; Provisional


Pssm-ID: 183558  Cd Length: 226  Bit Score: 42.55  E-value: 7.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204  834 SRGDTPVLDKGQG-DVATTANGKVNPSQSTEEATEATEVPDPGPSESEA-------TTVRPGPLTEHVFTDPAPTPSssT 905
Cdd:PRK12495   69 TEDGAAGDDAGDGaEATAPSDAGSQASPDDDAQPAAEAEAADQSAPPEAsstsatdEAATDPPATAAARDGPTPDPT--A 146
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 254540204  906 QPASENGSESNGTIVQPQVEPSGElSTTTSSAAPT 940
Cdd:PRK12495  147 QPATPDERRSPRQRPPVSGEPPTP-STPDAHVAGT 180
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
8-185 8.07e-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  Cd Length: 1164  Bit Score: 43.90  E-value: 8.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204     8 EGGGVVVYQDDYCSGSVMS--------ERVSGLAgsiyrEFERLIHcydeevvkelmplvvNVLENLDSVlsENQEHEVE 79
Cdd:TIGR02169  133 PEGYNVVLQGDVTDFISMSpverrkiiDEIAGVA-----EFDRKKE---------------KALEELEEV--EENIERLD 190
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204    80 LeLLREDNEQLLT-QYEREKALRKQA-EEKFIEFE--------DALEQEKKELQIQVEHYEFQTRQLELKAKNYADQISR 149
Cdd:TIGR02169  191 L-IIDEKRQQLERlRREREKAERYQAlLKEKREYEgyellkekEALERQKEAIERQLASLEEELEKLTEEISELEKRLEE 269
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 254540204   150 LEERESEMKKEYNALHQRHTEMIQTYVE--HIERSKMQ 185
Cdd:TIGR02169  270 IEQLLEELNKKIKDLGEEEQLRVKEKIGelEAEIASLE 307
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
61-188 8.55e-04

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 223496  Cd Length: 908  Bit Score: 43.60  E-value: 8.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204   61 NVLENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRkQAEEKFIEFEDALEQEKKELQIQVEHYEFQTRQLELKA 140
Cdd:COG0419   630 EAEEELESELEKLNLQAELEELLQAALEELEEKVEELEAEI-RRELQRIENEEQLEEKLEELEQLEEELEQLREELEELL 708
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 254540204  141 KNYADQISRLEEREsEMKKEYNALHQRHTEMIQTYVEHIE-RSKMQQVG 188
Cdd:COG0419   709 KKLGEIEQLIEELE-SRKAELEELKKELEKLEKALELLEElREKLGKAG 756
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
63-187 9.67e-04

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877  Cd Length: 569  Bit Score: 43.29  E-value: 9.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204   63 LENLDSVLSENQEHEVELEL--LREDNEQLLTQ----Y---EREKALRKQAEEKFIEFEDALE---QEKKELQIQVEH-- 128
Cdd:PRK04778  258 IQDLKEQIDENLALLEELDLdeAEEKNEEIQERidqlYdilEREVKARKYVEKNSDTLPDFLEhakEQNKELKEEIDRvk 337
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 254540204  129 --YEFQTRQLElKAKNYADQISRLEERESEMKKEYNALHQRHT---EMIQTYVEHIERSKMQQV 187
Cdd:PRK04778  338 qsYTLNESELE-SVRQLEKQLESLEKQYDEITERIAEQEIAYSelqEELEEILKQLEEIEKEQE 400
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
63-185 9.96e-04

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 223496  Cd Length: 908  Bit Score: 43.21  E-value: 9.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204   63 LENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRKQAEEKFIEFEDALEQEKKELQIqvehyEFQTRQLELKAKN 142
Cdd:COG0419   615 LLQSLELSEAENELEEAEEELESELEKLNLQAELEELLQAALEELEEKVEELEAEIRRELQR-----IENEEQLEEKLEE 689
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 254540204  143 YADQISRLEERESEMKKEYNALH--QRHTEMIQTYVEHIERSKMQ 185
Cdd:COG0419   690 LEQLEEELEQLREELEELLKKLGeiEQLIEELESRKAELEELKKE 734
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
79-517 1.08e-03

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


Pssm-ID: 224117  Cd Length: 1163  Bit Score: 43.16  E-value: 1.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204   79 ELELLREDNEQLLTQYEREKALRKQAEEKFIEFEDALEQEKK---ELQIQVEHYEFQTRQLELKAKNYADQISRLEERES 155
Cdd:COG1196   668 ELKELEEELAELEAQLEKLEEELKSLKNELRSLEDLLEELRRqleELERQLEELKRELAALEEELEQLQSRLEELEEELE 747
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204  156 EMKKEYNALHQRhtemiqtyVEHIERskmqqvggsgqtesslpgrsrkerptslnvfpladgmcpndEMsESGQSSAAAt 235
Cdd:COG1196   748 ELEEELEELQER--------LEELEE-----------------------------------------EL-ESLEEALAK- 776
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204  236 psttgtksntptssvpsaavtpLNESLQplgdyvSVTKNNKQAREKRNSRNMEVqvtqemrnvsigmgssdewSDVQDII 315
Cdd:COG1196   777 ----------------------LKEEIE------ELEEKRQALQEELEELEEEL-------------------EEAERRL 809
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204  316 DSTPELDVCPETRLERTGSSptqgivnkafginTDSLYHELstagSEVIGDVDEGADLLGEFSvrddffgmgKEVGNLLL 395
Cdd:COG1196   810 DALERELESLEQRRERLEQE-------------IEELEEEI----EELEEKLDELEEELEELE---------KELEELKE 863
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204  396 ENSQLLETKNALNVVKNDLIAKVDQLSGEQEVLKGELEAAKQAKVKLENRIKELEEELKRVKSEAVTARREPREEVEDVS 475
Cdd:COG1196   864 ELEELEAEKEELEDELKELEEEKEELEEELRELESELAELKEEIEKLRERLEELEAKLERLEVELPELEEELEEEYEDTL 943
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 254540204  476 SY-LCTELDKIPmAQRRRFTRVEMaRVLMERNQYKERLMELQE 517
Cdd:COG1196   944 ETeLEREIERLE-EEIEALGPVNL-RAIEEYEEVEERYEELKS 984
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
74-183 1.16e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 316391  Cd Length: 352  Bit Score: 42.58  E-value: 1.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204    74 QEHEVELELLREDNEQLL----TQYEREKALRKQAEEKFIEFEDALEQEKKELQIQVEHYEFQTRQLELKAKNYADQISR 149
Cdd:pfam13868   87 QKRQLEYEEKLQEKEQIDeiveRIQEEDQAEAEEKLEKQKELREEIDEFNEEQKERKEQEKEEEREEDERILEYLREKEE 166
                           90       100       110
                   ....*....|....*....|....*....|....
gi 254540204   150 LEERESEMKKEYNALHQRHTEMIQTYVEHIERSK 183
Cdd:pfam13868  167 REEEREAERREIEEEKEREIARLRAQQEKAQDEK 200
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
61-160 1.28e-03

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


Pssm-ID: 224117  Cd Length: 1163  Bit Score: 43.16  E-value: 1.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204   61 NVLENLDSVLSENQEhevELELLREDNEQLLTQYEREKALRKQAEEKFIEFED---ALEQEKKELQIQVEHYEFQTRQLE 137
Cdd:COG1196   239 KELEELEEELSRLEE---ELEELQEELEEAEKEIEELKSELEELREELEELQEellELKEEIEELEGEISLLRERLEELE 315
                          90       100
                  ....*....|....*....|...
gi 254540204  138 LKAKNYADQISRLEERESEMKKE 160
Cdd:COG1196   316 NELEELEERLEELKEKIEALKEE 338
DivIVA pfam05103
DivIVA protein; The Bacillus subtilis divIVA1 mutation causes misplacement of the septum ...
38-167 1.30e-03

DivIVA protein; The Bacillus subtilis divIVA1 mutation causes misplacement of the septum during cell division, resulting in the formation of small, circular, anucleate mini-cells. Inactivation of divIVA produces a mini-cell phenotype, whereas overproduction of DivIVA results in a filamentation phenotype. These proteins appear to contain coiled-coils.


Pssm-ID: 309994  Cd Length: 131  Bit Score: 40.25  E-value: 1.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204    38 REFERLIHCYDEEVVKELMPLVVnvlENLDSVLSENQEHEVELELLREDneqlLTQY-EREKALRK---QAEEkfiEFED 113
Cdd:pfam05103    9 KEFKKKFRGYDPDEVDEFLDQVA---EDYEALYRENAELKEKIAELEEK----LAHYkEIEETLQNtliVAQE---TAEE 78
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 254540204   114 ALEQEKKELQIQVEHYEFQTRQLELKAKNYADQISrlEEREsEMKKEYNALHQR 167
Cdd:pfam05103   79 VKANAQKEAELIIKEAEAKAERIVDDANEEAKKIN--DEIE-ELKRQRRQFRTR 129
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
52-177 1.37e-03

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


Pssm-ID: 224259  Cd Length: 294  Bit Score: 41.98  E-value: 1.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204   52 VKELMPLVVNVLENLDSVLSENQEHEVELELLREDNEQLLTQYERekaLRKQAEEKFIEfedALEQEKKELQIQVEHYEF 131
Cdd:COG1340    50 VRELREKAQELREERDEINEEVQELKEKRDEINAKLQELRKEYRE---LKEKRNEFNLG---GRSIKSLEREIERLEKKQ 123
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 254540204  132 QTRQLEL---------------------KAKNYADQISRLEERESEMKKEYNALHQR-----------HTEMIQTYVE 177
Cdd:COG1340   124 QTSVLTPeeerelvqkikelrkeledakKALEENEKLKELKAEIDELKKKAREIHEKiqelaneaqeyHEEMIKLFEE 201
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
74-185 1.44e-03

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


Pssm-ID: 224117  Cd Length: 1163  Bit Score: 42.78  E-value: 1.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204   74 QEHEVELELLREDNEQLLTQYEREKALRKQAEEKFIEFEDALEQEKKELQI-QVEHYEFQT--RQLELKAKNYADQISRL 150
Cdd:COG1196   235 KELRKELEELEEELSRLEEELEELQEELEEAEKEIEELKSELEELREELEElQEELLELKEeiEELEGEISLLRERLEEL 314
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 254540204  151 EERESEMKKEYNALHQRHtEMIQTYVEHIERSKMQ 185
Cdd:COG1196   315 ENELEELEERLEELKEKI-EALKEELEERETLLEE 348
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
64-185 1.47e-03

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


Pssm-ID: 274008  Cd Length: 1179  Bit Score: 42.74  E-value: 1.47e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204    64 ENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRKQAEEKFIEFEDALEQEKKELQIQVEHYEFQTRQLELKAKNY 143
Cdd:TIGR02168  817 EEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSEL 896
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 254540204   144 ADQISRLEERESEMKKEYNALHQRhTEMIQTYVEHIERSKMQ 185
Cdd:TIGR02168  897 EELSEELRELESKRSELRRELEEL-REKLAQLELRLEGLEVR 937
PKK pfam12474
Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino ...
76-171 1.53e-03

Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino acids in length. The family is found in association with pfam00069. Polo-like kinase 1 (Plx1) is essential during mitosis for the activation of Cdc25C, for spindle assembly, and for cyclin B degradation. This family is Polo kinase kinase (PKK) which phosphorylates Polo kinase and Polo-like kinase to activate them. PKK is a serine/threonine kinase.


Pssm-ID: 315199  Cd Length: 141  Bit Score: 40.23  E-value: 1.53e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204    76 HEVELELLREDNEQLLTQYEREKALRKQAEEKFI--EFEDALEQEKKELQIQVEhyefqtrqlELKAKNYADQISRLEER 153
Cdd:pfam12474   23 YEKELEQLERQQKRQIEKLEQSQALELKRLPKRIraEQKKRLKMFRESLKIEKK---------ELKQEVEREKLPKFQRK 93
                           90
                   ....*....|....*....
gi 254540204   154 ESE-MKKEYNALHQRHTEM 171
Cdd:pfam12474   94 EEKrQRKEELEQEQKHEEL 112
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
67-194 1.53e-03

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879  Cd Length: 291  Bit Score: 41.79  E-value: 1.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204   67 DSVLSEN-QEHEVELE-LLREDneQLLTQYEREKALRKQAEEkfiefedALEQEKKELQiqvEHYEFQTRQLELKAKNYA 144
Cdd:cd16269   169 EEVLQEFlQSKEAEAEaILQAD--QALTEKEKEIEAERAKAE-------AAEQERKLLE---EQQRELEQKLEDQERSYE 236
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 254540204  145 DQISRLEEresEMKKEYNALHQRHTEMIQTYVEHIERskMQQVGGSGQTE 194
Cdd:cd16269   237 EHLRQLKE---KMEEERENLLKEQERALESKLKEQEA--LLEEGFKEQAE 281
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
63-171 1.93e-03

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


Pssm-ID: 274009  Cd Length: 1164  Bit Score: 42.36  E-value: 1.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204    63 LENLDSVLSENQEHEVELELLREDNEQlltQYEREKALRKQAEEKFiefEDALEQEKKELQIQVEHYEFQTRQLELKAKN 142
Cdd:TIGR02169  239 KEAIERQLASLEEELEKLTEEISELEK---RLEEIEQLLEELNKKI---KDLGEEEQLRVKEKIGELEAEIASLERSIAE 312
                           90       100
                   ....*....|....*....|....*....
gi 254540204   143 YADQISRLEERESEMKKEYNALHQRHTEM 171
Cdd:TIGR02169  313 KERELEDAEERLAKLEAEIDKLLAEIEEL 341
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
72-203 2.07e-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: 307627  Cd Length: 1081  Bit Score: 42.47  E-value: 2.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204    72 ENQEHEVElELLREDNEQLLT------QYEREKA-LRKQAEEKfiefedalEQEKKELQIQVEHYEFQTRQLELKAKNYA 144
Cdd:pfam01576  467 ESQLQDTQ-ELLQEETRQKLAlssrlrQLEDEQNsLREQLEEE--------EEAKRNVEKQLQTLQAQLSDMKKKMEEDA 537
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 254540204   145 DQISRLEERESEMKKEYNALHQRHTEMIQTYvEHIERSK--MQQ--------VGGSGQTESSLPGRSRK 203
Cdd:pfam01576  538 GVLEALEEARKRLQRELESLTQQLEEKEAAY-DKLEKTKtrLQQelddllvdLDHQRQLVSNLEKKQKK 605
Med21 pfam11221
Subunit 21 of Mediator complex; Med21 has been known as Srb7 in yeasts, hSrb7 in humans and ...
404-474 2.13e-03

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


Pssm-ID: 314215  Cd Length: 140  Bit Score: 39.53  E-value: 2.13e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 254540204   404 KNALNVVKNDLIAKVDQLSGEQEVLKGELEAAKQakvkLENRIKELEEELKRVKSEAVTARREPREEVEDV 474
Cdd:pfam11221   65 EATQRELARDLILKAQQIEYLIDSLPGIGVSEEE----QLRRIKELEEELREAEEERQEAVKEKEELLKKV 131
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
39-170 2.26e-03

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


Pssm-ID: 274009  Cd Length: 1164  Bit Score: 42.36  E-value: 2.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204    39 EFERLIHCYDEEVVK-------ELMPLVVNVLENLDSVLSENQE--HEVELELLREDNEQLLTQYEREKALRKQAEEKfi 109
Cdd:TIGR02169  769 ELEEDLHKLEEALNDlearlshSRIPEIQAELSKLEEEVSRIEArlREIEQKLNRLTLEKEYLEKEIQELQEQRIDLK-- 846
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 254540204   110 EFEDALEQEKKELQIQVEHYEFQTRQLELKAKNYADQISRLEERESEMKKEYNALHQRHTE 170
Cdd:TIGR02169  847 EQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEE 907
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
78-167 2.29e-03

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


Pssm-ID: 224117  Cd Length: 1163  Bit Score: 42.39  E-value: 2.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204   78 VELELLREDNEQLLTQYEREKALRKQAEEKFIEFED---ALEQEKKELQIQVEHYEFQTRQLELKAKNYADQISRLEERE 154
Cdd:COG1196   232 AKLKELRKELEELEEELSRLEEELEELQEELEEAEKeieELKSELEELREELEELQEELLELKEEIEELEGEISLLRERL 311
                          90
                  ....*....|...
gi 254540204  155 SEMKKEYNALHQR 167
Cdd:COG1196   312 EELENELEELEER 324
CENP-Q pfam13094
CENP-Q, a CENPA-CAD centromere complex subunit; CENP-Q is one of the components that assembles ...
65-166 2.35e-03

CENP-Q, a CENPA-CAD centromere complex subunit; CENP-Q is one of the components that assembles onto the CENPA-nucleosome distal (CAD) centromere. The centromere, which is the basic element of chromosome inheritance, is epigenetically determined in mammals. CENP-A, the centromere-specific histone H3 variant, assembles an array of nucleosomes and it is this that seems to be the prime candidate for specifying centromere identity. CENPA nucleosomes directly recruit a proximal CENPA-nucleosome-associated complex (NAC) comprised of CENP-M, CENP-N and CENP-T, CENP-U(50), CENP-C and CENP-H. Assembly of the CENPA NAC at centromeres is dependent on CENP-M, CENP-N and CENP-T. Additionally, there are seven other subunits which make up the CENPA-nucleosome distal (CAD) centromere, CENP-K, CENP-L, CENP-O, CENP-P, CENP-Q, CENP-R and CENP-S, also assembling on the CENP-A NAC. Fta7 is the equivalent component of the fission yeast Sim4 complex.


Pssm-ID: 315707  Cd Length: 163  Bit Score: 39.96  E-value: 2.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204    65 NLDSVLSENQEHEVELELLREDNEQLLTQYEREkalrkqaeekfiefEDALEQEKKELQiqvehyefqtrQLELKAKNya 144
Cdd:pfam13094   21 DFEKLLDRNRALEAQLTPELHSLELLEEEIEKE--------------EALLESDEEYLE-----------ELEKNAKA-- 73
                           90       100
                   ....*....|....*....|..
gi 254540204   145 dQISRLEERESEMKKEYNALHQ 166
Cdd:pfam13094   74 -EERELRKEEEKAKKLHPLLQE 94
COG4913 COG4913
Uncharacterized protein, contains a C-terminal ATPase domain [Function unknown];
401-537 2.51e-03

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


Pssm-ID: 227250  Cd Length: 1104  Bit Score: 41.93  E-value: 2.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204  401 LETKNALNVVKNDLIAKVDQLSGEQEVLKGELEAAKQAKVKLEnrIKELEEELKRVKSEAVTARREPREEVEDVSSYLCT 480
Cdd:COG4913   275 QQSKDHANALKKALPTVGNRIKKEEQETLVRQFTVEQTQAKSK--VESAKIETDRAREMETLAHDNVKQIVGAQHGILSA 352
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 254540204  481 ELDKIPMAQRRRFTRVEMARVLMER-----NQYKERLMELQEAVRW-TEMIRASRE--HPSVQEK 537
Cdd:COG4913   353 KREGAVDKRRTISTARAGLDALVKGlggaaPESAEELLELNNAARLtVDEYPAAREalESAGQRN 417
SHE3 pfam17078
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ...
49-182 2.73e-03

SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an RNA-binding protein that binds specific mRNAs, including the mRNA of Ash1, which is invalid in cell-fate determination. She3 acts as an adapter protein that docks the myosin motor Myo4p onto an Ash1-She2p ribonucleoprotein complex. She3 seems to bind to Myo4p and Shep2p via different domains.


Pssm-ID: 293683  Cd Length: 228  Bit Score: 40.88  E-value: 2.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204    49 EEVVKELMPLVV---NVLENLDSVLSENQEHEVELELLREDNEQLLTQYER-EKALRKqaeekfiefedaLEQEKKELQI 124
Cdd:pfam17078   13 DALTKTNLQLTVqsqNLLSKLEIAQQKESKFLENLASLKHENDNLSSMLNRkERRLKD------------LEDQLSELKN 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 254540204   125 QVEHYEFQTRQLELKAKNYADQISRLEERESEMKKEYNAL---HQRHTEMIQTYVEHIERS 182
Cdd:pfam17078   81 SYEELTESNKQLKKRLENSSASETTLEAELERLQIQYDALvdsQNEYKDHYQQEINTLQES 141
APG6 pfam04111
Autophagy protein Apg6; In yeast, 15 Apg proteins coordinate the formation of autophagosomes. ...
412-459 3.11e-03

Autophagy protein Apg6; 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: 309295  Cd Length: 308  Bit Score: 41.01  E-value: 3.11e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 254540204   412 NDLIAKVDQLSGEQEVLKGELEAAKQAKVKLENRIKELEEELKRVKSE 459
Cdd:pfam04111   46 EALEKELEKLEKEEEELLQELEELEKEREELDAELEKLEEELEELDEE 93
DDRGK pfam09756
DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and ...
74-187 3.34e-03

DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and vertebrates. They contain a highly conserved DDRGK motif.


Pssm-ID: 313051  Cd Length: 188  Bit Score: 40.03  E-value: 3.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204    74 QEHEVELELlREDNEQLLTQYEREKALRKQAEEKFIEFEDALEQEKKELQIQVEHYEFQtrqlELKAknyadQISRLEER 153
Cdd:pfam09756   19 QQREAEEEE-REERKKLEEKKEKEYKEREEREEEAEKEKEEEERKQEEEQERKEQEEYE----KLKS-----QFVVEEEG 88
                           90       100       110
                   ....*....|....*....|....*....|....
gi 254540204   154 ESEMKKEYNAlhqrhtEMIQTYVEHIERSKMQQV 187
Cdd:pfam09756   89 TDKLSAEDES------QLLEDFINYIKLKKVVLL 116
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
86-181 3.42e-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: 214922  Cd Length: 140  Bit Score: 39.10  E-value: 3.42e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204     86 DNEQLLTQYEREKALRKQAEEKFIEFEDALEQEKKELQIQVEhyEFQTRQLELKAKNYADQISRLEERESEMKKEYNA-- 163
Cdd:smart00935    5 DVQKILQESPAGKAAQKQLEKEFKKRQAELEKLEKELQKLKE--KLQKDAATLSEAAREKKEKELQKKVQEFQRKQQKlq 82
                            90       100
                    ....*....|....*....|
gi 254540204    164 --LHQRHTEMIQTYVEHIER 181
Cdd:smart00935   83 qdLQKRQQEELQKILDKINK 102
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
64-165 3.52e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750  Cd Length: 782  Bit Score: 41.35  E-value: 3.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204   64 ENLDSVL--SENQEHEVE-----LELLREDNEQLLTQYEREKALRKQAEEKFI-----EFEDALEQEKKE---------L 122
Cdd:PRK00409  516 EKLNELIasLEELERELEqkaeeAEALLKEAEKLKEELEEKKEKLQEEEDKLLeeaekEAQQAIKEAKKEadeiikelrQ 595
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 254540204  123 QIQVEHYEFQTRQLELKAKNYADQISRLEERESEMKKEYNALH 165
Cdd:PRK00409  596 LQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEELK 638
SH3_and_anchor TIGR04211
SH3 domain protein; Members of this protein family have a signal peptide, a strongly conserved ...
388-466 3.76e-03

SH3 domain protein; Members of this protein family have a signal peptide, a strongly conserved SH3 domain, a variable region, and then a C-terminal hydrophobic transmembrane alpha helix region.


Pssm-ID: 275056  Cd Length: 198  Bit Score: 39.99  E-value: 3.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204   388 KEVGNLLLENSQLLETKNALNVVKNDLIAKVDQLSGEQEVLKGELEAAKQAK---VKLENRIKELEEELKRVKSEAVTAR 464
Cdd:TIGR04211   73 QELAELQEELAELQEQLAELRQENQELKQQLSTLEAELEELQKELERIKQISanaIELDEENRELREELAELKQENEALE 152

                   ..
gi 254540204   465 RE 466
Cdd:TIGR04211  153 AE 154
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
49-186 3.83e-03

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: 308206  Cd Length: 1162  Bit Score: 41.50  E-value: 3.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204    49 EEVVKELMPLVVNVLENLDSVLSENQEHEVELELLREDNEQLLtqyEREKALRKQAEEKFIEFEDALEQEKKELQIQ--- 125
Cdd:pfam02463  278 EEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKES---EKEKKKAEKELKKEKEEIEELEKELKELEIKrea 354
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 254540204   126 VEHYEFQTRQLELKAKNYADQI----SRLEERESEMKKEYNALHQRHTEMIQTYVEHIERSKMQQ 186
Cdd:pfam02463  355 EEEEEEELEKLQEKLEQLEEELlakkKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLE 419
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
72-186 4.19e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 316391  Cd Length: 352  Bit Score: 40.65  E-value: 4.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204    72 ENQEHEVElELLREDNEQLLTQYEREKALRKQaEEKFIEFEDALEQEKKELQIQVEHYEfQTRQLE----LKAKNYADQI 147
Cdd:pfam13868   30 EKKRIKAE-EKEEERRLDEMMEEERLKALEEE-EEKERERKEKRKEYRQELQEQIEERE-QKRQLEyeekLQEKEQIDEI 106
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 254540204   148 SRLEERESEMKKEYNALHQRHT--EMIQTYVEHIERSKMQQ 186
Cdd:pfam13868  107 VERIQEEDQAEAEEKLEKQKELreEIDEFNEEQKERKEQEK 147
DUF737 pfam05300
Protein of unknown function (DUF737); This family consists of several uncharacterized ...
71-159 4.22e-03

Protein of unknown function (DUF737); This family consists of several uncharacterized mammalian proteins of unknown function.


Pssm-ID: 310129  Cd Length: 169  Bit Score: 39.19  E-value: 4.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204    71 SENQEHEVELELLREDNEQLLTQYEREKALRKQAEEKFIEFE---------DALEQEK---KELQIQVEHY--EFQTRQL 136
Cdd:pfam05300   47 GAGPAPVGEEELRKKIKEELYKRLEQEQAKVQEELARVAEREreaaqehltRAILRERgstEDEKLKAQQLarQLEEKEA 126
                           90       100
                   ....*....|....*....|....*
gi 254540204   137 ELKAKN--YADQISRLEERESEMKK 159
Cdd:pfam05300  127 ELKKRDafYKEQLARLEEKNAEFYK 151
YkyA pfam10368
Putative cell-wall binding lipoprotein; YkyA is a family of proteins containing a lipoprotein ...
97-188 4.33e-03

Putative cell-wall binding lipoprotein; YkyA is a family of proteins containing a lipoprotein signal and a hydrolase domain. It is similar to cell wall binding proteins and might also be recognisable by a host immune defense system. It is thus likely to belong to pathways important for pathogenicity.


Pssm-ID: 313570  Cd Length: 203  Bit Score: 39.96  E-value: 4.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204    97 EKAlrKQAEEKFIEFEDAL-EQEKKELQIQVEHYEFQTRQLElKAKNYADQ-ISRLEERESEMKKEYNALHQRHTEM--I 172
Cdd:pfam10368   25 EKA--VKLEKPFVEQQEKLqELEEKEQELYEQIIELNMDDFD-EIKKLADEaLENAEKREKLLEKEKESIEKSKEEFkeA 101
                           90
                   ....*....|....*.
gi 254540204   173 QTYVEHIERSKMQQVG 188
Cdd:pfam10368  102 KESIEKIEDEELKKQA 117
ARGLU pfam15346
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ...
424-530 4.34e-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: 317717  Cd Length: 142  Bit Score: 38.80  E-value: 4.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204   424 EQEVLKGELEAAKQAKVKLENRI--KELEEELKRVKSEAVTARREPREEVEDvssyLCTELDKIpMAQRRRftRVEMARv 501
Cdd:pfam15346   27 ELNKRSEEIEAEIERRVEEARKAmeKQVLEELEREREAELEEARRKEEEERK----KREELERI-LEENNR--KVEEAQ- 98
                           90       100
                   ....*....|....*....|....*....
gi 254540204   502 lmeRNQYKERLMELqEAVRWTEMIRASRE 530
Cdd:pfam15346   99 ---RKLAEERLAEL-EEQQRQKEERQRRK 123
EzrA COG4477
Septation ring formation regulator EzrA [Cell cycle control, cell division, chromosome ...
39-185 4.39e-03

Septation ring formation regulator EzrA [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 226883  Cd Length: 570  Bit Score: 41.21  E-value: 4.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204   39 EFERLIHCYDEEVVKELMPLVVNV---LENLDSVLSENQ---------EHEVELELLREDNEQLLTQYEREKALRKQAEE 106
Cdd:COG4477   230 QLQDLKAGYRDMKEEGYHLEHVNIdsrLERLKEQLVENSelltqleldEAEEELGLIQEKIESLYDLLEREVEAKNVVEE 309
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204  107 KFIEFEDALEQEKKE---LQIQVEH----Y-----EFQT-RQLELKAKNYADQISRLEERESEMKKEYNALhQRHTEMIQ 173
Cdd:COG4477   310 NLPILPDYLEKAKENnehLKEEIERvkesYrlaetELGSvRKFEKELKELESVLDEILENIEAQEVAYSEL-QDNLEEIE 388
                         170
                  ....*....|..
gi 254540204  174 TYVEHIERSKMQ 185
Cdd:COG4477   389 KALTDIEDEQEK 400
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
79-186 4.42e-03

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


Pssm-ID: 274008  Cd Length: 1179  Bit Score: 41.20  E-value: 4.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204    79 ELELLREDNEQLLTQYEREKALRKQAEEKFIEFEDALEQEKKELQIQVEHYEfqtrQLELKAKNYADQISRLEERESEMK 158
Cdd:TIGR02168  734 DLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIE----ELEAQIEQLKEELKALREALDELR 809
                           90       100
                   ....*....|....*....|....*...
gi 254540204   159 KEYNALHQRHTEMIQTYVEHIERSKMQQ 186
Cdd:TIGR02168  810 AELTLLNEEAANLRERLESLERRIAATE 837
Ax_dynein_light pfam10211
Axonemal dynein light chain; Axonemal dynein light chain proteins play a dynamic role in ...
59-166 4.54e-03

Axonemal dynein light chain; Axonemal dynein light chain proteins play a dynamic role in flagellar and cilia motility. Eukaryotic cilia and flagella are complex organelles consisting of a core structure, the axoneme, which is composed of nine microtubule doublets forming a cylinder that surrounds a pair of central singlet microtubules. This ultra-structural arrangement seems to be one of the most stable micro-tubular assemblies known and is responsible for the flagellar and ciliary movement of a large number of organisms ranging from protozoan to mammals. This light chain interacts directly with the N-terminal half of the heavy chains.


Pssm-ID: 313442  Cd Length: 187  Bit Score: 39.45  E-value: 4.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204    59 VVNVLENLDSVLSENQEHEV-------EL------ELLR----EDNEQ--LL---------------TQYEREKA--LRK 102
Cdd:pfam10211   34 VINLQEQLDRRLQQRQARETgicpireELysqcfdELIRqvtiNCPERglLLlrvrdeirmtiaayqTLYESSVAfgMRK 113
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 254540204   103 --QAEEKFIEFED---ALEQEKKELQIQVEhyefqtrqlELKAKnyadqISRLEERESEMKKEYNALHQ 166
Cdd:pfam10211  114 alQAEQGKSELEKkiaDLEEEKEELEKQVA---------ELKAK-----CEAIEKREEERRQAEEKKHQ 168
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
386-539 4.56e-03

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


Pssm-ID: 224259  Cd Length: 294  Bit Score: 40.43  E-value: 4.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204  386 MGKEVGNLLLENSQLLETKNALNVVKNDLIAKVDQLSGEQEVLKGEL----EAAKQAKVK---LENRIKELEEELKRVKS 458
Cdd:COG1340     4 MLDKLDELELKRKQLKEEIEELKEKRDELRKEASELAEKRDELNAKVrelrEKAQELREErdeINEEVQELKEKRDEINA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204  459 EAVTARREPREEVEDVSSY---------LCTELDKIPMAQRRRFTRVEMARVLMER-NQYKERLMELQEAVRWTEMIRAS 528
Cdd:COG1340    84 KLQELRKEYRELKEKRNEFnlggrsiksLEREIERLEKKQQTSVLTPEEERELVQKiKELRKELEDAKKALEENEKLKEL 163
                         170
                  ....*....|.
gi 254540204  529 REHpsVQEKKK 539
Cdd:COG1340   164 KAE--IDELKK 172
GreA_GreB_N pfam03449
Transcription elongation factor, N-terminal; This domain adopts a long alpha-hairpin structure.
430-457 4.63e-03

Transcription elongation factor, N-terminal; This domain adopts a long alpha-hairpin structure.


Pssm-ID: 308835  Cd Length: 71  Bit Score: 38.11  E-value: 4.63e-03
                           10        20
                   ....*....|....*....|....*...
gi 254540204   430 GELEAAKQAKVKLENRIKELEEELKRVK 457
Cdd:pfam03449   43 AEYDAAKEEQAFIEARIRELEDKLANAE 70
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
416-518 4.84e-03

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


Pssm-ID: 274009  Cd Length: 1164  Bit Score: 41.21  E-value: 4.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204   416 AKVDQLSGEQEVLKGELEAAKQAKVKLENRIKELEEELKRVKSEAVTARREPREEVEDVSSyLCTELDKipMAQRRRFTR 495
Cdd:TIGR02169  294 EKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDK-LTEEYAE--LKEELEDLR 370
                           90       100
                   ....*....|....*....|...
gi 254540204   496 VEMARVLMERNQYKERLMELQEA 518
Cdd:TIGR02169  371 AELEEVDKEFAETRDELKDYREK 393
MRP-S26 pfam14943
Mitochondrial ribosome subunit S26; This family of proteins corresponds to mitochondrial ...
68-153 4.86e-03

Mitochondrial ribosome subunit S26; This family of proteins corresponds to mitochondrial ribosomal subunit S26 in eukaryotes


Pssm-ID: 317367  Cd Length: 169  Bit Score: 39.13  E-value: 4.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204    68 SVLSENQEHEVELELLREDNEQL--LTQYEREKALRKQAEEKFIEFEDALEQEKKELQIQVEHYEFQTRQLELKAKNYad 145
Cdd:pfam14943   62 ESEEKAEEEEEEHRELMAWNDEWnaELAELREERLAKEAEEREEEILERIEEKEQKEEEKKERAEEEVLQLKEESKTF-- 139
                           90
                   ....*....|
gi 254540204   146 qISR--LEER 153
Cdd:pfam14943  140 -ITRenLDAA 148
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
61-186 5.06e-03

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


Pssm-ID: 274008  Cd Length: 1179  Bit Score: 41.20  E-value: 5.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204    61 NVLENLDSVLSENQEHEVELELLREDNEQLLTQYERE-KALRKQAeekfiefeDALEQEKKELQI-------QVEHYEFQ 132
Cdd:TIGR02168  761 AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEElKALREAL--------DELRAELTLLNEeaanlreRLESLERR 832
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 254540204   133 TRQLELKAKNYADQISRLEERESEMKKEYNALHQRHTEMIQTYVEH-IERSKMQQ 186
Cdd:TIGR02168  833 IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALlNERASLEE 887
PRK03918 PRK03918
chromosome segregation protein; Provisional
389-542 5.20e-03

chromosome segregation protein; Provisional


Pssm-ID: 235175  Cd Length: 880  Bit Score: 40.82  E-value: 5.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204  389 EVGNLLLENSQLLETK----NALNVVKNDLIAKVDQLSGEQEVL---KGELEAAK-------QAKVKLENRIKELEEELK 454
Cdd:PRK03918  190 NIEELIKEKEKELEEVlreiNEISSELPELREELEKLEKEVKELeelKEEIEELEkelesleGSKRKLEEKIRELEERIE 269
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204  455 RVKSEAvtarREPREEVEDVssylcTELDKipmaqrrrftRVEMARVLME-RNQYKERLMELQ-EAVRWTEMIRASREHP 532
Cdd:PRK03918  270 ELKKEI----EELEEKVKEL-----KELKE----------KAEEYIKLSEfYEEYLDELREIEkRLSRLEEEINGIEERI 330
                         170
                  ....*....|
gi 254540204  533 SVQEKKKSTI 542
Cdd:PRK03918  331 KELEEKEERL 340
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
9-170 5.46e-03

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


Pssm-ID: 274008  Cd Length: 1179  Bit Score: 41.20  E-value: 5.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204     9 GGGVVVYQDDYCSGSVMSERvsglagsiyREFERLihcydEEVVKELMPLVVNVLENLDSVLSENQEHEVELELLR---E 85
Cdd:TIGR02168  657 PGGVITGGSAKTNSSILERR---------REIEEL-----EEKIEELEEKIAELEKALAELRKELEELEEELEQLRkelE 722
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204    86 DNEQLLTQYEREKALRKQAEEKFIEFEDALEQEKKELQIQVEHYEFQTRQLELKAKNYADQISRLEERESEMKKEYNALH 165
Cdd:TIGR02168  723 ELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR 802

                   ....*
gi 254540204   166 QRHTE 170
Cdd:TIGR02168  803 EALDE 807
FAM184 pfam15665
Family with sequence similarity 184, A and B; The function of FAM184 is not known.
73-181 6.02e-03

Family with sequence similarity 184, A and B; The function of FAM184 is not known.


Pssm-ID: 317968  Cd Length: 211  Bit Score: 39.65  E-value: 6.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204    73 NQEHEVELELLREDNEQLLTQYEREKALRKQAEEKFIEFEDALEQEKKELQIQVEHYEFQTRQLELKAKNYADqisRLEE 152
Cdd:pfam15665    9 NDEHEAEIQALKEAHEEEIQQILAETREKILQYKSKIGEELDLKRRIQNLEESLEQHEKEKRQALAEFEQYKR---RSED 85
                           90       100
                   ....*....|....*....|....*....
gi 254540204   153 RESEMKKEYNalhQRHTEMiQTYVEHIER 181
Cdd:pfam15665   86 RELCLEAEHS---QKVVAL-SREVEEAKR 110
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
64-181 6.99e-03

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


Pssm-ID: 224117  Cd Length: 1163  Bit Score: 40.47  E-value: 6.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204   64 ENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRKQAEEKfIEfedALEQEKKELQIQVEHYEFQTRQLELKAKNY 143
Cdd:COG1196   260 EELEEAEKEIEELKSELEELREELEELQEELLELKEEIEELEGE-IS---LLRERLEELENELEELEERLEELKEKIEAL 335
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 254540204  144 ADQISRLEERESEM---KKEYNALHQRHTEMIQTYVEHIER 181
Cdd:COG1196   336 KEELEERETLLEELeqlLAELEEAKEELEEKLSALLEELEE 376
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
388-539 7.33e-03

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


Pssm-ID: 274009  Cd Length: 1164  Bit Score: 40.44  E-value: 7.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204   388 KEVGNLLLENSQLLETKNALNVVKNDLIAKVDQLSGEQEVLKGELEAAKQAKVKLENRIKELEEELKRVKSEavtarrep 467
Cdd:TIGR02169  819 QKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKE-------- 890
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204   468 REEVEdvssylcTELDKIPMAQRRRFTRVEMARVLMERNQYK-----ERLMELQEAVRwtEMIRASREHPS---VQEKKK 539
Cdd:TIGR02169  891 RDELE-------AQLRELERKIEELEAQIEKKRKRLSELKAKlealeEELSEIEDPKG--EDEEIPEEELSledVQAELQ 961
COG4487 COG4487
Uncharacterized protein, contains DUF2130 domain [Function unknown];
49-180 8.25e-03

Uncharacterized protein, contains DUF2130 domain [Function unknown];


Pssm-ID: 226889  Cd Length: 438  Bit Score: 40.19  E-value: 8.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204   49 EEVVKELMPLVVNVLENLDSVLSENQEHEVELELL--------REDNEQLLTQYEREKALRKQAEEKFIEFEDALEQEKK 120
Cdd:COG4487    85 NEQIKQFELALQDEIAKLEALELLNLEKDKELELLekeldelsKELQKQLQNTAEIIEKKRENNKNEERLKFENEKKLEE 164
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 254540204  121 ELQIQVEHYEFQTRQLELKAKNYADQisrlEERESeMKKEYNALHQRH--TEMI-QTYVEHIE 180
Cdd:COG4487   165 SLELEREKFEEQLHEANLDLEFKENE----EQRES-KWAILKKLKRRAelGSQQvQGEALELP 222
ERM pfam00769
Ezrin/radixin/moesin family; This family of proteins contain a band 4.1 domain (pfam00373), at ...
431-537 8.78e-03

Ezrin/radixin/moesin family; This family of proteins contain a band 4.1 domain (pfam00373), at their amino terminus. This family represents the rest of these proteins.


Pssm-ID: 307079  Cd Length: 241  Bit Score: 39.12  E-value: 8.78e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204   431 ELEAAKQAKVKLENRIKELEEELKRVKSEAVTARREpREEVEDvssyLCTELDKIPMAQRRrfTRVEMARVLMERNQYKE 510
Cdd:pfam00769   20 EMRRAQEELEESEETAELLEEKRRRAEEEAELLEQK-AQEAEE----EKERLEESAEMQEE--EKEQLERELREAEEEIA 92
                           90       100       110
                   ....*....|....*....|....*....|...
gi 254540204   511 RLMEL-----QEAVRW-TEMIRASREHPSVQEK 537
Cdd:pfam00769   93 RLEEEverkeEEARRLqEELEEAREAEEEAKEK 125
PRK03918 PRK03918
chromosome segregation protein; Provisional
404-538 8.94e-03

chromosome segregation protein; Provisional


Pssm-ID: 235175  Cd Length: 880  Bit Score: 40.05  E-value: 8.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204  404 KNALNVVKNdliakvdqLSGEQEVLKGELEAAKQakvkLENRIKELEEELKRVK---SEAVTARREPREEVEDVSSYLcT 480
Cdd:PRK03918  165 KNLGEVIKE--------IKRRIERLEKFIKRTEN----IEELIKEKEKELEEVLreiNEISSELPELREELEKLEKEV-K 231
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204  481 ELDKIpmaqRRRFT--RVEMARVLMERNQYKERLMELQeavrwtEMIRASREHPSVQEKK 538
Cdd:PRK03918  232 ELEEL----KEEIEelEKELESLEGSKRKLEEKIRELE------ERIEELKKEIEELEEK 281
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
401-530 9.23e-03

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


Pssm-ID: 224117  Cd Length: 1163  Bit Score: 40.08  E-value: 9.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540204  401 LETKNALNVVKNDLIA-KVDQLSGEQEVLKGELEAAKQAKVKLENRIKELEEELKRVKSEavtaRREPREEVEDVSsylc 479
Cdd:COG1196   216 QELKAELRELELALLLaKLKELRKELEELEEELSRLEEELEELQEELEEAEKEIEELKSE----LEELREELEELQ---- 287
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 254540204  480 TELDKIPMAQRRRftRVEMARVLMERNQYKERLMELQEAVRWTEMIRASRE 530
Cdd:COG1196   288 EELLELKEEIEEL--EGEISLLRERLEELENELEELEERLEELKEKIEALK 336
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.16
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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